data_9NSR
# 
_entry.id   9NSR 
# 
_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   9NSR         pdb_00009nsr 10.2210/pdb9nsr/pdb 
WWPDB D_1000291967 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9NSR 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-17 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu                    Scott    Lovell ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 isabelle.phan@seattlechildrens.org Isabelle Phan   ? 'principal investigator/group leader' 0000-0001-6873-3401 
4 julie.early@seattlechildrens.org   Julie    Early  ? 'principal investigator/group leader' 0000-0003-1224-2747 
5 peter.myler@seattlechildrens.org   Peter    Myler  ? 'principal investigator/group leader' 0000-0002-0056-0513 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Seattle Structural Genomics Center for Infectious Disease'          1 ? 
'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 2 ? 
# 
_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 bifunctional farnesyl/geranylgeranyl pyrophosphate synthase (FPPS/GGPPS) from Plasmodium falciparum in complex with MMV019313
;
_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 'Lovell, S.'     1 0000-0002-3215-4472 
primary 'Cooper, A.'     2 0000-0001-8297-229X 
primary 'Liu, L.'        3 0000-0003-0514-281X 
primary 'Battaile, K.P.' 4 0000-0003-0833-3259 
# 
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 'Bifunctional farnesyl/geranylgeranyl diphosphate synthase'                                44668.910 1 2.5.1.29 
? ? ? 
2 non-polymer syn 'N-[3-(azepan-1-yl)propyl]-5-methyl-4-oxo-4,5-dihydrothieno[3,2-c]quinoline-2-carboxamide' 397.534   1 ?        
? ? ? 
# 
_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       
;GPMENEQNNQDSENGLDYFRSMYDRYRDVFINHINDYVLEDDIKIIISKYYKLLFDYNCLGGKNNRGILVILIYEYVKNR
DINCNEWEKVACIAWCIEILQASFLVADDIMDKGETRRNKHCWYLLKDVEIKNAVNDVFLLYNAIYKLLDVYLRNDNCYL
DLITSFREATLKTIVGQHLDTNIFSDKYSHIDKDIDVNNINISQENKININMLNFKVYQNIIIHKTAYYSFFLPIVCGMQ
MGGISLDNLLYKKVENIAILMGEYFQVHDDYIDTFGDSKKTGKVGSDIQNNKLTWPLIKAFELCSQPEKEDIIRNYGKDN
VTCIKFINDIYEHYNIRDHYVEYEKKQKMKILEAINQLHHEGIEYVLKYVMDILFTGA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPMENEQNNQDSENGLDYFRSMYDRYRDVFINHINDYVLEDDIKIIISKYYKLLFDYNCLGGKNNRGILVILIYEYVKNR
DINCNEWEKVACIAWCIEILQASFLVADDIMDKGETRRNKHCWYLLKDVEIKNAVNDVFLLYNAIYKLLDVYLRNDNCYL
DLITSFREATLKTIVGQHLDTNIFSDKYSHIDKDIDVNNINISQENKININMLNFKVYQNIIIHKTAYYSFFLPIVCGMQ
MGGISLDNLLYKKVENIAILMGEYFQVHDDYIDTFGDSKKTGKVGSDIQNNKLTWPLIKAFELCSQPEKEDIIRNYGKDN
VTCIKFINDIYEHYNIRDHYVEYEKKQKMKILEAINQLHHEGIEYVLKYVMDILFTGA
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        'N-[3-(azepan-1-yl)propyl]-5-methyl-4-oxo-4,5-dihydrothieno[3,2-c]quinoline-2-carboxamide' 
_pdbx_entity_nonpoly.comp_id     A1B0W 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   MET n 
1 4   GLU n 
1 5   ASN n 
1 6   GLU n 
1 7   GLN n 
1 8   ASN n 
1 9   ASN n 
1 10  GLN n 
1 11  ASP n 
1 12  SER n 
1 13  GLU n 
1 14  ASN n 
1 15  GLY n 
1 16  LEU n 
1 17  ASP n 
1 18  TYR n 
1 19  PHE n 
1 20  ARG n 
1 21  SER n 
1 22  MET n 
1 23  TYR n 
1 24  ASP n 
1 25  ARG n 
1 26  TYR n 
1 27  ARG n 
1 28  ASP n 
1 29  VAL n 
1 30  PHE n 
1 31  ILE n 
1 32  ASN n 
1 33  HIS n 
1 34  ILE n 
1 35  ASN n 
1 36  ASP n 
1 37  TYR n 
1 38  VAL n 
1 39  LEU n 
1 40  GLU n 
1 41  ASP n 
1 42  ASP n 
1 43  ILE n 
1 44  LYS n 
1 45  ILE n 
1 46  ILE n 
1 47  ILE n 
1 48  SER n 
1 49  LYS n 
1 50  TYR n 
1 51  TYR n 
1 52  LYS n 
1 53  LEU n 
1 54  LEU n 
1 55  PHE n 
1 56  ASP n 
1 57  TYR n 
1 58  ASN n 
1 59  CYS n 
1 60  LEU n 
1 61  GLY n 
1 62  GLY n 
1 63  LYS n 
1 64  ASN n 
1 65  ASN n 
1 66  ARG n 
1 67  GLY n 
1 68  ILE n 
1 69  LEU n 
1 70  VAL n 
1 71  ILE n 
1 72  LEU n 
1 73  ILE n 
1 74  TYR n 
1 75  GLU n 
1 76  TYR n 
1 77  VAL n 
1 78  LYS n 
1 79  ASN n 
1 80  ARG n 
1 81  ASP n 
1 82  ILE n 
1 83  ASN n 
1 84  CYS n 
1 85  ASN n 
1 86  GLU n 
1 87  TRP n 
1 88  GLU n 
1 89  LYS n 
1 90  VAL n 
1 91  ALA n 
1 92  CYS n 
1 93  ILE n 
1 94  ALA n 
1 95  TRP n 
1 96  CYS n 
1 97  ILE n 
1 98  GLU n 
1 99  ILE n 
1 100 LEU n 
1 101 GLN n 
1 102 ALA n 
1 103 SER n 
1 104 PHE n 
1 105 LEU n 
1 106 VAL n 
1 107 ALA n 
1 108 ASP n 
1 109 ASP n 
1 110 ILE n 
1 111 MET n 
1 112 ASP n 
1 113 LYS n 
1 114 GLY n 
1 115 GLU n 
1 116 THR n 
1 117 ARG n 
1 118 ARG n 
1 119 ASN n 
1 120 LYS n 
1 121 HIS n 
1 122 CYS n 
1 123 TRP n 
1 124 TYR n 
1 125 LEU n 
1 126 LEU n 
1 127 LYS n 
1 128 ASP n 
1 129 VAL n 
1 130 GLU n 
1 131 ILE n 
1 132 LYS n 
1 133 ASN n 
1 134 ALA n 
1 135 VAL n 
1 136 ASN n 
1 137 ASP n 
1 138 VAL n 
1 139 PHE n 
1 140 LEU n 
1 141 LEU n 
1 142 TYR n 
1 143 ASN n 
1 144 ALA n 
1 145 ILE n 
1 146 TYR n 
1 147 LYS n 
1 148 LEU n 
1 149 LEU n 
1 150 ASP n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ARG n 
1 155 ASN n 
1 156 ASP n 
1 157 ASN n 
1 158 CYS n 
1 159 TYR n 
1 160 LEU n 
1 161 ASP n 
1 162 LEU n 
1 163 ILE n 
1 164 THR n 
1 165 SER n 
1 166 PHE n 
1 167 ARG n 
1 168 GLU n 
1 169 ALA n 
1 170 THR n 
1 171 LEU n 
1 172 LYS n 
1 173 THR n 
1 174 ILE n 
1 175 VAL n 
1 176 GLY n 
1 177 GLN n 
1 178 HIS n 
1 179 LEU n 
1 180 ASP n 
1 181 THR n 
1 182 ASN n 
1 183 ILE n 
1 184 PHE n 
1 185 SER n 
1 186 ASP n 
1 187 LYS n 
1 188 TYR n 
1 189 SER n 
1 190 HIS n 
1 191 ILE n 
1 192 ASP n 
1 193 LYS n 
1 194 ASP n 
1 195 ILE n 
1 196 ASP n 
1 197 VAL n 
1 198 ASN n 
1 199 ASN n 
1 200 ILE n 
1 201 ASN n 
1 202 ILE n 
1 203 SER n 
1 204 GLN n 
1 205 GLU n 
1 206 ASN n 
1 207 LYS n 
1 208 ILE n 
1 209 ASN n 
1 210 ILE n 
1 211 ASN n 
1 212 MET n 
1 213 LEU n 
1 214 ASN n 
1 215 PHE n 
1 216 LYS n 
1 217 VAL n 
1 218 TYR n 
1 219 GLN n 
1 220 ASN n 
1 221 ILE n 
1 222 ILE n 
1 223 ILE n 
1 224 HIS n 
1 225 LYS n 
1 226 THR n 
1 227 ALA n 
1 228 TYR n 
1 229 TYR n 
1 230 SER n 
1 231 PHE n 
1 232 PHE n 
1 233 LEU n 
1 234 PRO n 
1 235 ILE n 
1 236 VAL n 
1 237 CYS n 
1 238 GLY n 
1 239 MET n 
1 240 GLN n 
1 241 MET n 
1 242 GLY n 
1 243 GLY n 
1 244 ILE n 
1 245 SER n 
1 246 LEU n 
1 247 ASP n 
1 248 ASN n 
1 249 LEU n 
1 250 LEU n 
1 251 TYR n 
1 252 LYS n 
1 253 LYS n 
1 254 VAL n 
1 255 GLU n 
1 256 ASN n 
1 257 ILE n 
1 258 ALA n 
1 259 ILE n 
1 260 LEU n 
1 261 MET n 
1 262 GLY n 
1 263 GLU n 
1 264 TYR n 
1 265 PHE n 
1 266 GLN n 
1 267 VAL n 
1 268 HIS n 
1 269 ASP n 
1 270 ASP n 
1 271 TYR n 
1 272 ILE n 
1 273 ASP n 
1 274 THR n 
1 275 PHE n 
1 276 GLY n 
1 277 ASP n 
1 278 SER n 
1 279 LYS n 
1 280 LYS n 
1 281 THR n 
1 282 GLY n 
1 283 LYS n 
1 284 VAL n 
1 285 GLY n 
1 286 SER n 
1 287 ASP n 
1 288 ILE n 
1 289 GLN n 
1 290 ASN n 
1 291 ASN n 
1 292 LYS n 
1 293 LEU n 
1 294 THR n 
1 295 TRP n 
1 296 PRO n 
1 297 LEU n 
1 298 ILE n 
1 299 LYS n 
1 300 ALA n 
1 301 PHE n 
1 302 GLU n 
1 303 LEU n 
1 304 CYS n 
1 305 SER n 
1 306 GLN n 
1 307 PRO n 
1 308 GLU n 
1 309 LYS n 
1 310 GLU n 
1 311 ASP n 
1 312 ILE n 
1 313 ILE n 
1 314 ARG n 
1 315 ASN n 
1 316 TYR n 
1 317 GLY n 
1 318 LYS n 
1 319 ASP n 
1 320 ASN n 
1 321 VAL n 
1 322 THR n 
1 323 CYS n 
1 324 ILE n 
1 325 LYS n 
1 326 PHE n 
1 327 ILE n 
1 328 ASN n 
1 329 ASP n 
1 330 ILE n 
1 331 TYR n 
1 332 GLU n 
1 333 HIS n 
1 334 TYR n 
1 335 ASN n 
1 336 ILE n 
1 337 ARG n 
1 338 ASP n 
1 339 HIS n 
1 340 TYR n 
1 341 VAL n 
1 342 GLU n 
1 343 TYR n 
1 344 GLU n 
1 345 LYS n 
1 346 LYS n 
1 347 GLN n 
1 348 LYS n 
1 349 MET n 
1 350 LYS n 
1 351 ILE n 
1 352 LEU n 
1 353 GLU n 
1 354 ALA n 
1 355 ILE n 
1 356 ASN n 
1 357 GLN n 
1 358 LEU n 
1 359 HIS n 
1 360 HIS n 
1 361 GLU n 
1 362 GLY n 
1 363 ILE n 
1 364 GLU n 
1 365 TYR n 
1 366 VAL n 
1 367 LEU n 
1 368 LYS n 
1 369 TYR n 
1 370 VAL n 
1 371 MET n 
1 372 ASP n 
1 373 ILE n 
1 374 LEU n 
1 375 PHE n 
1 376 THR n 
1 377 GLY n 
1 378 ALA 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                   378 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PF3D7_1128400 
_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      'Plasmodium falciparum 3D7' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     36329 
_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               'BL21(DE3)' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PlfaA.01374.a.BC1 
_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 
A1B0W non-polymer         . 'N-[3-(azepan-1-yl)propyl]-5-methyl-4-oxo-4,5-dihydrothieno[3,2-c]quinoline-2-carboxamide' ? 
'C22 H27 N3 O2 S' 397.534 
ALA   'L-peptide linking' y ALANINE                                                                                    ? 
'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                                                                   ? 
'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                 ? 
'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                            ? 
'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                   ? 
'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                  ? 
'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                            ? 
'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                                                    ? 
'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                  ? 
'C6 H10 N3 O2 1'  156.162 
ILE   'L-peptide linking' y ISOLEUCINE                                                                                 ? 
'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                    ? 
'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                                                     ? 
'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                                                 ? 
'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                              ? 
'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                                                    ? 
'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                                                     ? 
'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                                                  ? 
'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                 ? 
'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                   ? 
'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                                                     ? 
'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_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   GLY 1   19  ?   ?   ?   A . n 
A 1 2   PRO 2   20  ?   ?   ?   A . n 
A 1 3   MET 3   21  ?   ?   ?   A . n 
A 1 4   GLU 4   22  ?   ?   ?   A . n 
A 1 5   ASN 5   23  ?   ?   ?   A . n 
A 1 6   GLU 6   24  ?   ?   ?   A . n 
A 1 7   GLN 7   25  ?   ?   ?   A . n 
A 1 8   ASN 8   26  ?   ?   ?   A . n 
A 1 9   ASN 9   27  ?   ?   ?   A . n 
A 1 10  GLN 10  28  ?   ?   ?   A . n 
A 1 11  ASP 11  29  ?   ?   ?   A . n 
A 1 12  SER 12  30  ?   ?   ?   A . n 
A 1 13  GLU 13  31  ?   ?   ?   A . n 
A 1 14  ASN 14  32  ?   ?   ?   A . n 
A 1 15  GLY 15  33  ?   ?   ?   A . n 
A 1 16  LEU 16  34  ?   ?   ?   A . n 
A 1 17  ASP 17  35  35  ASP ASP A . n 
A 1 18  TYR 18  36  36  TYR TYR A . n 
A 1 19  PHE 19  37  37  PHE PHE A . n 
A 1 20  ARG 20  38  38  ARG ARG A . n 
A 1 21  SER 21  39  39  SER SER A . n 
A 1 22  MET 22  40  40  MET MET A . n 
A 1 23  TYR 23  41  41  TYR TYR A . n 
A 1 24  ASP 24  42  42  ASP ASP A . n 
A 1 25  ARG 25  43  43  ARG ARG A . n 
A 1 26  TYR 26  44  44  TYR TYR A . n 
A 1 27  ARG 27  45  45  ARG ARG A . n 
A 1 28  ASP 28  46  46  ASP ASP A . n 
A 1 29  VAL 29  47  47  VAL VAL A . n 
A 1 30  PHE 30  48  48  PHE PHE A . n 
A 1 31  ILE 31  49  49  ILE ILE A . n 
A 1 32  ASN 32  50  50  ASN ASN A . n 
A 1 33  HIS 33  51  51  HIS HIS A . n 
A 1 34  ILE 34  52  52  ILE ILE A . n 
A 1 35  ASN 35  53  53  ASN ASN A . n 
A 1 36  ASP 36  54  54  ASP ASP A . n 
A 1 37  TYR 37  55  55  TYR TYR A . n 
A 1 38  VAL 38  56  56  VAL VAL A . n 
A 1 39  LEU 39  57  57  LEU LEU A . n 
A 1 40  GLU 40  58  58  GLU GLU A . n 
A 1 41  ASP 41  59  59  ASP ASP A . n 
A 1 42  ASP 42  60  60  ASP ASP A . n 
A 1 43  ILE 43  61  61  ILE ILE A . n 
A 1 44  LYS 44  62  62  LYS LYS A . n 
A 1 45  ILE 45  63  63  ILE ILE A . n 
A 1 46  ILE 46  64  64  ILE ILE A . n 
A 1 47  ILE 47  65  65  ILE ILE A . n 
A 1 48  SER 48  66  66  SER SER A . n 
A 1 49  LYS 49  67  67  LYS LYS A . n 
A 1 50  TYR 50  68  68  TYR TYR A . n 
A 1 51  TYR 51  69  69  TYR TYR A . n 
A 1 52  LYS 52  70  70  LYS LYS A . n 
A 1 53  LEU 53  71  71  LEU LEU A . n 
A 1 54  LEU 54  72  72  LEU LEU A . n 
A 1 55  PHE 55  73  73  PHE PHE A . n 
A 1 56  ASP 56  74  74  ASP ASP A . n 
A 1 57  TYR 57  75  75  TYR TYR A . n 
A 1 58  ASN 58  76  76  ASN ASN A . n 
A 1 59  CYS 59  77  77  CYS CYS A . n 
A 1 60  LEU 60  78  78  LEU LEU A . n 
A 1 61  GLY 61  79  79  GLY GLY A . n 
A 1 62  GLY 62  80  80  GLY GLY A . n 
A 1 63  LYS 63  81  81  LYS LYS A . n 
A 1 64  ASN 64  82  82  ASN ASN A . n 
A 1 65  ASN 65  83  83  ASN ASN A . n 
A 1 66  ARG 66  84  84  ARG ARG A . n 
A 1 67  GLY 67  85  85  GLY GLY A . n 
A 1 68  ILE 68  86  86  ILE ILE A . n 
A 1 69  LEU 69  87  87  LEU LEU A . n 
A 1 70  VAL 70  88  88  VAL VAL A . n 
A 1 71  ILE 71  89  89  ILE ILE A . n 
A 1 72  LEU 72  90  90  LEU LEU A . n 
A 1 73  ILE 73  91  91  ILE ILE A . n 
A 1 74  TYR 74  92  92  TYR TYR A . n 
A 1 75  GLU 75  93  93  GLU GLU A . n 
A 1 76  TYR 76  94  94  TYR TYR A . n 
A 1 77  VAL 77  95  95  VAL VAL A . n 
A 1 78  LYS 78  96  96  LYS LYS A . n 
A 1 79  ASN 79  97  ?   ?   ?   A . n 
A 1 80  ARG 80  98  ?   ?   ?   A . n 
A 1 81  ASP 81  99  99  ASP ASP A . n 
A 1 82  ILE 82  100 100 ILE ILE A . n 
A 1 83  ASN 83  101 101 ASN ASN A . n 
A 1 84  CYS 84  102 102 CYS CYS A . n 
A 1 85  ASN 85  103 103 ASN ASN A . n 
A 1 86  GLU 86  104 104 GLU GLU A . n 
A 1 87  TRP 87  105 105 TRP TRP A . n 
A 1 88  GLU 88  106 106 GLU GLU A . n 
A 1 89  LYS 89  107 107 LYS LYS A . n 
A 1 90  VAL 90  108 108 VAL VAL A . n 
A 1 91  ALA 91  109 109 ALA ALA A . n 
A 1 92  CYS 92  110 110 CYS CYS A . n 
A 1 93  ILE 93  111 111 ILE ILE A . n 
A 1 94  ALA 94  112 112 ALA ALA A . n 
A 1 95  TRP 95  113 113 TRP TRP A . n 
A 1 96  CYS 96  114 114 CYS CYS A . n 
A 1 97  ILE 97  115 115 ILE ILE A . n 
A 1 98  GLU 98  116 116 GLU GLU A . n 
A 1 99  ILE 99  117 117 ILE ILE A . n 
A 1 100 LEU 100 118 118 LEU LEU A . n 
A 1 101 GLN 101 119 119 GLN GLN A . n 
A 1 102 ALA 102 120 120 ALA ALA A . n 
A 1 103 SER 103 121 121 SER SER A . n 
A 1 104 PHE 104 122 122 PHE PHE A . n 
A 1 105 LEU 105 123 123 LEU LEU A . n 
A 1 106 VAL 106 124 124 VAL VAL A . n 
A 1 107 ALA 107 125 125 ALA ALA A . n 
A 1 108 ASP 108 126 126 ASP ASP A . n 
A 1 109 ASP 109 127 127 ASP ASP A . n 
A 1 110 ILE 110 128 128 ILE ILE A . n 
A 1 111 MET 111 129 129 MET MET A . n 
A 1 112 ASP 112 130 130 ASP ASP A . n 
A 1 113 LYS 113 131 131 LYS LYS A . n 
A 1 114 GLY 114 132 132 GLY GLY A . n 
A 1 115 GLU 115 133 133 GLU GLU A . n 
A 1 116 THR 116 134 134 THR THR A . n 
A 1 117 ARG 117 135 135 ARG ARG A . n 
A 1 118 ARG 118 136 136 ARG ARG A . n 
A 1 119 ASN 119 137 137 ASN ASN A . n 
A 1 120 LYS 120 138 138 LYS LYS A . n 
A 1 121 HIS 121 139 139 HIS HIS A . n 
A 1 122 CYS 122 140 140 CYS CYS A . n 
A 1 123 TRP 123 141 141 TRP TRP A . n 
A 1 124 TYR 124 142 142 TYR TYR A . n 
A 1 125 LEU 125 143 143 LEU LEU A . n 
A 1 126 LEU 126 144 144 LEU LEU A . n 
A 1 127 LYS 127 145 145 LYS LYS A . n 
A 1 128 ASP 128 146 146 ASP ASP A . n 
A 1 129 VAL 129 147 147 VAL VAL A . n 
A 1 130 GLU 130 148 148 GLU GLU A . n 
A 1 131 ILE 131 149 149 ILE ILE A . n 
A 1 132 LYS 132 150 150 LYS LYS A . n 
A 1 133 ASN 133 151 151 ASN ASN A . n 
A 1 134 ALA 134 152 152 ALA ALA A . n 
A 1 135 VAL 135 153 153 VAL VAL A . n 
A 1 136 ASN 136 154 154 ASN ASN A . n 
A 1 137 ASP 137 155 155 ASP ASP A . n 
A 1 138 VAL 138 156 156 VAL VAL A . n 
A 1 139 PHE 139 157 157 PHE PHE A . n 
A 1 140 LEU 140 158 158 LEU LEU A . n 
A 1 141 LEU 141 159 159 LEU LEU A . n 
A 1 142 TYR 142 160 160 TYR TYR A . n 
A 1 143 ASN 143 161 161 ASN ASN A . n 
A 1 144 ALA 144 162 162 ALA ALA A . n 
A 1 145 ILE 145 163 163 ILE ILE A . n 
A 1 146 TYR 146 164 164 TYR TYR A . n 
A 1 147 LYS 147 165 165 LYS LYS A . n 
A 1 148 LEU 148 166 166 LEU LEU A . n 
A 1 149 LEU 149 167 167 LEU LEU A . n 
A 1 150 ASP 150 168 168 ASP ASP A . n 
A 1 151 VAL 151 169 169 VAL VAL A . n 
A 1 152 TYR 152 170 170 TYR TYR A . n 
A 1 153 LEU 153 171 171 LEU LEU A . n 
A 1 154 ARG 154 172 172 ARG ARG A . n 
A 1 155 ASN 155 173 173 ASN ASN A . n 
A 1 156 ASP 156 174 174 ASP ASP A . n 
A 1 157 ASN 157 175 175 ASN ASN A . n 
A 1 158 CYS 158 176 176 CYS CYS A . n 
A 1 159 TYR 159 177 177 TYR TYR A . n 
A 1 160 LEU 160 178 178 LEU LEU A . n 
A 1 161 ASP 161 179 179 ASP ASP A . n 
A 1 162 LEU 162 180 180 LEU LEU A . n 
A 1 163 ILE 163 181 181 ILE ILE A . n 
A 1 164 THR 164 182 182 THR THR A . n 
A 1 165 SER 165 183 183 SER SER A . n 
A 1 166 PHE 166 184 184 PHE PHE A . n 
A 1 167 ARG 167 185 185 ARG ARG A . n 
A 1 168 GLU 168 186 186 GLU GLU A . n 
A 1 169 ALA 169 187 187 ALA ALA A . n 
A 1 170 THR 170 188 188 THR THR A . n 
A 1 171 LEU 171 189 189 LEU LEU A . n 
A 1 172 LYS 172 190 190 LYS LYS A . n 
A 1 173 THR 173 191 191 THR THR A . n 
A 1 174 ILE 174 192 192 ILE ILE A . n 
A 1 175 VAL 175 193 193 VAL VAL A . n 
A 1 176 GLY 176 194 194 GLY GLY A . n 
A 1 177 GLN 177 195 195 GLN GLN A . n 
A 1 178 HIS 178 196 196 HIS HIS A . n 
A 1 179 LEU 179 197 197 LEU LEU A . n 
A 1 180 ASP 180 198 198 ASP ASP A . n 
A 1 181 THR 181 199 199 THR THR A . n 
A 1 182 ASN 182 200 200 ASN ASN A . n 
A 1 183 ILE 183 201 201 ILE ILE A . n 
A 1 184 PHE 184 202 202 PHE PHE A . n 
A 1 185 SER 185 203 203 SER SER A . n 
A 1 186 ASP 186 204 204 ASP ASP A . n 
A 1 187 LYS 187 205 205 LYS LYS A . n 
A 1 188 TYR 188 206 206 TYR TYR A . n 
A 1 189 SER 189 207 207 SER SER A . n 
A 1 190 HIS 190 208 208 HIS HIS A . n 
A 1 191 ILE 191 209 209 ILE ILE A . n 
A 1 192 ASP 192 210 ?   ?   ?   A . n 
A 1 193 LYS 193 211 ?   ?   ?   A . n 
A 1 194 ASP 194 212 212 ASP ASP A . n 
A 1 195 ILE 195 213 213 ILE ILE A . n 
A 1 196 ASP 196 214 214 ASP ASP A . n 
A 1 197 VAL 197 215 215 VAL VAL A . n 
A 1 198 ASN 198 216 ?   ?   ?   A . n 
A 1 199 ASN 199 217 ?   ?   ?   A . n 
A 1 200 ILE 200 218 ?   ?   ?   A . n 
A 1 201 ASN 201 219 ?   ?   ?   A . n 
A 1 202 ILE 202 220 ?   ?   ?   A . n 
A 1 203 SER 203 221 ?   ?   ?   A . n 
A 1 204 GLN 204 222 ?   ?   ?   A . n 
A 1 205 GLU 205 223 ?   ?   ?   A . n 
A 1 206 ASN 206 224 ?   ?   ?   A . n 
A 1 207 LYS 207 225 225 LYS LYS A . n 
A 1 208 ILE 208 226 226 ILE ILE A . n 
A 1 209 ASN 209 227 227 ASN ASN A . n 
A 1 210 ILE 210 228 228 ILE ILE A . n 
A 1 211 ASN 211 229 229 ASN ASN A . n 
A 1 212 MET 212 230 230 MET MET A . n 
A 1 213 LEU 213 231 231 LEU LEU A . n 
A 1 214 ASN 214 232 232 ASN ASN A . n 
A 1 215 PHE 215 233 233 PHE PHE A . n 
A 1 216 LYS 216 234 234 LYS LYS A . n 
A 1 217 VAL 217 235 235 VAL VAL A . n 
A 1 218 TYR 218 236 236 TYR TYR A . n 
A 1 219 GLN 219 237 237 GLN GLN A . n 
A 1 220 ASN 220 238 238 ASN ASN A . n 
A 1 221 ILE 221 239 239 ILE ILE A . n 
A 1 222 ILE 222 240 240 ILE ILE A . n 
A 1 223 ILE 223 241 241 ILE ILE A . n 
A 1 224 HIS 224 242 242 HIS HIS A . n 
A 1 225 LYS 225 243 243 LYS LYS A . n 
A 1 226 THR 226 244 244 THR THR A . n 
A 1 227 ALA 227 245 245 ALA ALA A . n 
A 1 228 TYR 228 246 246 TYR TYR A . n 
A 1 229 TYR 229 247 247 TYR TYR A . n 
A 1 230 SER 230 248 248 SER SER A . n 
A 1 231 PHE 231 249 249 PHE PHE A . n 
A 1 232 PHE 232 250 250 PHE PHE A . n 
A 1 233 LEU 233 251 251 LEU LEU A . n 
A 1 234 PRO 234 252 252 PRO PRO A . n 
A 1 235 ILE 235 253 253 ILE ILE A . n 
A 1 236 VAL 236 254 254 VAL VAL A . n 
A 1 237 CYS 237 255 255 CYS CYS A . n 
A 1 238 GLY 238 256 256 GLY GLY A . n 
A 1 239 MET 239 257 257 MET MET A . n 
A 1 240 GLN 240 258 258 GLN GLN A . n 
A 1 241 MET 241 259 259 MET MET A . n 
A 1 242 GLY 242 260 260 GLY GLY A . n 
A 1 243 GLY 243 261 261 GLY GLY A . n 
A 1 244 ILE 244 262 262 ILE ILE A . n 
A 1 245 SER 245 263 263 SER SER A . n 
A 1 246 LEU 246 264 264 LEU LEU A . n 
A 1 247 ASP 247 265 265 ASP ASP A . n 
A 1 248 ASN 248 266 266 ASN ASN A . n 
A 1 249 LEU 249 267 267 LEU LEU A . n 
A 1 250 LEU 250 268 268 LEU LEU A . n 
A 1 251 TYR 251 269 269 TYR TYR A . n 
A 1 252 LYS 252 270 270 LYS LYS A . n 
A 1 253 LYS 253 271 271 LYS LYS A . n 
A 1 254 VAL 254 272 272 VAL VAL A . n 
A 1 255 GLU 255 273 273 GLU GLU A . n 
A 1 256 ASN 256 274 274 ASN ASN A . n 
A 1 257 ILE 257 275 275 ILE ILE A . n 
A 1 258 ALA 258 276 276 ALA ALA A . n 
A 1 259 ILE 259 277 277 ILE ILE A . n 
A 1 260 LEU 260 278 278 LEU LEU A . n 
A 1 261 MET 261 279 279 MET MET A . n 
A 1 262 GLY 262 280 280 GLY GLY A . n 
A 1 263 GLU 263 281 281 GLU GLU A . n 
A 1 264 TYR 264 282 282 TYR TYR A . n 
A 1 265 PHE 265 283 283 PHE PHE A . n 
A 1 266 GLN 266 284 284 GLN GLN A . n 
A 1 267 VAL 267 285 285 VAL VAL A . n 
A 1 268 HIS 268 286 286 HIS HIS A . n 
A 1 269 ASP 269 287 287 ASP ASP A . n 
A 1 270 ASP 270 288 288 ASP ASP A . n 
A 1 271 TYR 271 289 289 TYR TYR A . n 
A 1 272 ILE 272 290 290 ILE ILE A . n 
A 1 273 ASP 273 291 291 ASP ASP A . n 
A 1 274 THR 274 292 292 THR THR A . n 
A 1 275 PHE 275 293 293 PHE PHE A . n 
A 1 276 GLY 276 294 ?   ?   ?   A . n 
A 1 277 ASP 277 295 ?   ?   ?   A . n 
A 1 278 SER 278 296 ?   ?   ?   A . n 
A 1 279 LYS 279 297 ?   ?   ?   A . n 
A 1 280 LYS 280 298 ?   ?   ?   A . n 
A 1 281 THR 281 299 ?   ?   ?   A . n 
A 1 282 GLY 282 300 ?   ?   ?   A . n 
A 1 283 LYS 283 301 ?   ?   ?   A . n 
A 1 284 VAL 284 302 ?   ?   ?   A . n 
A 1 285 GLY 285 303 ?   ?   ?   A . n 
A 1 286 SER 286 304 304 SER SER A . n 
A 1 287 ASP 287 305 305 ASP ASP A . n 
A 1 288 ILE 288 306 306 ILE ILE A . n 
A 1 289 GLN 289 307 307 GLN GLN A . n 
A 1 290 ASN 290 308 308 ASN ASN A . n 
A 1 291 ASN 291 309 309 ASN ASN A . n 
A 1 292 LYS 292 310 310 LYS LYS A . n 
A 1 293 LEU 293 311 311 LEU LEU A . n 
A 1 294 THR 294 312 312 THR THR A . n 
A 1 295 TRP 295 313 313 TRP TRP A . n 
A 1 296 PRO 296 314 314 PRO PRO A . n 
A 1 297 LEU 297 315 315 LEU LEU A . n 
A 1 298 ILE 298 316 316 ILE ILE A . n 
A 1 299 LYS 299 317 317 LYS LYS A . n 
A 1 300 ALA 300 318 318 ALA ALA A . n 
A 1 301 PHE 301 319 319 PHE PHE A . n 
A 1 302 GLU 302 320 320 GLU GLU A . n 
A 1 303 LEU 303 321 321 LEU LEU A . n 
A 1 304 CYS 304 322 322 CYS CYS A . n 
A 1 305 SER 305 323 323 SER SER A . n 
A 1 306 GLN 306 324 324 GLN GLN A . n 
A 1 307 PRO 307 325 325 PRO PRO A . n 
A 1 308 GLU 308 326 326 GLU GLU A . n 
A 1 309 LYS 309 327 327 LYS LYS A . n 
A 1 310 GLU 310 328 328 GLU GLU A . n 
A 1 311 ASP 311 329 329 ASP ASP A . n 
A 1 312 ILE 312 330 330 ILE ILE A . n 
A 1 313 ILE 313 331 331 ILE ILE A . n 
A 1 314 ARG 314 332 332 ARG ARG A . n 
A 1 315 ASN 315 333 333 ASN ASN A . n 
A 1 316 TYR 316 334 ?   ?   ?   A . n 
A 1 317 GLY 317 335 ?   ?   ?   A . n 
A 1 318 LYS 318 336 336 LYS LYS A . n 
A 1 319 ASP 319 337 337 ASP ASP A . n 
A 1 320 ASN 320 338 338 ASN ASN A . n 
A 1 321 VAL 321 339 339 VAL VAL A . n 
A 1 322 THR 322 340 340 THR THR A . n 
A 1 323 CYS 323 341 341 CYS CYS A . n 
A 1 324 ILE 324 342 342 ILE ILE A . n 
A 1 325 LYS 325 343 343 LYS LYS A . n 
A 1 326 PHE 326 344 344 PHE PHE A . n 
A 1 327 ILE 327 345 345 ILE ILE A . n 
A 1 328 ASN 328 346 346 ASN ASN A . n 
A 1 329 ASP 329 347 347 ASP ASP A . n 
A 1 330 ILE 330 348 348 ILE ILE A . n 
A 1 331 TYR 331 349 349 TYR TYR A . n 
A 1 332 GLU 332 350 350 GLU GLU A . n 
A 1 333 HIS 333 351 351 HIS HIS A . n 
A 1 334 TYR 334 352 352 TYR TYR A . n 
A 1 335 ASN 335 353 353 ASN ASN A . n 
A 1 336 ILE 336 354 354 ILE ILE A . n 
A 1 337 ARG 337 355 355 ARG ARG A . n 
A 1 338 ASP 338 356 356 ASP ASP A . n 
A 1 339 HIS 339 357 357 HIS HIS A . n 
A 1 340 TYR 340 358 358 TYR TYR A . n 
A 1 341 VAL 341 359 359 VAL VAL A . n 
A 1 342 GLU 342 360 360 GLU GLU A . n 
A 1 343 TYR 343 361 361 TYR TYR A . n 
A 1 344 GLU 344 362 362 GLU GLU A . n 
A 1 345 LYS 345 363 363 LYS LYS A . n 
A 1 346 LYS 346 364 364 LYS LYS A . n 
A 1 347 GLN 347 365 365 GLN GLN A . n 
A 1 348 LYS 348 366 366 LYS LYS A . n 
A 1 349 MET 349 367 367 MET MET A . n 
A 1 350 LYS 350 368 368 LYS LYS A . n 
A 1 351 ILE 351 369 369 ILE ILE A . n 
A 1 352 LEU 352 370 370 LEU LEU A . n 
A 1 353 GLU 353 371 371 GLU GLU A . n 
A 1 354 ALA 354 372 372 ALA ALA A . n 
A 1 355 ILE 355 373 373 ILE ILE A . n 
A 1 356 ASN 356 374 374 ASN ASN A . n 
A 1 357 GLN 357 375 375 GLN GLN A . n 
A 1 358 LEU 358 376 376 LEU LEU A . n 
A 1 359 HIS 359 377 377 HIS HIS A . n 
A 1 360 HIS 360 378 378 HIS HIS A . n 
A 1 361 GLU 361 379 379 GLU GLU A . n 
A 1 362 GLY 362 380 380 GLY GLY A . n 
A 1 363 ILE 363 381 381 ILE ILE A . n 
A 1 364 GLU 364 382 382 GLU GLU A . n 
A 1 365 TYR 365 383 383 TYR TYR A . n 
A 1 366 VAL 366 384 384 VAL VAL A . n 
A 1 367 LEU 367 385 385 LEU LEU A . n 
A 1 368 LYS 368 386 386 LYS LYS A . n 
A 1 369 TYR 369 387 387 TYR TYR A . n 
A 1 370 VAL 370 388 388 VAL VAL A . n 
A 1 371 MET 371 389 389 MET MET A . n 
A 1 372 ASP 372 390 390 ASP ASP A . n 
A 1 373 ILE 373 391 391 ILE ILE A . n 
A 1 374 LEU 374 392 392 LEU LEU A . n 
A 1 375 PHE 375 393 ?   ?   ?   A . n 
A 1 376 THR 376 394 ?   ?   ?   A . n 
A 1 377 GLY 377 395 ?   ?   ?   A . n 
A 1 378 ALA 378 396 ?   ?   ?   A . n 
# 
_pdbx_nonpoly_scheme.asym_id         B 
_pdbx_nonpoly_scheme.entity_id       2 
_pdbx_nonpoly_scheme.mon_id          A1B0W 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     401 
_pdbx_nonpoly_scheme.auth_seq_num    401 
_pdbx_nonpoly_scheme.pdb_mon_id      A1B0W 
_pdbx_nonpoly_scheme.auth_mon_id     LIG 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
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 LYS 336 ? CG ? A LYS 318 CG 
2 1 Y 1 A LYS 336 ? CD ? A LYS 318 CD 
3 1 Y 1 A LYS 336 ? CE ? A LYS 318 CE 
4 1 Y 1 A LYS 336 ? NZ ? A LYS 318 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(dev_5533: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NSR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     70.689 
_cell.length_a_esd                 ? 
_cell.length_b                     70.689 
_cell.length_b_esd                 ? 
_cell.length_c                     203.818 
_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                         9NSR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                94 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 42 21 2' 
_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                   9NSR 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.85 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.84 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Grid Salt HT D2: 1.5 M Sodium malonate pH 6.0. PlfaA.01374.a.BC1.PS38722 at 25 mg/mL. His tag cleaved with 3C protease. 2mM MMV019313 added prior to crystallization, plate 13887 well D2 drop 2, Puck: PSL2016, Cryo: 2.5M sodium malonate pH 6.0.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 EIGER2 XE 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-24 
_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                    'Double Crystal Si 111' 
_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   0.9786 
_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                        'NSLS-II BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9786 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9NSR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.24 
_reflns.d_resolution_low                               50.00 
_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                                     8801 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                16.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.05 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.249 
_reflns.pdbx_Rpim_I_all                                0.060 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.241 
_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                                    3.25 
_reflns_shell.d_res_low                                     3.51 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1759 
_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                               17.4 
_reflns_shell.pdbx_chi_squared                              1.09 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               2.020 
_reflns_shell.pdbx_Rpim_I_all                               0.480 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.748 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.961 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9NSR 
_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                            3.25 
_refine.ls_d_res_low                             44.88 
_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                     8760 
_refine.ls_number_reflns_R_free                  448 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 5.11 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2533 
_refine.ls_R_factor_R_free                       0.2947 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2511 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 33.98 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.44 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.25 
_refine_hist.d_res_low                        44.88 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               2825 
_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        2797 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_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' ? 0.002  ? 2884 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.441  ? 3894 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.165 ? 1063 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.037  ? 427  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 482  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.25 3.72  . . 151 2690 100.00 . . . . 0.2858 . . . . . . . . . . . . . . . 0.3405 
'X-RAY DIFFRACTION' 3.72 4.69  . . 136 2731 100.00 . . . . 0.2557 . . . . . . . . . . . . . . . 0.2886 
'X-RAY DIFFRACTION' 4.69 44.88 . . 161 2891 100.00 . . . . 0.2383 . . . . . . . . . . . . . . . 0.2836 
# 
_struct.entry_id                     9NSR 
_struct.title                        
;Crystal structure of bifunctional farnesyl/geranylgeranyl pyrophosphate synthase (FPPS/GGPPS) from Plasmodium falciparum in complex with MMV019313
;
_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        9NSR 
_struct_keywords.text            
;SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, geranylgeranyl pyrophosphate synthase, TRANSFERASE
;
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q8II79_PLAF7 
_struct_ref.pdbx_db_accession          Q8II79 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MENEQNNQDSENGLDYFRSMYDRYRDVFINHINDYVLEDDIKIIISKYYKLLFDYNCLGGKNNRGILVILIYEYVKNRDI
NCNEWEKVACIAWCIEILQASFLVADDIMDKGETRRNKHCWYLLKDVEIKNAVNDVFLLYNAIYKLLDVYLRNDNCYLDL
ITSFREATLKTIVGQHLDTNIFSDKYSHIDKDIDVNNINISQENKININMLNFKVYQNIIIHKTAYYSFFLPIVCGMQMG
GISLDNLLYKKVENIAILMGEYFQVHDDYIDTFGDSKKTGKVGSDIQNNKLTWPLIKAFELCSQPEKEDIIRNYGKDNVT
CIKFINDIYEHYNIRDHYVEYEKKQKMKILEAINQLHHEGIEYVLKYVMDILFTGA
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9NSR 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 378 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8II79 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  376 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       21 
_struct_ref_seq.pdbx_auth_seq_align_end       396 
# 
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 9NSR GLY A 1 ? UNP Q8II79 ? ? 'expression tag' 19 1 
1 9NSR PRO A 2 ? UNP Q8II79 ? ? 'expression tag' 20 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6620  ? 
1 MORE         -40   ? 
1 'SSA (A^2)'  27970 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_545 -x,-y-1,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 -70.6890000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 21  ? ASP A 36  ? SER A 39  ASP A 54  1 ? 16 
HELX_P HELX_P2  AA2 GLU A 40  ? CYS A 59  ? GLU A 58  CYS A 77  1 ? 20 
HELX_P HELX_P3  AA3 ASN A 64  ? LYS A 78  ? ASN A 82  LYS A 96  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 83  ? LYS A 113 ? ASN A 101 LYS A 131 1 ? 31 
HELX_P HELX_P5  AA5 TRP A 123 ? LEU A 126 ? TRP A 141 LEU A 144 5 ? 4  
HELX_P HELX_P6  AA6 GLU A 130 ? ARG A 154 ? GLU A 148 ARG A 172 1 ? 25 
HELX_P HELX_P7  AA7 CYS A 158 ? ILE A 183 ? CYS A 176 ILE A 201 1 ? 26 
HELX_P HELX_P8  AA8 ASN A 209 ? LEU A 213 ? ASN A 227 LEU A 231 5 ? 5  
HELX_P HELX_P9  AA9 ASN A 214 ? THR A 226 ? ASN A 232 THR A 244 1 ? 13 
HELX_P HELX_P10 AB1 THR A 226 ? PHE A 231 ? THR A 244 PHE A 249 1 ? 6  
HELX_P HELX_P11 AB2 PHE A 231 ? GLY A 243 ? PHE A 249 GLY A 261 1 ? 13 
HELX_P HELX_P12 AB3 LEU A 249 ? PHE A 275 ? LEU A 267 PHE A 293 1 ? 27 
HELX_P HELX_P13 AB4 THR A 294 ? CYS A 304 ? THR A 312 CYS A 322 1 ? 11 
HELX_P HELX_P14 AB5 SER A 305 ? ASN A 315 ? SER A 323 ASN A 333 1 ? 11 
HELX_P HELX_P15 AB6 ASN A 320 ? TYR A 334 ? ASN A 338 TYR A 352 1 ? 15 
HELX_P HELX_P16 AB7 ASN A 335 ? GLN A 357 ? ASN A 353 GLN A 375 1 ? 23 
HELX_P HELX_P17 AB8 HIS A 360 ? LEU A 374 ? HIS A 378 LEU A 392 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        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 THR A 116 ? ARG A 117 ? THR A 134 ARG A 135 
AA1 2 LYS A 120 ? HIS A 121 ? LYS A 138 HIS A 139 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   ARG 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    117 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    ARG 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     135 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   LYS 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    120 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    LYS 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     138 
# 
_pdbx_entry_details.entry_id                   9NSR 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    TYR 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     36 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -93.55 
_pdbx_validate_torsion.psi             55.22 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Seattle Structural Genomics Center for Infectious Disease' 
_pdbx_SG_project.initial_of_center     SSGCID 
# 
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 14.2363 -45.0457 36.5478 0.7228 ? 0.0348  ? 0.0228  ? 0.4248 ? -0.1226 ? 0.8891 ? 2.9387 ? 1.3786  
? 0.3371  ? 5.3883 ? 2.1244  ? 3.2806 ? -0.2007 ? 0.5941 ? -0.9327 ? -0.1550 ? -0.0106 ? -0.3028 ? 0.6166  ? 0.1718  ? 0.0726  ? 
2 'X-RAY DIFFRACTION' ? refined 9.9771  -38.7345 30.2609 0.7112 ? -0.0281 ? 0.0394  ? 0.5655 ? -0.1261 ? 0.8951 ? 5.0503 ? -0.2485 
? 1.5416  ? 4.6189 ? -2.4197 ? 7.5498 ? -0.4375 ? 0.8764 ? -0.2646 ? -0.5097 ? -0.0650 ? -0.5076 ? 0.1643  ? 0.1712  ? 0.4671  ? 
3 'X-RAY DIFFRACTION' ? refined 3.4028  -20.4229 29.9285 0.8046 ? -0.0362 ? -0.0202 ? 0.4149 ? 0.0798  ? 0.8665 ? 3.6956 ? -1.3665 
? 1.2416  ? 3.4254 ? 0.1971  ? 2.9381 ? 0.1643  ? 0.5912 ? 0.5161  ? -0.3918 ? 0.2011  ? 0.4685  ? -0.3421 ? -0.0751 ? -0.0883 ? 
4 'X-RAY DIFFRACTION' ? refined 16.0144 -21.5375 38.8677 0.7859 ? -0.0289 ? -0.0074 ? 0.4298 ? -0.0060 ? 0.9007 ? 4.4336 ? 0.5623  
? 2.4703  ? 9.4079 ? 0.1401  ? 4.2851 ? -0.3681 ? 0.6021 ? -0.1413 ? 0.0997  ? 0.2495  ? 0.4081  ? -0.4570 ? -0.4456 ? 0.0841  ? 
5 'X-RAY DIFFRACTION' ? refined 16.0379 -12.6715 11.2364 1.1920 ? -0.3393 ? 0.1761  ? 1.2783 ? 0.2208  ? 1.0397 ? 2.8478 ? -1.1093 
? 1.5221  ? 0.5577 ? -0.3607 ? 4.6649 ? -0.5142 ? 1.8173 ? 0.6632  ? -0.6432 ? -0.0675 ? 0.0319  ? -0.4050 ? 1.5555  ? 0.4248  ? 
6 'X-RAY DIFFRACTION' ? refined 26.3039 -16.3166 38.0846 0.8802 ? -0.1595 ? 0.0080  ? 0.8656 ? -0.1086 ? 1.4930 ? 3.4719 ? -0.5561 
? -0.5298 ? 6.9480 ? -2.4962 ? 2.1929 ? 0.1546  ? 0.0541 ? 0.3617  ? 0.8908  ? -0.2587 ? -1.0825 ? 0.5102  ? 0.9005  ? 0.2846  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 35 through 101 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 102 through 171 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 172 through 243 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 244 through 292 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 293 through 356 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 357 through 392 )
;
# 
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 GLY 19  ? A GLY 1   
2  1 Y 1 A PRO 20  ? A PRO 2   
3  1 Y 1 A MET 21  ? A MET 3   
4  1 Y 1 A GLU 22  ? A GLU 4   
5  1 Y 1 A ASN 23  ? A ASN 5   
6  1 Y 1 A GLU 24  ? A GLU 6   
7  1 Y 1 A GLN 25  ? A GLN 7   
8  1 Y 1 A ASN 26  ? A ASN 8   
9  1 Y 1 A ASN 27  ? A ASN 9   
10 1 Y 1 A GLN 28  ? A GLN 10  
11 1 Y 1 A ASP 29  ? A ASP 11  
12 1 Y 1 A SER 30  ? A SER 12  
13 1 Y 1 A GLU 31  ? A GLU 13  
14 1 Y 1 A ASN 32  ? A ASN 14  
15 1 Y 1 A GLY 33  ? A GLY 15  
16 1 Y 1 A LEU 34  ? A LEU 16  
17 1 Y 1 A ASN 97  ? A ASN 79  
18 1 Y 1 A ARG 98  ? A ARG 80  
19 1 Y 1 A ASP 210 ? A ASP 192 
20 1 Y 1 A LYS 211 ? A LYS 193 
21 1 Y 1 A ASN 216 ? A ASN 198 
22 1 Y 1 A ASN 217 ? A ASN 199 
23 1 Y 1 A ILE 218 ? A ILE 200 
24 1 Y 1 A ASN 219 ? A ASN 201 
25 1 Y 1 A ILE 220 ? A ILE 202 
26 1 Y 1 A SER 221 ? A SER 203 
27 1 Y 1 A GLN 222 ? A GLN 204 
28 1 Y 1 A GLU 223 ? A GLU 205 
29 1 Y 1 A ASN 224 ? A ASN 206 
30 1 Y 1 A GLY 294 ? A GLY 276 
31 1 Y 1 A ASP 295 ? A ASP 277 
32 1 Y 1 A SER 296 ? A SER 278 
33 1 Y 1 A LYS 297 ? A LYS 279 
34 1 Y 1 A LYS 298 ? A LYS 280 
35 1 Y 1 A THR 299 ? A THR 281 
36 1 Y 1 A GLY 300 ? A GLY 282 
37 1 Y 1 A LYS 301 ? A LYS 283 
38 1 Y 1 A VAL 302 ? A VAL 284 
39 1 Y 1 A GLY 303 ? A GLY 285 
40 1 Y 1 A TYR 334 ? A TYR 316 
41 1 Y 1 A GLY 335 ? A GLY 317 
42 1 Y 1 A PHE 393 ? A PHE 375 
43 1 Y 1 A THR 394 ? A THR 376 
44 1 Y 1 A GLY 395 ? A GLY 377 
45 1 Y 1 A ALA 396 ? A ALA 378 
# 
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 
A1B0W C15  C N N 1   
A1B0W C20  C N N 2   
A1B0W C21  C N N 3   
A1B0W C22  C N N 4   
A1B0W C26  C Y N 5   
A1B0W C02  C N N 6   
A1B0W C03  C Y N 7   
A1B0W C04  C Y N 8   
A1B0W C05  C Y N 9   
A1B0W C06  C Y N 10  
A1B0W C07  C Y N 11  
A1B0W C08  C Y N 12  
A1B0W C09  C Y N 13  
A1B0W C11  C Y N 14  
A1B0W C12  C N N 15  
A1B0W C14  C N N 16  
A1B0W C16  C N N 17  
A1B0W C18  C N N 18  
A1B0W C19  C N N 19  
A1B0W C23  C N N 20  
A1B0W C25  C Y N 21  
A1B0W C27  C N N 22  
A1B0W N01  N N N 23  
A1B0W N13  N N N 24  
A1B0W N17  N N N 25  
A1B0W O24  O N N 26  
A1B0W O28  O N N 27  
A1B0W S10  S Y N 28  
A1B0W H1   H N N 29  
A1B0W H2   H N N 30  
A1B0W H3   H N N 31  
A1B0W H4   H N N 32  
A1B0W H5   H N N 33  
A1B0W H6   H N N 34  
A1B0W H7   H N N 35  
A1B0W H8   H N N 36  
A1B0W H9   H N N 37  
A1B0W H10  H N N 38  
A1B0W H11  H N N 39  
A1B0W H12  H N N 40  
A1B0W H13  H N N 41  
A1B0W H14  H N N 42  
A1B0W H15  H N N 43  
A1B0W H16  H N N 44  
A1B0W H17  H N N 45  
A1B0W H18  H N N 46  
A1B0W H19  H N N 47  
A1B0W H20  H N N 48  
A1B0W H21  H N N 49  
A1B0W H22  H N N 50  
A1B0W H23  H N N 51  
A1B0W H24  H N N 52  
A1B0W H25  H N N 53  
A1B0W H26  H N N 54  
A1B0W H27  H N N 55  
ALA   N    N N N 56  
ALA   CA   C N S 57  
ALA   C    C N N 58  
ALA   O    O N N 59  
ALA   CB   C N N 60  
ALA   OXT  O N N 61  
ALA   H    H N N 62  
ALA   H2   H N N 63  
ALA   HA   H N N 64  
ALA   HB1  H N N 65  
ALA   HB2  H N N 66  
ALA   HB3  H N N 67  
ALA   HXT  H N N 68  
ARG   N    N N N 69  
ARG   CA   C N S 70  
ARG   C    C N N 71  
ARG   O    O N N 72  
ARG   CB   C N N 73  
ARG   CG   C N N 74  
ARG   CD   C N N 75  
ARG   NE   N N N 76  
ARG   CZ   C N N 77  
ARG   NH1  N N N 78  
ARG   NH2  N N N 79  
ARG   OXT  O N N 80  
ARG   H    H N N 81  
ARG   H2   H N N 82  
ARG   HA   H N N 83  
ARG   HB2  H N N 84  
ARG   HB3  H N N 85  
ARG   HG2  H N N 86  
ARG   HG3  H N N 87  
ARG   HD2  H N N 88  
ARG   HD3  H N N 89  
ARG   HE   H N N 90  
ARG   HH11 H N N 91  
ARG   HH12 H N N 92  
ARG   HH21 H N N 93  
ARG   HH22 H N N 94  
ARG   HXT  H N N 95  
ASN   N    N N N 96  
ASN   CA   C N S 97  
ASN   C    C N N 98  
ASN   O    O N N 99  
ASN   CB   C N N 100 
ASN   CG   C N N 101 
ASN   OD1  O N N 102 
ASN   ND2  N N N 103 
ASN   OXT  O N N 104 
ASN   H    H N N 105 
ASN   H2   H N N 106 
ASN   HA   H N N 107 
ASN   HB2  H N N 108 
ASN   HB3  H N N 109 
ASN   HD21 H N N 110 
ASN   HD22 H N N 111 
ASN   HXT  H N N 112 
ASP   N    N N N 113 
ASP   CA   C N S 114 
ASP   C    C N N 115 
ASP   O    O N N 116 
ASP   CB   C N N 117 
ASP   CG   C N N 118 
ASP   OD1  O N N 119 
ASP   OD2  O N N 120 
ASP   OXT  O N N 121 
ASP   H    H N N 122 
ASP   H2   H N N 123 
ASP   HA   H N N 124 
ASP   HB2  H N N 125 
ASP   HB3  H N N 126 
ASP   HD2  H N N 127 
ASP   HXT  H N N 128 
CYS   N    N N N 129 
CYS   CA   C N R 130 
CYS   C    C N N 131 
CYS   O    O N N 132 
CYS   CB   C N N 133 
CYS   SG   S N N 134 
CYS   OXT  O N N 135 
CYS   H    H N N 136 
CYS   H2   H N N 137 
CYS   HA   H N N 138 
CYS   HB2  H N N 139 
CYS   HB3  H N N 140 
CYS   HG   H N N 141 
CYS   HXT  H N N 142 
GLN   N    N N N 143 
GLN   CA   C N S 144 
GLN   C    C N N 145 
GLN   O    O N N 146 
GLN   CB   C N N 147 
GLN   CG   C N N 148 
GLN   CD   C N N 149 
GLN   OE1  O N N 150 
GLN   NE2  N N N 151 
GLN   OXT  O N N 152 
GLN   H    H N N 153 
GLN   H2   H N N 154 
GLN   HA   H N N 155 
GLN   HB2  H N N 156 
GLN   HB3  H N N 157 
GLN   HG2  H N N 158 
GLN   HG3  H N N 159 
GLN   HE21 H N N 160 
GLN   HE22 H N N 161 
GLN   HXT  H N N 162 
GLU   N    N N N 163 
GLU   CA   C N S 164 
GLU   C    C N N 165 
GLU   O    O N N 166 
GLU   CB   C N N 167 
GLU   CG   C N N 168 
GLU   CD   C N N 169 
GLU   OE1  O N N 170 
GLU   OE2  O N N 171 
GLU   OXT  O N N 172 
GLU   H    H N N 173 
GLU   H2   H N N 174 
GLU   HA   H N N 175 
GLU   HB2  H N N 176 
GLU   HB3  H N N 177 
GLU   HG2  H N N 178 
GLU   HG3  H N N 179 
GLU   HE2  H N N 180 
GLU   HXT  H N N 181 
GLY   N    N N N 182 
GLY   CA   C N N 183 
GLY   C    C N N 184 
GLY   O    O N N 185 
GLY   OXT  O N N 186 
GLY   H    H N N 187 
GLY   H2   H N N 188 
GLY   HA2  H N N 189 
GLY   HA3  H N N 190 
GLY   HXT  H N N 191 
HIS   N    N N N 192 
HIS   CA   C N S 193 
HIS   C    C N N 194 
HIS   O    O N N 195 
HIS   CB   C N N 196 
HIS   CG   C Y N 197 
HIS   ND1  N Y N 198 
HIS   CD2  C Y N 199 
HIS   CE1  C Y N 200 
HIS   NE2  N Y N 201 
HIS   OXT  O N N 202 
HIS   H    H N N 203 
HIS   H2   H N N 204 
HIS   HA   H N N 205 
HIS   HB2  H N N 206 
HIS   HB3  H N N 207 
HIS   HD1  H N N 208 
HIS   HD2  H N N 209 
HIS   HE1  H N N 210 
HIS   HE2  H N N 211 
HIS   HXT  H N N 212 
ILE   N    N N N 213 
ILE   CA   C N S 214 
ILE   C    C N N 215 
ILE   O    O N N 216 
ILE   CB   C N S 217 
ILE   CG1  C N N 218 
ILE   CG2  C N N 219 
ILE   CD1  C N N 220 
ILE   OXT  O N N 221 
ILE   H    H N N 222 
ILE   H2   H N N 223 
ILE   HA   H N N 224 
ILE   HB   H N N 225 
ILE   HG12 H N N 226 
ILE   HG13 H N N 227 
ILE   HG21 H N N 228 
ILE   HG22 H N N 229 
ILE   HG23 H N N 230 
ILE   HD11 H N N 231 
ILE   HD12 H N N 232 
ILE   HD13 H N N 233 
ILE   HXT  H N N 234 
LEU   N    N N N 235 
LEU   CA   C N S 236 
LEU   C    C N N 237 
LEU   O    O N N 238 
LEU   CB   C N N 239 
LEU   CG   C N N 240 
LEU   CD1  C N N 241 
LEU   CD2  C N N 242 
LEU   OXT  O N N 243 
LEU   H    H N N 244 
LEU   H2   H N N 245 
LEU   HA   H N N 246 
LEU   HB2  H N N 247 
LEU   HB3  H N N 248 
LEU   HG   H N N 249 
LEU   HD11 H N N 250 
LEU   HD12 H N N 251 
LEU   HD13 H N N 252 
LEU   HD21 H N N 253 
LEU   HD22 H N N 254 
LEU   HD23 H N N 255 
LEU   HXT  H N N 256 
LYS   N    N N N 257 
LYS   CA   C N S 258 
LYS   C    C N N 259 
LYS   O    O N N 260 
LYS   CB   C N N 261 
LYS   CG   C N N 262 
LYS   CD   C N N 263 
LYS   CE   C N N 264 
LYS   NZ   N N N 265 
LYS   OXT  O N N 266 
LYS   H    H N N 267 
LYS   H2   H N N 268 
LYS   HA   H N N 269 
LYS   HB2  H N N 270 
LYS   HB3  H N N 271 
LYS   HG2  H N N 272 
LYS   HG3  H N N 273 
LYS   HD2  H N N 274 
LYS   HD3  H N N 275 
LYS   HE2  H N N 276 
LYS   HE3  H N N 277 
LYS   HZ1  H N N 278 
LYS   HZ2  H N N 279 
LYS   HZ3  H N N 280 
LYS   HXT  H N N 281 
MET   N    N N N 282 
MET   CA   C N S 283 
MET   C    C N N 284 
MET   O    O N N 285 
MET   CB   C N N 286 
MET   CG   C N N 287 
MET   SD   S N N 288 
MET   CE   C N N 289 
MET   OXT  O N N 290 
MET   H    H N N 291 
MET   H2   H N N 292 
MET   HA   H N N 293 
MET   HB2  H N N 294 
MET   HB3  H N N 295 
MET   HG2  H N N 296 
MET   HG3  H N N 297 
MET   HE1  H N N 298 
MET   HE2  H N N 299 
MET   HE3  H N N 300 
MET   HXT  H N N 301 
PHE   N    N N N 302 
PHE   CA   C N S 303 
PHE   C    C N N 304 
PHE   O    O N N 305 
PHE   CB   C N N 306 
PHE   CG   C Y N 307 
PHE   CD1  C Y N 308 
PHE   CD2  C Y N 309 
PHE   CE1  C Y N 310 
PHE   CE2  C Y N 311 
PHE   CZ   C Y N 312 
PHE   OXT  O N N 313 
PHE   H    H N N 314 
PHE   H2   H N N 315 
PHE   HA   H N N 316 
PHE   HB2  H N N 317 
PHE   HB3  H N N 318 
PHE   HD1  H N N 319 
PHE   HD2  H N N 320 
PHE   HE1  H N N 321 
PHE   HE2  H N N 322 
PHE   HZ   H N N 323 
PHE   HXT  H N N 324 
PRO   N    N N N 325 
PRO   CA   C N S 326 
PRO   C    C N N 327 
PRO   O    O N N 328 
PRO   CB   C N N 329 
PRO   CG   C N N 330 
PRO   CD   C N N 331 
PRO   OXT  O N N 332 
PRO   H    H N N 333 
PRO   HA   H N N 334 
PRO   HB2  H N N 335 
PRO   HB3  H N N 336 
PRO   HG2  H N N 337 
PRO   HG3  H N N 338 
PRO   HD2  H N N 339 
PRO   HD3  H N N 340 
PRO   HXT  H N N 341 
SER   N    N N N 342 
SER   CA   C N S 343 
SER   C    C N N 344 
SER   O    O N N 345 
SER   CB   C N N 346 
SER   OG   O N N 347 
SER   OXT  O N N 348 
SER   H    H N N 349 
SER   H2   H N N 350 
SER   HA   H N N 351 
SER   HB2  H N N 352 
SER   HB3  H N N 353 
SER   HG   H N N 354 
SER   HXT  H N N 355 
THR   N    N N N 356 
THR   CA   C N S 357 
THR   C    C N N 358 
THR   O    O N N 359 
THR   CB   C N R 360 
THR   OG1  O N N 361 
THR   CG2  C N N 362 
THR   OXT  O N N 363 
THR   H    H N N 364 
THR   H2   H N N 365 
THR   HA   H N N 366 
THR   HB   H N N 367 
THR   HG1  H N N 368 
THR   HG21 H N N 369 
THR   HG22 H N N 370 
THR   HG23 H N N 371 
THR   HXT  H N N 372 
TRP   N    N N N 373 
TRP   CA   C N S 374 
TRP   C    C N N 375 
TRP   O    O N N 376 
TRP   CB   C N N 377 
TRP   CG   C Y N 378 
TRP   CD1  C Y N 379 
TRP   CD2  C Y N 380 
TRP   NE1  N Y N 381 
TRP   CE2  C Y N 382 
TRP   CE3  C Y N 383 
TRP   CZ2  C Y N 384 
TRP   CZ3  C Y N 385 
TRP   CH2  C Y N 386 
TRP   OXT  O N N 387 
TRP   H    H N N 388 
TRP   H2   H N N 389 
TRP   HA   H N N 390 
TRP   HB2  H N N 391 
TRP   HB3  H N N 392 
TRP   HD1  H N N 393 
TRP   HE1  H N N 394 
TRP   HE3  H N N 395 
TRP   HZ2  H N N 396 
TRP   HZ3  H N N 397 
TRP   HH2  H N N 398 
TRP   HXT  H N N 399 
TYR   N    N N N 400 
TYR   CA   C N S 401 
TYR   C    C N N 402 
TYR   O    O N N 403 
TYR   CB   C N N 404 
TYR   CG   C Y N 405 
TYR   CD1  C Y N 406 
TYR   CD2  C Y N 407 
TYR   CE1  C Y N 408 
TYR   CE2  C Y N 409 
TYR   CZ   C Y N 410 
TYR   OH   O N N 411 
TYR   OXT  O N N 412 
TYR   H    H N N 413 
TYR   H2   H N N 414 
TYR   HA   H N N 415 
TYR   HB2  H N N 416 
TYR   HB3  H N N 417 
TYR   HD1  H N N 418 
TYR   HD2  H N N 419 
TYR   HE1  H N N 420 
TYR   HE2  H N N 421 
TYR   HH   H N N 422 
TYR   HXT  H N N 423 
VAL   N    N N N 424 
VAL   CA   C N S 425 
VAL   C    C N N 426 
VAL   O    O N N 427 
VAL   CB   C N N 428 
VAL   CG1  C N N 429 
VAL   CG2  C N N 430 
VAL   OXT  O N N 431 
VAL   H    H N N 432 
VAL   H2   H N N 433 
VAL   HA   H N N 434 
VAL   HB   H N N 435 
VAL   HG11 H N N 436 
VAL   HG12 H N N 437 
VAL   HG13 H N N 438 
VAL   HG21 H N N 439 
VAL   HG22 H N N 440 
VAL   HG23 H N N 441 
VAL   HXT  H N N 442 
# 
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 
A1B0W C23 C22  sing N N 1   
A1B0W C23 N17  sing N N 2   
A1B0W C22 C21  sing N N 3   
A1B0W C21 C20  sing N N 4   
A1B0W C16 N17  sing N N 5   
A1B0W C16 C15  sing N N 6   
A1B0W N17 C18  sing N N 7   
A1B0W C15 C14  sing N N 8   
A1B0W C14 N13  sing N N 9   
A1B0W C20 C19  sing N N 10  
A1B0W O24 C12  doub N N 11  
A1B0W C18 C19  sing N N 12  
A1B0W N13 C12  sing N N 13  
A1B0W C12 C11  sing N N 14  
A1B0W S10 C11  sing Y N 15  
A1B0W S10 C09  sing Y N 16  
A1B0W C11 C25  doub Y N 17  
A1B0W C25 C26  sing Y N 18  
A1B0W C05 C06  doub Y N 19  
A1B0W C05 C04  sing Y N 20  
A1B0W C09 C04  sing N N 21  
A1B0W C09 C26  doub Y N 22  
A1B0W C06 C07  sing Y N 23  
A1B0W C04 C03  doub Y N 24  
A1B0W C26 C27  sing N N 25  
A1B0W C07 C08  doub Y N 26  
A1B0W C03 C08  sing Y N 27  
A1B0W C03 N01  sing N N 28  
A1B0W C27 N01  sing N N 29  
A1B0W C27 O28  doub N N 30  
A1B0W N01 C02  sing N N 31  
A1B0W C15 H1   sing N N 32  
A1B0W C15 H2   sing N N 33  
A1B0W C20 H3   sing N N 34  
A1B0W C20 H4   sing N N 35  
A1B0W C21 H5   sing N N 36  
A1B0W C21 H6   sing N N 37  
A1B0W C22 H7   sing N N 38  
A1B0W C22 H8   sing N N 39  
A1B0W C02 H9   sing N N 40  
A1B0W C02 H10  sing N N 41  
A1B0W C02 H11  sing N N 42  
A1B0W C05 H12  sing N N 43  
A1B0W C06 H13  sing N N 44  
A1B0W C07 H14  sing N N 45  
A1B0W C08 H15  sing N N 46  
A1B0W C14 H16  sing N N 47  
A1B0W C14 H17  sing N N 48  
A1B0W C16 H18  sing N N 49  
A1B0W C16 H19  sing N N 50  
A1B0W C18 H20  sing N N 51  
A1B0W C18 H21  sing N N 52  
A1B0W C19 H22  sing N N 53  
A1B0W C19 H23  sing N N 54  
A1B0W C23 H24  sing N N 55  
A1B0W C23 H25  sing N N 56  
A1B0W C25 H26  sing N N 57  
A1B0W N13 H27  sing N N 58  
ALA   N   CA   sing N N 59  
ALA   N   H    sing N N 60  
ALA   N   H2   sing N N 61  
ALA   CA  C    sing N N 62  
ALA   CA  CB   sing N N 63  
ALA   CA  HA   sing N N 64  
ALA   C   O    doub N N 65  
ALA   C   OXT  sing N N 66  
ALA   CB  HB1  sing N N 67  
ALA   CB  HB2  sing N N 68  
ALA   CB  HB3  sing N N 69  
ALA   OXT HXT  sing N N 70  
ARG   N   CA   sing N N 71  
ARG   N   H    sing N N 72  
ARG   N   H2   sing N N 73  
ARG   CA  C    sing N N 74  
ARG   CA  CB   sing N N 75  
ARG   CA  HA   sing N N 76  
ARG   C   O    doub N N 77  
ARG   C   OXT  sing N N 78  
ARG   CB  CG   sing N N 79  
ARG   CB  HB2  sing N N 80  
ARG   CB  HB3  sing N N 81  
ARG   CG  CD   sing N N 82  
ARG   CG  HG2  sing N N 83  
ARG   CG  HG3  sing N N 84  
ARG   CD  NE   sing N N 85  
ARG   CD  HD2  sing N N 86  
ARG   CD  HD3  sing N N 87  
ARG   NE  CZ   sing N N 88  
ARG   NE  HE   sing N N 89  
ARG   CZ  NH1  sing N N 90  
ARG   CZ  NH2  doub N N 91  
ARG   NH1 HH11 sing N N 92  
ARG   NH1 HH12 sing N N 93  
ARG   NH2 HH21 sing N N 94  
ARG   NH2 HH22 sing N N 95  
ARG   OXT HXT  sing N N 96  
ASN   N   CA   sing N N 97  
ASN   N   H    sing N N 98  
ASN   N   H2   sing N N 99  
ASN   CA  C    sing N N 100 
ASN   CA  CB   sing N N 101 
ASN   CA  HA   sing N N 102 
ASN   C   O    doub N N 103 
ASN   C   OXT  sing N N 104 
ASN   CB  CG   sing N N 105 
ASN   CB  HB2  sing N N 106 
ASN   CB  HB3  sing N N 107 
ASN   CG  OD1  doub N N 108 
ASN   CG  ND2  sing N N 109 
ASN   ND2 HD21 sing N N 110 
ASN   ND2 HD22 sing N N 111 
ASN   OXT HXT  sing N N 112 
ASP   N   CA   sing N N 113 
ASP   N   H    sing N N 114 
ASP   N   H2   sing N N 115 
ASP   CA  C    sing N N 116 
ASP   CA  CB   sing N N 117 
ASP   CA  HA   sing N N 118 
ASP   C   O    doub N N 119 
ASP   C   OXT  sing N N 120 
ASP   CB  CG   sing N N 121 
ASP   CB  HB2  sing N N 122 
ASP   CB  HB3  sing N N 123 
ASP   CG  OD1  doub N N 124 
ASP   CG  OD2  sing N N 125 
ASP   OD2 HD2  sing N N 126 
ASP   OXT HXT  sing N N 127 
CYS   N   CA   sing N N 128 
CYS   N   H    sing N N 129 
CYS   N   H2   sing N N 130 
CYS   CA  C    sing N N 131 
CYS   CA  CB   sing N N 132 
CYS   CA  HA   sing N N 133 
CYS   C   O    doub N N 134 
CYS   C   OXT  sing N N 135 
CYS   CB  SG   sing N N 136 
CYS   CB  HB2  sing N N 137 
CYS   CB  HB3  sing N N 138 
CYS   SG  HG   sing N N 139 
CYS   OXT HXT  sing N N 140 
GLN   N   CA   sing N N 141 
GLN   N   H    sing N N 142 
GLN   N   H2   sing N N 143 
GLN   CA  C    sing N N 144 
GLN   CA  CB   sing N N 145 
GLN   CA  HA   sing N N 146 
GLN   C   O    doub N N 147 
GLN   C   OXT  sing N N 148 
GLN   CB  CG   sing N N 149 
GLN   CB  HB2  sing N N 150 
GLN   CB  HB3  sing N N 151 
GLN   CG  CD   sing N N 152 
GLN   CG  HG2  sing N N 153 
GLN   CG  HG3  sing N N 154 
GLN   CD  OE1  doub N N 155 
GLN   CD  NE2  sing N N 156 
GLN   NE2 HE21 sing N N 157 
GLN   NE2 HE22 sing N N 158 
GLN   OXT HXT  sing N N 159 
GLU   N   CA   sing N N 160 
GLU   N   H    sing N N 161 
GLU   N   H2   sing N N 162 
GLU   CA  C    sing N N 163 
GLU   CA  CB   sing N N 164 
GLU   CA  HA   sing N N 165 
GLU   C   O    doub N N 166 
GLU   C   OXT  sing N N 167 
GLU   CB  CG   sing N N 168 
GLU   CB  HB2  sing N N 169 
GLU   CB  HB3  sing N N 170 
GLU   CG  CD   sing N N 171 
GLU   CG  HG2  sing N N 172 
GLU   CG  HG3  sing N N 173 
GLU   CD  OE1  doub N N 174 
GLU   CD  OE2  sing N N 175 
GLU   OE2 HE2  sing N N 176 
GLU   OXT HXT  sing N N 177 
GLY   N   CA   sing N N 178 
GLY   N   H    sing N N 179 
GLY   N   H2   sing N N 180 
GLY   CA  C    sing N N 181 
GLY   CA  HA2  sing N N 182 
GLY   CA  HA3  sing N N 183 
GLY   C   O    doub N N 184 
GLY   C   OXT  sing N N 185 
GLY   OXT HXT  sing N N 186 
HIS   N   CA   sing N N 187 
HIS   N   H    sing N N 188 
HIS   N   H2   sing N N 189 
HIS   CA  C    sing N N 190 
HIS   CA  CB   sing N N 191 
HIS   CA  HA   sing N N 192 
HIS   C   O    doub N N 193 
HIS   C   OXT  sing N N 194 
HIS   CB  CG   sing N N 195 
HIS   CB  HB2  sing N N 196 
HIS   CB  HB3  sing N N 197 
HIS   CG  ND1  sing Y N 198 
HIS   CG  CD2  doub Y N 199 
HIS   ND1 CE1  doub Y N 200 
HIS   ND1 HD1  sing N N 201 
HIS   CD2 NE2  sing Y N 202 
HIS   CD2 HD2  sing N N 203 
HIS   CE1 NE2  sing Y N 204 
HIS   CE1 HE1  sing N N 205 
HIS   NE2 HE2  sing N N 206 
HIS   OXT HXT  sing N N 207 
ILE   N   CA   sing N N 208 
ILE   N   H    sing N N 209 
ILE   N   H2   sing N N 210 
ILE   CA  C    sing N N 211 
ILE   CA  CB   sing N N 212 
ILE   CA  HA   sing N N 213 
ILE   C   O    doub N N 214 
ILE   C   OXT  sing N N 215 
ILE   CB  CG1  sing N N 216 
ILE   CB  CG2  sing N N 217 
ILE   CB  HB   sing N N 218 
ILE   CG1 CD1  sing N N 219 
ILE   CG1 HG12 sing N N 220 
ILE   CG1 HG13 sing N N 221 
ILE   CG2 HG21 sing N N 222 
ILE   CG2 HG22 sing N N 223 
ILE   CG2 HG23 sing N N 224 
ILE   CD1 HD11 sing N N 225 
ILE   CD1 HD12 sing N N 226 
ILE   CD1 HD13 sing N N 227 
ILE   OXT HXT  sing N N 228 
LEU   N   CA   sing N N 229 
LEU   N   H    sing N N 230 
LEU   N   H2   sing N N 231 
LEU   CA  C    sing N N 232 
LEU   CA  CB   sing N N 233 
LEU   CA  HA   sing N N 234 
LEU   C   O    doub N N 235 
LEU   C   OXT  sing N N 236 
LEU   CB  CG   sing N N 237 
LEU   CB  HB2  sing N N 238 
LEU   CB  HB3  sing N N 239 
LEU   CG  CD1  sing N N 240 
LEU   CG  CD2  sing N N 241 
LEU   CG  HG   sing N N 242 
LEU   CD1 HD11 sing N N 243 
LEU   CD1 HD12 sing N N 244 
LEU   CD1 HD13 sing N N 245 
LEU   CD2 HD21 sing N N 246 
LEU   CD2 HD22 sing N N 247 
LEU   CD2 HD23 sing N N 248 
LEU   OXT HXT  sing N N 249 
LYS   N   CA   sing N N 250 
LYS   N   H    sing N N 251 
LYS   N   H2   sing N N 252 
LYS   CA  C    sing N N 253 
LYS   CA  CB   sing N N 254 
LYS   CA  HA   sing N N 255 
LYS   C   O    doub N N 256 
LYS   C   OXT  sing N N 257 
LYS   CB  CG   sing N N 258 
LYS   CB  HB2  sing N N 259 
LYS   CB  HB3  sing N N 260 
LYS   CG  CD   sing N N 261 
LYS   CG  HG2  sing N N 262 
LYS   CG  HG3  sing N N 263 
LYS   CD  CE   sing N N 264 
LYS   CD  HD2  sing N N 265 
LYS   CD  HD3  sing N N 266 
LYS   CE  NZ   sing N N 267 
LYS   CE  HE2  sing N N 268 
LYS   CE  HE3  sing N N 269 
LYS   NZ  HZ1  sing N N 270 
LYS   NZ  HZ2  sing N N 271 
LYS   NZ  HZ3  sing N N 272 
LYS   OXT HXT  sing N N 273 
MET   N   CA   sing N N 274 
MET   N   H    sing N N 275 
MET   N   H2   sing N N 276 
MET   CA  C    sing N N 277 
MET   CA  CB   sing N N 278 
MET   CA  HA   sing N N 279 
MET   C   O    doub N N 280 
MET   C   OXT  sing N N 281 
MET   CB  CG   sing N N 282 
MET   CB  HB2  sing N N 283 
MET   CB  HB3  sing N N 284 
MET   CG  SD   sing N N 285 
MET   CG  HG2  sing N N 286 
MET   CG  HG3  sing N N 287 
MET   SD  CE   sing N N 288 
MET   CE  HE1  sing N N 289 
MET   CE  HE2  sing N N 290 
MET   CE  HE3  sing N N 291 
MET   OXT HXT  sing N N 292 
PHE   N   CA   sing N N 293 
PHE   N   H    sing N N 294 
PHE   N   H2   sing N N 295 
PHE   CA  C    sing N N 296 
PHE   CA  CB   sing N N 297 
PHE   CA  HA   sing N N 298 
PHE   C   O    doub N N 299 
PHE   C   OXT  sing N N 300 
PHE   CB  CG   sing N N 301 
PHE   CB  HB2  sing N N 302 
PHE   CB  HB3  sing N N 303 
PHE   CG  CD1  doub Y N 304 
PHE   CG  CD2  sing Y N 305 
PHE   CD1 CE1  sing Y N 306 
PHE   CD1 HD1  sing N N 307 
PHE   CD2 CE2  doub Y N 308 
PHE   CD2 HD2  sing N N 309 
PHE   CE1 CZ   doub Y N 310 
PHE   CE1 HE1  sing N N 311 
PHE   CE2 CZ   sing Y N 312 
PHE   CE2 HE2  sing N N 313 
PHE   CZ  HZ   sing N N 314 
PHE   OXT HXT  sing N N 315 
PRO   N   CA   sing N N 316 
PRO   N   CD   sing N N 317 
PRO   N   H    sing N N 318 
PRO   CA  C    sing N N 319 
PRO   CA  CB   sing N N 320 
PRO   CA  HA   sing N N 321 
PRO   C   O    doub N N 322 
PRO   C   OXT  sing N N 323 
PRO   CB  CG   sing N N 324 
PRO   CB  HB2  sing N N 325 
PRO   CB  HB3  sing N N 326 
PRO   CG  CD   sing N N 327 
PRO   CG  HG2  sing N N 328 
PRO   CG  HG3  sing N N 329 
PRO   CD  HD2  sing N N 330 
PRO   CD  HD3  sing N N 331 
PRO   OXT HXT  sing N N 332 
SER   N   CA   sing N N 333 
SER   N   H    sing N N 334 
SER   N   H2   sing N N 335 
SER   CA  C    sing N N 336 
SER   CA  CB   sing N N 337 
SER   CA  HA   sing N N 338 
SER   C   O    doub N N 339 
SER   C   OXT  sing N N 340 
SER   CB  OG   sing N N 341 
SER   CB  HB2  sing N N 342 
SER   CB  HB3  sing N N 343 
SER   OG  HG   sing N N 344 
SER   OXT HXT  sing N N 345 
THR   N   CA   sing N N 346 
THR   N   H    sing N N 347 
THR   N   H2   sing N N 348 
THR   CA  C    sing N N 349 
THR   CA  CB   sing N N 350 
THR   CA  HA   sing N N 351 
THR   C   O    doub N N 352 
THR   C   OXT  sing N N 353 
THR   CB  OG1  sing N N 354 
THR   CB  CG2  sing N N 355 
THR   CB  HB   sing N N 356 
THR   OG1 HG1  sing N N 357 
THR   CG2 HG21 sing N N 358 
THR   CG2 HG22 sing N N 359 
THR   CG2 HG23 sing N N 360 
THR   OXT HXT  sing N N 361 
TRP   N   CA   sing N N 362 
TRP   N   H    sing N N 363 
TRP   N   H2   sing N N 364 
TRP   CA  C    sing N N 365 
TRP   CA  CB   sing N N 366 
TRP   CA  HA   sing N N 367 
TRP   C   O    doub N N 368 
TRP   C   OXT  sing N N 369 
TRP   CB  CG   sing N N 370 
TRP   CB  HB2  sing N N 371 
TRP   CB  HB3  sing N N 372 
TRP   CG  CD1  doub Y N 373 
TRP   CG  CD2  sing Y N 374 
TRP   CD1 NE1  sing Y N 375 
TRP   CD1 HD1  sing N N 376 
TRP   CD2 CE2  doub Y N 377 
TRP   CD2 CE3  sing Y N 378 
TRP   NE1 CE2  sing Y N 379 
TRP   NE1 HE1  sing N N 380 
TRP   CE2 CZ2  sing Y N 381 
TRP   CE3 CZ3  doub Y N 382 
TRP   CE3 HE3  sing N N 383 
TRP   CZ2 CH2  doub Y N 384 
TRP   CZ2 HZ2  sing N N 385 
TRP   CZ3 CH2  sing Y N 386 
TRP   CZ3 HZ3  sing N N 387 
TRP   CH2 HH2  sing N N 388 
TRP   OXT HXT  sing N N 389 
TYR   N   CA   sing N N 390 
TYR   N   H    sing N N 391 
TYR   N   H2   sing N N 392 
TYR   CA  C    sing N N 393 
TYR   CA  CB   sing N N 394 
TYR   CA  HA   sing N N 395 
TYR   C   O    doub N N 396 
TYR   C   OXT  sing N N 397 
TYR   CB  CG   sing N N 398 
TYR   CB  HB2  sing N N 399 
TYR   CB  HB3  sing N N 400 
TYR   CG  CD1  doub Y N 401 
TYR   CG  CD2  sing Y N 402 
TYR   CD1 CE1  sing Y N 403 
TYR   CD1 HD1  sing N N 404 
TYR   CD2 CE2  doub Y N 405 
TYR   CD2 HD2  sing N N 406 
TYR   CE1 CZ   doub Y N 407 
TYR   CE1 HE1  sing N N 408 
TYR   CE2 CZ   sing Y N 409 
TYR   CE2 HE2  sing N N 410 
TYR   CZ  OH   sing N N 411 
TYR   OH  HH   sing N N 412 
TYR   OXT HXT  sing N N 413 
VAL   N   CA   sing N N 414 
VAL   N   H    sing N N 415 
VAL   N   H2   sing N N 416 
VAL   CA  C    sing N N 417 
VAL   CA  CB   sing N N 418 
VAL   CA  HA   sing N N 419 
VAL   C   O    doub N N 420 
VAL   C   OXT  sing N N 421 
VAL   CB  CG1  sing N N 422 
VAL   CB  CG2  sing N N 423 
VAL   CB  HB   sing N N 424 
VAL   CG1 HG11 sing N N 425 
VAL   CG1 HG12 sing N N 426 
VAL   CG1 HG13 sing N N 427 
VAL   CG2 HG21 sing N N 428 
VAL   CG2 HG22 sing N N 429 
VAL   CG2 HG23 sing N N 430 
VAL   OXT HXT  sing N N 431 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 75N93022C00036 1 
'National Institutes of Health/Office of the Director'                                            'United States' S10OD030394    2 
# 
_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   3CC9 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9NSR 
_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]   0.014146 
_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]   0.014146 
_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]   0.004906 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 17  ? 29.486  -39.243 42.868 1.00 111.59 ? 35  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 17  ? 28.230  -39.038 42.156 1.00 153.97 ? 35  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 17  ? 27.641  -40.373 41.703 1.00 148.19 ? 35  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 17  ? 27.783  -40.767 40.545 1.00 144.03 ? 35  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 17  ? 28.441  -38.117 40.954 1.00 125.06 ? 35  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 17  ? 27.148  -37.776 40.251 1.00 109.53 ? 35  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 17  ? 26.383  -36.948 40.788 1.00 120.39 ? 35  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 17  ? 26.895  -38.339 39.165 1.00 110.94 ? 35  ASP   A OD2 1 
ATOM   9    N N   . TYR   A 1 18  ? 26.978  -41.065 42.629 1.00 143.83 ? 36  TYR   A N   1 
ATOM   10   C CA  . TYR   A 1 18  ? 26.414  -42.390 42.366 1.00 119.88 ? 36  TYR   A CA  1 
ATOM   11   C C   . TYR   A 1 18  ? 24.952  -42.268 41.929 1.00 124.11 ? 36  TYR   A C   1 
ATOM   12   O O   . TYR   A 1 18  ? 24.039  -42.868 42.496 1.00 114.85 ? 36  TYR   A O   1 
ATOM   13   C CB  . TYR   A 1 18  ? 26.558  -43.266 43.605 1.00 126.58 ? 36  TYR   A CB  1 
ATOM   14   C CG  . TYR   A 1 18  ? 26.389  -44.745 43.347 1.00 149.72 ? 36  TYR   A CG  1 
ATOM   15   C CD1 . TYR   A 1 18  ? 27.386  -45.477 42.716 1.00 154.58 ? 36  TYR   A CD1 1 
ATOM   16   C CD2 . TYR   A 1 18  ? 25.241  -45.413 43.751 1.00 152.27 ? 36  TYR   A CD2 1 
ATOM   17   C CE1 . TYR   A 1 18  ? 27.240  -46.832 42.483 1.00 132.80 ? 36  TYR   A CE1 1 
ATOM   18   C CE2 . TYR   A 1 18  ? 25.086  -46.768 43.524 1.00 142.58 ? 36  TYR   A CE2 1 
ATOM   19   C CZ  . TYR   A 1 18  ? 26.089  -47.472 42.890 1.00 141.38 ? 36  TYR   A CZ  1 
ATOM   20   O OH  . TYR   A 1 18  ? 25.939  -48.821 42.659 1.00 156.56 ? 36  TYR   A OH  1 
ATOM   21   N N   . PHE   A 1 19  ? 24.751  -41.471 40.880 1.00 118.88 ? 37  PHE   A N   1 
ATOM   22   C CA  . PHE   A 1 19  ? 23.427  -41.098 40.395 1.00 106.91 ? 37  PHE   A CA  1 
ATOM   23   C C   . PHE   A 1 19  ? 22.938  -41.995 39.262 1.00 103.22 ? 37  PHE   A C   1 
ATOM   24   O O   . PHE   A 1 19  ? 21.824  -42.522 39.327 1.00 103.32 ? 37  PHE   A O   1 
ATOM   25   C CB  . PHE   A 1 19  ? 23.459  -39.631 39.946 1.00 98.57  ? 37  PHE   A CB  1 
ATOM   26   C CG  . PHE   A 1 19  ? 22.243  -39.188 39.182 1.00 92.73  ? 37  PHE   A CG  1 
ATOM   27   C CD1 . PHE   A 1 19  ? 20.972  -39.338 39.710 1.00 84.84  ? 37  PHE   A CD1 1 
ATOM   28   C CD2 . PHE   A 1 19  ? 22.381  -38.589 37.941 1.00 102.00 ? 37  PHE   A CD2 1 
ATOM   29   C CE1 . PHE   A 1 19  ? 19.860  -38.913 39.003 1.00 84.86  ? 37  PHE   A CE1 1 
ATOM   30   C CE2 . PHE   A 1 19  ? 21.274  -38.164 37.230 1.00 90.53  ? 37  PHE   A CE2 1 
ATOM   31   C CZ  . PHE   A 1 19  ? 20.013  -38.325 37.761 1.00 84.85  ? 37  PHE   A CZ  1 
ATOM   32   N N   . ARG   A 1 20  ? 23.758  -42.187 38.225 1.00 125.15 ? 38  ARG   A N   1 
ATOM   33   C CA  . ARG   A 1 20  ? 23.330  -42.981 37.077 1.00 125.43 ? 38  ARG   A CA  1 
ATOM   34   C C   . ARG   A 1 20  ? 23.031  -44.422 37.472 1.00 124.33 ? 38  ARG   A C   1 
ATOM   35   O O   . ARG   A 1 20  ? 22.057  -45.016 36.994 1.00 128.08 ? 38  ARG   A O   1 
ATOM   36   C CB  . ARG   A 1 20  ? 24.403  -42.942 35.989 1.00 137.17 ? 38  ARG   A CB  1 
ATOM   37   C CG  . ARG   A 1 20  ? 24.372  -41.690 35.122 1.00 147.13 ? 38  ARG   A CG  1 
ATOM   38   C CD  . ARG   A 1 20  ? 23.207  -41.702 34.136 1.00 156.43 ? 38  ARG   A CD  1 
ATOM   39   N NE  . ARG   A 1 20  ? 23.282  -42.812 33.191 1.00 159.03 ? 38  ARG   A NE  1 
ATOM   40   C CZ  . ARG   A 1 20  ? 22.659  -43.976 33.333 1.00 148.74 ? 38  ARG   A CZ  1 
ATOM   41   N NH1 . ARG   A 1 20  ? 21.897  -44.232 34.385 1.00 144.15 ? 38  ARG   A NH1 1 
ATOM   42   N NH2 . ARG   A 1 20  ? 22.806  -44.908 32.396 1.00 146.85 ? 38  ARG   A NH2 1 
ATOM   43   N N   . SER   A 1 21  ? 23.861  -45.005 38.338 1.00 105.57 ? 39  SER   A N   1 
ATOM   44   C CA  . SER   A 1 21  ? 23.672  -46.402 38.715 1.00 98.91  ? 39  SER   A CA  1 
ATOM   45   C C   . SER   A 1 21  ? 22.301  -46.639 39.336 1.00 116.29 ? 39  SER   A C   1 
ATOM   46   O O   . SER   A 1 21  ? 21.759  -47.746 39.237 1.00 111.80 ? 39  SER   A O   1 
ATOM   47   C CB  . SER   A 1 21  ? 24.771  -46.824 39.686 1.00 131.97 ? 39  SER   A CB  1 
ATOM   48   O OG  . SER   A 1 21  ? 24.826  -45.934 40.785 1.00 155.24 ? 39  SER   A OG  1 
ATOM   49   N N   . MET   A 1 22  ? 21.731  -45.621 39.983 1.00 109.48 ? 40  MET   A N   1 
ATOM   50   C CA  . MET   A 1 22  ? 20.421  -45.761 40.606 1.00 104.09 ? 40  MET   A CA  1 
ATOM   51   C C   . MET   A 1 22  ? 19.295  -45.833 39.584 1.00 86.89  ? 40  MET   A C   1 
ATOM   52   O O   . MET   A 1 22  ? 18.214  -46.338 39.908 1.00 75.73  ? 40  MET   A O   1 
ATOM   53   C CB  . MET   A 1 22  ? 20.173  -44.588 41.555 1.00 100.73 ? 40  MET   A CB  1 
ATOM   54   C CG  . MET   A 1 22  ? 21.175  -44.489 42.689 1.00 123.41 ? 40  MET   A CG  1 
ATOM   55   S SD  . MET   A 1 22  ? 21.099  -45.902 43.803 1.00 114.51 ? 40  MET   A SD  1 
ATOM   56   C CE  . MET   A 1 22  ? 19.434  -45.737 44.441 1.00 109.15 ? 40  MET   A CE  1 
ATOM   57   N N   . TYR   A 1 23  ? 19.532  -45.354 38.361 1.00 84.29  ? 41  TYR   A N   1 
ATOM   58   C CA  . TYR   A 1 23  ? 18.475  -45.257 37.359 1.00 77.37  ? 41  TYR   A CA  1 
ATOM   59   C C   . TYR   A 1 23  ? 17.646  -46.533 37.288 1.00 82.15  ? 41  TYR   A C   1 
ATOM   60   O O   . TYR   A 1 23  ? 16.430  -46.514 37.511 1.00 78.16  ? 41  TYR   A O   1 
ATOM   61   C CB  . TYR   A 1 23  ? 19.092  -44.946 35.997 1.00 74.15  ? 41  TYR   A CB  1 
ATOM   62   C CG  . TYR   A 1 23  ? 18.140  -45.135 34.843 1.00 86.54  ? 41  TYR   A CG  1 
ATOM   63   C CD1 . TYR   A 1 23  ? 17.194  -44.170 34.533 1.00 78.22  ? 41  TYR   A CD1 1 
ATOM   64   C CD2 . TYR   A 1 23  ? 18.189  -46.280 34.061 1.00 105.45 ? 41  TYR   A CD2 1 
ATOM   65   C CE1 . TYR   A 1 23  ? 16.323  -44.339 33.479 1.00 86.94  ? 41  TYR   A CE1 1 
ATOM   66   C CE2 . TYR   A 1 23  ? 17.322  -46.458 33.005 1.00 108.99 ? 41  TYR   A CE2 1 
ATOM   67   C CZ  . TYR   A 1 23  ? 16.392  -45.485 32.718 1.00 86.10  ? 41  TYR   A CZ  1 
ATOM   68   O OH  . TYR   A 1 23  ? 15.528  -45.659 31.664 1.00 90.39  ? 41  TYR   A OH  1 
ATOM   69   N N   . ASP   A 1 24  ? 18.296  -47.659 36.990 1.00 83.47  ? 42  ASP   A N   1 
ATOM   70   C CA  . ASP   A 1 24  ? 17.569  -48.916 36.846 1.00 74.12  ? 42  ASP   A CA  1 
ATOM   71   C C   . ASP   A 1 24  ? 16.667  -49.156 38.048 1.00 77.65  ? 42  ASP   A C   1 
ATOM   72   O O   . ASP   A 1 24  ? 15.464  -49.412 37.902 1.00 72.85  ? 42  ASP   A O   1 
ATOM   73   C CB  . ASP   A 1 24  ? 18.554  -50.075 36.680 1.00 102.78 ? 42  ASP   A CB  1 
ATOM   74   C CG  . ASP   A 1 24  ? 19.653  -49.773 35.679 1.00 106.88 ? 42  ASP   A CG  1 
ATOM   75   O OD1 . ASP   A 1 24  ? 20.555  -48.974 36.010 1.00 110.86 ? 42  ASP   A OD1 1 
ATOM   76   O OD2 . ASP   A 1 24  ? 19.618  -50.336 34.566 1.00 134.38 ? 42  ASP   A OD2 1 
ATOM   77   N N   . ARG   A 1 25  ? 17.226  -49.006 39.253 1.00 93.19  ? 43  ARG   A N   1 
ATOM   78   C CA  . ARG   A 1 25  ? 16.484  -49.320 40.467 1.00 90.78  ? 43  ARG   A CA  1 
ATOM   79   C C   . ARG   A 1 25  ? 15.144  -48.608 40.500 1.00 83.48  ? 43  ARG   A C   1 
ATOM   80   O O   . ARG   A 1 25  ? 14.161  -49.154 41.014 1.00 80.57  ? 43  ARG   A O   1 
ATOM   81   C CB  . ARG   A 1 25  ? 17.311  -48.934 41.695 1.00 103.26 ? 43  ARG   A CB  1 
ATOM   82   C CG  . ARG   A 1 25  ? 18.674  -49.603 41.763 1.00 135.46 ? 43  ARG   A CG  1 
ATOM   83   C CD  . ARG   A 1 25  ? 19.473  -49.094 42.947 1.00 138.12 ? 43  ARG   A CD  1 
ATOM   84   N NE  . ARG   A 1 25  ? 20.791  -49.712 43.027 1.00 152.14 ? 43  ARG   A NE  1 
ATOM   85   C CZ  . ARG   A 1 25  ? 21.697  -49.429 43.954 1.00 168.66 ? 43  ARG   A CZ  1 
ATOM   86   N NH1 . ARG   A 1 25  ? 21.462  -48.533 44.900 1.00 167.04 ? 43  ARG   A NH1 1 
ATOM   87   N NH2 . ARG   A 1 25  ? 22.868  -50.059 43.931 1.00 154.55 ? 43  ARG   A NH2 1 
ATOM   88   N N   . TYR   A 1 26  ? 15.080  -47.395 39.953 1.00 76.86  ? 44  TYR   A N   1 
ATOM   89   C CA  . TYR   A 1 26  ? 13.813  -46.676 39.904 1.00 74.80  ? 44  TYR   A CA  1 
ATOM   90   C C   . TYR   A 1 26  ? 12.971  -47.136 38.721 1.00 73.72  ? 44  TYR   A C   1 
ATOM   91   O O   . TYR   A 1 26  ? 11.802  -47.507 38.890 1.00 79.96  ? 44  TYR   A O   1 
ATOM   92   C CB  . TYR   A 1 26  ? 14.078  -45.172 39.837 1.00 76.75  ? 44  TYR   A CB  1 
ATOM   93   C CG  . TYR   A 1 26  ? 14.926  -44.677 40.985 1.00 75.85  ? 44  TYR   A CG  1 
ATOM   94   C CD1 . TYR   A 1 26  ? 14.648  -45.065 42.288 1.00 77.81  ? 44  TYR   A CD1 1 
ATOM   95   C CD2 . TYR   A 1 26  ? 16.015  -43.843 40.768 1.00 70.15  ? 44  TYR   A CD2 1 
ATOM   96   C CE1 . TYR   A 1 26  ? 15.419  -44.628 43.343 1.00 74.14  ? 44  TYR   A CE1 1 
ATOM   97   C CE2 . TYR   A 1 26  ? 16.794  -43.400 41.821 1.00 71.28  ? 44  TYR   A CE2 1 
ATOM   98   C CZ  . TYR   A 1 26  ? 16.490  -43.798 43.106 1.00 69.91  ? 44  TYR   A CZ  1 
ATOM   99   O OH  . TYR   A 1 26  ? 17.254  -43.371 44.166 1.00 87.80  ? 44  TYR   A OH  1 
ATOM   100  N N   . ARG   A 1 27  ? 13.559  -47.159 37.524 1.00 76.73  ? 45  ARG   A N   1 
ATOM   101  C CA  . ARG   A 1 27  ? 12.786  -47.515 36.339 1.00 74.16  ? 45  ARG   A CA  1 
ATOM   102  C C   . ARG   A 1 27  ? 12.125  -48.872 36.523 1.00 83.09  ? 45  ARG   A C   1 
ATOM   103  O O   . ARG   A 1 27  ? 10.896  -48.997 36.446 1.00 83.89  ? 45  ARG   A O   1 
ATOM   104  C CB  . ARG   A 1 27  ? 13.695  -47.519 35.109 1.00 74.03  ? 45  ARG   A CB  1 
ATOM   105  C CG  . ARG   A 1 27  ? 13.050  -48.039 33.826 1.00 83.50  ? 45  ARG   A CG  1 
ATOM   106  C CD  . ARG   A 1 27  ? 14.093  -48.649 32.906 1.00 85.19  ? 45  ARG   A CD  1 
ATOM   107  N NE  . ARG   A 1 27  ? 14.772  -49.772 33.539 1.00 88.17  ? 45  ARG   A NE  1 
ATOM   108  C CZ  . ARG   A 1 27  ? 15.901  -50.311 33.101 1.00 89.45  ? 45  ARG   A CZ  1 
ATOM   109  N NH1 . ARG   A 1 27  ? 16.512  -49.852 32.021 1.00 99.90  ? 45  ARG   A NH1 1 
ATOM   110  N NH2 . ARG   A 1 27  ? 16.435  -51.331 33.767 1.00 90.90  ? 45  ARG   A NH2 1 
ATOM   111  N N   . ASP   A 1 28  ? 12.927  -49.894 36.829 1.00 74.20  ? 46  ASP   A N   1 
ATOM   112  C CA  . ASP   A 1 28  ? 12.366  -51.220 37.044 1.00 84.43  ? 46  ASP   A CA  1 
ATOM   113  C C   . ASP   A 1 28  ? 11.220  -51.160 38.042 1.00 82.90  ? 46  ASP   A C   1 
ATOM   114  O O   . ASP   A 1 28  ? 10.146  -51.725 37.801 1.00 87.53  ? 46  ASP   A O   1 
ATOM   115  C CB  . ASP   A 1 28  ? 13.457  -52.173 37.531 1.00 105.89 ? 46  ASP   A CB  1 
ATOM   116  C CG  . ASP   A 1 28  ? 14.638  -52.240 36.582 1.00 96.39  ? 46  ASP   A CG  1 
ATOM   117  O OD1 . ASP   A 1 28  ? 14.435  -52.043 35.367 1.00 90.25  ? 46  ASP   A OD1 1 
ATOM   118  O OD2 . ASP   A 1 28  ? 15.769  -52.489 37.051 1.00 90.50  ? 46  ASP   A OD2 1 
ATOM   119  N N   . VAL   A 1 29  ? 11.406  -50.421 39.139 1.00 77.96  ? 47  VAL   A N   1 
ATOM   120  C CA  . VAL   A 1 29  ? 10.372  -50.364 40.167 1.00 96.27  ? 47  VAL   A CA  1 
ATOM   121  C C   . VAL   A 1 29  ? 9.051   -49.926 39.553 1.00 89.77  ? 47  VAL   A C   1 
ATOM   122  O O   . VAL   A 1 29  ? 8.015   -50.580 39.729 1.00 86.35  ? 47  VAL   A O   1 
ATOM   123  C CB  . VAL   A 1 29  ? 10.803  -49.429 41.311 1.00 71.21  ? 47  VAL   A CB  1 
ATOM   124  C CG1 . VAL   A 1 29  ? 9.589   -48.882 42.045 1.00 89.70  ? 47  VAL   A CG1 1 
ATOM   125  C CG2 . VAL   A 1 29  ? 11.717  -50.166 42.278 1.00 89.42  ? 47  VAL   A CG2 1 
ATOM   126  N N   . PHE   A 1 30  ? 9.075   -48.841 38.778 1.00 87.09  ? 48  PHE   A N   1 
ATOM   127  C CA  . PHE   A 1 30  ? 7.839   -48.379 38.159 1.00 79.21  ? 48  PHE   A CA  1 
ATOM   128  C C   . PHE   A 1 30  ? 7.250   -49.469 37.276 1.00 85.35  ? 48  PHE   A C   1 
ATOM   129  O O   . PHE   A 1 30  ? 6.058   -49.789 37.372 1.00 82.68  ? 48  PHE   A O   1 
ATOM   130  C CB  . PHE   A 1 30  ? 8.091   -47.104 37.354 1.00 79.63  ? 48  PHE   A CB  1 
ATOM   131  C CG  . PHE   A 1 30  ? 6.901   -46.651 36.559 1.00 75.91  ? 48  PHE   A CG  1 
ATOM   132  C CD1 . PHE   A 1 30  ? 5.781   -46.142 37.195 1.00 72.53  ? 48  PHE   A CD1 1 
ATOM   133  C CD2 . PHE   A 1 30  ? 6.900   -46.739 35.178 1.00 81.64  ? 48  PHE   A CD2 1 
ATOM   134  C CE1 . PHE   A 1 30  ? 4.682   -45.728 36.469 1.00 69.32  ? 48  PHE   A CE1 1 
ATOM   135  C CE2 . PHE   A 1 30  ? 5.804   -46.325 34.444 1.00 87.44  ? 48  PHE   A CE2 1 
ATOM   136  C CZ  . PHE   A 1 30  ? 4.693   -45.820 35.091 1.00 83.58  ? 48  PHE   A CZ  1 
ATOM   137  N N   . ILE   A 1 31  ? 8.086   -50.090 36.442 1.00 94.81  ? 49  ILE   A N   1 
ATOM   138  C CA  . ILE   A 1 31  ? 7.591   -51.149 35.572 1.00 100.82 ? 49  ILE   A CA  1 
ATOM   139  C C   . ILE   A 1 31  ? 7.044   -52.294 36.412 1.00 100.61 ? 49  ILE   A C   1 
ATOM   140  O O   . ILE   A 1 31  ? 6.037   -52.919 36.056 1.00 91.61  ? 49  ILE   A O   1 
ATOM   141  C CB  . ILE   A 1 31  ? 8.700   -51.612 34.608 1.00 116.55 ? 49  ILE   A CB  1 
ATOM   142  C CG1 . ILE   A 1 31  ? 9.153   -50.435 33.736 1.00 94.27  ? 49  ILE   A CG1 1 
ATOM   143  C CG2 . ILE   A 1 31  ? 8.208   -52.765 33.737 1.00 137.51 ? 49  ILE   A CG2 1 
ATOM   144  C CD1 . ILE   A 1 31  ? 10.232  -50.772 32.726 1.00 126.51 ? 49  ILE   A CD1 1 
ATOM   145  N N   . ASN   A 1 32  ? 7.679   -52.568 37.557 1.00 118.94 ? 50  ASN   A N   1 
ATOM   146  C CA  . ASN   A 1 32  ? 7.170   -53.616 38.435 1.00 122.09 ? 50  ASN   A CA  1 
ATOM   147  C C   . ASN   A 1 32  ? 5.749   -53.305 38.880 1.00 117.68 ? 50  ASN   A C   1 
ATOM   148  O O   . ASN   A 1 32  ? 4.896   -54.201 38.931 1.00 118.03 ? 50  ASN   A O   1 
ATOM   149  C CB  . ASN   A 1 32  ? 8.089   -53.791 39.645 1.00 132.11 ? 50  ASN   A CB  1 
ATOM   150  C CG  . ASN   A 1 32  ? 9.382   -54.496 39.295 1.00 135.08 ? 50  ASN   A CG  1 
ATOM   151  O OD1 . ASN   A 1 32  ? 9.420   -55.335 38.396 1.00 135.62 ? 50  ASN   A OD1 1 
ATOM   152  N ND2 . ASN   A 1 32  ? 10.452  -54.158 40.005 1.00 138.55 ? 50  ASN   A ND2 1 
ATOM   153  N N   . HIS   A 1 33  ? 5.467   -52.038 39.195 1.00 92.41  ? 51  HIS   A N   1 
ATOM   154  C CA  . HIS   A 1 33  ? 4.098   -51.668 39.533 1.00 89.40  ? 51  HIS   A CA  1 
ATOM   155  C C   . HIS   A 1 33  ? 3.154   -52.026 38.396 1.00 81.35  ? 51  HIS   A C   1 
ATOM   156  O O   . HIS   A 1 33  ? 2.058   -52.551 38.626 1.00 76.21  ? 51  HIS   A O   1 
ATOM   157  C CB  . HIS   A 1 33  ? 4.007   -50.176 39.850 1.00 107.75 ? 51  HIS   A CB  1 
ATOM   158  C CG  . HIS   A 1 33  ? 2.607   -49.644 39.834 1.00 92.32  ? 51  HIS   A CG  1 
ATOM   159  N ND1 . HIS   A 1 33  ? 1.611   -50.149 40.641 1.00 97.50  ? 51  HIS   A ND1 1 
ATOM   160  C CD2 . HIS   A 1 33  ? 2.035   -48.658 39.103 1.00 87.40  ? 51  HIS   A CD2 1 
ATOM   161  C CE1 . HIS   A 1 33  ? 0.486   -49.495 40.411 1.00 73.15  ? 51  HIS   A CE1 1 
ATOM   162  N NE2 . HIS   A 1 33  ? 0.716   -48.585 39.482 1.00 86.45  ? 51  HIS   A NE2 1 
ATOM   163  N N   . ILE   A 1 34  ? 3.568   -51.756 37.157 1.00 93.55  ? 52  ILE   A N   1 
ATOM   164  C CA  . ILE   A 1 34  ? 2.744   -52.129 36.016 1.00 86.02  ? 52  ILE   A CA  1 
ATOM   165  C C   . ILE   A 1 34  ? 2.704   -53.644 35.865 1.00 88.28  ? 52  ILE   A C   1 
ATOM   166  O O   . ILE   A 1 34  ? 1.701   -54.202 35.407 1.00 97.54  ? 52  ILE   A O   1 
ATOM   167  C CB  . ILE   A 1 34  ? 3.262   -51.430 34.746 1.00 88.42  ? 52  ILE   A CB  1 
ATOM   168  C CG1 . ILE   A 1 34  ? 3.323   -49.916 34.983 1.00 79.05  ? 52  ILE   A CG1 1 
ATOM   169  C CG2 . ILE   A 1 34  ? 2.372   -51.754 33.553 1.00 78.80  ? 52  ILE   A CG2 1 
ATOM   170  C CD1 . ILE   A 1 34  ? 3.656   -49.100 33.754 1.00 79.08  ? 52  ILE   A CD1 1 
ATOM   171  N N   . ASN   A 1 35  ? 3.780   -54.337 36.246 1.00 102.85 ? 53  ASN   A N   1 
ATOM   172  C CA  . ASN   A 1 35  ? 3.771   -55.796 36.189 1.00 93.59  ? 53  ASN   A CA  1 
ATOM   173  C C   . ASN   A 1 35  ? 2.736   -56.375 37.144 1.00 95.67  ? 53  ASN   A C   1 
ATOM   174  O O   . ASN   A 1 35  ? 2.091   -57.384 36.837 1.00 100.26 ? 53  ASN   A O   1 
ATOM   175  C CB  . ASN   A 1 35  ? 5.160   -56.346 36.512 1.00 100.53 ? 53  ASN   A CB  1 
ATOM   176  C CG  . ASN   A 1 35  ? 6.081   -56.355 35.305 1.00 98.72  ? 53  ASN   A CG  1 
ATOM   177  O OD1 . ASN   A 1 35  ? 5.755   -55.804 34.255 1.00 101.89 ? 53  ASN   A OD1 1 
ATOM   178  N ND2 . ASN   A 1 35  ? 7.241   -56.985 35.452 1.00 116.26 ? 53  ASN   A ND2 1 
ATOM   179  N N   . ASP   A 1 36  ? 2.566   -55.753 38.312 1.00 90.04  ? 54  ASP   A N   1 
ATOM   180  C CA  . ASP   A 1 36  ? 1.595   -56.235 39.287 1.00 89.96  ? 54  ASP   A CA  1 
ATOM   181  C C   . ASP   A 1 36  ? 0.159   -56.107 38.798 1.00 80.46  ? 54  ASP   A C   1 
ATOM   182  O O   . ASP   A 1 36  ? -0.735  -56.715 39.398 1.00 82.14  ? 54  ASP   A O   1 
ATOM   183  C CB  . ASP   A 1 36  ? 1.762   -55.478 40.607 1.00 95.97  ? 54  ASP   A CB  1 
ATOM   184  C CG  . ASP   A 1 36  ? 3.126   -55.692 41.235 1.00 108.80 ? 54  ASP   A CG  1 
ATOM   185  O OD1 . ASP   A 1 36  ? 3.896   -56.526 40.714 1.00 114.97 ? 54  ASP   A OD1 1 
ATOM   186  O OD2 . ASP   A 1 36  ? 3.429   -55.026 42.247 1.00 118.84 ? 54  ASP   A OD2 1 
ATOM   187  N N   . TYR   A 1 37  ? -0.085  -55.338 37.739 1.00 79.93  ? 55  TYR   A N   1 
ATOM   188  C CA  . TYR   A 1 37  ? -1.428  -55.226 37.190 1.00 79.82  ? 55  TYR   A CA  1 
ATOM   189  C C   . TYR   A 1 37  ? -1.973  -56.607 36.838 1.00 86.55  ? 55  TYR   A C   1 
ATOM   190  O O   . TYR   A 1 37  ? -1.230  -57.577 36.669 1.00 92.98  ? 55  TYR   A O   1 
ATOM   191  C CB  . TYR   A 1 37  ? -1.433  -54.338 35.945 1.00 85.81  ? 55  TYR   A CB  1 
ATOM   192  C CG  . TYR   A 1 37  ? -1.347  -52.845 36.208 1.00 94.35  ? 55  TYR   A CG  1 
ATOM   193  C CD1 . TYR   A 1 37  ? -1.194  -52.343 37.496 1.00 81.28  ? 55  TYR   A CD1 1 
ATOM   194  C CD2 . TYR   A 1 37  ? -1.433  -51.936 35.161 1.00 94.79  ? 55  TYR   A CD2 1 
ATOM   195  C CE1 . TYR   A 1 37  ? -1.120  -50.982 37.727 1.00 75.51  ? 55  TYR   A CE1 1 
ATOM   196  C CE2 . TYR   A 1 37  ? -1.361  -50.576 35.386 1.00 71.78  ? 55  TYR   A CE2 1 
ATOM   197  C CZ  . TYR   A 1 37  ? -1.205  -50.104 36.668 1.00 74.99  ? 55  TYR   A CZ  1 
ATOM   198  O OH  . TYR   A 1 37  ? -1.133  -48.749 36.891 1.00 91.53  ? 55  TYR   A OH  1 
ATOM   199  N N   . VAL   A 1 38  ? -3.298  -56.686 36.723 1.00 101.42 ? 56  VAL   A N   1 
ATOM   200  C CA  . VAL   A 1 38  ? -3.970  -57.945 36.421 1.00 102.67 ? 56  VAL   A CA  1 
ATOM   201  C C   . VAL   A 1 38  ? -3.978  -58.149 34.913 1.00 100.07 ? 56  VAL   A C   1 
ATOM   202  O O   . VAL   A 1 38  ? -4.940  -57.785 34.228 1.00 102.20 ? 56  VAL   A O   1 
ATOM   203  C CB  . VAL   A 1 38  ? -5.402  -57.965 36.988 1.00 110.72 ? 56  VAL   A CB  1 
ATOM   204  C CG1 . VAL   A 1 38  ? -6.047  -59.321 36.753 1.00 97.42  ? 56  VAL   A CG1 1 
ATOM   205  C CG2 . VAL   A 1 38  ? -5.395  -57.614 38.471 1.00 117.18 ? 56  VAL   A CG2 1 
ATOM   206  N N   . LEU   A 1 39  ? -2.906  -58.740 34.390 1.00 100.67 ? 57  LEU   A N   1 
ATOM   207  C CA  . LEU   A 1 39  ? -2.747  -58.946 32.960 1.00 113.47 ? 57  LEU   A CA  1 
ATOM   208  C C   . LEU   A 1 39  ? -2.194  -60.342 32.717 1.00 127.64 ? 57  LEU   A C   1 
ATOM   209  O O   . LEU   A 1 39  ? -1.763  -61.036 33.642 1.00 125.81 ? 57  LEU   A O   1 
ATOM   210  C CB  . LEU   A 1 39  ? -1.816  -57.894 32.344 1.00 108.02 ? 57  LEU   A CB  1 
ATOM   211  C CG  . LEU   A 1 39  ? -2.229  -56.435 32.536 1.00 107.60 ? 57  LEU   A CG  1 
ATOM   212  C CD1 . LEU   A 1 39  ? -1.067  -55.512 32.222 1.00 103.81 ? 57  LEU   A CD1 1 
ATOM   213  C CD2 . LEU   A 1 39  ? -3.429  -56.099 31.666 1.00 115.78 ? 57  LEU   A CD2 1 
ATOM   214  N N   . GLU   A 1 40  ? -2.217  -60.753 31.455 1.00 152.03 ? 58  GLU   A N   1 
ATOM   215  C CA  . GLU   A 1 40  ? -1.603  -62.010 31.061 1.00 154.31 ? 58  GLU   A CA  1 
ATOM   216  C C   . GLU   A 1 40  ? -0.101  -61.827 30.892 1.00 149.58 ? 58  GLU   A C   1 
ATOM   217  O O   . GLU   A 1 40  ? 0.382   -60.736 30.575 1.00 146.19 ? 58  GLU   A O   1 
ATOM   218  C CB  . GLU   A 1 40  ? -2.227  -62.524 29.766 1.00 160.24 ? 58  GLU   A CB  1 
ATOM   219  C CG  . GLU   A 1 40  ? -3.703  -62.866 29.901 1.00 174.57 ? 58  GLU   A CG  1 
ATOM   220  C CD  . GLU   A 1 40  ? -4.513  -62.433 28.697 1.00 176.77 ? 58  GLU   A CD  1 
ATOM   221  O OE1 . GLU   A 1 40  ? -4.015  -62.574 27.561 1.00 182.60 ? 58  GLU   A OE1 1 
ATOM   222  O OE2 . GLU   A 1 40  ? -5.645  -61.941 28.889 1.00 173.96 ? 58  GLU   A OE2 1 
ATOM   223  N N   . ASP   A 1 41  ? 0.641   -62.917 31.103 1.00 141.00 ? 59  ASP   A N   1 
ATOM   224  C CA  . ASP   A 1 41  ? 2.098   -62.826 31.121 1.00 141.73 ? 59  ASP   A CA  1 
ATOM   225  C C   . ASP   A 1 41  ? 2.639   -62.271 29.809 1.00 130.42 ? 59  ASP   A C   1 
ATOM   226  O O   . ASP   A 1 41  ? 3.624   -61.525 29.803 1.00 129.85 ? 59  ASP   A O   1 
ATOM   227  C CB  . ASP   A 1 41  ? 2.704   -64.198 31.412 1.00 147.30 ? 59  ASP   A CB  1 
ATOM   228  C CG  . ASP   A 1 41  ? 2.367   -64.700 32.803 1.00 163.24 ? 59  ASP   A CG  1 
ATOM   229  O OD1 . ASP   A 1 41  ? 1.207   -65.102 33.026 1.00 168.93 ? 59  ASP   A OD1 1 
ATOM   230  O OD2 . ASP   A 1 41  ? 3.264   -64.689 33.673 1.00 180.91 ? 59  ASP   A OD2 1 
ATOM   231  N N   . ASP   A 1 42  ? 2.015   -62.626 28.685 1.00 164.54 ? 60  ASP   A N   1 
ATOM   232  C CA  . ASP   A 1 42  ? 2.492   -62.142 27.393 1.00 128.11 ? 60  ASP   A CA  1 
ATOM   233  C C   . ASP   A 1 42  ? 2.353   -60.627 27.292 1.00 140.05 ? 60  ASP   A C   1 
ATOM   234  O O   . ASP   A 1 42  ? 3.302   -59.924 26.915 1.00 123.13 ? 60  ASP   A O   1 
ATOM   235  C CB  . ASP   A 1 42  ? 1.722   -62.834 26.268 1.00 145.71 ? 60  ASP   A CB  1 
ATOM   236  C CG  . ASP   A 1 42  ? 2.591   -63.130 25.062 1.00 129.45 ? 60  ASP   A CG  1 
ATOM   237  O OD1 . ASP   A 1 42  ? 3.561   -62.378 24.827 1.00 138.47 ? 60  ASP   A OD1 1 
ATOM   238  O OD2 . ASP   A 1 42  ? 2.305   -64.117 24.352 1.00 140.05 ? 60  ASP   A OD2 1 
ATOM   239  N N   . ILE   A 1 43  ? 1.172   -60.104 27.631 1.00 141.16 ? 61  ILE   A N   1 
ATOM   240  C CA  . ILE   A 1 43  ? 0.972   -58.659 27.615 1.00 137.02 ? 61  ILE   A CA  1 
ATOM   241  C C   . ILE   A 1 43  ? 1.939   -57.989 28.579 1.00 141.52 ? 61  ILE   A C   1 
ATOM   242  O O   . ILE   A 1 43  ? 2.479   -56.913 28.294 1.00 107.88 ? 61  ILE   A O   1 
ATOM   243  C CB  . ILE   A 1 43  ? -0.491  -58.310 27.953 1.00 141.60 ? 61  ILE   A CB  1 
ATOM   244  C CG1 . ILE   A 1 43  ? -1.427  -58.728 26.815 1.00 95.56  ? 61  ILE   A CG1 1 
ATOM   245  C CG2 . ILE   A 1 43  ? -0.631  -56.818 28.236 1.00 164.76 ? 61  ILE   A CG2 1 
ATOM   246  C CD1 . ILE   A 1 43  ? -2.060  -60.087 27.010 1.00 191.11 ? 61  ILE   A CD1 1 
ATOM   247  N N   . LYS   A 1 44  ? 2.161   -58.609 29.741 1.00 109.65 ? 62  LYS   A N   1 
ATOM   248  C CA  . LYS   A 1 44  ? 3.109   -58.060 30.704 1.00 112.97 ? 62  LYS   A CA  1 
ATOM   249  C C   . LYS   A 1 44  ? 4.492   -57.930 30.082 1.00 116.76 ? 62  LYS   A C   1 
ATOM   250  O O   . LYS   A 1 44  ? 5.144   -56.886 30.196 1.00 126.09 ? 62  LYS   A O   1 
ATOM   251  C CB  . LYS   A 1 44  ? 3.162   -58.946 31.950 1.00 104.66 ? 62  LYS   A CB  1 
ATOM   252  C CG  . LYS   A 1 44  ? 1.903   -58.915 32.800 1.00 118.83 ? 62  LYS   A CG  1 
ATOM   253  C CD  . LYS   A 1 44  ? 2.108   -59.646 34.117 1.00 106.01 ? 62  LYS   A CD  1 
ATOM   254  C CE  . LYS   A 1 44  ? 0.907   -59.484 35.034 1.00 111.21 ? 62  LYS   A CE  1 
ATOM   255  N NZ  . LYS   A 1 44  ? 1.165   -60.016 36.401 1.00 100.29 ? 62  LYS   A NZ  1 
ATOM   256  N N   . ILE   A 1 45  ? 4.947   -58.985 29.405 1.00 117.37 ? 63  ILE   A N   1 
ATOM   257  C CA  . ILE   A 1 45  ? 6.264   -58.959 28.777 1.00 116.69 ? 63  ILE   A CA  1 
ATOM   258  C C   . ILE   A 1 45  ? 6.336   -57.835 27.753 1.00 115.01 ? 63  ILE   A C   1 
ATOM   259  O O   . ILE   A 1 45  ? 7.299   -57.057 27.719 1.00 119.55 ? 63  ILE   A O   1 
ATOM   260  C CB  . ILE   A 1 45  ? 6.571   -60.323 28.132 1.00 118.29 ? 63  ILE   A CB  1 
ATOM   261  C CG1 . ILE   A 1 45  ? 6.732   -61.400 29.208 1.00 125.57 ? 63  ILE   A CG1 1 
ATOM   262  C CG2 . ILE   A 1 45  ? 7.816   -60.233 27.255 1.00 133.73 ? 63  ILE   A CG2 1 
ATOM   263  C CD1 . ILE   A 1 45  ? 6.706   -62.815 28.667 1.00 106.13 ? 63  ILE   A CD1 1 
ATOM   264  N N   . ILE   A 1 46  ? 5.313   -57.732 26.904 1.00 115.00 ? 64  ILE   A N   1 
ATOM   265  C CA  . ILE   A 1 46  ? 5.365   -56.754 25.821 1.00 112.46 ? 64  ILE   A CA  1 
ATOM   266  C C   . ILE   A 1 46  ? 5.380   -55.334 26.381 1.00 115.33 ? 64  ILE   A C   1 
ATOM   267  O O   . ILE   A 1 46  ? 6.181   -54.491 25.955 1.00 106.98 ? 64  ILE   A O   1 
ATOM   268  C CB  . ILE   A 1 46  ? 4.196   -56.961 24.843 1.00 145.27 ? 64  ILE   A CB  1 
ATOM   269  C CG1 . ILE   A 1 46  ? 4.183   -58.393 24.299 1.00 117.08 ? 64  ILE   A CG1 1 
ATOM   270  C CG2 . ILE   A 1 46  ? 4.307   -55.984 23.694 1.00 114.99 ? 64  ILE   A CG2 1 
ATOM   271  C CD1 . ILE   A 1 46  ? 5.467   -58.820 23.618 1.00 127.71 ? 64  ILE   A CD1 1 
ATOM   272  N N   . ILE   A 1 47  ? 4.500   -55.043 27.343 1.00 120.14 ? 65  ILE   A N   1 
ATOM   273  C CA  . ILE   A 1 47  ? 4.437   -53.686 27.879 1.00 104.24 ? 65  ILE   A CA  1 
ATOM   274  C C   . ILE   A 1 47  ? 5.706   -53.359 28.654 1.00 105.00 ? 65  ILE   A C   1 
ATOM   275  O O   . ILE   A 1 47  ? 6.187   -52.220 28.622 1.00 102.03 ? 65  ILE   A O   1 
ATOM   276  C CB  . ILE   A 1 47  ? 3.180   -53.486 28.749 1.00 95.16  ? 65  ILE   A CB  1 
ATOM   277  C CG1 . ILE   A 1 47  ? 3.234   -54.372 29.998 1.00 111.31 ? 65  ILE   A CG1 1 
ATOM   278  C CG2 . ILE   A 1 47  ? 1.923   -53.736 27.927 1.00 111.61 ? 65  ILE   A CG2 1 
ATOM   279  C CD1 . ILE   A 1 47  ? 2.020   -54.247 30.887 1.00 120.41 ? 65  ILE   A CD1 1 
ATOM   280  N N   . SER   A 1 48  ? 6.261   -54.334 29.378 1.00 107.32 ? 66  SER   A N   1 
ATOM   281  C CA  . SER   A 1 48  ? 7.512   -54.086 30.083 1.00 96.23  ? 66  SER   A CA  1 
ATOM   282  C C   . SER   A 1 48  ? 8.622   -53.743 29.101 1.00 104.39 ? 66  SER   A C   1 
ATOM   283  O O   . SER   A 1 48  ? 9.371   -52.783 29.309 1.00 98.57  ? 66  SER   A O   1 
ATOM   284  C CB  . SER   A 1 48  ? 7.890   -55.300 30.932 1.00 101.58 ? 66  SER   A CB  1 
ATOM   285  O OG  . SER   A 1 48  ? 7.993   -56.467 30.137 1.00 132.69 ? 66  SER   A OG  1 
ATOM   286  N N   . LYS   A 1 49  ? 8.729   -54.504 28.007 1.00 112.11 ? 67  LYS   A N   1 
ATOM   287  C CA  . LYS   A 1 49  ? 9.709   -54.172 26.977 1.00 102.63 ? 67  LYS   A CA  1 
ATOM   288  C C   . LYS   A 1 49  ? 9.499   -52.752 26.467 1.00 107.23 ? 67  LYS   A C   1 
ATOM   289  O O   . LYS   A 1 49  ? 10.443  -51.954 26.397 1.00 95.16  ? 67  LYS   A O   1 
ATOM   290  C CB  . LYS   A 1 49  ? 9.616   -55.165 25.815 1.00 101.01 ? 67  LYS   A CB  1 
ATOM   291  C CG  . LYS   A 1 49  ? 10.148  -56.558 26.108 1.00 119.49 ? 67  LYS   A CG  1 
ATOM   292  C CD  . LYS   A 1 49  ? 10.151  -57.413 24.844 1.00 135.64 ? 67  LYS   A CD  1 
ATOM   293  C CE  . LYS   A 1 49  ? 10.784  -58.775 25.080 1.00 141.46 ? 67  LYS   A CE  1 
ATOM   294  N NZ  . LYS   A 1 49  ? 10.902  -59.563 23.819 1.00 148.66 ? 67  LYS   A NZ  1 
ATOM   295  N N   . TYR   A 1 50  ? 8.256   -52.416 26.114 1.00 104.18 ? 68  TYR   A N   1 
ATOM   296  C CA  . TYR   A 1 50  ? 7.987   -51.125 25.490 1.00 94.86  ? 68  TYR   A CA  1 
ATOM   297  C C   . TYR   A 1 50  ? 8.306   -49.972 26.434 1.00 94.99  ? 68  TYR   A C   1 
ATOM   298  O O   . TYR   A 1 50  ? 8.942   -48.988 26.039 1.00 92.70  ? 68  TYR   A O   1 
ATOM   299  C CB  . TYR   A 1 50  ? 6.529   -51.056 25.038 1.00 86.79  ? 68  TYR   A CB  1 
ATOM   300  C CG  . TYR   A 1 50  ? 6.170   -49.750 24.373 1.00 90.30  ? 68  TYR   A CG  1 
ATOM   301  C CD1 . TYR   A 1 50  ? 6.373   -49.562 23.013 1.00 103.21 ? 68  TYR   A CD1 1 
ATOM   302  C CD2 . TYR   A 1 50  ? 5.636   -48.701 25.105 1.00 91.63  ? 68  TYR   A CD2 1 
ATOM   303  C CE1 . TYR   A 1 50  ? 6.049   -48.368 22.402 1.00 110.02 ? 68  TYR   A CE1 1 
ATOM   304  C CE2 . TYR   A 1 50  ? 5.310   -47.503 24.505 1.00 98.10  ? 68  TYR   A CE2 1 
ATOM   305  C CZ  . TYR   A 1 50  ? 5.518   -47.341 23.154 1.00 102.55 ? 68  TYR   A CZ  1 
ATOM   306  O OH  . TYR   A 1 50  ? 5.193   -46.149 22.552 1.00 100.57 ? 68  TYR   A OH  1 
ATOM   307  N N   . TYR   A 1 51  ? 7.870   -50.070 27.691 1.00 95.21  ? 69  TYR   A N   1 
ATOM   308  C CA  . TYR   A 1 51  ? 8.087   -48.969 28.622 1.00 87.13  ? 69  TYR   A CA  1 
ATOM   309  C C   . TYR   A 1 51  ? 9.543   -48.883 29.061 1.00 88.55  ? 69  TYR   A C   1 
ATOM   310  O O   . TYR   A 1 51  ? 10.058  -47.779 29.273 1.00 95.51  ? 69  TYR   A O   1 
ATOM   311  C CB  . TYR   A 1 51  ? 7.159   -49.112 29.830 1.00 77.03  ? 69  TYR   A CB  1 
ATOM   312  C CG  . TYR   A 1 51  ? 5.709   -48.738 29.557 1.00 67.05  ? 69  TYR   A CG  1 
ATOM   313  C CD1 . TYR   A 1 51  ? 5.351   -47.999 28.433 1.00 68.25  ? 69  TYR   A CD1 1 
ATOM   314  C CD2 . TYR   A 1 51  ? 4.698   -49.120 30.430 1.00 70.83  ? 69  TYR   A CD2 1 
ATOM   315  C CE1 . TYR   A 1 51  ? 4.036   -47.659 28.185 1.00 80.98  ? 69  TYR   A CE1 1 
ATOM   316  C CE2 . TYR   A 1 51  ? 3.377   -48.780 30.189 1.00 68.07  ? 69  TYR   A CE2 1 
ATOM   317  C CZ  . TYR   A 1 51  ? 3.054   -48.050 29.065 1.00 69.07  ? 69  TYR   A CZ  1 
ATOM   318  O OH  . TYR   A 1 51  ? 1.745   -47.707 28.815 1.00 78.71  ? 69  TYR   A OH  1 
ATOM   319  N N   . LYS   A 1 52  ? 10.231  -50.019 29.186 1.00 91.19  ? 70  LYS   A N   1 
ATOM   320  C CA  . LYS   A 1 52  ? 11.665  -49.965 29.429 1.00 88.68  ? 70  LYS   A CA  1 
ATOM   321  C C   . LYS   A 1 52  ? 12.369  -49.244 28.290 1.00 88.64  ? 70  LYS   A C   1 
ATOM   322  O O   . LYS   A 1 52  ? 13.255  -48.413 28.524 1.00 75.54  ? 70  LYS   A O   1 
ATOM   323  C CB  . LYS   A 1 52  ? 12.221  -51.378 29.598 1.00 91.85  ? 70  LYS   A CB  1 
ATOM   324  C CG  . LYS   A 1 52  ? 13.719  -51.422 29.825 1.00 102.28 ? 70  LYS   A CG  1 
ATOM   325  C CD  . LYS   A 1 52  ? 14.220  -52.844 29.978 1.00 91.36  ? 70  LYS   A CD  1 
ATOM   326  C CE  . LYS   A 1 52  ? 15.733  -52.880 30.143 1.00 103.13 ? 70  LYS   A CE  1 
ATOM   327  N NZ  . LYS   A 1 52  ? 16.449  -52.313 28.962 1.00 90.65  ? 70  LYS   A NZ  1 
ATOM   328  N N   . LEU   A 1 53  ? 11.981  -49.544 27.048 1.00 89.65  ? 71  LEU   A N   1 
ATOM   329  C CA  . LEU   A 1 53  ? 12.553  -48.839 25.906 1.00 90.87  ? 71  LEU   A CA  1 
ATOM   330  C C   . LEU   A 1 53  ? 12.258  -47.348 25.987 1.00 92.13  ? 71  LEU   A C   1 
ATOM   331  O O   . LEU   A 1 53  ? 13.140  -46.516 25.756 1.00 91.10  ? 71  LEU   A O   1 
ATOM   332  C CB  . LEU   A 1 53  ? 12.003  -49.422 24.605 1.00 99.23  ? 71  LEU   A CB  1 
ATOM   333  C CG  . LEU   A 1 53  ? 12.357  -48.651 23.331 1.00 97.67  ? 71  LEU   A CG  1 
ATOM   334  C CD1 . LEU   A 1 53  ? 13.863  -48.612 23.116 1.00 103.46 ? 71  LEU   A CD1 1 
ATOM   335  C CD2 . LEU   A 1 53  ? 11.653  -49.264 22.134 1.00 115.47 ? 71  LEU   A CD2 1 
ATOM   336  N N   . LEU   A 1 54  ? 11.014  -46.993 26.305 1.00 88.29  ? 72  LEU   A N   1 
ATOM   337  C CA  . LEU   A 1 54  ? 10.646  -45.586 26.423 1.00 83.20  ? 72  LEU   A CA  1 
ATOM   338  C C   . LEU   A 1 54  ? 11.556  -44.867 27.411 1.00 89.93  ? 72  LEU   A C   1 
ATOM   339  O O   . LEU   A 1 54  ? 12.152  -43.828 27.093 1.00 96.08  ? 72  LEU   A O   1 
ATOM   340  C CB  . LEU   A 1 54  ? 9.185   -45.480 26.861 1.00 83.82  ? 72  LEU   A CB  1 
ATOM   341  C CG  . LEU   A 1 54  ? 8.679   -44.107 27.303 1.00 83.94  ? 72  LEU   A CG  1 
ATOM   342  C CD1 . LEU   A 1 54  ? 8.628   -43.155 26.124 1.00 89.42  ? 72  LEU   A CD1 1 
ATOM   343  C CD2 . LEU   A 1 54  ? 7.312   -44.237 27.954 1.00 74.70  ? 72  LEU   A CD2 1 
ATOM   344  N N   . PHE   A 1 55  ? 11.679  -45.418 28.619 1.00 85.47  ? 73  PHE   A N   1 
ATOM   345  C CA  . PHE   A 1 55  ? 12.488  -44.777 29.649 1.00 77.87  ? 73  PHE   A CA  1 
ATOM   346  C C   . PHE   A 1 55  ? 13.950  -44.692 29.226 1.00 88.70  ? 73  PHE   A C   1 
ATOM   347  O O   . PHE   A 1 55  ? 14.572  -43.628 29.316 1.00 91.87  ? 73  PHE   A O   1 
ATOM   348  C CB  . PHE   A 1 55  ? 12.351  -45.536 30.968 1.00 75.78  ? 73  PHE   A CB  1 
ATOM   349  C CG  . PHE   A 1 55  ? 11.117  -45.179 31.747 1.00 81.19  ? 73  PHE   A CG  1 
ATOM   350  C CD1 . PHE   A 1 55  ? 9.866   -45.600 31.326 1.00 85.18  ? 73  PHE   A CD1 1 
ATOM   351  C CD2 . PHE   A 1 55  ? 11.210  -44.425 32.903 1.00 68.71  ? 73  PHE   A CD2 1 
ATOM   352  C CE1 . PHE   A 1 55  ? 8.731   -45.273 32.042 1.00 82.54  ? 73  PHE   A CE1 1 
ATOM   353  C CE2 . PHE   A 1 55  ? 10.078  -44.093 33.624 1.00 72.21  ? 73  PHE   A CE2 1 
ATOM   354  C CZ  . PHE   A 1 55  ? 8.837   -44.519 33.193 1.00 78.87  ? 73  PHE   A CZ  1 
ATOM   355  N N   . ASP   A 1 56  ? 14.516  -45.803 28.749 1.00 89.99  ? 74  ASP   A N   1 
ATOM   356  C CA  . ASP   A 1 56  ? 15.923  -45.809 28.370 1.00 83.20  ? 74  ASP   A CA  1 
ATOM   357  C C   . ASP   A 1 56  ? 16.203  -44.917 27.169 1.00 84.40  ? 74  ASP   A C   1 
ATOM   358  O O   . ASP   A 1 56  ? 17.347  -44.491 26.981 1.00 87.23  ? 74  ASP   A O   1 
ATOM   359  C CB  . ASP   A 1 56  ? 16.378  -47.236 28.061 1.00 87.62  ? 74  ASP   A CB  1 
ATOM   360  C CG  . ASP   A 1 56  ? 16.244  -48.163 29.252 1.00 92.05  ? 74  ASP   A CG  1 
ATOM   361  O OD1 . ASP   A 1 56  ? 15.886  -47.681 30.349 1.00 85.18  ? 74  ASP   A OD1 1 
ATOM   362  O OD2 . ASP   A 1 56  ? 16.496  -49.376 29.091 1.00 92.52  ? 74  ASP   A OD2 1 
ATOM   363  N N   . TYR   A 1 57  ? 15.190  -44.628 26.357 1.00 91.91  ? 75  TYR   A N   1 
ATOM   364  C CA  . TYR   A 1 57  ? 15.370  -43.843 25.147 1.00 99.27  ? 75  TYR   A CA  1 
ATOM   365  C C   . TYR   A 1 57  ? 15.266  -42.349 25.420 1.00 90.85  ? 75  TYR   A C   1 
ATOM   366  O O   . TYR   A 1 57  ? 16.114  -41.573 24.967 1.00 100.06 ? 75  TYR   A O   1 
ATOM   367  C CB  . TYR   A 1 57  ? 14.326  -44.265 24.110 1.00 80.59  ? 75  TYR   A CB  1 
ATOM   368  C CG  . TYR   A 1 57  ? 14.553  -43.717 22.722 1.00 91.02  ? 75  TYR   A CG  1 
ATOM   369  C CD1 . TYR   A 1 57  ? 14.063  -42.471 22.355 1.00 101.16 ? 75  TYR   A CD1 1 
ATOM   370  C CD2 . TYR   A 1 57  ? 15.245  -44.454 21.771 1.00 111.96 ? 75  TYR   A CD2 1 
ATOM   371  C CE1 . TYR   A 1 57  ? 14.263  -41.971 21.082 1.00 112.23 ? 75  TYR   A CE1 1 
ATOM   372  C CE2 . TYR   A 1 57  ? 15.451  -43.963 20.497 1.00 102.16 ? 75  TYR   A CE2 1 
ATOM   373  C CZ  . TYR   A 1 57  ? 14.957  -42.722 20.157 1.00 92.80  ? 75  TYR   A CZ  1 
ATOM   374  O OH  . TYR   A 1 57  ? 15.162  -42.233 18.887 1.00 95.20  ? 75  TYR   A OH  1 
ATOM   375  N N   . ASN   A 1 58  ? 14.240  -41.930 26.163 1.00 89.84  ? 76  ASN   A N   1 
ATOM   376  C CA  . ASN   A 1 58  ? 13.977  -40.510 26.351 1.00 88.09  ? 76  ASN   A CA  1 
ATOM   377  C C   . ASN   A 1 58  ? 14.552  -39.941 27.640 1.00 91.19  ? 76  ASN   A C   1 
ATOM   378  O O   . ASN   A 1 58  ? 14.605  -38.714 27.780 1.00 103.49 ? 76  ASN   A O   1 
ATOM   379  C CB  . ASN   A 1 58  ? 12.469  -40.248 26.311 1.00 93.05  ? 76  ASN   A CB  1 
ATOM   380  C CG  . ASN   A 1 58  ? 11.870  -40.544 24.955 1.00 87.49  ? 76  ASN   A CG  1 
ATOM   381  O OD1 . ASN   A 1 58  ? 11.861  -39.691 24.067 1.00 97.19  ? 76  ASN   A OD1 1 
ATOM   382  N ND2 . ASN   A 1 58  ? 11.376  -41.762 24.783 1.00 80.53  ? 76  ASN   A ND2 1 
ATOM   383  N N   . CYS   A 1 59  ? 14.984  -40.782 28.578 1.00 95.60  ? 77  CYS   A N   1 
ATOM   384  C CA  . CYS   A 1 59  ? 15.564  -40.314 29.829 1.00 97.67  ? 77  CYS   A CA  1 
ATOM   385  C C   . CYS   A 1 59  ? 17.066  -40.537 29.910 1.00 112.46 ? 77  CYS   A C   1 
ATOM   386  O O   . CYS   A 1 59  ? 17.665  -40.242 30.951 1.00 82.47  ? 77  CYS   A O   1 
ATOM   387  C CB  . CYS   A 1 59  ? 14.883  -41.002 31.017 1.00 78.40  ? 77  CYS   A CB  1 
ATOM   388  S SG  . CYS   A 1 59  ? 13.110  -40.682 31.130 1.00 86.94  ? 77  CYS   A SG  1 
ATOM   389  N N   . LEU   A 1 60  ? 17.690  -41.043 28.848 1.00 102.41 ? 78  LEU   A N   1 
ATOM   390  C CA  . LEU   A 1 60  ? 19.121  -41.301 28.829 1.00 109.67 ? 78  LEU   A CA  1 
ATOM   391  C C   . LEU   A 1 60  ? 19.740  -40.647 27.602 1.00 108.93 ? 78  LEU   A C   1 
ATOM   392  O O   . LEU   A 1 60  ? 19.071  -40.403 26.596 1.00 107.23 ? 78  LEU   A O   1 
ATOM   393  C CB  . LEU   A 1 60  ? 19.422  -42.804 28.829 1.00 107.51 ? 78  LEU   A CB  1 
ATOM   394  C CG  . LEU   A 1 60  ? 18.866  -43.600 30.012 1.00 89.22  ? 78  LEU   A CG  1 
ATOM   395  C CD1 . LEU   A 1 60  ? 19.208  -45.074 29.871 1.00 112.12 ? 78  LEU   A CD1 1 
ATOM   396  C CD2 . LEU   A 1 60  ? 19.394  -43.051 31.328 1.00 98.28  ? 78  LEU   A CD2 1 
ATOM   397  N N   . GLY   A 1 61  ? 21.038  -40.365 27.702 1.00 112.07 ? 79  GLY   A N   1 
ATOM   398  C CA  . GLY   A 1 61  ? 21.786  -39.715 26.653 1.00 119.63 ? 79  GLY   A CA  1 
ATOM   399  C C   . GLY   A 1 61  ? 22.010  -38.234 26.873 1.00 121.43 ? 79  GLY   A C   1 
ATOM   400  O O   . GLY   A 1 61  ? 22.887  -37.651 26.226 1.00 142.87 ? 79  GLY   A O   1 
ATOM   401  N N   . GLY   A 1 62  ? 21.239  -37.612 27.766 1.00 142.44 ? 80  GLY   A N   1 
ATOM   402  C CA  . GLY   A 1 62  ? 21.414  -36.213 28.082 1.00 125.81 ? 80  GLY   A CA  1 
ATOM   403  C C   . GLY   A 1 62  ? 22.450  -35.999 29.168 1.00 125.79 ? 80  GLY   A C   1 
ATOM   404  O O   . GLY   A 1 62  ? 23.041  -36.932 29.708 1.00 95.29  ? 80  GLY   A O   1 
ATOM   405  N N   . LYS   A 1 63  ? 22.666  -34.726 29.491 1.00 101.36 ? 81  LYS   A N   1 
ATOM   406  C CA  . LYS   A 1 63  ? 23.628  -34.366 30.521 1.00 100.86 ? 81  LYS   A CA  1 
ATOM   407  C C   . LYS   A 1 63  ? 23.061  -34.501 31.927 1.00 90.10  ? 81  LYS   A C   1 
ATOM   408  O O   . LYS   A 1 63  ? 23.832  -34.486 32.892 1.00 92.31  ? 81  LYS   A O   1 
ATOM   409  C CB  . LYS   A 1 63  ? 24.119  -32.934 30.291 1.00 109.09 ? 81  LYS   A CB  1 
ATOM   410  C CG  . LYS   A 1 63  ? 24.474  -32.630 28.837 1.00 118.46 ? 81  LYS   A CG  1 
ATOM   411  C CD  . LYS   A 1 63  ? 25.485  -33.626 28.275 1.00 139.11 ? 81  LYS   A CD  1 
ATOM   412  C CE  . LYS   A 1 63  ? 25.676  -33.447 26.776 1.00 144.50 ? 81  LYS   A CE  1 
ATOM   413  N NZ  . LYS   A 1 63  ? 26.217  -32.107 26.421 1.00 148.12 ? 81  LYS   A NZ  1 
ATOM   414  N N   . ASN   A 1 64  ? 21.745  -34.645 32.063 1.00 91.56  ? 82  ASN   A N   1 
ATOM   415  C CA  . ASN   A 1 64  ? 21.102  -34.824 33.364 1.00 88.34  ? 82  ASN   A CA  1 
ATOM   416  C C   . ASN   A 1 64  ? 21.471  -33.692 34.321 1.00 83.40  ? 82  ASN   A C   1 
ATOM   417  O O   . ASN   A 1 64  ? 21.801  -33.914 35.487 1.00 80.51  ? 82  ASN   A O   1 
ATOM   418  C CB  . ASN   A 1 64  ? 21.461  -36.184 33.964 1.00 84.74  ? 82  ASN   A CB  1 
ATOM   419  C CG  . ASN   A 1 64  ? 21.269  -37.321 32.983 1.00 104.52 ? 82  ASN   A CG  1 
ATOM   420  O OD1 . ASN   A 1 64  ? 20.158  -37.822 32.806 1.00 88.00  ? 82  ASN   A OD1 1 
ATOM   421  N ND2 . ASN   A 1 64  ? 22.353  -37.735 32.337 1.00 116.22 ? 82  ASN   A ND2 1 
ATOM   422  N N   . ASN   A 1 65  ? 21.416  -32.460 33.813 1.00 82.83  ? 83  ASN   A N   1 
ATOM   423  C CA  . ASN   A 1 65  ? 21.817  -31.312 34.619 1.00 75.66  ? 83  ASN   A CA  1 
ATOM   424  C C   . ASN   A 1 65  ? 20.898  -31.121 35.821 1.00 78.58  ? 83  ASN   A C   1 
ATOM   425  O O   . ASN   A 1 65  ? 21.369  -30.858 36.934 1.00 75.52  ? 83  ASN   A O   1 
ATOM   426  C CB  . ASN   A 1 65  ? 21.837  -30.051 33.756 1.00 84.18  ? 83  ASN   A CB  1 
ATOM   427  C CG  . ASN   A 1 65  ? 22.940  -30.071 32.713 1.00 84.81  ? 83  ASN   A CG  1 
ATOM   428  O OD1 . ASN   A 1 65  ? 24.031  -30.585 32.957 1.00 74.87  ? 83  ASN   A OD1 1 
ATOM   429  N ND2 . ASN   A 1 65  ? 22.661  -29.504 31.544 1.00 87.39  ? 83  ASN   A ND2 1 
ATOM   430  N N   . ARG   A 1 66  ? 19.584  -31.247 35.621 1.00 77.84  ? 84  ARG   A N   1 
ATOM   431  C CA  . ARG   A 1 66  ? 18.640  -30.955 36.698 1.00 74.12  ? 84  ARG   A CA  1 
ATOM   432  C C   . ARG   A 1 66  ? 18.847  -31.886 37.889 1.00 80.04  ? 84  ARG   A C   1 
ATOM   433  O O   . ARG   A 1 66  ? 18.939  -31.438 39.040 1.00 83.53  ? 84  ARG   A O   1 
ATOM   434  C CB  . ARG   A 1 66  ? 17.203  -31.064 36.185 1.00 76.74  ? 84  ARG   A CB  1 
ATOM   435  C CG  . ARG   A 1 66  ? 16.758  -29.945 35.251 1.00 69.23  ? 84  ARG   A CG  1 
ATOM   436  C CD  . ARG   A 1 66  ? 17.224  -30.163 33.822 1.00 75.01  ? 84  ARG   A CD  1 
ATOM   437  N NE  . ARG   A 1 66  ? 16.607  -29.211 32.905 1.00 65.71  ? 84  ARG   A NE  1 
ATOM   438  C CZ  . ARG   A 1 66  ? 16.983  -29.026 31.647 1.00 82.18  ? 84  ARG   A CZ  1 
ATOM   439  N NH1 . ARG   A 1 66  ? 17.986  -29.708 31.118 1.00 95.34  ? 84  ARG   A NH1 1 
ATOM   440  N NH2 . ARG   A 1 66  ? 16.340  -28.131 30.903 1.00 96.62  ? 84  ARG   A NH2 1 
ATOM   441  N N   . GLY   A 1 67  ? 18.904  -33.194 37.632 1.00 71.32  ? 85  GLY   A N   1 
ATOM   442  C CA  . GLY   A 1 67  ? 19.061  -34.141 38.724 1.00 67.63  ? 85  GLY   A CA  1 
ATOM   443  C C   . GLY   A 1 67  ? 20.371  -33.955 39.461 1.00 67.33  ? 85  GLY   A C   1 
ATOM   444  O O   . GLY   A 1 67  ? 20.428  -34.046 40.693 1.00 73.61  ? 85  GLY   A O   1 
ATOM   445  N N   . ILE   A 1 68  ? 21.446  -33.699 38.716 1.00 68.30  ? 86  ILE   A N   1 
ATOM   446  C CA  . ILE   A 1 68  ? 22.738  -33.449 39.342 1.00 75.94  ? 86  ILE   A CA  1 
ATOM   447  C C   . ILE   A 1 68  ? 22.666  -32.205 40.215 1.00 79.72  ? 86  ILE   A C   1 
ATOM   448  O O   . ILE   A 1 68  ? 23.248  -32.158 41.306 1.00 79.06  ? 86  ILE   A O   1 
ATOM   449  C CB  . ILE   A 1 68  ? 23.830  -33.334 38.264 1.00 79.02  ? 86  ILE   A CB  1 
ATOM   450  C CG1 . ILE   A 1 68  ? 24.006  -34.682 37.554 1.00 78.13  ? 86  ILE   A CG1 1 
ATOM   451  C CG2 . ILE   A 1 68  ? 25.136  -32.863 38.884 1.00 92.43  ? 86  ILE   A CG2 1 
ATOM   452  C CD1 . ILE   A 1 68  ? 24.881  -34.624 36.322 1.00 89.51  ? 86  ILE   A CD1 1 
ATOM   453  N N   . LEU   A 1 69  ? 21.964  -31.172 39.747 1.00 78.83  ? 87  LEU   A N   1 
ATOM   454  C CA  . LEU   A 1 69  ? 21.775  -29.979 40.564 1.00 74.69  ? 87  LEU   A CA  1 
ATOM   455  C C   . LEU   A 1 69  ? 21.068  -30.329 41.866 1.00 76.89  ? 87  LEU   A C   1 
ATOM   456  O O   . LEU   A 1 69  ? 21.474  -29.888 42.949 1.00 82.74  ? 87  LEU   A O   1 
ATOM   457  C CB  . LEU   A 1 69  ? 20.979  -28.936 39.781 1.00 71.65  ? 87  LEU   A CB  1 
ATOM   458  C CG  . LEU   A 1 69  ? 20.742  -27.589 40.467 1.00 90.40  ? 87  LEU   A CG  1 
ATOM   459  C CD1 . LEU   A 1 69  ? 22.064  -26.918 40.799 1.00 76.19  ? 87  LEU   A CD1 1 
ATOM   460  C CD2 . LEU   A 1 69  ? 19.893  -26.689 39.584 1.00 79.59  ? 87  LEU   A CD2 1 
ATOM   461  N N   . VAL   A 1 70  ? 20.008  -31.135 41.775 1.00 81.47  ? 88  VAL   A N   1 
ATOM   462  C CA  . VAL   A 1 70  ? 19.295  -31.559 42.978 1.00 75.70  ? 88  VAL   A CA  1 
ATOM   463  C C   . VAL   A 1 70  ? 20.260  -32.224 43.947 1.00 78.58  ? 88  VAL   A C   1 
ATOM   464  O O   . VAL   A 1 70  ? 20.303  -31.901 45.143 1.00 88.12  ? 88  VAL   A O   1 
ATOM   465  C CB  . VAL   A 1 70  ? 18.142  -32.514 42.620 1.00 69.21  ? 88  VAL   A CB  1 
ATOM   466  C CG1 . VAL   A 1 70  ? 17.457  -33.011 43.885 1.00 64.69  ? 88  VAL   A CG1 1 
ATOM   467  C CG2 . VAL   A 1 70  ? 17.142  -31.848 41.714 1.00 74.57  ? 88  VAL   A CG2 1 
ATOM   468  N N   . ILE   A 1 71  ? 21.048  -33.170 43.437 1.00 77.24  ? 89  ILE   A N   1 
ATOM   469  C CA  . ILE   A 1 71  ? 21.913  -33.964 44.304 1.00 85.50  ? 89  ILE   A CA  1 
ATOM   470  C C   . ILE   A 1 71  ? 22.956  -33.076 44.966 1.00 82.45  ? 89  ILE   A C   1 
ATOM   471  O O   . ILE   A 1 71  ? 23.190  -33.157 46.179 1.00 87.57  ? 89  ILE   A O   1 
ATOM   472  C CB  . ILE   A 1 71  ? 22.568  -35.104 43.506 1.00 84.75  ? 89  ILE   A CB  1 
ATOM   473  C CG1 . ILE   A 1 71  ? 21.497  -36.044 42.950 1.00 76.22  ? 89  ILE   A CG1 1 
ATOM   474  C CG2 . ILE   A 1 71  ? 23.543  -35.870 44.386 1.00 103.62 ? 89  ILE   A CG2 1 
ATOM   475  C CD1 . ILE   A 1 71  ? 22.006  -36.979 41.886 1.00 103.81 ? 89  ILE   A CD1 1 
ATOM   476  N N   . LEU   A 1 72  ? 23.604  -32.217 44.176 1.00 78.82  ? 90  LEU   A N   1 
ATOM   477  C CA  . LEU   A 1 72  ? 24.638  -31.347 44.722 1.00 86.93  ? 90  LEU   A CA  1 
ATOM   478  C C   . LEU   A 1 72  ? 24.068  -30.425 45.788 1.00 81.56  ? 90  LEU   A C   1 
ATOM   479  O O   . LEU   A 1 72  ? 24.672  -30.241 46.853 1.00 87.57  ? 90  LEU   A O   1 
ATOM   480  C CB  . LEU   A 1 72  ? 25.281  -30.529 43.602 1.00 89.38  ? 90  LEU   A CB  1 
ATOM   481  C CG  . LEU   A 1 72  ? 26.034  -31.322 42.536 1.00 80.80  ? 90  LEU   A CG  1 
ATOM   482  C CD1 . LEU   A 1 72  ? 26.456  -30.406 41.398 1.00 72.02  ? 90  LEU   A CD1 1 
ATOM   483  C CD2 . LEU   A 1 72  ? 27.237  -32.017 43.146 1.00 78.40  ? 90  LEU   A CD2 1 
ATOM   484  N N   . ILE   A 1 73  ? 22.906  -29.829 45.519 1.00 65.88  ? 91  ILE   A N   1 
ATOM   485  C CA  . ILE   A 1 73  ? 22.331  -28.895 46.479 1.00 73.70  ? 91  ILE   A CA  1 
ATOM   486  C C   . ILE   A 1 73  ? 21.974  -29.617 47.769 1.00 88.25  ? 91  ILE   A C   1 
ATOM   487  O O   . ILE   A 1 73  ? 22.247  -29.119 48.869 1.00 104.57 ? 91  ILE   A O   1 
ATOM   488  C CB  . ILE   A 1 73  ? 21.120  -28.177 45.860 1.00 76.86  ? 91  ILE   A CB  1 
ATOM   489  C CG1 . ILE   A 1 73  ? 21.606  -27.258 44.740 1.00 82.63  ? 91  ILE   A CG1 1 
ATOM   490  C CG2 . ILE   A 1 73  ? 20.361  -27.396 46.924 1.00 84.76  ? 91  ILE   A CG2 1 
ATOM   491  C CD1 . ILE   A 1 73  ? 20.518  -26.683 43.902 1.00 81.94  ? 91  ILE   A CD1 1 
ATOM   492  N N   . TYR   A 1 74  ? 21.377  -30.807 47.663 1.00 91.75  ? 92  TYR   A N   1 
ATOM   493  C CA  . TYR   A 1 74  ? 21.063  -31.557 48.874 1.00 94.29  ? 92  TYR   A CA  1 
ATOM   494  C C   . TYR   A 1 74  ? 22.325  -31.891 49.656 1.00 93.02  ? 92  TYR   A C   1 
ATOM   495  O O   . TYR   A 1 74  ? 22.356  -31.762 50.886 1.00 87.13  ? 92  TYR   A O   1 
ATOM   496  C CB  . TYR   A 1 74  ? 20.312  -32.842 48.539 1.00 105.62 ? 92  TYR   A CB  1 
ATOM   497  C CG  . TYR   A 1 74  ? 20.057  -33.689 49.767 1.00 98.72  ? 92  TYR   A CG  1 
ATOM   498  C CD1 . TYR   A 1 74  ? 19.020  -33.384 50.638 1.00 86.91  ? 92  TYR   A CD1 1 
ATOM   499  C CD2 . TYR   A 1 74  ? 20.864  -34.777 50.068 1.00 100.58 ? 92  TYR   A CD2 1 
ATOM   500  C CE1 . TYR   A 1 74  ? 18.786  -34.147 51.766 1.00 102.21 ? 92  TYR   A CE1 1 
ATOM   501  C CE2 . TYR   A 1 74  ? 20.635  -35.548 51.196 1.00 108.81 ? 92  TYR   A CE2 1 
ATOM   502  C CZ  . TYR   A 1 74  ? 19.594  -35.227 52.040 1.00 103.96 ? 92  TYR   A CZ  1 
ATOM   503  O OH  . TYR   A 1 74  ? 19.357  -35.984 53.165 1.00 90.04  ? 92  TYR   A OH  1 
ATOM   504  N N   . GLU   A 1 75  ? 23.375  -32.333 48.965 1.00 95.14  ? 93  GLU   A N   1 
ATOM   505  C CA  . GLU   A 1 75  ? 24.598  -32.705 49.665 1.00 102.66 ? 93  GLU   A CA  1 
ATOM   506  C C   . GLU   A 1 75  ? 25.202  -31.506 50.381 1.00 95.47  ? 93  GLU   A C   1 
ATOM   507  O O   . GLU   A 1 75  ? 25.655  -31.618 51.526 1.00 93.66  ? 93  GLU   A O   1 
ATOM   508  C CB  . GLU   A 1 75  ? 25.606  -33.306 48.687 1.00 101.29 ? 93  GLU   A CB  1 
ATOM   509  C CG  . GLU   A 1 75  ? 26.891  -33.780 49.350 1.00 126.78 ? 93  GLU   A CG  1 
ATOM   510  C CD  . GLU   A 1 75  ? 27.775  -34.579 48.413 1.00 155.79 ? 93  GLU   A CD  1 
ATOM   511  O OE1 . GLU   A 1 75  ? 27.359  -34.819 47.260 1.00 142.30 ? 93  GLU   A OE1 1 
ATOM   512  O OE2 . GLU   A 1 75  ? 28.886  -34.970 48.832 1.00 163.00 ? 93  GLU   A OE2 1 
ATOM   513  N N   . TYR   A 1 76  ? 25.213  -30.346 49.725 1.00 90.72  ? 94  TYR   A N   1 
ATOM   514  C CA  . TYR   A 1 76  ? 25.878  -29.188 50.310 1.00 110.10 ? 94  TYR   A CA  1 
ATOM   515  C C   . TYR   A 1 76  ? 25.059  -28.538 51.419 1.00 101.24 ? 94  TYR   A C   1 
ATOM   516  O O   . TYR   A 1 76  ? 25.640  -27.977 52.355 1.00 96.54  ? 94  TYR   A O   1 
ATOM   517  C CB  . TYR   A 1 76  ? 26.212  -28.177 49.216 1.00 97.60  ? 94  TYR   A CB  1 
ATOM   518  C CG  . TYR   A 1 76  ? 27.516  -28.501 48.533 1.00 95.90  ? 94  TYR   A CG  1 
ATOM   519  C CD1 . TYR   A 1 76  ? 28.723  -28.076 49.069 1.00 99.86  ? 94  TYR   A CD1 1 
ATOM   520  C CD2 . TYR   A 1 76  ? 27.545  -29.255 47.370 1.00 96.90  ? 94  TYR   A CD2 1 
ATOM   521  C CE1 . TYR   A 1 76  ? 29.922  -28.378 48.457 1.00 120.18 ? 94  TYR   A CE1 1 
ATOM   522  C CE2 . TYR   A 1 76  ? 28.739  -29.563 46.749 1.00 122.29 ? 94  TYR   A CE2 1 
ATOM   523  C CZ  . TYR   A 1 76  ? 29.924  -29.123 47.298 1.00 140.29 ? 94  TYR   A CZ  1 
ATOM   524  O OH  . TYR   A 1 76  ? 31.115  -29.428 46.683 1.00 140.98 ? 94  TYR   A OH  1 
ATOM   525  N N   . VAL   A 1 77  ? 23.727  -28.596 51.348 1.00 98.68  ? 95  VAL   A N   1 
ATOM   526  C CA  . VAL   A 1 77  ? 22.919  -28.101 52.458 1.00 90.32  ? 95  VAL   A CA  1 
ATOM   527  C C   . VAL   A 1 77  ? 22.991  -29.011 53.675 1.00 107.45 ? 95  VAL   A C   1 
ATOM   528  O O   . VAL   A 1 77  ? 22.598  -28.597 54.772 1.00 109.89 ? 95  VAL   A O   1 
ATOM   529  C CB  . VAL   A 1 77  ? 21.443  -27.916 52.047 1.00 93.97  ? 95  VAL   A CB  1 
ATOM   530  C CG1 . VAL   A 1 77  ? 21.325  -26.889 50.931 1.00 85.24  ? 95  VAL   A CG1 1 
ATOM   531  C CG2 . VAL   A 1 77  ? 20.831  -29.238 51.633 1.00 108.98 ? 95  VAL   A CG2 1 
ATOM   532  N N   . LYS   A 1 78  ? 23.482  -30.235 53.512 1.00 111.35 ? 96  LYS   A N   1 
ATOM   533  C CA  . LYS   A 1 78  ? 23.625  -31.162 54.629 1.00 91.37  ? 96  LYS   A CA  1 
ATOM   534  C C   . LYS   A 1 78  ? 25.032  -31.097 55.210 1.00 90.40  ? 96  LYS   A C   1 
ATOM   535  O O   . LYS   A 1 78  ? 25.212  -30.747 56.375 1.00 127.12 ? 96  LYS   A O   1 
ATOM   536  C CB  . LYS   A 1 78  ? 23.305  -32.591 54.184 1.00 101.17 ? 96  LYS   A CB  1 
ATOM   537  C CG  . LYS   A 1 78  ? 21.821  -32.933 54.180 1.00 96.00  ? 96  LYS   A CG  1 
ATOM   538  C CD  . LYS   A 1 78  ? 21.266  -33.006 55.597 1.00 108.88 ? 96  LYS   A CD  1 
ATOM   539  C CE  . LYS   A 1 78  ? 19.813  -33.452 55.615 1.00 130.03 ? 96  LYS   A CE  1 
ATOM   540  N NZ  . LYS   A 1 78  ? 19.255  -33.459 56.996 1.00 157.34 ? 96  LYS   A NZ  1 
ATOM   541  N N   . ASP   A 1 81  ? 28.026  -35.942 55.178 1.00 121.56 ? 99  ASP   A N   1 
ATOM   542  C CA  . ASP   A 1 81  ? 27.634  -37.099 55.974 1.00 139.17 ? 99  ASP   A CA  1 
ATOM   543  C C   . ASP   A 1 81  ? 26.147  -37.392 55.793 1.00 129.94 ? 99  ASP   A C   1 
ATOM   544  O O   . ASP   A 1 81  ? 25.302  -36.803 56.468 1.00 124.17 ? 99  ASP   A O   1 
ATOM   545  C CB  . ASP   A 1 81  ? 27.953  -36.862 57.451 1.00 146.40 ? 99  ASP   A CB  1 
ATOM   546  C CG  . ASP   A 1 81  ? 29.424  -36.577 57.689 1.00 143.71 ? 99  ASP   A CG  1 
ATOM   547  O OD1 . ASP   A 1 81  ? 30.268  -37.169 56.984 1.00 154.72 ? 99  ASP   A OD1 1 
ATOM   548  O OD2 . ASP   A 1 81  ? 29.737  -35.757 58.578 1.00 131.82 ? 99  ASP   A OD2 1 
ATOM   549  N N   . ILE   A 1 82  ? 25.837  -38.303 54.873 1.00 161.69 ? 100 ILE   A N   1 
ATOM   550  C CA  . ILE   A 1 82  ? 24.462  -38.620 54.502 1.00 131.87 ? 100 ILE   A CA  1 
ATOM   551  C C   . ILE   A 1 82  ? 24.319  -40.133 54.416 1.00 112.59 ? 100 ILE   A C   1 
ATOM   552  O O   . ILE   A 1 82  ? 25.201  -40.821 53.893 1.00 142.12 ? 100 ILE   A O   1 
ATOM   553  C CB  . ILE   A 1 82  ? 24.076  -37.946 53.168 1.00 148.41 ? 100 ILE   A CB  1 
ATOM   554  C CG1 . ILE   A 1 82  ? 24.202  -36.424 53.294 1.00 159.36 ? 100 ILE   A CG1 1 
ATOM   555  C CG2 . ILE   A 1 82  ? 22.661  -38.333 52.761 1.00 135.34 ? 100 ILE   A CG2 1 
ATOM   556  C CD1 . ILE   A 1 82  ? 24.123  -35.682 51.979 1.00 120.55 ? 100 ILE   A CD1 1 
ATOM   557  N N   . ASN   A 1 83  ? 23.203  -40.653 54.928 1.00 113.56 ? 101 ASN   A N   1 
ATOM   558  C CA  . ASN   A 1 83  ? 22.985  -42.090 54.983 1.00 109.95 ? 101 ASN   A CA  1 
ATOM   559  C C   . ASN   A 1 83  ? 22.363  -42.594 53.678 1.00 103.69 ? 101 ASN   A C   1 
ATOM   560  O O   . ASN   A 1 83  ? 22.161  -41.845 52.720 1.00 131.01 ? 101 ASN   A O   1 
ATOM   561  C CB  . ASN   A 1 83  ? 22.118  -42.451 56.192 1.00 105.91 ? 101 ASN   A CB  1 
ATOM   562  C CG  . ASN   A 1 83  ? 20.696  -41.928 56.081 1.00 131.58 ? 101 ASN   A CG  1 
ATOM   563  O OD1 . ASN   A 1 83  ? 20.276  -41.433 55.036 1.00 136.87 ? 101 ASN   A OD1 1 
ATOM   564  N ND2 . ASN   A 1 83  ? 19.943  -42.048 57.169 1.00 102.78 ? 101 ASN   A ND2 1 
ATOM   565  N N   . CYS   A 1 84  ? 22.047  -43.892 53.649 1.00 113.62 ? 102 CYS   A N   1 
ATOM   566  C CA  . CYS   A 1 84  ? 21.622  -44.540 52.411 1.00 112.48 ? 102 CYS   A CA  1 
ATOM   567  C C   . CYS   A 1 84  ? 20.194  -44.174 52.024 1.00 95.51  ? 102 CYS   A C   1 
ATOM   568  O O   . CYS   A 1 84  ? 19.906  -43.976 50.840 1.00 104.70 ? 102 CYS   A O   1 
ATOM   569  C CB  . CYS   A 1 84  ? 21.755  -46.055 52.545 1.00 110.49 ? 102 CYS   A CB  1 
ATOM   570  S SG  . CYS   A 1 84  ? 23.451  -46.616 52.779 1.00 134.16 ? 102 CYS   A SG  1 
ATOM   571  N N   . ASN   A 1 85  ? 19.282  -44.101 52.995 1.00 97.23  ? 103 ASN   A N   1 
ATOM   572  C CA  . ASN   A 1 85  ? 17.899  -43.761 52.672 1.00 98.17  ? 103 ASN   A CA  1 
ATOM   573  C C   . ASN   A 1 85  ? 17.802  -42.360 52.083 1.00 105.87 ? 103 ASN   A C   1 
ATOM   574  O O   . ASN   A 1 85  ? 17.051  -42.125 51.127 1.00 100.69 ? 103 ASN   A O   1 
ATOM   575  C CB  . ASN   A 1 85  ? 17.029  -43.882 53.921 1.00 99.17  ? 103 ASN   A CB  1 
ATOM   576  C CG  . ASN   A 1 85  ? 16.993  -45.295 54.468 1.00 105.41 ? 103 ASN   A CG  1 
ATOM   577  O OD1 . ASN   A 1 85  ? 17.084  -46.266 53.716 1.00 105.89 ? 103 ASN   A OD1 1 
ATOM   578  N ND2 . ASN   A 1 85  ? 16.865  -45.419 55.783 1.00 113.85 ? 103 ASN   A ND2 1 
ATOM   579  N N   . GLU   A 1 86  ? 18.555  -41.413 52.645 1.00 107.92 ? 104 GLU   A N   1 
ATOM   580  C CA  . GLU   A 1 86  ? 18.572  -40.061 52.101 1.00 99.24  ? 104 GLU   A CA  1 
ATOM   581  C C   . GLU   A 1 86  ? 19.098  -40.049 50.671 1.00 96.13  ? 104 GLU   A C   1 
ATOM   582  O O   . GLU   A 1 86  ? 18.539  -39.367 49.803 1.00 92.98  ? 104 GLU   A O   1 
ATOM   583  C CB  . GLU   A 1 86  ? 19.417  -39.158 52.998 1.00 105.44 ? 104 GLU   A CB  1 
ATOM   584  C CG  . GLU   A 1 86  ? 18.776  -38.865 54.346 1.00 114.08 ? 104 GLU   A CG  1 
ATOM   585  C CD  . GLU   A 1 86  ? 19.712  -38.141 55.295 1.00 126.69 ? 104 GLU   A CD  1 
ATOM   586  O OE1 . GLU   A 1 86  ? 20.841  -38.630 55.509 1.00 116.36 ? 104 GLU   A OE1 1 
ATOM   587  O OE2 . GLU   A 1 86  ? 19.319  -37.080 55.824 1.00 160.27 ? 104 GLU   A OE2 1 
ATOM   588  N N   . TRP   A 1 87  ? 20.174  -40.795 50.406 1.00 97.10  ? 105 TRP   A N   1 
ATOM   589  C CA  . TRP   A 1 87  ? 20.699  -40.866 49.046 1.00 98.71  ? 105 TRP   A CA  1 
ATOM   590  C C   . TRP   A 1 87  ? 19.672  -41.464 48.094 1.00 91.61  ? 105 TRP   A C   1 
ATOM   591  O O   . TRP   A 1 87  ? 19.507  -40.990 46.965 1.00 87.50  ? 105 TRP   A O   1 
ATOM   592  C CB  . TRP   A 1 87  ? 21.989  -41.686 49.014 1.00 95.66  ? 105 TRP   A CB  1 
ATOM   593  C CG  . TRP   A 1 87  ? 23.197  -40.943 49.500 1.00 123.02 ? 105 TRP   A CG  1 
ATOM   594  C CD1 . TRP   A 1 87  ? 24.063  -41.334 50.480 1.00 131.00 ? 105 TRP   A CD1 1 
ATOM   595  C CD2 . TRP   A 1 87  ? 23.673  -39.675 49.027 1.00 128.94 ? 105 TRP   A CD2 1 
ATOM   596  N NE1 . TRP   A 1 87  ? 25.049  -40.391 50.645 1.00 125.73 ? 105 TRP   A NE1 1 
ATOM   597  C CE2 . TRP   A 1 87  ? 24.831  -39.362 49.766 1.00 133.47 ? 105 TRP   A CE2 1 
ATOM   598  C CE3 . TRP   A 1 87  ? 23.231  -38.776 48.052 1.00 122.18 ? 105 TRP   A CE3 1 
ATOM   599  C CZ2 . TRP   A 1 87  ? 25.554  -38.188 49.559 1.00 152.80 ? 105 TRP   A CZ2 1 
ATOM   600  C CZ3 . TRP   A 1 87  ? 23.948  -37.611 47.849 1.00 145.18 ? 105 TRP   A CZ3 1 
ATOM   601  C CH2 . TRP   A 1 87  ? 25.097  -37.328 48.599 1.00 150.36 ? 105 TRP   A CH2 1 
ATOM   602  N N   . GLU   A 1 88  ? 18.980  -42.516 48.530 1.00 88.87  ? 106 GLU   A N   1 
ATOM   603  C CA  . GLU   A 1 88  ? 17.958  -43.130 47.691 1.00 85.43  ? 106 GLU   A CA  1 
ATOM   604  C C   . GLU   A 1 88  ? 16.857  -42.131 47.360 1.00 84.60  ? 106 GLU   A C   1 
ATOM   605  O O   . GLU   A 1 88  ? 16.458  -41.989 46.198 1.00 87.05  ? 106 GLU   A O   1 
ATOM   606  C CB  . GLU   A 1 88  ? 17.387  -44.356 48.401 1.00 89.76  ? 106 GLU   A CB  1 
ATOM   607  C CG  . GLU   A 1 88  ? 16.409  -45.166 47.577 1.00 84.64  ? 106 GLU   A CG  1 
ATOM   608  C CD  . GLU   A 1 88  ? 15.851  -46.345 48.349 1.00 93.70  ? 106 GLU   A CD  1 
ATOM   609  O OE1 . GLU   A 1 88  ? 15.714  -46.237 49.587 1.00 97.96  ? 106 GLU   A OE1 1 
ATOM   610  O OE2 . GLU   A 1 88  ? 15.560  -47.385 47.721 1.00 93.29  ? 106 GLU   A OE2 1 
ATOM   611  N N   . LYS   A 1 89  ? 16.364  -41.412 48.372 1.00 89.44  ? 107 LYS   A N   1 
ATOM   612  C CA  . LYS   A 1 89  ? 15.314  -40.427 48.132 1.00 85.04  ? 107 LYS   A CA  1 
ATOM   613  C C   . LYS   A 1 89  ? 15.792  -39.334 47.183 1.00 83.56  ? 107 LYS   A C   1 
ATOM   614  O O   . LYS   A 1 89  ? 15.067  -38.933 46.264 1.00 80.87  ? 107 LYS   A O   1 
ATOM   615  C CB  . LYS   A 1 89  ? 14.857  -39.813 49.457 1.00 85.22  ? 107 LYS   A CB  1 
ATOM   616  C CG  . LYS   A 1 89  ? 14.213  -40.788 50.435 1.00 77.76  ? 107 LYS   A CG  1 
ATOM   617  C CD  . LYS   A 1 89  ? 14.068  -40.151 51.814 1.00 88.30  ? 107 LYS   A CD  1 
ATOM   618  C CE  . LYS   A 1 89  ? 13.484  -41.113 52.840 1.00 68.75  ? 107 LYS   A CE  1 
ATOM   619  N NZ  . LYS   A 1 89  ? 12.083  -41.495 52.520 1.00 93.67  ? 107 LYS   A NZ  1 
ATOM   620  N N   . VAL   A 1 90  ? 17.014  -38.841 47.390 1.00 88.50  ? 108 VAL   A N   1 
ATOM   621  C CA  . VAL   A 1 90  ? 17.517  -37.738 46.579 1.00 80.27  ? 108 VAL   A CA  1 
ATOM   622  C C   . VAL   A 1 90  ? 17.710  -38.177 45.135 1.00 76.53  ? 108 VAL   A C   1 
ATOM   623  O O   . VAL   A 1 90  ? 17.375  -37.442 44.199 1.00 63.55  ? 108 VAL   A O   1 
ATOM   624  C CB  . VAL   A 1 90  ? 18.821  -37.190 47.185 1.00 78.92  ? 108 VAL   A CB  1 
ATOM   625  C CG1 . VAL   A 1 90  ? 19.437  -36.145 46.269 1.00 101.24 ? 108 VAL   A CG1 1 
ATOM   626  C CG2 . VAL   A 1 90  ? 18.558  -36.609 48.564 1.00 85.28  ? 108 VAL   A CG2 1 
ATOM   627  N N   . ALA   A 1 91  ? 18.271  -39.370 44.926 1.00 85.01  ? 109 ALA   A N   1 
ATOM   628  C CA  . ALA   A 1 91  ? 18.437  -39.873 43.568 1.00 67.87  ? 109 ALA   A CA  1 
ATOM   629  C C   . ALA   A 1 91  ? 17.086  -40.111 42.911 1.00 65.22  ? 109 ALA   A C   1 
ATOM   630  O O   . ALA   A 1 91  ? 16.924  -39.882 41.706 1.00 59.86  ? 109 ALA   A O   1 
ATOM   631  C CB  . ALA   A 1 91  ? 19.273  -41.152 43.581 1.00 67.10  ? 109 ALA   A CB  1 
ATOM   632  N N   . CYS   A 1 92  ? 16.097  -40.560 43.689 1.00 72.66  ? 110 CYS   A N   1 
ATOM   633  C CA  . CYS   A 1 92  ? 14.751  -40.694 43.147 1.00 78.28  ? 110 CYS   A CA  1 
ATOM   634  C C   . CYS   A 1 92  ? 14.217  -39.349 42.680 1.00 92.60  ? 110 CYS   A C   1 
ATOM   635  O O   . CYS   A 1 92  ? 13.629  -39.249 41.600 1.00 113.54 ? 110 CYS   A O   1 
ATOM   636  C CB  . CYS   A 1 92  ? 13.816  -41.298 44.193 1.00 74.74  ? 110 CYS   A CB  1 
ATOM   637  S SG  . CYS   A 1 92  ? 12.067  -41.140 43.754 1.00 60.83  ? 110 CYS   A SG  1 
ATOM   638  N N   . ILE   A 1 93  ? 14.409  -38.302 43.482 1.00 81.27  ? 111 ILE   A N   1 
ATOM   639  C CA  . ILE   A 1 93  ? 13.944  -36.974 43.087 1.00 67.06  ? 111 ILE   A CA  1 
ATOM   640  C C   . ILE   A 1 93  ? 14.665  -36.511 41.827 1.00 61.48  ? 111 ILE   A C   1 
ATOM   641  O O   . ILE   A 1 93  ? 14.054  -35.945 40.911 1.00 68.78  ? 111 ILE   A O   1 
ATOM   642  C CB  . ILE   A 1 93  ? 14.136  -35.977 44.244 1.00 69.96  ? 111 ILE   A CB  1 
ATOM   643  C CG1 . ILE   A 1 93  ? 13.234  -36.362 45.418 1.00 67.69  ? 111 ILE   A CG1 1 
ATOM   644  C CG2 . ILE   A 1 93  ? 13.850  -34.551 43.775 1.00 62.82  ? 111 ILE   A CG2 1 
ATOM   645  C CD1 . ILE   A 1 93  ? 13.441  -35.516 46.651 1.00 62.80  ? 111 ILE   A CD1 1 
ATOM   646  N N   . ALA   A 1 94  ? 15.979  -36.727 41.771 1.00 61.84  ? 112 ALA   A N   1 
ATOM   647  C CA  . ALA   A 1 94  ? 16.753  -36.310 40.607 1.00 63.53  ? 112 ALA   A CA  1 
ATOM   648  C C   . ALA   A 1 94  ? 16.256  -37.007 39.347 1.00 69.90  ? 112 ALA   A C   1 
ATOM   649  O O   . ALA   A 1 94  ? 16.064  -36.373 38.302 1.00 69.58  ? 112 ALA   A O   1 
ATOM   650  C CB  . ALA   A 1 94  ? 18.235  -36.603 40.838 1.00 68.67  ? 112 ALA   A CB  1 
ATOM   651  N N   . TRP   A 1 95  ? 16.018  -38.315 39.432 1.00 81.44  ? 113 TRP   A N   1 
ATOM   652  C CA  . TRP   A 1 95  ? 15.542  -39.030 38.256 1.00 77.47  ? 113 TRP   A CA  1 
ATOM   653  C C   . TRP   A 1 95  ? 14.093  -38.688 37.941 1.00 71.64  ? 113 TRP   A C   1 
ATOM   654  O O   . TRP   A 1 95  ? 13.683  -38.759 36.781 1.00 62.93  ? 113 TRP   A O   1 
ATOM   655  C CB  . TRP   A 1 95  ? 15.722  -40.534 38.443 1.00 70.21  ? 113 TRP   A CB  1 
ATOM   656  C CG  . TRP   A 1 95  ? 17.097  -40.978 38.070 1.00 65.50  ? 113 TRP   A CG  1 
ATOM   657  C CD1 . TRP   A 1 95  ? 18.010  -41.599 38.872 1.00 70.80  ? 113 TRP   A CD1 1 
ATOM   658  C CD2 . TRP   A 1 95  ? 17.727  -40.814 36.795 1.00 63.24  ? 113 TRP   A CD2 1 
ATOM   659  N NE1 . TRP   A 1 95  ? 19.168  -41.840 38.170 1.00 69.30  ? 113 TRP   A NE1 1 
ATOM   660  C CE2 . TRP   A 1 95  ? 19.018  -41.367 36.892 1.00 74.04  ? 113 TRP   A CE2 1 
ATOM   661  C CE3 . TRP   A 1 95  ? 17.320  -40.258 35.578 1.00 67.35  ? 113 TRP   A CE3 1 
ATOM   662  C CZ2 . TRP   A 1 95  ? 19.906  -41.378 35.819 1.00 85.96  ? 113 TRP   A CZ2 1 
ATOM   663  C CZ3 . TRP   A 1 95  ? 18.202  -40.270 34.515 1.00 69.87  ? 113 TRP   A CZ3 1 
ATOM   664  C CH2 . TRP   A 1 95  ? 19.480  -40.827 34.642 1.00 82.91  ? 113 TRP   A CH2 1 
ATOM   665  N N   . CYS   A 1 96  ? 13.311  -38.292 38.944 1.00 69.23  ? 114 CYS   A N   1 
ATOM   666  C CA  . CYS   A 1 96  ? 11.960  -37.818 38.672 1.00 72.34  ? 114 CYS   A CA  1 
ATOM   667  C C   . CYS   A 1 96  ? 11.994  -36.519 37.880 1.00 70.63  ? 114 CYS   A C   1 
ATOM   668  O O   . CYS   A 1 96  ? 11.208  -36.329 36.944 1.00 81.69  ? 114 CYS   A O   1 
ATOM   669  C CB  . CYS   A 1 96  ? 11.199  -37.639 39.985 1.00 73.05  ? 114 CYS   A CB  1 
ATOM   670  S SG  . CYS   A 1 96  ? 10.566  -39.179 40.695 1.00 114.01 ? 114 CYS   A SG  1 
ATOM   671  N N   . ILE   A 1 97  ? 12.910  -35.617 38.230 1.00 67.70  ? 115 ILE   A N   1 
ATOM   672  C CA  . ILE   A 1 97  ? 13.058  -34.393 37.448 1.00 76.77  ? 115 ILE   A CA  1 
ATOM   673  C C   . ILE   A 1 97  ? 13.582  -34.718 36.053 1.00 73.46  ? 115 ILE   A C   1 
ATOM   674  O O   . ILE   A 1 97  ? 13.210  -34.069 35.069 1.00 65.78  ? 115 ILE   A O   1 
ATOM   675  C CB  . ILE   A 1 97  ? 13.961  -33.385 38.183 1.00 71.90  ? 115 ILE   A CB  1 
ATOM   676  C CG1 . ILE   A 1 97  ? 13.356  -33.046 39.548 1.00 68.88  ? 115 ILE   A CG1 1 
ATOM   677  C CG2 . ILE   A 1 97  ? 14.130  -32.118 37.350 1.00 67.37  ? 115 ILE   A CG2 1 
ATOM   678  C CD1 . ILE   A 1 97  ? 14.006  -31.873 40.256 1.00 67.84  ? 115 ILE   A CD1 1 
ATOM   679  N N   . GLU   A 1 98  ? 14.454  -35.723 35.941 1.00 72.78  ? 116 GLU   A N   1 
ATOM   680  C CA  . GLU   A 1 98  ? 14.917  -36.143 34.619 1.00 72.28  ? 116 GLU   A CA  1 
ATOM   681  C C   . GLU   A 1 98  ? 13.764  -36.684 33.778 1.00 70.48  ? 116 GLU   A C   1 
ATOM   682  O O   . GLU   A 1 98  ? 13.693  -36.436 32.570 1.00 70.58  ? 116 GLU   A O   1 
ATOM   683  C CB  . GLU   A 1 98  ? 16.020  -37.191 34.755 1.00 63.12  ? 116 GLU   A CB  1 
ATOM   684  C CG  . GLU   A 1 98  ? 17.338  -36.632 35.262 1.00 74.93  ? 116 GLU   A CG  1 
ATOM   685  C CD  . GLU   A 1 98  ? 17.918  -35.585 34.334 1.00 84.37  ? 116 GLU   A CD  1 
ATOM   686  O OE1 . GLU   A 1 98  ? 17.814  -35.757 33.100 1.00 71.30  ? 116 GLU   A OE1 1 
ATOM   687  O OE2 . GLU   A 1 98  ? 18.472  -34.584 34.839 1.00 81.54  ? 116 GLU   A OE2 1 
ATOM   688  N N   . ILE   A 1 99  ? 12.854  -37.433 34.400 1.00 70.10  ? 117 ILE   A N   1 
ATOM   689  C CA  . ILE   A 1 99  ? 11.684  -37.930 33.684 1.00 74.24  ? 117 ILE   A CA  1 
ATOM   690  C C   . ILE   A 1 99  ? 10.774  -36.777 33.287 1.00 76.87  ? 117 ILE   A C   1 
ATOM   691  O O   . ILE   A 1 99  ? 10.152  -36.799 32.220 1.00 86.62  ? 117 ILE   A O   1 
ATOM   692  C CB  . ILE   A 1 99  ? 10.934  -38.967 34.538 1.00 80.32  ? 117 ILE   A CB  1 
ATOM   693  C CG1 . ILE   A 1 99  ? 11.814  -40.194 34.780 1.00 66.66  ? 117 ILE   A CG1 1 
ATOM   694  C CG2 . ILE   A 1 99  ? 9.634   -39.370 33.851 1.00 70.63  ? 117 ILE   A CG2 1 
ATOM   695  C CD1 . ILE   A 1 99  ? 11.289  -41.120 35.857 1.00 78.36  ? 117 ILE   A CD1 1 
ATOM   696  N N   . LEU   A 1 100 ? 10.651  -35.770 34.151 1.00 70.89  ? 118 LEU   A N   1 
ATOM   697  C CA  . LEU   A 1 100 ? 9.889   -34.581 33.781 1.00 76.58  ? 118 LEU   A CA  1 
ATOM   698  C C   . LEU   A 1 100 ? 10.506  -33.910 32.560 1.00 78.16  ? 118 LEU   A C   1 
ATOM   699  O O   . LEU   A 1 100 ? 9.794   -33.502 31.632 1.00 78.52  ? 118 LEU   A O   1 
ATOM   700  C CB  . LEU   A 1 100 ? 9.837   -33.613 34.962 1.00 76.01  ? 118 LEU   A CB  1 
ATOM   701  C CG  . LEU   A 1 100 ? 8.997   -32.350 34.780 1.00 71.78  ? 118 LEU   A CG  1 
ATOM   702  C CD1 . LEU   A 1 100 ? 7.542   -32.695 34.523 1.00 88.85  ? 118 LEU   A CD1 1 
ATOM   703  C CD2 . LEU   A 1 100 ? 9.129   -31.450 35.998 1.00 78.99  ? 118 LEU   A CD2 1 
ATOM   704  N N   . GLN   A 1 101 ? 11.835  -33.797 32.548 1.00 89.25  ? 119 GLN   A N   1 
ATOM   705  C CA  . GLN   A 1 101 ? 12.541  -33.280 31.381 1.00 85.75  ? 119 GLN   A CA  1 
ATOM   706  C C   . GLN   A 1 101 ? 12.226  -34.113 30.148 1.00 88.63  ? 119 GLN   A C   1 
ATOM   707  O O   . GLN   A 1 101 ? 11.979  -33.570 29.070 1.00 89.52  ? 119 GLN   A O   1 
ATOM   708  C CB  . GLN   A 1 101 ? 14.048  -33.268 31.654 1.00 81.84  ? 119 GLN   A CB  1 
ATOM   709  C CG  . GLN   A 1 101 ? 14.949  -33.042 30.434 1.00 91.70  ? 119 GLN   A CG  1 
ATOM   710  C CD  . GLN   A 1 101 ? 15.086  -31.581 30.057 1.00 98.76  ? 119 GLN   A CD  1 
ATOM   711  O OE1 . GLN   A 1 101 ? 14.269  -30.748 30.444 1.00 107.09 ? 119 GLN   A OE1 1 
ATOM   712  N NE2 . GLN   A 1 101 ? 16.133  -31.262 29.303 1.00 113.27 ? 119 GLN   A NE2 1 
ATOM   713  N N   . ALA   A 1 102 ? 12.245  -35.438 30.287 1.00 81.76  ? 120 ALA   A N   1 
ATOM   714  C CA  . ALA   A 1 102 ? 11.978  -36.305 29.144 1.00 80.79  ? 120 ALA   A CA  1 
ATOM   715  C C   . ALA   A 1 102 ? 10.563  -36.108 28.619 1.00 77.27  ? 120 ALA   A C   1 
ATOM   716  O O   . ALA   A 1 102 ? 10.344  -36.059 27.404 1.00 86.39  ? 120 ALA   A O   1 
ATOM   717  C CB  . ALA   A 1 102 ? 12.203  -37.767 29.530 1.00 75.18  ? 120 ALA   A CB  1 
ATOM   718  N N   . SER   A 1 103 ? 9.587   -36.010 29.522 1.00 77.21  ? 121 SER   A N   1 
ATOM   719  C CA  . SER   A 1 103 ? 8.203   -35.822 29.101 1.00 69.49  ? 121 SER   A CA  1 
ATOM   720  C C   . SER   A 1 103 ? 8.031   -34.491 28.380 1.00 80.37  ? 121 SER   A C   1 
ATOM   721  O O   . SER   A 1 103 ? 7.404   -34.422 27.315 1.00 71.89  ? 121 SER   A O   1 
ATOM   722  C CB  . SER   A 1 103 ? 7.273   -35.909 30.311 1.00 68.02  ? 121 SER   A CB  1 
ATOM   723  O OG  . SER   A 1 103 ? 7.599   -34.921 31.272 1.00 72.38  ? 121 SER   A OG  1 
ATOM   724  N N   . PHE   A 1 104 ? 8.599   -33.418 28.940 1.00 82.41  ? 122 PHE   A N   1 
ATOM   725  C CA  . PHE   A 1 104 ? 8.548   -32.126 28.264 1.00 78.42  ? 122 PHE   A CA  1 
ATOM   726  C C   . PHE   A 1 104 ? 9.245   -32.191 26.913 1.00 88.27  ? 122 PHE   A C   1 
ATOM   727  O O   . PHE   A 1 104 ? 8.784   -31.593 25.936 1.00 92.97  ? 122 PHE   A O   1 
ATOM   728  C CB  . PHE   A 1 104 ? 9.193   -31.044 29.130 1.00 79.84  ? 122 PHE   A CB  1 
ATOM   729  C CG  . PHE   A 1 104 ? 8.381   -30.645 30.333 1.00 79.36  ? 122 PHE   A CG  1 
ATOM   730  C CD1 . PHE   A 1 104 ? 6.996   -30.698 30.315 1.00 76.44  ? 122 PHE   A CD1 1 
ATOM   731  C CD2 . PHE   A 1 104 ? 9.012   -30.203 31.484 1.00 82.56  ? 122 PHE   A CD2 1 
ATOM   732  C CE1 . PHE   A 1 104 ? 6.261   -30.325 31.422 1.00 83.54  ? 122 PHE   A CE1 1 
ATOM   733  C CE2 . PHE   A 1 104 ? 8.281   -29.829 32.592 1.00 82.38  ? 122 PHE   A CE2 1 
ATOM   734  C CZ  . PHE   A 1 104 ? 6.905   -29.891 32.562 1.00 83.33  ? 122 PHE   A CZ  1 
ATOM   735  N N   . LEU   A 1 105 ? 10.366  -32.907 26.845 1.00 80.08  ? 123 LEU   A N   1 
ATOM   736  C CA  . LEU   A 1 105 ? 11.128  -33.006 25.608 1.00 84.71  ? 123 LEU   A CA  1 
ATOM   737  C C   . LEU   A 1 105 ? 10.329  -33.714 24.524 1.00 87.99  ? 123 LEU   A C   1 
ATOM   738  O O   . LEU   A 1 105 ? 10.286  -33.261 23.373 1.00 100.55 ? 123 LEU   A O   1 
ATOM   739  C CB  . LEU   A 1 105 ? 12.442  -33.731 25.904 1.00 86.32  ? 123 LEU   A CB  1 
ATOM   740  C CG  . LEU   A 1 105 ? 13.292  -34.309 24.777 1.00 117.88 ? 123 LEU   A CG  1 
ATOM   741  C CD1 . LEU   A 1 105 ? 14.740  -34.353 25.234 1.00 137.11 ? 123 LEU   A CD1 1 
ATOM   742  C CD2 . LEU   A 1 105 ? 12.812  -35.704 24.383 1.00 115.62 ? 123 LEU   A CD2 1 
ATOM   743  N N   . VAL   A 1 106 ? 9.676   -34.822 24.874 1.00 84.21  ? 124 VAL   A N   1 
ATOM   744  C CA  . VAL   A 1 106 ? 8.865   -35.541 23.897 1.00 88.87  ? 124 VAL   A CA  1 
ATOM   745  C C   . VAL   A 1 106 ? 7.662   -34.700 23.485 1.00 93.57  ? 124 VAL   A C   1 
ATOM   746  O O   . VAL   A 1 106 ? 7.279   -34.670 22.306 1.00 98.73  ? 124 VAL   A O   1 
ATOM   747  C CB  . VAL   A 1 106 ? 8.437   -36.910 24.457 1.00 84.84  ? 124 VAL   A CB  1 
ATOM   748  C CG1 . VAL   A 1 106 ? 7.569   -37.646 23.448 1.00 85.29  ? 124 VAL   A CG1 1 
ATOM   749  C CG2 . VAL   A 1 106 ? 9.658   -37.747 24.814 1.00 101.13 ? 124 VAL   A CG2 1 
ATOM   750  N N   . ALA   A 1 107 ? 7.048   -34.000 24.442 1.00 95.01  ? 125 ALA   A N   1 
ATOM   751  C CA  . ALA   A 1 107 ? 5.930   -33.127 24.104 1.00 87.62  ? 125 ALA   A CA  1 
ATOM   752  C C   . ALA   A 1 107 ? 6.363   -32.037 23.133 1.00 97.04  ? 125 ALA   A C   1 
ATOM   753  O O   . ALA   A 1 107 ? 5.644   -31.726 22.177 1.00 86.02  ? 125 ALA   A O   1 
ATOM   754  C CB  . ALA   A 1 107 ? 5.343   -32.516 25.375 1.00 99.90  ? 125 ALA   A CB  1 
ATOM   755  N N   . ASP   A 1 108 ? 7.534   -31.441 23.364 1.00 99.93  ? 126 ASP   A N   1 
ATOM   756  C CA  . ASP   A 1 108 ? 8.025   -30.400 22.468 1.00 105.88 ? 126 ASP   A CA  1 
ATOM   757  C C   . ASP   A 1 108 ? 8.367   -30.972 21.099 1.00 104.57 ? 126 ASP   A C   1 
ATOM   758  O O   . ASP   A 1 108 ? 8.152   -30.314 20.077 1.00 116.74 ? 126 ASP   A O   1 
ATOM   759  C CB  . ASP   A 1 108 ? 9.242   -29.709 23.081 1.00 101.23 ? 126 ASP   A CB  1 
ATOM   760  C CG  . ASP   A 1 108 ? 9.688   -28.495 22.286 1.00 134.11 ? 126 ASP   A CG  1 
ATOM   761  O OD1 . ASP   A 1 108 ? 9.989   -28.643 21.082 1.00 131.85 ? 126 ASP   A OD1 1 
ATOM   762  O OD2 . ASP   A 1 108 ? 9.727   -27.388 22.863 1.00 147.20 ? 126 ASP   A OD2 1 
ATOM   763  N N   . ASP   A 1 109 ? 8.914   -32.187 21.057 1.00 96.38  ? 127 ASP   A N   1 
ATOM   764  C CA  . ASP   A 1 109 ? 9.168   -32.822 19.769 1.00 98.46  ? 127 ASP   A CA  1 
ATOM   765  C C   . ASP   A 1 109 ? 7.870   -33.003 18.994 1.00 98.56  ? 127 ASP   A C   1 
ATOM   766  O O   . ASP   A 1 109 ? 7.824   -32.777 17.779 1.00 102.70 ? 127 ASP   A O   1 
ATOM   767  C CB  . ASP   A 1 109 ? 9.864   -34.168 19.969 1.00 106.04 ? 127 ASP   A CB  1 
ATOM   768  C CG  . ASP   A 1 109 ? 11.294  -34.020 20.448 1.00 126.92 ? 127 ASP   A CG  1 
ATOM   769  O OD1 . ASP   A 1 109 ? 11.925  -32.989 20.132 1.00 123.99 ? 127 ASP   A OD1 1 
ATOM   770  O OD2 . ASP   A 1 109 ? 11.789  -34.938 21.136 1.00 110.95 ? 127 ASP   A OD2 1 
ATOM   771  N N   . ILE   A 1 110 ? 6.803   -33.409 19.684 1.00 99.37  ? 128 ILE   A N   1 
ATOM   772  C CA  . ILE   A 1 110 ? 5.506   -33.552 19.025 1.00 90.14  ? 128 ILE   A CA  1 
ATOM   773  C C   . ILE   A 1 110 ? 5.002   -32.195 18.543 1.00 104.71 ? 128 ILE   A C   1 
ATOM   774  O O   . ILE   A 1 110 ? 4.536   -32.052 17.406 1.00 105.56 ? 128 ILE   A O   1 
ATOM   775  C CB  . ILE   A 1 110 ? 4.493   -34.217 19.974 1.00 92.79  ? 128 ILE   A CB  1 
ATOM   776  C CG1 . ILE   A 1 110 ? 4.942   -35.635 20.335 1.00 104.29 ? 128 ILE   A CG1 1 
ATOM   777  C CG2 . ILE   A 1 110 ? 3.107   -34.241 19.340 1.00 100.47 ? 128 ILE   A CG2 1 
ATOM   778  C CD1 . ILE   A 1 110 ? 4.130   -36.263 21.449 1.00 120.82 ? 128 ILE   A CD1 1 
ATOM   779  N N   . MET   A 1 111 ? 5.090   -31.177 19.402 1.00 112.00 ? 129 MET   A N   1 
ATOM   780  C CA  . MET   A 1 111 ? 4.469   -29.889 19.101 1.00 106.79 ? 129 MET   A CA  1 
ATOM   781  C C   . MET   A 1 111 ? 5.198   -29.164 17.976 1.00 109.80 ? 129 MET   A C   1 
ATOM   782  O O   . MET   A 1 111 ? 4.568   -28.652 17.043 1.00 112.59 ? 129 MET   A O   1 
ATOM   783  C CB  . MET   A 1 111 ? 4.437   -29.019 20.360 1.00 106.36 ? 129 MET   A CB  1 
ATOM   784  C CG  . MET   A 1 111 ? 3.464   -29.497 21.428 1.00 101.61 ? 129 MET   A CG  1 
ATOM   785  S SD  . MET   A 1 111 ? 3.415   -28.420 22.872 1.00 97.02  ? 129 MET   A SD  1 
ATOM   786  C CE  . MET   A 1 111 ? 4.731   -29.126 23.855 1.00 120.42 ? 129 MET   A CE  1 
ATOM   787  N N   . ASP   A 1 112 ? 6.524   -29.113 18.044 1.00 126.41 ? 130 ASP   A N   1 
ATOM   788  C CA  . ASP   A 1 112 ? 7.331   -28.337 17.112 1.00 131.60 ? 130 ASP   A CA  1 
ATOM   789  C C   . ASP   A 1 112 ? 7.654   -29.093 15.831 1.00 127.78 ? 130 ASP   A C   1 
ATOM   790  O O   . ASP   A 1 112 ? 8.358   -28.551 14.973 1.00 136.54 ? 130 ASP   A O   1 
ATOM   791  C CB  . ASP   A 1 112 ? 8.633   -27.900 17.791 1.00 138.02 ? 130 ASP   A CB  1 
ATOM   792  C CG  . ASP   A 1 112 ? 8.397   -26.943 18.946 1.00 138.41 ? 130 ASP   A CG  1 
ATOM   793  O OD1 . ASP   A 1 112 ? 7.228   -26.574 19.185 1.00 143.86 ? 130 ASP   A OD1 1 
ATOM   794  O OD2 . ASP   A 1 112 ? 9.380   -26.559 19.615 1.00 134.96 ? 130 ASP   A OD2 1 
ATOM   795  N N   . LYS   A 1 113 ? 7.161   -30.321 15.680 1.00 129.01 ? 131 LYS   A N   1 
ATOM   796  C CA  . LYS   A 1 113 ? 7.435   -31.127 14.492 1.00 116.83 ? 131 LYS   A CA  1 
ATOM   797  C C   . LYS   A 1 113 ? 8.938   -31.287 14.279 1.00 123.30 ? 131 LYS   A C   1 
ATOM   798  O O   . LYS   A 1 113 ? 9.445   -31.159 13.163 1.00 130.59 ? 131 LYS   A O   1 
ATOM   799  C CB  . LYS   A 1 113 ? 6.769   -30.522 13.254 1.00 113.13 ? 131 LYS   A CB  1 
ATOM   800  C CG  . LYS   A 1 113 ? 5.249   -30.502 13.322 1.00 138.18 ? 131 LYS   A CG  1 
ATOM   801  C CD  . LYS   A 1 113 ? 4.637   -29.954 12.042 1.00 122.57 ? 131 LYS   A CD  1 
ATOM   802  C CE  . LYS   A 1 113 ? 3.116   -30.011 12.086 1.00 129.73 ? 131 LYS   A CE  1 
ATOM   803  N NZ  . LYS   A 1 113 ? 2.497   -29.501 10.830 1.00 141.16 ? 131 LYS   A NZ  1 
ATOM   804  N N   . GLY   A 1 114 ? 9.657   -31.566 15.367 1.00 120.11 ? 132 GLY   A N   1 
ATOM   805  C CA  . GLY   A 1 114 ? 11.086  -31.764 15.287 1.00 123.78 ? 132 GLY   A CA  1 
ATOM   806  C C   . GLY   A 1 114 ? 11.444  -33.111 14.693 1.00 125.82 ? 132 GLY   A C   1 
ATOM   807  O O   . GLY   A 1 114 ? 10.616  -34.013 14.574 1.00 125.13 ? 132 GLY   A O   1 
ATOM   808  N N   . GLU   A 1 115 ? 12.716  -33.243 14.323 1.00 138.40 ? 133 GLU   A N   1 
ATOM   809  C CA  . GLU   A 1 115 ? 13.216  -34.436 13.651 1.00 142.10 ? 133 GLU   A CA  1 
ATOM   810  C C   . GLU   A 1 115 ? 14.170  -35.246 14.514 1.00 134.71 ? 133 GLU   A C   1 
ATOM   811  O O   . GLU   A 1 115 ? 13.968  -36.450 14.695 1.00 125.01 ? 133 GLU   A O   1 
ATOM   812  C CB  . GLU   A 1 115 ? 13.906  -34.040 12.337 1.00 144.61 ? 133 GLU   A CB  1 
ATOM   813  C CG  . GLU   A 1 115 ? 12.974  -33.371 11.338 1.00 139.22 ? 133 GLU   A CG  1 
ATOM   814  C CD  . GLU   A 1 115 ? 13.655  -33.048 10.024 1.00 162.06 ? 133 GLU   A CD  1 
ATOM   815  O OE1 . GLU   A 1 115 ? 14.850  -33.378 9.874  1.00 157.47 ? 133 GLU   A OE1 1 
ATOM   816  O OE2 . GLU   A 1 115 ? 12.994  -32.463 9.140  1.00 174.75 ? 133 GLU   A OE2 1 
ATOM   817  N N   . THR   A 1 116 ? 15.208  -34.616 15.056 1.00 147.67 ? 134 THR   A N   1 
ATOM   818  C CA  . THR   A 1 116 ? 16.203  -35.297 15.871 1.00 122.41 ? 134 THR   A CA  1 
ATOM   819  C C   . THR   A 1 116 ? 16.280  -34.650 17.246 1.00 129.74 ? 134 THR   A C   1 
ATOM   820  O O   . THR   A 1 116 ? 16.297  -33.422 17.367 1.00 159.37 ? 134 THR   A O   1 
ATOM   821  C CB  . THR   A 1 116 ? 17.583  -35.261 15.208 1.00 149.89 ? 134 THR   A CB  1 
ATOM   822  O OG1 . THR   A 1 116 ? 17.990  -33.900 15.020 1.00 133.99 ? 134 THR   A OG1 1 
ATOM   823  C CG2 . THR   A 1 116 ? 17.550  -35.972 13.863 1.00 139.01 ? 134 THR   A CG2 1 
ATOM   824  N N   . ARG   A 1 117 ? 16.320  -35.487 18.278 1.00 118.04 ? 135 ARG   A N   1 
ATOM   825  C CA  . ARG   A 1 117 ? 16.517  -35.046 19.652 1.00 132.36 ? 135 ARG   A CA  1 
ATOM   826  C C   . ARG   A 1 117 ? 17.618  -35.897 20.265 1.00 131.53 ? 135 ARG   A C   1 
ATOM   827  O O   . ARG   A 1 117 ? 17.572  -37.128 20.182 1.00 144.74 ? 135 ARG   A O   1 
ATOM   828  C CB  . ARG   A 1 117 ? 15.225  -35.165 20.465 1.00 132.77 ? 135 ARG   A CB  1 
ATOM   829  C CG  . ARG   A 1 117 ? 15.338  -34.664 21.898 1.00 125.64 ? 135 ARG   A CG  1 
ATOM   830  C CD  . ARG   A 1 117 ? 15.397  -33.147 21.974 1.00 118.73 ? 135 ARG   A CD  1 
ATOM   831  N NE  . ARG   A 1 117 ? 14.139  -32.528 21.570 1.00 124.97 ? 135 ARG   A NE  1 
ATOM   832  C CZ  . ARG   A 1 117 ? 13.882  -31.230 21.648 1.00 146.23 ? 135 ARG   A CZ  1 
ATOM   833  N NH1 . ARG   A 1 117 ? 14.775  -30.374 22.120 1.00 135.99 ? 135 ARG   A NH1 1 
ATOM   834  N NH2 . ARG   A 1 117 ? 12.699  -30.777 21.243 1.00 126.41 ? 135 ARG   A NH2 1 
ATOM   835  N N   . ARG   A 1 118 ? 18.602  -35.241 20.880 1.00 140.54 ? 136 ARG   A N   1 
ATOM   836  C CA  . ARG   A 1 118 ? 19.790  -35.925 21.393 1.00 141.26 ? 136 ARG   A CA  1 
ATOM   837  C C   . ARG   A 1 118 ? 20.468  -36.731 20.287 1.00 143.97 ? 136 ARG   A C   1 
ATOM   838  O O   . ARG   A 1 118 ? 20.975  -37.832 20.513 1.00 144.52 ? 136 ARG   A O   1 
ATOM   839  C CB  . ARG   A 1 118 ? 19.444  -36.813 22.591 1.00 134.34 ? 136 ARG   A CB  1 
ATOM   840  C CG  . ARG   A 1 118 ? 19.149  -36.030 23.865 1.00 134.48 ? 136 ARG   A CG  1 
ATOM   841  C CD  . ARG   A 1 118 ? 18.743  -36.936 25.017 1.00 130.18 ? 136 ARG   A CD  1 
ATOM   842  N NE  . ARG   A 1 118 ? 18.552  -36.187 26.255 1.00 137.56 ? 136 ARG   A NE  1 
ATOM   843  C CZ  . ARG   A 1 118 ? 18.092  -36.705 27.386 1.00 133.72 ? 136 ARG   A CZ  1 
ATOM   844  N NH1 . ARG   A 1 118 ? 17.751  -37.981 27.475 1.00 132.50 ? 136 ARG   A NH1 1 
ATOM   845  N NH2 . ARG   A 1 118 ? 17.969  -35.923 28.455 1.00 130.32 ? 136 ARG   A NH2 1 
ATOM   846  N N   . ASN   A 1 119 ? 20.472  -36.172 19.075 1.00 135.45 ? 137 ASN   A N   1 
ATOM   847  C CA  . ASN   A 1 119 ? 21.131  -36.777 17.917 1.00 139.02 ? 137 ASN   A CA  1 
ATOM   848  C C   . ASN   A 1 119 ? 20.556  -38.151 17.580 1.00 135.58 ? 137 ASN   A C   1 
ATOM   849  O O   . ASN   A 1 119 ? 21.267  -39.029 17.086 1.00 126.34 ? 137 ASN   A O   1 
ATOM   850  C CB  . ASN   A 1 119 ? 22.645  -36.870 18.133 1.00 144.58 ? 137 ASN   A CB  1 
ATOM   851  C CG  . ASN   A 1 119 ? 23.318  -35.511 18.122 1.00 156.91 ? 137 ASN   A CG  1 
ATOM   852  O OD1 . ASN   A 1 119 ? 22.928  -34.619 17.368 1.00 155.32 ? 137 ASN   A OD1 1 
ATOM   853  N ND2 . ASN   A 1 119 ? 24.332  -35.345 18.961 1.00 148.63 ? 137 ASN   A ND2 1 
ATOM   854  N N   . LYS   A 1 120 ? 19.265  -38.348 17.840 1.00 138.45 ? 138 LYS   A N   1 
ATOM   855  C CA  . LYS   A 1 120 ? 18.576  -39.559 17.417 1.00 121.06 ? 138 LYS   A CA  1 
ATOM   856  C C   . LYS   A 1 120 ? 17.128  -39.208 17.107 1.00 114.74 ? 138 LYS   A C   1 
ATOM   857  O O   . LYS   A 1 120 ? 16.626  -38.153 17.502 1.00 118.37 ? 138 LYS   A O   1 
ATOM   858  C CB  . LYS   A 1 120 ? 18.662  -40.671 18.473 1.00 107.03 ? 138 LYS   A CB  1 
ATOM   859  C CG  . LYS   A 1 120 ? 18.173  -40.291 19.863 1.00 105.72 ? 138 LYS   A CG  1 
ATOM   860  C CD  . LYS   A 1 120 ? 18.340  -41.457 20.835 1.00 98.70  ? 138 LYS   A CD  1 
ATOM   861  C CE  . LYS   A 1 120 ? 17.932  -41.082 22.254 1.00 108.07 ? 138 LYS   A CE  1 
ATOM   862  N NZ  . LYS   A 1 120 ? 18.103  -42.216 23.209 1.00 99.83  ? 138 LYS   A NZ  1 
ATOM   863  N N   . HIS   A 1 121 ? 16.466  -40.105 16.380 1.00 123.32 ? 139 HIS   A N   1 
ATOM   864  C CA  . HIS   A 1 121 ? 15.104  -39.841 15.935 1.00 119.74 ? 139 HIS   A CA  1 
ATOM   865  C C   . HIS   A 1 121 ? 14.188  -39.593 17.125 1.00 112.72 ? 139 HIS   A C   1 
ATOM   866  O O   . HIS   A 1 121 ? 14.299  -40.246 18.166 1.00 98.75  ? 139 HIS   A O   1 
ATOM   867  C CB  . HIS   A 1 121 ? 14.579  -41.014 15.109 1.00 103.63 ? 139 HIS   A CB  1 
ATOM   868  C CG  . HIS   A 1 121 ? 15.317  -41.226 13.825 1.00 110.45 ? 139 HIS   A CG  1 
ATOM   869  N ND1 . HIS   A 1 121 ? 15.360  -40.276 12.827 1.00 114.28 ? 139 HIS   A ND1 1 
ATOM   870  C CD2 . HIS   A 1 121 ? 16.038  -42.279 13.374 1.00 115.56 ? 139 HIS   A CD2 1 
ATOM   871  C CE1 . HIS   A 1 121 ? 16.078  -40.735 11.818 1.00 119.80 ? 139 HIS   A CE1 1 
ATOM   872  N NE2 . HIS   A 1 121 ? 16.501  -41.948 12.124 1.00 121.38 ? 139 HIS   A NE2 1 
ATOM   873  N N   . CYS   A 1 122 ? 13.278  -38.637 16.963 1.00 111.93 ? 140 CYS   A N   1 
ATOM   874  C CA  . CYS   A 1 122 ? 12.339  -38.318 18.026 1.00 110.09 ? 140 CYS   A CA  1 
ATOM   875  C C   . CYS   A 1 122 ? 11.439  -39.513 18.316 1.00 93.54  ? 140 CYS   A C   1 
ATOM   876  O O   . CYS   A 1 122 ? 11.100  -40.298 17.426 1.00 93.41  ? 140 CYS   A O   1 
ATOM   877  C CB  . CYS   A 1 122 ? 11.499  -37.100 17.644 1.00 103.88 ? 140 CYS   A CB  1 
ATOM   878  S SG  . CYS   A 1 122 ? 12.470  -35.601 17.361 1.00 117.81 ? 140 CYS   A SG  1 
ATOM   879  N N   . TRP   A 1 123 ? 11.053  -39.645 19.587 1.00 104.39 ? 141 TRP   A N   1 
ATOM   880  C CA  . TRP   A 1 123 ? 10.280  -40.806 20.017 1.00 97.63  ? 141 TRP   A CA  1 
ATOM   881  C C   . TRP   A 1 123 ? 9.015   -40.976 19.184 1.00 101.55 ? 141 TRP   A C   1 
ATOM   882  O O   . TRP   A 1 123 ? 8.611   -42.105 18.882 1.00 103.74 ? 141 TRP   A O   1 
ATOM   883  C CB  . TRP   A 1 123 ? 9.936   -40.673 21.500 1.00 87.75  ? 141 TRP   A CB  1 
ATOM   884  C CG  . TRP   A 1 123 ? 9.187   -41.840 22.067 1.00 83.58  ? 141 TRP   A CG  1 
ATOM   885  C CD1 . TRP   A 1 123 ? 7.890   -41.854 22.485 1.00 84.84  ? 141 TRP   A CD1 1 
ATOM   886  C CD2 . TRP   A 1 123 ? 9.693   -43.163 22.282 1.00 86.15  ? 141 TRP   A CD2 1 
ATOM   887  N NE1 . TRP   A 1 123 ? 7.555   -43.103 22.949 1.00 83.69  ? 141 TRP   A NE1 1 
ATOM   888  C CE2 . TRP   A 1 123 ? 8.645   -43.925 22.835 1.00 89.27  ? 141 TRP   A CE2 1 
ATOM   889  C CE3 . TRP   A 1 123 ? 10.930  -43.776 22.062 1.00 86.85  ? 141 TRP   A CE3 1 
ATOM   890  C CZ2 . TRP   A 1 123 ? 8.796   -45.269 23.170 1.00 102.01 ? 141 TRP   A CZ2 1 
ATOM   891  C CZ3 . TRP   A 1 123 ? 11.078  -45.110 22.395 1.00 83.58  ? 141 TRP   A CZ3 1 
ATOM   892  C CH2 . TRP   A 1 123 ? 10.017  -45.842 22.942 1.00 87.44  ? 141 TRP   A CH2 1 
ATOM   893  N N   . TYR   A 1 124 ? 8.377   -39.870 18.803 1.00 113.38 ? 142 TYR   A N   1 
ATOM   894  C CA  . TYR   A 1 124 ? 7.142   -39.942 18.032 1.00 98.24  ? 142 TYR   A CA  1 
ATOM   895  C C   . TYR   A 1 124 ? 7.376   -40.248 16.557 1.00 95.61  ? 142 TYR   A C   1 
ATOM   896  O O   . TYR   A 1 124 ? 6.407   -40.508 15.836 1.00 93.56  ? 142 TYR   A O   1 
ATOM   897  C CB  . TYR   A 1 124 ? 6.365   -38.629 18.167 1.00 104.59 ? 142 TYR   A CB  1 
ATOM   898  C CG  . TYR   A 1 124 ? 6.888   -37.501 17.305 1.00 101.05 ? 142 TYR   A CG  1 
ATOM   899  C CD1 . TYR   A 1 124 ? 7.987   -36.748 17.698 1.00 100.92 ? 142 TYR   A CD1 1 
ATOM   900  C CD2 . TYR   A 1 124 ? 6.275   -37.183 16.100 1.00 101.51 ? 142 TYR   A CD2 1 
ATOM   901  C CE1 . TYR   A 1 124 ? 8.463   -35.714 16.912 1.00 102.12 ? 142 TYR   A CE1 1 
ATOM   902  C CE2 . TYR   A 1 124 ? 6.744   -36.153 15.307 1.00 100.06 ? 142 TYR   A CE2 1 
ATOM   903  C CZ  . TYR   A 1 124 ? 7.838   -35.421 15.718 1.00 107.51 ? 142 TYR   A CZ  1 
ATOM   904  O OH  . TYR   A 1 124 ? 8.306   -34.392 14.932 1.00 110.19 ? 142 TYR   A OH  1 
ATOM   905  N N   . LEU   A 1 125 ? 8.625   -40.224 16.093 1.00 100.35 ? 143 LEU   A N   1 
ATOM   906  C CA  . LEU   A 1 125 ? 8.936   -40.502 14.697 1.00 112.02 ? 143 LEU   A CA  1 
ATOM   907  C C   . LEU   A 1 125 ? 9.273   -41.963 14.433 1.00 122.69 ? 143 LEU   A C   1 
ATOM   908  O O   . LEU   A 1 125 ? 9.368   -42.356 13.265 1.00 128.99 ? 143 LEU   A O   1 
ATOM   909  C CB  . LEU   A 1 125 ? 10.112  -39.636 14.236 1.00 100.72 ? 143 LEU   A CB  1 
ATOM   910  C CG  . LEU   A 1 125 ? 9.851   -38.134 14.124 1.00 105.62 ? 143 LEU   A CG  1 
ATOM   911  C CD1 . LEU   A 1 125 ? 11.115  -37.420 13.682 1.00 108.28 ? 143 LEU   A CD1 1 
ATOM   912  C CD2 . LEU   A 1 125 ? 8.707   -37.851 13.161 1.00 105.38 ? 143 LEU   A CD2 1 
ATOM   913  N N   . LEU   A 1 126 ? 9.456   -42.771 15.471 1.00 108.49 ? 144 LEU   A N   1 
ATOM   914  C CA  . LEU   A 1 126 ? 9.835   -44.160 15.272 1.00 110.77 ? 144 LEU   A CA  1 
ATOM   915  C C   . LEU   A 1 126 ? 8.707   -44.941 14.606 1.00 134.19 ? 144 LEU   A C   1 
ATOM   916  O O   . LEU   A 1 126 ? 7.523   -44.633 14.768 1.00 103.05 ? 144 LEU   A O   1 
ATOM   917  C CB  . LEU   A 1 126 ? 10.208  -44.807 16.605 1.00 111.56 ? 144 LEU   A CB  1 
ATOM   918  C CG  . LEU   A 1 126 ? 11.690  -44.717 16.978 1.00 131.07 ? 144 LEU   A CG  1 
ATOM   919  C CD1 . LEU   A 1 126 ? 12.170  -43.275 16.960 1.00 119.13 ? 144 LEU   A CD1 1 
ATOM   920  C CD2 . LEU   A 1 126 ? 11.939  -45.349 18.340 1.00 145.53 ? 144 LEU   A CD2 1 
ATOM   921  N N   . LYS   A 1 127 ? 9.095   -45.967 13.844 1.00 131.78 ? 145 LYS   A N   1 
ATOM   922  C CA  . LYS   A 1 127 ? 8.110   -46.819 13.185 1.00 128.89 ? 145 LYS   A CA  1 
ATOM   923  C C   . LYS   A 1 127 ? 7.145   -47.422 14.197 1.00 125.35 ? 145 LYS   A C   1 
ATOM   924  O O   . LYS   A 1 127 ? 5.929   -47.441 13.974 1.00 127.35 ? 145 LYS   A O   1 
ATOM   925  C CB  . LYS   A 1 127 ? 8.826   -47.920 12.398 1.00 137.11 ? 145 LYS   A CB  1 
ATOM   926  C CG  . LYS   A 1 127 ? 7.980   -49.156 12.102 1.00 150.89 ? 145 LYS   A CG  1 
ATOM   927  C CD  . LYS   A 1 127 ? 8.780   -50.210 11.352 1.00 147.92 ? 145 LYS   A CD  1 
ATOM   928  C CE  . LYS   A 1 127 ? 8.004   -51.514 11.225 1.00 168.11 ? 145 LYS   A CE  1 
ATOM   929  N NZ  . LYS   A 1 127 ? 7.686   -52.114 12.553 1.00 146.66 ? 145 LYS   A NZ  1 
ATOM   930  N N   . ASP   A 1 128 ? 7.668   -47.916 15.316 1.00 120.40 ? 146 ASP   A N   1 
ATOM   931  C CA  . ASP   A 1 128 ? 6.853   -48.555 16.339 1.00 129.33 ? 146 ASP   A CA  1 
ATOM   932  C C   . ASP   A 1 128 ? 6.187   -47.558 17.279 1.00 122.08 ? 146 ASP   A C   1 
ATOM   933  O O   . ASP   A 1 128 ? 5.394   -47.973 18.132 1.00 127.62 ? 146 ASP   A O   1 
ATOM   934  C CB  . ASP   A 1 128 ? 7.715   -49.531 17.145 1.00 136.08 ? 146 ASP   A CB  1 
ATOM   935  C CG  . ASP   A 1 128 ? 8.219   -50.693 16.308 1.00 143.95 ? 146 ASP   A CG  1 
ATOM   936  O OD1 . ASP   A 1 128 ? 9.126   -50.480 15.476 1.00 143.81 ? 146 ASP   A OD1 1 
ATOM   937  O OD2 . ASP   A 1 128 ? 7.709   -51.819 16.483 1.00 157.44 ? 146 ASP   A OD2 1 
ATOM   938  N N   . VAL   A 1 129 ? 6.482   -46.265 17.146 1.00 133.37 ? 147 VAL   A N   1 
ATOM   939  C CA  . VAL   A 1 129 ? 5.907   -45.244 18.014 1.00 117.95 ? 147 VAL   A CA  1 
ATOM   940  C C   . VAL   A 1 129 ? 5.503   -44.039 17.177 1.00 114.53 ? 147 VAL   A C   1 
ATOM   941  O O   . VAL   A 1 129 ? 6.351   -43.231 16.785 1.00 127.96 ? 147 VAL   A O   1 
ATOM   942  C CB  . VAL   A 1 129 ? 6.898   -44.825 19.117 1.00 110.15 ? 147 VAL   A CB  1 
ATOM   943  C CG1 . VAL   A 1 129 ? 6.220   -43.907 20.126 1.00 118.11 ? 147 VAL   A CG1 1 
ATOM   944  C CG2 . VAL   A 1 129 ? 7.484   -46.048 19.802 1.00 103.68 ? 147 VAL   A CG2 1 
ATOM   945  N N   . GLU   A 1 130 ? 4.210   -43.909 16.898 1.00 100.29 ? 148 GLU   A N   1 
ATOM   946  C CA  . GLU   A 1 130 ? 3.691   -42.727 16.230 1.00 120.80 ? 148 GLU   A CA  1 
ATOM   947  C C   . GLU   A 1 130 ? 3.274   -41.704 17.285 1.00 106.16 ? 148 GLU   A C   1 
ATOM   948  O O   . GLU   A 1 130 ? 3.550   -41.859 18.478 1.00 97.88  ? 148 GLU   A O   1 
ATOM   949  C CB  . GLU   A 1 130 ? 2.537   -43.103 15.303 1.00 129.32 ? 148 GLU   A CB  1 
ATOM   950  C CG  . GLU   A 1 130 ? 2.977   -43.461 13.896 1.00 109.51 ? 148 GLU   A CG  1 
ATOM   951  C CD  . GLU   A 1 130 ? 3.711   -44.782 13.836 1.00 129.36 ? 148 GLU   A CD  1 
ATOM   952  O OE1 . GLU   A 1 130 ? 3.241   -45.753 14.465 1.00 156.86 ? 148 GLU   A OE1 1 
ATOM   953  O OE2 . GLU   A 1 130 ? 4.760   -44.850 13.162 1.00 173.88 ? 148 GLU   A OE2 1 
ATOM   954  N N   . ILE   A 1 131 ? 2.603   -40.638 16.848 1.00 93.22  ? 149 ILE   A N   1 
ATOM   955  C CA  . ILE   A 1 131 ? 2.080   -39.649 17.785 1.00 99.62  ? 149 ILE   A CA  1 
ATOM   956  C C   . ILE   A 1 131 ? 1.123   -40.314 18.765 1.00 111.50 ? 149 ILE   A C   1 
ATOM   957  O O   . ILE   A 1 131 ? 1.095   -39.984 19.961 1.00 106.49 ? 149 ILE   A O   1 
ATOM   958  C CB  . ILE   A 1 131 ? 1.392   -38.506 17.016 1.00 101.03 ? 149 ILE   A CB  1 
ATOM   959  C CG1 . ILE   A 1 131 ? 2.361   -37.856 16.023 1.00 107.40 ? 149 ILE   A CG1 1 
ATOM   960  C CG2 . ILE   A 1 131 ? 0.849   -37.466 17.984 1.00 111.63 ? 149 ILE   A CG2 1 
ATOM   961  C CD1 . ILE   A 1 131 ? 1.702   -37.442 14.722 1.00 126.24 ? 149 ILE   A CD1 1 
ATOM   962  N N   . LYS   A 1 132 ? 0.321   -41.260 18.270 1.00 108.74 ? 150 LYS   A N   1 
ATOM   963  C CA  . LYS   A 1 132 ? -0.644  -41.952 19.117 1.00 102.72 ? 150 LYS   A CA  1 
ATOM   964  C C   . LYS   A 1 132 ? 0.035   -42.547 20.344 1.00 109.36 ? 150 LYS   A C   1 
ATOM   965  O O   . LYS   A 1 132 ? -0.453  -42.404 21.471 1.00 99.19  ? 150 LYS   A O   1 
ATOM   966  C CB  . LYS   A 1 132 ? -1.358  -43.039 18.309 1.00 102.88 ? 150 LYS   A CB  1 
ATOM   967  C CG  . LYS   A 1 132 ? -0.425  -44.029 17.613 1.00 97.58  ? 150 LYS   A CG  1 
ATOM   968  C CD  . LYS   A 1 132 ? -1.204  -45.115 16.886 1.00 101.32 ? 150 LYS   A CD  1 
ATOM   969  C CE  . LYS   A 1 132 ? -0.283  -46.210 16.369 1.00 113.58 ? 150 LYS   A CE  1 
ATOM   970  N NZ  . LYS   A 1 132 ? -1.041  -47.367 15.813 1.00 122.27 ? 150 LYS   A NZ  1 
ATOM   971  N N   . ASN   A 1 133 ? 1.170   -43.218 20.141 1.00 110.51 ? 151 ASN   A N   1 
ATOM   972  C CA  . ASN   A 1 133 ? 1.914   -43.773 21.265 1.00 105.77 ? 151 ASN   A CA  1 
ATOM   973  C C   . ASN   A 1 133 ? 2.651   -42.692 22.040 1.00 104.36 ? 151 ASN   A C   1 
ATOM   974  O O   . ASN   A 1 133 ? 2.809   -42.809 23.260 1.00 105.70 ? 151 ASN   A O   1 
ATOM   975  C CB  . ASN   A 1 133 ? 2.909   -44.823 20.772 1.00 111.63 ? 151 ASN   A CB  1 
ATOM   976  C CG  . ASN   A 1 133 ? 2.382   -46.238 20.901 1.00 112.18 ? 151 ASN   A CG  1 
ATOM   977  O OD1 . ASN   A 1 133 ? 1.500   -46.516 21.713 1.00 111.17 ? 151 ASN   A OD1 1 
ATOM   978  N ND2 . ASN   A 1 133 ? 2.935   -47.145 20.104 1.00 119.42 ? 151 ASN   A ND2 1 
ATOM   979  N N   . ALA   A 1 134 ? 3.119   -41.647 21.354 1.00 98.85  ? 152 ALA   A N   1 
ATOM   980  C CA  . ALA   A 1 134 ? 3.932   -40.632 22.016 1.00 104.59 ? 152 ALA   A CA  1 
ATOM   981  C C   . ALA   A 1 134 ? 3.136   -39.884 23.081 1.00 109.00 ? 152 ALA   A C   1 
ATOM   982  O O   . ALA   A 1 134 ? 3.649   -39.621 24.174 1.00 100.63 ? 152 ALA   A O   1 
ATOM   983  C CB  . ALA   A 1 134 ? 4.495   -39.658 20.982 1.00 117.00 ? 152 ALA   A CB  1 
ATOM   984  N N   . VAL   A 1 135 ? 1.882   -39.537 22.784 1.00 100.32 ? 153 VAL   A N   1 
ATOM   985  C CA  . VAL   A 1 135 ? 1.062   -38.824 23.766 1.00 99.86  ? 153 VAL   A CA  1 
ATOM   986  C C   . VAL   A 1 135 ? 0.860   -39.682 25.012 1.00 91.82  ? 153 VAL   A C   1 
ATOM   987  O O   . VAL   A 1 135 ? 1.084   -39.240 26.152 1.00 86.21  ? 153 VAL   A O   1 
ATOM   988  C CB  . VAL   A 1 135 ? -0.287  -38.426 23.138 1.00 98.07  ? 153 VAL   A CB  1 
ATOM   989  C CG1 . VAL   A 1 135 ? -1.188  -37.769 24.171 1.00 99.65  ? 153 VAL   A CG1 1 
ATOM   990  C CG2 . VAL   A 1 135 ? -0.072  -37.507 21.946 1.00 99.33  ? 153 VAL   A CG2 1 
ATOM   991  N N   . ASN   A 1 136 ? 0.437   -40.929 24.805 1.00 95.00  ? 154 ASN   A N   1 
ATOM   992  C CA  . ASN   A 1 136 ? 0.185   -41.829 25.921 1.00 85.00  ? 154 ASN   A CA  1 
ATOM   993  C C   . ASN   A 1 136 ? 1.451   -42.048 26.736 1.00 89.08  ? 154 ASN   A C   1 
ATOM   994  O O   . ASN   A 1 136 ? 1.404   -42.098 27.969 1.00 92.79  ? 154 ASN   A O   1 
ATOM   995  C CB  . ASN   A 1 136 ? -0.363  -43.153 25.387 1.00 92.32  ? 154 ASN   A CB  1 
ATOM   996  C CG  . ASN   A 1 136 ? -0.820  -44.083 26.486 1.00 92.28  ? 154 ASN   A CG  1 
ATOM   997  O OD1 . ASN   A 1 136 ? -1.934  -43.963 26.994 1.00 83.74  ? 154 ASN   A OD1 1 
ATOM   998  N ND2 . ASN   A 1 136 ? 0.037   -45.027 26.852 1.00 108.71 ? 154 ASN   A ND2 1 
ATOM   999  N N   . ASP   A 1 137 ? 2.599   -42.159 26.064 1.00 89.29  ? 155 ASP   A N   1 
ATOM   1000 C CA  . ASP   A 1 137 ? 3.855   -42.383 26.770 1.00 89.41  ? 155 ASP   A CA  1 
ATOM   1001 C C   . ASP   A 1 137 ? 4.276   -41.157 27.571 1.00 87.48  ? 155 ASP   A C   1 
ATOM   1002 O O   . ASP   A 1 137 ? 4.815   -41.288 28.675 1.00 85.70  ? 155 ASP   A O   1 
ATOM   1003 C CB  . ASP   A 1 137 ? 4.944   -42.777 25.774 1.00 91.43  ? 155 ASP   A CB  1 
ATOM   1004 C CG  . ASP   A 1 137 ? 4.698   -44.138 25.151 1.00 100.29 ? 155 ASP   A CG  1 
ATOM   1005 O OD1 . ASP   A 1 137 ? 3.745   -44.827 25.578 1.00 91.10  ? 155 ASP   A OD1 1 
ATOM   1006 O OD2 . ASP   A 1 137 ? 5.455   -44.517 24.233 1.00 100.64 ? 155 ASP   A OD2 1 
ATOM   1007 N N   . VAL   A 1 138 ? 4.058   -39.955 27.033 1.00 83.92  ? 156 VAL   A N   1 
ATOM   1008 C CA  . VAL   A 1 138 ? 4.394   -38.755 27.795 1.00 86.85  ? 156 VAL   A CA  1 
ATOM   1009 C C   . VAL   A 1 138 ? 3.553   -38.698 29.061 1.00 80.77  ? 156 VAL   A C   1 
ATOM   1010 O O   . VAL   A 1 138 ? 4.053   -38.374 30.148 1.00 87.36  ? 156 VAL   A O   1 
ATOM   1011 C CB  . VAL   A 1 138 ? 4.209   -37.488 26.938 1.00 84.49  ? 156 VAL   A CB  1 
ATOM   1012 C CG1 . VAL   A 1 138 ? 4.649   -36.253 27.717 1.00 81.16  ? 156 VAL   A CG1 1 
ATOM   1013 C CG2 . VAL   A 1 138 ? 5.000   -37.588 25.641 1.00 114.96 ? 156 VAL   A CG2 1 
ATOM   1014 N N   . PHE   A 1 139 ? 2.262   -39.010 28.944 1.00 83.36  ? 157 PHE   A N   1 
ATOM   1015 C CA  . PHE   A 1 139 ? 1.425   -39.033 30.141 1.00 82.93  ? 157 PHE   A CA  1 
ATOM   1016 C C   . PHE   A 1 139 ? 1.877   -40.121 31.108 1.00 79.73  ? 157 PHE   A C   1 
ATOM   1017 O O   . PHE   A 1 139 ? 1.854   -39.928 32.331 1.00 77.35  ? 157 PHE   A O   1 
ATOM   1018 C CB  . PHE   A 1 139 ? -0.039  -39.207 29.753 1.00 79.78  ? 157 PHE   A CB  1 
ATOM   1019 C CG  . PHE   A 1 139 ? -0.657  -37.953 29.217 1.00 111.57 ? 157 PHE   A CG  1 
ATOM   1020 C CD1 . PHE   A 1 139 ? -1.012  -36.927 30.075 1.00 120.21 ? 157 PHE   A CD1 1 
ATOM   1021 C CD2 . PHE   A 1 139 ? -0.857  -37.786 27.859 1.00 116.25 ? 157 PHE   A CD2 1 
ATOM   1022 C CE1 . PHE   A 1 139 ? -1.569  -35.763 29.589 1.00 125.09 ? 157 PHE   A CE1 1 
ATOM   1023 C CE2 . PHE   A 1 139 ? -1.414  -36.624 27.367 1.00 120.94 ? 157 PHE   A CE2 1 
ATOM   1024 C CZ  . PHE   A 1 139 ? -1.766  -35.611 28.233 1.00 125.53 ? 157 PHE   A CZ  1 
ATOM   1025 N N   . LEU   A 1 140 ? 2.305   -41.270 30.580 1.00 77.44  ? 158 LEU   A N   1 
ATOM   1026 C CA  . LEU   A 1 140 ? 2.824   -42.325 31.442 1.00 72.87  ? 158 LEU   A CA  1 
ATOM   1027 C C   . LEU   A 1 140 ? 4.041   -41.848 32.218 1.00 75.76  ? 158 LEU   A C   1 
ATOM   1028 O O   . LEU   A 1 140 ? 4.163   -42.110 33.416 1.00 81.16  ? 158 LEU   A O   1 
ATOM   1029 C CB  . LEU   A 1 140 ? 3.183   -43.556 30.611 1.00 79.91  ? 158 LEU   A CB  1 
ATOM   1030 C CG  . LEU   A 1 140 ? 3.840   -44.710 31.377 1.00 76.52  ? 158 LEU   A CG  1 
ATOM   1031 C CD1 . LEU   A 1 140 ? 2.796   -45.691 31.897 1.00 75.63  ? 158 LEU   A CD1 1 
ATOM   1032 C CD2 . LEU   A 1 140 ? 4.865   -45.405 30.503 1.00 86.12  ? 158 LEU   A CD2 1 
ATOM   1033 N N   . LEU   A 1 141 ? 4.968   -41.168 31.542 1.00 82.13  ? 159 LEU   A N   1 
ATOM   1034 C CA  . LEU   A 1 141 ? 6.155   -40.659 32.222 1.00 90.23  ? 159 LEU   A CA  1 
ATOM   1035 C C   . LEU   A 1 141 ? 5.776   -39.645 33.292 1.00 78.13  ? 159 LEU   A C   1 
ATOM   1036 O O   . LEU   A 1 141 ? 6.309   -39.669 34.413 1.00 75.68  ? 159 LEU   A O   1 
ATOM   1037 C CB  . LEU   A 1 141 ? 7.103   -40.026 31.203 1.00 72.11  ? 159 LEU   A CB  1 
ATOM   1038 C CG  . LEU   A 1 141 ? 7.639   -40.969 30.126 1.00 70.07  ? 159 LEU   A CG  1 
ATOM   1039 C CD1 . LEU   A 1 141 ? 8.306   -40.185 29.009 1.00 85.72  ? 159 LEU   A CD1 1 
ATOM   1040 C CD2 . LEU   A 1 141 ? 8.607   -41.968 30.736 1.00 87.76  ? 159 LEU   A CD2 1 
ATOM   1041 N N   . TYR   A 1 142 ? 4.846   -38.747 32.963 1.00 80.75  ? 160 TYR   A N   1 
ATOM   1042 C CA  . TYR   A 1 142 ? 4.434   -37.740 33.930 1.00 77.48  ? 160 TYR   A CA  1 
ATOM   1043 C C   . TYR   A 1 142 ? 3.835   -38.390 35.171 1.00 82.27  ? 160 TYR   A C   1 
ATOM   1044 O O   . TYR   A 1 142 ? 4.120   -37.972 36.299 1.00 79.91  ? 160 TYR   A O   1 
ATOM   1045 C CB  . TYR   A 1 142 ? 3.441   -36.773 33.288 1.00 79.97  ? 160 TYR   A CB  1 
ATOM   1046 C CG  . TYR   A 1 142 ? 3.154   -35.574 34.155 1.00 82.85  ? 160 TYR   A CG  1 
ATOM   1047 C CD1 . TYR   A 1 142 ? 4.137   -34.627 34.403 1.00 77.14  ? 160 TYR   A CD1 1 
ATOM   1048 C CD2 . TYR   A 1 142 ? 1.908   -35.392 34.735 1.00 86.98  ? 160 TYR   A CD2 1 
ATOM   1049 C CE1 . TYR   A 1 142 ? 3.888   -33.533 35.203 1.00 80.41  ? 160 TYR   A CE1 1 
ATOM   1050 C CE2 . TYR   A 1 142 ? 1.646   -34.299 35.537 1.00 84.91  ? 160 TYR   A CE2 1 
ATOM   1051 C CZ  . TYR   A 1 142 ? 2.640   -33.372 35.767 1.00 92.73  ? 160 TYR   A CZ  1 
ATOM   1052 O OH  . TYR   A 1 142 ? 2.388   -32.279 36.563 1.00 93.92  ? 160 TYR   A OH  1 
ATOM   1053 N N   . ASN   A 1 143 ? 3.009   -39.422 34.985 1.00 109.18 ? 161 ASN   A N   1 
ATOM   1054 C CA  . ASN   A 1 143 ? 2.454   -40.128 36.137 1.00 108.60 ? 161 ASN   A CA  1 
ATOM   1055 C C   . ASN   A 1 143 ? 3.517   -40.932 36.876 1.00 107.16 ? 161 ASN   A C   1 
ATOM   1056 O O   . ASN   A 1 143 ? 3.453   -41.057 38.104 1.00 106.80 ? 161 ASN   A O   1 
ATOM   1057 C CB  . ASN   A 1 143 ? 1.312   -41.041 35.693 1.00 110.53 ? 161 ASN   A CB  1 
ATOM   1058 C CG  . ASN   A 1 143 ? 0.028   -40.279 35.433 1.00 119.62 ? 161 ASN   A CG  1 
ATOM   1059 O OD1 . ASN   A 1 143 ? -0.490  -39.593 36.315 1.00 121.06 ? 161 ASN   A OD1 1 
ATOM   1060 N ND2 . ASN   A 1 143 ? -0.485  -40.384 34.214 1.00 123.01 ? 161 ASN   A ND2 1 
ATOM   1061 N N   . ALA   A 1 144 ? 4.490   -41.489 36.154 1.00 91.57  ? 162 ALA   A N   1 
ATOM   1062 C CA  . ALA   A 1 144 ? 5.549   -42.257 36.795 1.00 101.66 ? 162 ALA   A CA  1 
ATOM   1063 C C   . ALA   A 1 144 ? 6.361   -41.385 37.738 1.00 67.25  ? 162 ALA   A C   1 
ATOM   1064 O O   . ALA   A 1 144 ? 6.847   -41.862 38.770 1.00 70.89  ? 162 ALA   A O   1 
ATOM   1065 C CB  . ALA   A 1 144 ? 6.458   -42.875 35.735 1.00 102.82 ? 162 ALA   A CB  1 
ATOM   1066 N N   . ILE   A 1 145 ? 6.542   -40.112 37.384 1.00 80.50  ? 163 ILE   A N   1 
ATOM   1067 C CA  . ILE   A 1 145 ? 7.226   -39.183 38.287 1.00 72.64  ? 163 ILE   A CA  1 
ATOM   1068 C C   . ILE   A 1 145 ? 6.600   -39.249 39.677 1.00 74.59  ? 163 ILE   A C   1 
ATOM   1069 O O   . ILE   A 1 145 ? 7.260   -39.575 40.675 1.00 59.70  ? 163 ILE   A O   1 
ATOM   1070 C CB  . ILE   A 1 145 ? 7.173   -37.751 37.730 1.00 56.02  ? 163 ILE   A CB  1 
ATOM   1071 C CG1 . ILE   A 1 145 ? 7.938   -37.660 36.409 1.00 70.90  ? 163 ILE   A CG1 1 
ATOM   1072 C CG2 . ILE   A 1 145 ? 7.737   -36.769 38.744 1.00 65.19  ? 163 ILE   A CG2 1 
ATOM   1073 C CD1 . ILE   A 1 145 ? 7.611   -36.417 35.614 1.00 80.83  ? 163 ILE   A CD1 1 
ATOM   1074 N N   . TYR   A 1 146 ? 5.305   -38.943 39.754 1.00 71.05  ? 164 TYR   A N   1 
ATOM   1075 C CA  . TYR   A 1 146 ? 4.631   -38.919 41.044 1.00 63.27  ? 164 TYR   A CA  1 
ATOM   1076 C C   . TYR   A 1 146 ? 4.505   -40.313 41.635 1.00 64.17  ? 164 TYR   A C   1 
ATOM   1077 O O   . TYR   A 1 146 ? 4.466   -40.458 42.860 1.00 74.13  ? 164 TYR   A O   1 
ATOM   1078 C CB  . TYR   A 1 146 ? 3.259   -38.264 40.903 1.00 66.23  ? 164 TYR   A CB  1 
ATOM   1079 C CG  . TYR   A 1 146 ? 3.353   -36.824 40.461 1.00 63.43  ? 164 TYR   A CG  1 
ATOM   1080 C CD1 . TYR   A 1 146 ? 3.462   -35.798 41.390 1.00 57.30  ? 164 TYR   A CD1 1 
ATOM   1081 C CD2 . TYR   A 1 146 ? 3.359   -36.492 39.113 1.00 67.41  ? 164 TYR   A CD2 1 
ATOM   1082 C CE1 . TYR   A 1 146 ? 3.558   -34.481 40.990 1.00 59.39  ? 164 TYR   A CE1 1 
ATOM   1083 C CE2 . TYR   A 1 146 ? 3.455   -35.178 38.702 1.00 65.14  ? 164 TYR   A CE2 1 
ATOM   1084 C CZ  . TYR   A 1 146 ? 3.557   -34.176 39.645 1.00 63.14  ? 164 TYR   A CZ  1 
ATOM   1085 O OH  . TYR   A 1 146 ? 3.655   -32.863 39.243 1.00 56.40  ? 164 TYR   A OH  1 
ATOM   1086 N N   . LYS   A 1 147 ? 4.459   -41.347 40.795 1.00 62.75  ? 165 LYS   A N   1 
ATOM   1087 C CA  . LYS   A 1 147 ? 4.445   -42.708 41.321 1.00 70.10  ? 165 LYS   A CA  1 
ATOM   1088 C C   . LYS   A 1 147 ? 5.701   -42.979 42.135 1.00 64.67  ? 165 LYS   A C   1 
ATOM   1089 O O   . LYS   A 1 147 ? 5.629   -43.422 43.286 1.00 58.00  ? 165 LYS   A O   1 
ATOM   1090 C CB  . LYS   A 1 147 ? 4.317   -43.716 40.178 1.00 77.10  ? 165 LYS   A CB  1 
ATOM   1091 C CG  . LYS   A 1 147 ? 4.245   -45.171 40.634 1.00 69.18  ? 165 LYS   A CG  1 
ATOM   1092 C CD  . LYS   A 1 147 ? 2.989   -45.447 41.452 1.00 76.16  ? 165 LYS   A CD  1 
ATOM   1093 C CE  . LYS   A 1 147 ? 3.048   -46.804 42.132 1.00 89.72  ? 165 LYS   A CE  1 
ATOM   1094 N NZ  . LYS   A 1 147 ? 1.793   -47.106 42.875 1.00 98.38  ? 165 LYS   A NZ  1 
ATOM   1095 N N   . LEU   A 1 148 ? 6.867   -42.702 41.550 1.00 69.09  ? 166 LEU   A N   1 
ATOM   1096 C CA  . LEU   A 1 148 ? 8.123   -42.902 42.263 1.00 60.24  ? 166 LEU   A CA  1 
ATOM   1097 C C   . LEU   A 1 148 ? 8.212   -42.002 43.490 1.00 69.69  ? 166 LEU   A C   1 
ATOM   1098 O O   . LEU   A 1 148 ? 8.690   -42.429 44.550 1.00 68.07  ? 166 LEU   A O   1 
ATOM   1099 C CB  . LEU   A 1 148 ? 9.296   -42.641 41.321 1.00 66.86  ? 166 LEU   A CB  1 
ATOM   1100 C CG  . LEU   A 1 148 ? 9.336   -43.540 40.087 1.00 56.26  ? 166 LEU   A CG  1 
ATOM   1101 C CD1 . LEU   A 1 148 ? 10.334  -43.004 39.078 1.00 73.78  ? 166 LEU   A CD1 1 
ATOM   1102 C CD2 . LEU   A 1 148 ? 9.684   -44.966 40.478 1.00 70.85  ? 166 LEU   A CD2 1 
ATOM   1103 N N   . LEU   A 1 149 ? 7.774   -40.747 43.362 1.00 60.61  ? 167 LEU   A N   1 
ATOM   1104 C CA  . LEU   A 1 149 ? 7.796   -39.854 44.517 1.00 54.71  ? 167 LEU   A CA  1 
ATOM   1105 C C   . LEU   A 1 149 ? 6.972   -40.429 45.662 1.00 68.18  ? 167 LEU   A C   1 
ATOM   1106 O O   . LEU   A 1 149 ? 7.404   -40.418 46.820 1.00 64.88  ? 167 LEU   A O   1 
ATOM   1107 C CB  . LEU   A 1 149 ? 7.274   -38.473 44.126 1.00 61.40  ? 167 LEU   A CB  1 
ATOM   1108 C CG  . LEU   A 1 149 ? 8.152   -37.656 43.181 1.00 66.82  ? 167 LEU   A CG  1 
ATOM   1109 C CD1 . LEU   A 1 149 ? 7.440   -36.374 42.796 1.00 70.21  ? 167 LEU   A CD1 1 
ATOM   1110 C CD2 . LEU   A 1 149 ? 9.502   -37.355 43.816 1.00 76.28  ? 167 LEU   A CD2 1 
ATOM   1111 N N   . ASP   A 1 150 ? 5.780   -40.940 45.354 1.00 75.54  ? 168 ASP   A N   1 
ATOM   1112 C CA  . ASP   A 1 150 ? 4.954   -41.570 46.375 1.00 72.88  ? 168 ASP   A CA  1 
ATOM   1113 C C   . ASP   A 1 150 ? 5.649   -42.787 46.963 1.00 66.80  ? 168 ASP   A C   1 
ATOM   1114 O O   . ASP   A 1 150 ? 5.643   -42.989 48.183 1.00 70.65  ? 168 ASP   A O   1 
ATOM   1115 C CB  . ASP   A 1 150 ? 3.608   -41.968 45.773 1.00 71.77  ? 168 ASP   A CB  1 
ATOM   1116 C CG  . ASP   A 1 150 ? 2.619   -42.439 46.818 1.00 75.90  ? 168 ASP   A CG  1 
ATOM   1117 O OD1 . ASP   A 1 150 ? 2.885   -42.244 48.022 1.00 79.36  ? 168 ASP   A OD1 1 
ATOM   1118 O OD2 . ASP   A 1 150 ? 1.576   -43.007 46.434 1.00 68.19  ? 168 ASP   A OD2 1 
ATOM   1119 N N   . VAL   A 1 151 ? 6.261   -43.604 46.107 1.00 69.24  ? 169 VAL   A N   1 
ATOM   1120 C CA  . VAL   A 1 151 ? 6.871   -44.848 46.564 1.00 74.06  ? 169 VAL   A CA  1 
ATOM   1121 C C   . VAL   A 1 151 ? 8.000   -44.563 47.544 1.00 75.48  ? 169 VAL   A C   1 
ATOM   1122 O O   . VAL   A 1 151 ? 8.163   -45.268 48.548 1.00 62.10  ? 169 VAL   A O   1 
ATOM   1123 C CB  . VAL   A 1 151 ? 7.366   -45.668 45.358 1.00 67.80  ? 169 VAL   A CB  1 
ATOM   1124 C CG1 . VAL   A 1 151 ? 8.342   -46.740 45.805 1.00 64.88  ? 169 VAL   A CG1 1 
ATOM   1125 C CG2 . VAL   A 1 151 ? 6.189   -46.290 44.624 1.00 69.60  ? 169 VAL   A CG2 1 
ATOM   1126 N N   . TYR   A 1 152 ? 8.796   -43.529 47.271 1.00 72.69  ? 170 TYR   A N   1 
ATOM   1127 C CA  . TYR   A 1 152 ? 10.036  -43.326 48.008 1.00 73.24  ? 170 TYR   A CA  1 
ATOM   1128 C C   . TYR   A 1 152 ? 9.954   -42.272 49.102 1.00 75.01  ? 170 TYR   A C   1 
ATOM   1129 O O   . TYR   A 1 152 ? 10.761  -42.322 50.037 1.00 76.16  ? 170 TYR   A O   1 
ATOM   1130 C CB  . TYR   A 1 152 ? 11.160  -42.940 47.043 1.00 73.75  ? 170 TYR   A CB  1 
ATOM   1131 C CG  . TYR   A 1 152 ? 11.682  -44.101 46.232 1.00 72.49  ? 170 TYR   A CG  1 
ATOM   1132 C CD1 . TYR   A 1 152 ? 12.693  -44.914 46.724 1.00 68.35  ? 170 TYR   A CD1 1 
ATOM   1133 C CD2 . TYR   A 1 152 ? 11.161  -44.389 44.978 1.00 81.29  ? 170 TYR   A CD2 1 
ATOM   1134 C CE1 . TYR   A 1 152 ? 13.172  -45.980 45.992 1.00 71.45  ? 170 TYR   A CE1 1 
ATOM   1135 C CE2 . TYR   A 1 152 ? 11.635  -45.452 44.237 1.00 83.10  ? 170 TYR   A CE2 1 
ATOM   1136 C CZ  . TYR   A 1 152 ? 12.640  -46.244 44.749 1.00 75.88  ? 170 TYR   A CZ  1 
ATOM   1137 O OH  . TYR   A 1 152 ? 13.114  -47.305 44.012 1.00 82.24  ? 170 TYR   A OH  1 
ATOM   1138 N N   . LEU   A 1 153 ? 9.014   -41.328 49.025 1.00 90.45  ? 171 LEU   A N   1 
ATOM   1139 C CA  . LEU   A 1 153 ? 9.032   -40.178 49.918 1.00 92.49  ? 171 LEU   A CA  1 
ATOM   1140 C C   . LEU   A 1 153 ? 7.684   -39.860 50.550 1.00 85.55  ? 171 LEU   A C   1 
ATOM   1141 O O   . LEU   A 1 153 ? 7.540   -38.786 51.144 1.00 82.90  ? 171 LEU   A O   1 
ATOM   1142 C CB  . LEU   A 1 153 ? 9.536   -38.937 49.171 1.00 80.96  ? 171 LEU   A CB  1 
ATOM   1143 C CG  . LEU   A 1 153 ? 11.020  -38.951 48.809 1.00 97.17  ? 171 LEU   A CG  1 
ATOM   1144 C CD1 . LEU   A 1 153 ? 11.223  -39.393 47.369 1.00 80.77  ? 171 LEU   A CD1 1 
ATOM   1145 C CD2 . LEU   A 1 153 ? 11.628  -37.583 49.054 1.00 89.04  ? 171 LEU   A CD2 1 
ATOM   1146 N N   . ARG   A 1 154 ? 6.695   -40.751 50.460 1.00 72.40  ? 172 ARG   A N   1 
ATOM   1147 C CA  . ARG   A 1 154 ? 5.401   -40.423 51.047 1.00 73.66  ? 172 ARG   A CA  1 
ATOM   1148 C C   . ARG   A 1 154 ? 5.532   -40.180 52.544 1.00 77.31  ? 172 ARG   A C   1 
ATOM   1149 O O   . ARG   A 1 154 ? 4.901   -39.268 53.090 1.00 95.22  ? 172 ARG   A O   1 
ATOM   1150 C CB  . ARG   A 1 154 ? 4.379   -41.526 50.786 1.00 71.44  ? 172 ARG   A CB  1 
ATOM   1151 C CG  . ARG   A 1 154 ? 2.959   -41.060 51.091 1.00 96.57  ? 172 ARG   A CG  1 
ATOM   1152 C CD  . ARG   A 1 154 ? 2.034   -42.191 51.478 1.00 79.47  ? 172 ARG   A CD  1 
ATOM   1153 N NE  . ARG   A 1 154 ? 1.504   -42.877 50.308 1.00 98.91  ? 172 ARG   A NE  1 
ATOM   1154 C CZ  . ARG   A 1 154 ? 0.427   -42.492 49.637 1.00 84.40  ? 172 ARG   A CZ  1 
ATOM   1155 N NH1 . ARG   A 1 154 ? -0.259  -41.415 49.987 1.00 73.63  ? 172 ARG   A NH1 1 
ATOM   1156 N NH2 . ARG   A 1 154 ? 0.028   -43.204 48.588 1.00 105.46 ? 172 ARG   A NH2 1 
ATOM   1157 N N   . ASN   A 1 155 ? 6.343   -40.987 53.224 1.00 79.32  ? 173 ASN   A N   1 
ATOM   1158 C CA  . ASN   A 1 155 ? 6.498   -40.852 54.665 1.00 76.40  ? 173 ASN   A CA  1 
ATOM   1159 C C   . ASN   A 1 155 ? 7.380   -39.675 55.059 1.00 89.21  ? 173 ASN   A C   1 
ATOM   1160 O O   . ASN   A 1 155 ? 7.347   -39.260 56.222 1.00 97.79  ? 173 ASN   A O   1 
ATOM   1161 C CB  . ASN   A 1 155 ? 7.070   -42.147 55.246 1.00 111.37 ? 173 ASN   A CB  1 
ATOM   1162 C CG  . ASN   A 1 155 ? 6.129   -43.321 55.075 1.00 107.24 ? 173 ASN   A CG  1 
ATOM   1163 O OD1 . ASN   A 1 155 ? 4.911   -43.150 55.037 1.00 83.52  ? 173 ASN   A OD1 1 
ATOM   1164 N ND2 . ASN   A 1 155 ? 6.688   -44.522 54.971 1.00 119.83 ? 173 ASN   A ND2 1 
ATOM   1165 N N   . ASP   A 1 156 ? 8.162   -39.131 54.130 1.00 90.10  ? 174 ASP   A N   1 
ATOM   1166 C CA  . ASP   A 1 156 ? 9.019   -38.001 54.455 1.00 93.98  ? 174 ASP   A CA  1 
ATOM   1167 C C   . ASP   A 1 156 ? 8.178   -36.750 54.693 1.00 92.70  ? 174 ASP   A C   1 
ATOM   1168 O O   . ASP   A 1 156 ? 7.112   -36.565 54.099 1.00 83.19  ? 174 ASP   A O   1 
ATOM   1169 C CB  . ASP   A 1 156 ? 10.034  -37.756 53.338 1.00 92.41  ? 174 ASP   A CB  1 
ATOM   1170 C CG  . ASP   A 1 156 ? 11.163  -36.830 53.767 1.00 100.95 ? 174 ASP   A CG  1 
ATOM   1171 O OD1 . ASP   A 1 156 ? 10.894  -35.855 54.502 1.00 125.50 ? 174 ASP   A OD1 1 
ATOM   1172 O OD2 . ASP   A 1 156 ? 12.323  -37.080 53.374 1.00 81.32  ? 174 ASP   A OD2 1 
ATOM   1173 N N   . ASN   A 1 157 ? 8.676   -35.882 55.577 1.00 100.52 ? 175 ASN   A N   1 
ATOM   1174 C CA  . ASN   A 1 157 ? 7.908   -34.716 55.996 1.00 95.44  ? 175 ASN   A CA  1 
ATOM   1175 C C   . ASN   A 1 157 ? 7.677   -33.723 54.865 1.00 86.20  ? 175 ASN   A C   1 
ATOM   1176 O O   . ASN   A 1 157 ? 6.810   -32.852 54.993 1.00 93.22  ? 175 ASN   A O   1 
ATOM   1177 C CB  . ASN   A 1 157 ? 8.615   -34.012 57.156 1.00 95.10  ? 175 ASN   A CB  1 
ATOM   1178 C CG  . ASN   A 1 157 ? 8.822   -34.923 58.351 1.00 127.01 ? 175 ASN   A CG  1 
ATOM   1179 O OD1 . ASN   A 1 157 ? 7.942   -35.058 59.202 1.00 129.00 ? 175 ASN   A OD1 1 
ATOM   1180 N ND2 . ASN   A 1 157 ? 9.989   -35.552 58.421 1.00 125.87 ? 175 ASN   A ND2 1 
ATOM   1181 N N   . CYS   A 1 158 ? 8.423   -33.829 53.765 1.00 77.59  ? 176 CYS   A N   1 
ATOM   1182 C CA  . CYS   A 1 158 ? 8.331   -32.876 52.667 1.00 84.93  ? 176 CYS   A CA  1 
ATOM   1183 C C   . CYS   A 1 158 ? 7.664   -33.473 51.432 1.00 73.62  ? 176 CYS   A C   1 
ATOM   1184 O O   . CYS   A 1 158 ? 7.881   -32.984 50.319 1.00 71.86  ? 176 CYS   A O   1 
ATOM   1185 C CB  . CYS   A 1 158 ? 9.722   -32.352 52.309 1.00 89.84  ? 176 CYS   A CB  1 
ATOM   1186 S SG  . CYS   A 1 158 ? 10.798  -33.587 51.559 1.00 67.77  ? 176 CYS   A SG  1 
ATOM   1187 N N   . TYR   A 1 159 ? 6.855   -34.520 51.605 1.00 73.82  ? 177 TYR   A N   1 
ATOM   1188 C CA  . TYR   A 1 159 ? 6.227   -35.168 50.458 1.00 75.16  ? 177 TYR   A CA  1 
ATOM   1189 C C   . TYR   A 1 159 ? 5.288   -34.211 49.731 1.00 70.14  ? 177 TYR   A C   1 
ATOM   1190 O O   . TYR   A 1 159 ? 5.365   -34.053 48.503 1.00 64.44  ? 177 TYR   A O   1 
ATOM   1191 C CB  . TYR   A 1 159 ? 5.474   -36.417 50.917 1.00 69.01  ? 177 TYR   A CB  1 
ATOM   1192 C CG  . TYR   A 1 159 ? 4.781   -37.160 49.799 1.00 72.04  ? 177 TYR   A CG  1 
ATOM   1193 C CD1 . TYR   A 1 159 ? 5.501   -37.673 48.730 1.00 71.68  ? 177 TYR   A CD1 1 
ATOM   1194 C CD2 . TYR   A 1 159 ? 3.409   -37.369 49.823 1.00 66.81  ? 177 TYR   A CD2 1 
ATOM   1195 C CE1 . TYR   A 1 159 ? 4.874   -38.354 47.709 1.00 61.77  ? 177 TYR   A CE1 1 
ATOM   1196 C CE2 . TYR   A 1 159 ? 2.774   -38.053 48.805 1.00 69.42  ? 177 TYR   A CE2 1 
ATOM   1197 C CZ  . TYR   A 1 159 ? 3.512   -38.543 47.752 1.00 61.00  ? 177 TYR   A CZ  1 
ATOM   1198 O OH  . TYR   A 1 159 ? 2.883   -39.222 46.734 1.00 81.78  ? 177 TYR   A OH  1 
ATOM   1199 N N   . LEU   A 1 160 ? 4.395   -33.555 50.478 1.00 58.98  ? 178 LEU   A N   1 
ATOM   1200 C CA  . LEU   A 1 160 ? 3.451   -32.633 49.856 1.00 59.51  ? 178 LEU   A CA  1 
ATOM   1201 C C   . LEU   A 1 160 ? 4.170   -31.446 49.238 1.00 72.22  ? 178 LEU   A C   1 
ATOM   1202 O O   . LEU   A 1 160 ? 3.817   -31.003 48.138 1.00 67.98  ? 178 LEU   A O   1 
ATOM   1203 C CB  . LEU   A 1 160 ? 2.422   -32.156 50.877 1.00 64.08  ? 178 LEU   A CB  1 
ATOM   1204 C CG  . LEU   A 1 160 ? 1.604   -33.237 51.583 1.00 82.73  ? 178 LEU   A CG  1 
ATOM   1205 C CD1 . LEU   A 1 160 ? 0.284   -32.640 52.055 1.00 92.53  ? 178 LEU   A CD1 1 
ATOM   1206 C CD2 . LEU   A 1 160 ? 1.360   -34.460 50.705 1.00 93.62  ? 178 LEU   A CD2 1 
ATOM   1207 N N   . ASP   A 1 161 ? 5.183   -30.919 49.928 1.00 72.38  ? 179 ASP   A N   1 
ATOM   1208 C CA  . ASP   A 1 161 ? 5.948   -29.811 49.374 1.00 65.96  ? 179 ASP   A CA  1 
ATOM   1209 C C   . ASP   A 1 161 ? 6.566   -30.196 48.038 1.00 59.84  ? 179 ASP   A C   1 
ATOM   1210 O O   . ASP   A 1 161 ? 6.511   -29.426 47.075 1.00 67.75  ? 179 ASP   A O   1 
ATOM   1211 C CB  . ASP   A 1 161 ? 7.032   -29.376 50.359 1.00 86.28  ? 179 ASP   A CB  1 
ATOM   1212 C CG  . ASP   A 1 161 ? 6.475   -29.047 51.730 1.00 102.01 ? 179 ASP   A CG  1 
ATOM   1213 O OD1 . ASP   A 1 161 ? 5.280   -28.691 51.819 1.00 105.63 ? 179 ASP   A OD1 1 
ATOM   1214 O OD2 . ASP   A 1 161 ? 7.233   -29.145 52.719 1.00 113.82 ? 179 ASP   A OD2 1 
ATOM   1215 N N   . LEU   A 1 162 ? 7.142   -31.394 47.955 1.00 66.72  ? 180 LEU   A N   1 
ATOM   1216 C CA  . LEU   A 1 162 ? 7.795   -31.814 46.721 1.00 64.14  ? 180 LEU   A CA  1 
ATOM   1217 C C   . LEU   A 1 162 ? 6.785   -32.010 45.597 1.00 69.70  ? 180 LEU   A C   1 
ATOM   1218 O O   . LEU   A 1 162 ? 6.994   -31.534 44.473 1.00 70.33  ? 180 LEU   A O   1 
ATOM   1219 C CB  . LEU   A 1 162 ? 8.589   -33.094 46.969 1.00 63.65  ? 180 LEU   A CB  1 
ATOM   1220 C CG  . LEU   A 1 162 ? 9.848   -32.893 47.814 1.00 60.12  ? 180 LEU   A CG  1 
ATOM   1221 C CD1 . LEU   A 1 162 ? 10.397  -34.224 48.289 1.00 76.51  ? 180 LEU   A CD1 1 
ATOM   1222 C CD2 . LEU   A 1 162 ? 10.900  -32.126 47.018 1.00 69.08  ? 180 LEU   A CD2 1 
ATOM   1223 N N   . ILE   A 1 163 ? 5.685   -32.714 45.872 1.00 61.42  ? 181 ILE   A N   1 
ATOM   1224 C CA  . ILE   A 1 163 ? 4.719   -32.963 44.805 1.00 65.31  ? 181 ILE   A CA  1 
ATOM   1225 C C   . ILE   A 1 163 ? 4.101   -31.652 44.334 1.00 62.60  ? 181 ILE   A C   1 
ATOM   1226 O O   . ILE   A 1 163 ? 3.850   -31.465 43.138 1.00 62.17  ? 181 ILE   A O   1 
ATOM   1227 C CB  . ILE   A 1 163 ? 3.644   -33.975 45.248 1.00 57.67  ? 181 ILE   A CB  1 
ATOM   1228 C CG1 . ILE   A 1 163 ? 2.883   -33.468 46.471 1.00 70.49  ? 181 ILE   A CG1 1 
ATOM   1229 C CG2 . ILE   A 1 163 ? 4.276   -35.332 45.531 1.00 73.85  ? 181 ILE   A CG2 1 
ATOM   1230 C CD1 . ILE   A 1 163 ? 1.873   -34.466 47.017 1.00 72.79  ? 181 ILE   A CD1 1 
ATOM   1231 N N   . THR   A 1 164 ? 3.871   -30.709 45.252 1.00 65.50  ? 182 THR   A N   1 
ATOM   1232 C CA  . THR   A 1 164 ? 3.308   -29.428 44.838 1.00 70.71  ? 182 THR   A CA  1 
ATOM   1233 C C   . THR   A 1 164 ? 4.330   -28.577 44.092 1.00 65.71  ? 182 THR   A C   1 
ATOM   1234 O O   . THR   A 1 164 ? 3.960   -27.824 43.181 1.00 66.04  ? 182 THR   A O   1 
ATOM   1235 C CB  . THR   A 1 164 ? 2.757   -28.678 46.051 1.00 67.74  ? 182 THR   A CB  1 
ATOM   1236 O OG1 . THR   A 1 164 ? 3.788   -28.512 47.030 1.00 86.79  ? 182 THR   A OG1 1 
ATOM   1237 C CG2 . THR   A 1 164 ? 1.593   -29.449 46.664 1.00 79.49  ? 182 THR   A CG2 1 
ATOM   1238 N N   . SER   A 1 165 ? 5.610   -28.682 44.451 1.00 62.17  ? 183 SER   A N   1 
ATOM   1239 C CA  . SER   A 1 165 ? 6.645   -28.027 43.663 1.00 63.50  ? 183 SER   A CA  1 
ATOM   1240 C C   . SER   A 1 165 ? 6.637   -28.548 42.235 1.00 51.60  ? 183 SER   A C   1 
ATOM   1241 O O   . SER   A 1 165 ? 6.715   -27.768 41.278 1.00 63.92  ? 183 SER   A O   1 
ATOM   1242 C CB  . SER   A 1 165 ? 8.011   -28.254 44.308 1.00 57.36  ? 183 SER   A CB  1 
ATOM   1243 O OG  . SER   A 1 165 ? 7.993   -27.887 45.676 1.00 77.48  ? 183 SER   A OG  1 
ATOM   1244 N N   . PHE   A 1 166 ? 6.535   -29.868 42.076 1.00 62.47  ? 184 PHE   A N   1 
ATOM   1245 C CA  . PHE   A 1 166 ? 6.438   -30.439 40.737 1.00 59.56  ? 184 PHE   A CA  1 
ATOM   1246 C C   . PHE   A 1 166 ? 5.191   -29.939 40.016 1.00 64.84  ? 184 PHE   A C   1 
ATOM   1247 O O   . PHE   A 1 166 ? 5.250   -29.585 38.832 1.00 61.66  ? 184 PHE   A O   1 
ATOM   1248 C CB  . PHE   A 1 166 ? 6.441   -31.966 40.819 1.00 74.09  ? 184 PHE   A CB  1 
ATOM   1249 C CG  . PHE   A 1 166 ? 7.819   -32.566 40.893 1.00 66.97  ? 184 PHE   A CG  1 
ATOM   1250 C CD1 . PHE   A 1 166 ? 8.541   -32.538 42.074 1.00 54.59  ? 184 PHE   A CD1 1 
ATOM   1251 C CD2 . PHE   A 1 166 ? 8.389   -33.165 39.781 1.00 61.91  ? 184 PHE   A CD2 1 
ATOM   1252 C CE1 . PHE   A 1 166 ? 9.806   -33.089 42.144 1.00 55.97  ? 184 PHE   A CE1 1 
ATOM   1253 C CE2 . PHE   A 1 166 ? 9.654   -33.719 39.846 1.00 60.40  ? 184 PHE   A CE2 1 
ATOM   1254 C CZ  . PHE   A 1 166 ? 10.363  -33.681 41.029 1.00 62.05  ? 184 PHE   A CZ  1 
ATOM   1255 N N   . ARG   A 1 167 ? 4.054   -29.899 40.716 1.00 69.29  ? 185 ARG   A N   1 
ATOM   1256 C CA  . ARG   A 1 167 ? 2.823   -29.385 40.121 1.00 70.45  ? 185 ARG   A CA  1 
ATOM   1257 C C   . ARG   A 1 167 ? 3.030   -27.986 39.556 1.00 80.01  ? 185 ARG   A C   1 
ATOM   1258 O O   . ARG   A 1 167 ? 2.718   -27.716 38.390 1.00 91.20  ? 185 ARG   A O   1 
ATOM   1259 C CB  . ARG   A 1 167 ? 1.703   -29.356 41.167 1.00 72.26  ? 185 ARG   A CB  1 
ATOM   1260 C CG  . ARG   A 1 167 ? 0.992   -30.675 41.402 1.00 90.90  ? 185 ARG   A CG  1 
ATOM   1261 C CD  . ARG   A 1 167 ? 0.267   -30.700 42.753 1.00 113.94 ? 185 ARG   A CD  1 
ATOM   1262 N NE  . ARG   A 1 167 ? -0.796  -29.707 42.888 1.00 94.22  ? 185 ARG   A NE  1 
ATOM   1263 C CZ  . ARG   A 1 167 ? -0.651  -28.498 43.420 1.00 93.32  ? 185 ARG   A CZ  1 
ATOM   1264 N NH1 . ARG   A 1 167 ? 0.530   -28.037 43.790 1.00 98.70  ? 185 ARG   A NH1 1 
ATOM   1265 N NH2 . ARG   A 1 167 ? -1.724  -27.733 43.592 1.00 101.01 ? 185 ARG   A NH2 1 
ATOM   1266 N N   . GLU   A 1 168 ? 3.553   -27.076 40.382 1.00 63.35  ? 186 GLU   A N   1 
ATOM   1267 C CA  . GLU   A 1 168 ? 3.684   -25.686 39.959 1.00 62.66  ? 186 GLU   A CA  1 
ATOM   1268 C C   . GLU   A 1 168 ? 4.712   -25.537 38.846 1.00 64.97  ? 186 GLU   A C   1 
ATOM   1269 O O   . GLU   A 1 168 ? 4.495   -24.777 37.892 1.00 81.29  ? 186 GLU   A O   1 
ATOM   1270 C CB  . GLU   A 1 168 ? 4.052   -24.804 41.151 1.00 77.17  ? 186 GLU   A CB  1 
ATOM   1271 C CG  . GLU   A 1 168 ? 2.881   -24.493 42.069 1.00 83.40  ? 186 GLU   A CG  1 
ATOM   1272 C CD  . GLU   A 1 168 ? 1.744   -23.793 41.346 1.00 101.85 ? 186 GLU   A CD  1 
ATOM   1273 O OE1 . GLU   A 1 168 ? 1.985   -23.232 40.253 1.00 85.64  ? 186 GLU   A OE1 1 
ATOM   1274 O OE2 . GLU   A 1 168 ? 0.609   -23.810 41.869 1.00 95.51  ? 186 GLU   A OE2 1 
ATOM   1275 N N   . ALA   A 1 169 ? 5.842   -26.238 38.951 1.00 60.73  ? 187 ALA   A N   1 
ATOM   1276 C CA  . ALA   A 1 169 ? 6.839   -26.165 37.892 1.00 63.47  ? 187 ALA   A CA  1 
ATOM   1277 C C   . ALA   A 1 169 ? 6.255   -26.638 36.570 1.00 78.95  ? 187 ALA   A C   1 
ATOM   1278 O O   . ALA   A 1 169 ? 6.459   -26.002 35.529 1.00 89.23  ? 187 ALA   A O   1 
ATOM   1279 C CB  . ALA   A 1 169 ? 8.065   -26.995 38.269 1.00 88.43  ? 187 ALA   A CB  1 
ATOM   1280 N N   . THR   A 1 170 ? 5.507   -27.744 36.594 1.00 88.01  ? 188 THR   A N   1 
ATOM   1281 C CA  . THR   A 1 170 ? 4.895   -28.242 35.369 1.00 89.85  ? 188 THR   A CA  1 
ATOM   1282 C C   . THR   A 1 170 ? 3.862   -27.263 34.826 1.00 91.66  ? 188 THR   A C   1 
ATOM   1283 O O   . THR   A 1 170 ? 3.787   -27.048 33.613 1.00 93.65  ? 188 THR   A O   1 
ATOM   1284 C CB  . THR   A 1 170 ? 4.257   -29.607 35.620 1.00 84.07  ? 188 THR   A CB  1 
ATOM   1285 O OG1 . THR   A 1 170 ? 5.231   -30.495 36.183 1.00 74.54  ? 188 THR   A OG1 1 
ATOM   1286 C CG2 . THR   A 1 170 ? 3.731   -30.198 34.319 1.00 103.95 ? 188 THR   A CG2 1 
ATOM   1287 N N   . LEU   A 1 171 ? 3.046   -26.671 35.701 1.00 95.91  ? 189 LEU   A N   1 
ATOM   1288 C CA  . LEU   A 1 171 ? 2.041   -25.718 35.235 1.00 82.09  ? 189 LEU   A CA  1 
ATOM   1289 C C   . LEU   A 1 171 ? 2.697   -24.522 34.558 1.00 78.79  ? 189 LEU   A C   1 
ATOM   1290 O O   . LEU   A 1 171 ? 2.277   -24.093 33.476 1.00 97.84  ? 189 LEU   A O   1 
ATOM   1291 C CB  . LEU   A 1 171 ? 1.173   -25.250 36.404 1.00 88.80  ? 189 LEU   A CB  1 
ATOM   1292 C CG  . LEU   A 1 171 ? -0.209  -25.887 36.536 1.00 125.51 ? 189 LEU   A CG  1 
ATOM   1293 C CD1 . LEU   A 1 171 ? -0.863  -25.460 37.839 1.00 105.32 ? 189 LEU   A CD1 1 
ATOM   1294 C CD2 . LEU   A 1 171 ? -1.083  -25.508 35.352 1.00 105.02 ? 189 LEU   A CD2 1 
ATOM   1295 N N   . LYS   A 1 172 ? 3.726   -23.962 35.192 1.00 85.45  ? 190 LYS   A N   1 
ATOM   1296 C CA  . LYS   A 1 172 ? 4.396   -22.806 34.610 1.00 73.65  ? 190 LYS   A CA  1 
ATOM   1297 C C   . LYS   A 1 172 ? 5.095   -23.175 33.308 1.00 78.32  ? 190 LYS   A C   1 
ATOM   1298 O O   . LYS   A 1 172 ? 5.080   -22.395 32.350 1.00 80.94  ? 190 LYS   A O   1 
ATOM   1299 C CB  . LYS   A 1 172 ? 5.374   -22.210 35.619 1.00 64.90  ? 190 LYS   A CB  1 
ATOM   1300 C CG  . LYS   A 1 172 ? 4.672   -21.468 36.747 1.00 89.76  ? 190 LYS   A CG  1 
ATOM   1301 C CD  . LYS   A 1 172 ? 5.647   -20.918 37.769 1.00 72.33  ? 190 LYS   A CD  1 
ATOM   1302 C CE  . LYS   A 1 172 ? 4.929   -20.082 38.821 1.00 74.15  ? 190 LYS   A CE  1 
ATOM   1303 N NZ  . LYS   A 1 172 ? 3.809   -20.823 39.471 1.00 89.32  ? 190 LYS   A NZ  1 
ATOM   1304 N N   . THR   A 1 173 ? 5.700   -24.364 33.245 1.00 92.50  ? 191 THR   A N   1 
ATOM   1305 C CA  . THR   A 1 173 ? 6.320   -24.805 32.000 1.00 81.47  ? 191 THR   A CA  1 
ATOM   1306 C C   . THR   A 1 173 ? 5.281   -24.975 30.899 1.00 77.53  ? 191 THR   A C   1 
ATOM   1307 O O   . THR   A 1 173 ? 5.535   -24.642 29.737 1.00 80.93  ? 191 THR   A O   1 
ATOM   1308 C CB  . THR   A 1 173 ? 7.080   -26.111 32.229 1.00 74.95  ? 191 THR   A CB  1 
ATOM   1309 O OG1 . THR   A 1 173 ? 8.105   -25.905 33.210 1.00 77.13  ? 191 THR   A OG1 1 
ATOM   1310 C CG2 . THR   A 1 173 ? 7.713   -26.594 30.935 1.00 81.66  ? 191 THR   A CG2 1 
ATOM   1311 N N   . ILE   A 1 174 ? 4.104   -25.496 31.244 1.00 83.26  ? 192 ILE   A N   1 
ATOM   1312 C CA  . ILE   A 1 174 ? 3.043   -25.668 30.258 1.00 89.28  ? 192 ILE   A CA  1 
ATOM   1313 C C   . ILE   A 1 174 ? 2.580   -24.316 29.734 1.00 89.19  ? 192 ILE   A C   1 
ATOM   1314 O O   . ILE   A 1 174 ? 2.393   -24.130 28.525 1.00 97.10  ? 192 ILE   A O   1 
ATOM   1315 C CB  . ILE   A 1 174 ? 1.882   -26.469 30.876 1.00 92.13  ? 192 ILE   A CB  1 
ATOM   1316 C CG1 . ILE   A 1 174 ? 2.247   -27.953 30.926 1.00 84.89  ? 192 ILE   A CG1 1 
ATOM   1317 C CG2 . ILE   A 1 174 ? 0.591   -26.239 30.100 1.00 90.52  ? 192 ILE   A CG2 1 
ATOM   1318 C CD1 . ILE   A 1 174 ? 1.249   -28.805 31.669 1.00 107.24 ? 192 ILE   A CD1 1 
ATOM   1319 N N   . VAL   A 1 175 ? 2.378   -23.354 30.635 1.00 90.61  ? 193 VAL   A N   1 
ATOM   1320 C CA  . VAL   A 1 175 ? 1.965   -22.020 30.208 1.00 86.14  ? 193 VAL   A CA  1 
ATOM   1321 C C   . VAL   A 1 175 ? 3.038   -21.392 29.326 1.00 80.58  ? 193 VAL   A C   1 
ATOM   1322 O O   . VAL   A 1 175 ? 2.736   -20.760 28.305 1.00 84.11  ? 193 VAL   A O   1 
ATOM   1323 C CB  . VAL   A 1 175 ? 1.649   -21.142 31.433 1.00 95.73  ? 193 VAL   A CB  1 
ATOM   1324 C CG1 . VAL   A 1 175 ? 1.384   -19.706 31.008 1.00 81.47  ? 193 VAL   A CG1 1 
ATOM   1325 C CG2 . VAL   A 1 175 ? 0.457   -21.706 32.189 1.00 69.48  ? 193 VAL   A CG2 1 
ATOM   1326 N N   . GLY   A 1 176 ? 4.306   -21.555 29.705 1.00 89.25  ? 194 GLY   A N   1 
ATOM   1327 C CA  . GLY   A 1 176 ? 5.384   -21.010 28.900 1.00 81.06  ? 194 GLY   A CA  1 
ATOM   1328 C C   . GLY   A 1 176 ? 5.456   -21.634 27.521 1.00 88.61  ? 194 GLY   A C   1 
ATOM   1329 O O   . GLY   A 1 176 ? 5.707   -20.946 26.532 1.00 101.64 ? 194 GLY   A O   1 
ATOM   1330 N N   . GLN   A 1 177 ? 5.256   -22.950 27.437 1.00 95.93  ? 195 GLN   A N   1 
ATOM   1331 C CA  . GLN   A 1 177 ? 5.243   -23.615 26.139 1.00 93.78  ? 195 GLN   A CA  1 
ATOM   1332 C C   . GLN   A 1 177 ? 4.077   -23.126 25.290 1.00 96.20  ? 195 GLN   A C   1 
ATOM   1333 O O   . GLN   A 1 177 ? 4.229   -22.880 24.087 1.00 108.28 ? 195 GLN   A O   1 
ATOM   1334 C CB  . GLN   A 1 177 ? 5.172   -25.129 26.336 1.00 90.56  ? 195 GLN   A CB  1 
ATOM   1335 C CG  . GLN   A 1 177 ? 5.326   -25.936 25.060 1.00 115.81 ? 195 GLN   A CG  1 
ATOM   1336 C CD  . GLN   A 1 177 ? 6.706   -25.803 24.444 1.00 123.05 ? 195 GLN   A CD  1 
ATOM   1337 O OE1 . GLN   A 1 177 ? 7.624   -25.264 25.061 1.00 112.88 ? 195 GLN   A OE1 1 
ATOM   1338 N NE2 . GLN   A 1 177 ? 6.859   -26.296 23.220 1.00 142.70 ? 195 GLN   A NE2 1 
ATOM   1339 N N   . HIS   A 1 178 ? 2.904   -22.969 25.906 1.00 97.50  ? 196 HIS   A N   1 
ATOM   1340 C CA  . HIS   A 1 178 ? 1.755   -22.428 25.191 1.00 91.19  ? 196 HIS   A CA  1 
ATOM   1341 C C   . HIS   A 1 178 ? 2.072   -21.054 24.617 1.00 93.48  ? 196 HIS   A C   1 
ATOM   1342 O O   . HIS   A 1 178 ? 1.775   -20.768 23.449 1.00 98.70  ? 196 HIS   A O   1 
ATOM   1343 C CB  . HIS   A 1 178 ? 0.555   -22.354 26.135 1.00 111.99 ? 196 HIS   A CB  1 
ATOM   1344 C CG  . HIS   A 1 178 ? -0.616  -21.616 25.569 1.00 98.43  ? 196 HIS   A CG  1 
ATOM   1345 N ND1 . HIS   A 1 178 ? -1.512  -22.198 24.699 1.00 98.61  ? 196 HIS   A ND1 1 
ATOM   1346 C CD2 . HIS   A 1 178 ? -1.041  -20.345 25.752 1.00 87.95  ? 196 HIS   A CD2 1 
ATOM   1347 C CE1 . HIS   A 1 178 ? -2.438  -21.316 24.369 1.00 88.13  ? 196 HIS   A CE1 1 
ATOM   1348 N NE2 . HIS   A 1 178 ? -2.175  -20.183 24.995 1.00 107.66 ? 196 HIS   A NE2 1 
ATOM   1349 N N   . LEU   A 1 179 ? 2.682   -20.188 25.429 1.00 109.03 ? 197 LEU   A N   1 
ATOM   1350 C CA  . LEU   A 1 179 ? 3.060   -18.863 24.949 1.00 87.63  ? 197 LEU   A CA  1 
ATOM   1351 C C   . LEU   A 1 179 ? 4.066   -18.962 23.809 1.00 89.99  ? 197 LEU   A C   1 
ATOM   1352 O O   . LEU   A 1 179 ? 3.895   -18.339 22.755 1.00 100.40 ? 197 LEU   A O   1 
ATOM   1353 C CB  . LEU   A 1 179 ? 3.635   -18.037 26.099 1.00 92.77  ? 197 LEU   A CB  1 
ATOM   1354 C CG  . LEU   A 1 179 ? 2.672   -17.678 27.232 1.00 107.25 ? 197 LEU   A CG  1 
ATOM   1355 C CD1 . LEU   A 1 179 ? 3.388   -16.854 28.293 1.00 108.27 ? 197 LEU   A CD1 1 
ATOM   1356 C CD2 . LEU   A 1 179 ? 1.466   -16.931 26.693 1.00 91.48  ? 197 LEU   A CD2 1 
ATOM   1357 N N   . ASP   A 1 180 ? 5.120   -19.758 24.000 1.00 98.37  ? 198 ASP   A N   1 
ATOM   1358 C CA  . ASP   A 1 180 ? 6.148   -19.900 22.976 1.00 102.18 ? 198 ASP   A CA  1 
ATOM   1359 C C   . ASP   A 1 180 ? 5.566   -20.418 21.671 1.00 94.10  ? 198 ASP   A C   1 
ATOM   1360 O O   . ASP   A 1 180 ? 6.125   -20.166 20.597 1.00 100.92 ? 198 ASP   A O   1 
ATOM   1361 C CB  . ASP   A 1 180 ? 7.248   -20.839 23.475 1.00 106.34 ? 198 ASP   A CB  1 
ATOM   1362 C CG  . ASP   A 1 180 ? 8.286   -21.139 22.414 1.00 130.48 ? 198 ASP   A CG  1 
ATOM   1363 O OD1 . ASP   A 1 180 ? 9.050   -20.221 22.048 1.00 133.21 ? 198 ASP   A OD1 1 
ATOM   1364 O OD2 . ASP   A 1 180 ? 8.341   -22.297 21.948 1.00 166.14 ? 198 ASP   A OD2 1 
ATOM   1365 N N   . THR   A 1 181 ? 4.451   -21.141 21.740 1.00 99.58  ? 199 THR   A N   1 
ATOM   1366 C CA  . THR   A 1 181 ? 3.873   -21.727 20.539 1.00 92.99  ? 199 THR   A CA  1 
ATOM   1367 C C   . THR   A 1 181 ? 2.862   -20.814 19.851 1.00 91.31  ? 199 THR   A C   1 
ATOM   1368 O O   . THR   A 1 181 ? 2.818   -20.773 18.617 1.00 94.39  ? 199 THR   A O   1 
ATOM   1369 C CB  . THR   A 1 181 ? 3.207   -23.063 20.883 1.00 140.35 ? 199 THR   A CB  1 
ATOM   1370 O OG1 . THR   A 1 181 ? 4.191   -23.977 21.387 1.00 137.06 ? 199 THR   A OG1 1 
ATOM   1371 C CG2 . THR   A 1 181 ? 2.545   -23.666 19.654 1.00 167.77 ? 199 THR   A CG2 1 
ATOM   1372 N N   . ASN   A 1 182 ? 2.047   -20.077 20.609 1.00 102.86 ? 200 ASN   A N   1 
ATOM   1373 C CA  . ASN   A 1 182 ? 0.865   -19.430 20.044 1.00 101.20 ? 200 ASN   A CA  1 
ATOM   1374 C C   . ASN   A 1 182 ? 0.895   -17.905 20.080 1.00 101.91 ? 200 ASN   A C   1 
ATOM   1375 O O   . ASN   A 1 182 ? -0.127  -17.278 19.779 1.00 108.08 ? 200 ASN   A O   1 
ATOM   1376 C CB  . ASN   A 1 182 ? -0.390  -19.921 20.773 1.00 101.71 ? 200 ASN   A CB  1 
ATOM   1377 C CG  . ASN   A 1 182 ? -0.598  -21.411 20.630 1.00 99.97  ? 200 ASN   A CG  1 
ATOM   1378 O OD1 . ASN   A 1 182 ? -1.201  -21.874 19.661 1.00 96.53  ? 200 ASN   A OD1 1 
ATOM   1379 N ND2 . ASN   A 1 182 ? -0.095  -22.174 21.594 1.00 103.67 ? 200 ASN   A ND2 1 
ATOM   1380 N N   . ILE   A 1 183 ? 2.023   -17.283 20.422 1.00 105.71 ? 201 ILE   A N   1 
ATOM   1381 C CA  . ILE   A 1 183 ? 2.019   -15.832 20.596 1.00 114.88 ? 201 ILE   A CA  1 
ATOM   1382 C C   . ILE   A 1 183 ? 1.859   -15.119 19.257 1.00 112.19 ? 201 ILE   A C   1 
ATOM   1383 O O   . ILE   A 1 183 ? 1.166   -14.098 19.166 1.00 107.28 ? 201 ILE   A O   1 
ATOM   1384 C CB  . ILE   A 1 183 ? 3.284   -15.379 21.346 1.00 96.73  ? 201 ILE   A CB  1 
ATOM   1385 C CG1 . ILE   A 1 183 ? 3.012   -15.428 22.851 1.00 115.55 ? 201 ILE   A CG1 1 
ATOM   1386 C CG2 . ILE   A 1 183 ? 3.696   -13.978 20.921 1.00 100.59 ? 201 ILE   A CG2 1 
ATOM   1387 C CD1 . ILE   A 1 183 ? 4.220   -15.217 23.715 1.00 127.05 ? 201 ILE   A CD1 1 
ATOM   1388 N N   . PHE   A 1 184 ? 2.495   -15.626 18.205 1.00 111.64 ? 202 PHE   A N   1 
ATOM   1389 C CA  . PHE   A 1 184 ? 2.377   -15.010 16.888 1.00 123.97 ? 202 PHE   A CA  1 
ATOM   1390 C C   . PHE   A 1 184 ? 1.132   -15.451 16.131 1.00 112.77 ? 202 PHE   A C   1 
ATOM   1391 O O   . PHE   A 1 184 ? 0.882   -14.936 15.036 1.00 120.96 ? 202 PHE   A O   1 
ATOM   1392 C CB  . PHE   A 1 184 ? 3.614   -15.325 16.040 1.00 131.81 ? 202 PHE   A CB  1 
ATOM   1393 C CG  . PHE   A 1 184 ? 4.858   -14.581 16.456 1.00 139.42 ? 202 PHE   A CG  1 
ATOM   1394 C CD1 . PHE   A 1 184 ? 4.783   -13.372 17.133 1.00 115.13 ? 202 PHE   A CD1 1 
ATOM   1395 C CD2 . PHE   A 1 184 ? 6.108   -15.093 16.156 1.00 136.19 ? 202 PHE   A CD2 1 
ATOM   1396 C CE1 . PHE   A 1 184 ? 5.928   -12.697 17.504 1.00 111.90 ? 202 PHE   A CE1 1 
ATOM   1397 C CE2 . PHE   A 1 184 ? 7.256   -14.421 16.525 1.00 143.72 ? 202 PHE   A CE2 1 
ATOM   1398 C CZ  . PHE   A 1 184 ? 7.165   -13.222 17.200 1.00 137.32 ? 202 PHE   A CZ  1 
ATOM   1399 N N   . SER   A 1 185 ? 0.347   -16.375 16.676 1.00 110.11 ? 203 SER   A N   1 
ATOM   1400 C CA  . SER   A 1 185 ? -0.815  -16.875 15.962 1.00 120.59 ? 203 SER   A CA  1 
ATOM   1401 C C   . SER   A 1 185 ? -1.854  -15.769 15.784 1.00 123.65 ? 203 SER   A C   1 
ATOM   1402 O O   . SER   A 1 185 ? -1.758  -14.681 16.359 1.00 119.80 ? 203 SER   A O   1 
ATOM   1403 C CB  . SER   A 1 185 ? -1.423  -18.062 16.704 1.00 114.78 ? 203 SER   A CB  1 
ATOM   1404 O OG  . SER   A 1 185 ? -1.777  -17.700 18.027 1.00 129.81 ? 203 SER   A OG  1 
ATOM   1405 N N   . ASP   A 1 186 ? -2.862  -16.065 14.961 1.00 127.73 ? 204 ASP   A N   1 
ATOM   1406 C CA  . ASP   A 1 186 ? -3.916  -15.090 14.702 1.00 131.83 ? 204 ASP   A CA  1 
ATOM   1407 C C   . ASP   A 1 186 ? -4.710  -14.782 15.966 1.00 128.70 ? 204 ASP   A C   1 
ATOM   1408 O O   . ASP   A 1 186 ? -5.091  -13.629 16.202 1.00 134.83 ? 204 ASP   A O   1 
ATOM   1409 C CB  . ASP   A 1 186 ? -4.843  -15.603 13.599 1.00 135.64 ? 204 ASP   A CB  1 
ATOM   1410 C CG  . ASP   A 1 186 ? -4.144  -15.723 12.255 1.00 152.83 ? 204 ASP   A CG  1 
ATOM   1411 O OD1 . ASP   A 1 186 ? -2.918  -15.492 12.195 1.00 149.43 ? 204 ASP   A OD1 1 
ATOM   1412 O OD2 . ASP   A 1 186 ? -4.824  -16.046 11.257 1.00 160.25 ? 204 ASP   A OD2 1 
ATOM   1413 N N   . LYS   A 1 187 ? -4.965  -15.797 16.796 1.00 126.24 ? 205 LYS   A N   1 
ATOM   1414 C CA  . LYS   A 1 187 ? -5.799  -15.593 17.977 1.00 134.27 ? 205 LYS   A CA  1 
ATOM   1415 C C   . LYS   A 1 187 ? -5.188  -14.557 18.913 1.00 135.22 ? 205 LYS   A C   1 
ATOM   1416 O O   . LYS   A 1 187 ? -5.903  -13.730 19.490 1.00 122.11 ? 205 LYS   A O   1 
ATOM   1417 C CB  . LYS   A 1 187 ? -6.009  -16.921 18.710 1.00 131.76 ? 205 LYS   A CB  1 
ATOM   1418 C CG  . LYS   A 1 187 ? -4.887  -17.305 19.675 1.00 133.27 ? 205 LYS   A CG  1 
ATOM   1419 C CD  . LYS   A 1 187 ? -5.111  -18.678 20.297 1.00 118.85 ? 205 LYS   A CD  1 
ATOM   1420 C CE  . LYS   A 1 187 ? -4.899  -19.801 19.294 1.00 140.28 ? 205 LYS   A CE  1 
ATOM   1421 N NZ  . LYS   A 1 187 ? -3.514  -19.829 18.753 1.00 120.26 ? 205 LYS   A NZ  1 
ATOM   1422 N N   . TYR   A 1 188 ? -3.864  -14.584 19.071 1.00 128.76 ? 206 TYR   A N   1 
ATOM   1423 C CA  . TYR   A 1 188 ? -3.194  -13.669 19.985 1.00 121.70 ? 206 TYR   A CA  1 
ATOM   1424 C C   . TYR   A 1 188 ? -3.183  -12.233 19.483 1.00 123.34 ? 206 TYR   A C   1 
ATOM   1425 O O   . TYR   A 1 188 ? -2.732  -11.346 20.215 1.00 129.27 ? 206 TYR   A O   1 
ATOM   1426 C CB  . TYR   A 1 188 ? -1.762  -14.142 20.235 1.00 124.56 ? 206 TYR   A CB  1 
ATOM   1427 C CG  . TYR   A 1 188 ? -1.629  -14.972 21.488 1.00 113.73 ? 206 TYR   A CG  1 
ATOM   1428 C CD1 . TYR   A 1 188 ? -2.163  -16.252 21.555 1.00 111.29 ? 206 TYR   A CD1 1 
ATOM   1429 C CD2 . TYR   A 1 188 ? -0.984  -14.472 22.610 1.00 110.15 ? 206 TYR   A CD2 1 
ATOM   1430 C CE1 . TYR   A 1 188 ? -2.050  -17.013 22.700 1.00 118.96 ? 206 TYR   A CE1 1 
ATOM   1431 C CE2 . TYR   A 1 188 ? -0.867  -15.225 23.760 1.00 112.65 ? 206 TYR   A CE2 1 
ATOM   1432 C CZ  . TYR   A 1 188 ? -1.401  -16.494 23.799 1.00 110.92 ? 206 TYR   A CZ  1 
ATOM   1433 O OH  . TYR   A 1 188 ? -1.289  -17.247 24.943 1.00 102.22 ? 206 TYR   A OH  1 
ATOM   1434 N N   . SER   A 1 189 ? -3.659  -11.984 18.270 1.00 172.37 ? 207 SER   A N   1 
ATOM   1435 C CA  . SER   A 1 189 ? -3.680  -10.647 17.695 1.00 170.65 ? 207 SER   A CA  1 
ATOM   1436 C C   . SER   A 1 189 ? -5.056  -10.023 17.884 1.00 134.66 ? 207 SER   A C   1 
ATOM   1437 O O   . SER   A 1 189 ? -6.073  -10.628 17.529 1.00 174.44 ? 207 SER   A O   1 
ATOM   1438 C CB  . SER   A 1 189 ? -3.322  -10.698 16.209 1.00 157.12 ? 207 SER   A CB  1 
ATOM   1439 O OG  . SER   A 1 189 ? -2.078  -11.349 16.010 1.00 160.77 ? 207 SER   A OG  1 
ATOM   1440 N N   . HIS   A 1 190 ? -5.081  -8.820  18.453 1.00 151.99 ? 208 HIS   A N   1 
ATOM   1441 C CA  . HIS   A 1 190 ? -6.235  -7.928  18.558 1.00 168.73 ? 208 HIS   A CA  1 
ATOM   1442 C C   . HIS   A 1 190 ? -7.211  -8.309  19.669 1.00 165.56 ? 208 HIS   A C   1 
ATOM   1443 O O   . HIS   A 1 190 ? -8.255  -7.654  19.789 1.00 167.42 ? 208 HIS   A O   1 
ATOM   1444 C CB  . HIS   A 1 190 ? -7.022  -7.838  17.240 1.00 177.16 ? 208 HIS   A CB  1 
ATOM   1445 C CG  . HIS   A 1 190 ? -6.182  -7.448  16.064 1.00 178.84 ? 208 HIS   A CG  1 
ATOM   1446 N ND1 . HIS   A 1 190 ? -5.831  -6.141  15.801 1.00 178.96 ? 208 HIS   A ND1 1 
ATOM   1447 C CD2 . HIS   A 1 190 ? -5.619  -8.193  15.084 1.00 180.22 ? 208 HIS   A CD2 1 
ATOM   1448 C CE1 . HIS   A 1 190 ? -5.091  -6.097  14.709 1.00 181.61 ? 208 HIS   A CE1 1 
ATOM   1449 N NE2 . HIS   A 1 190 ? -4.947  -7.329  14.253 1.00 185.94 ? 208 HIS   A NE2 1 
ATOM   1450 N N   . ILE   A 1 191 ? -6.924  -9.321  20.480 1.00 154.24 ? 209 ILE   A N   1 
ATOM   1451 C CA  . ILE   A 1 191 ? -7.776  -9.639  21.621 1.00 172.87 ? 209 ILE   A CA  1 
ATOM   1452 C C   . ILE   A 1 191 ? -9.201  -9.921  21.156 1.00 201.08 ? 209 ILE   A C   1 
ATOM   1453 O O   . ILE   A 1 191 ? -9.546  -11.055 20.826 1.00 212.53 ? 209 ILE   A O   1 
ATOM   1454 C CB  . ILE   A 1 191 ? -7.761  -8.496  22.657 1.00 141.39 ? 209 ILE   A CB  1 
ATOM   1455 C CG1 . ILE   A 1 191 ? -6.330  -8.211  23.119 1.00 122.09 ? 209 ILE   A CG1 1 
ATOM   1456 C CG2 . ILE   A 1 191 ? -8.637  -8.846  23.850 1.00 130.69 ? 209 ILE   A CG2 1 
ATOM   1457 C CD1 . ILE   A 1 191 ? -6.161  -6.864  23.783 1.00 190.76 ? 209 ILE   A CD1 1 
ATOM   1458 N N   . ASP   A 1 194 ? -12.117 -13.159 21.120 1.00 140.45 ? 212 ASP   A N   1 
ATOM   1459 C CA  . ASP   A 1 194 ? -12.797 -14.420 20.851 1.00 139.08 ? 212 ASP   A CA  1 
ATOM   1460 C C   . ASP   A 1 194 ? -11.965 -15.293 19.917 1.00 135.76 ? 212 ASP   A C   1 
ATOM   1461 O O   . ASP   A 1 194 ? -10.998 -14.826 19.315 1.00 150.72 ? 212 ASP   A O   1 
ATOM   1462 C CB  . ASP   A 1 194 ? -14.180 -14.164 20.249 1.00 148.80 ? 212 ASP   A CB  1 
ATOM   1463 C CG  . ASP   A 1 194 ? -15.067 -13.338 21.160 1.00 145.63 ? 212 ASP   A CG  1 
ATOM   1464 O OD1 . ASP   A 1 194 ? -14.599 -12.941 22.248 1.00 151.81 ? 212 ASP   A OD1 1 
ATOM   1465 O OD2 . ASP   A 1 194 ? -16.233 -13.086 20.789 1.00 148.30 ? 212 ASP   A OD2 1 
ATOM   1466 N N   . ILE   A 1 195 ? -12.349 -16.562 19.801 1.00 142.05 ? 213 ILE   A N   1 
ATOM   1467 C CA  . ILE   A 1 195 ? -11.618 -17.548 19.016 1.00 150.41 ? 213 ILE   A CA  1 
ATOM   1468 C C   . ILE   A 1 195 ? -12.545 -18.109 17.947 1.00 143.70 ? 213 ILE   A C   1 
ATOM   1469 O O   . ILE   A 1 195 ? -13.734 -18.338 18.199 1.00 142.49 ? 213 ILE   A O   1 
ATOM   1470 C CB  . ILE   A 1 195 ? -11.060 -18.683 19.901 1.00 163.84 ? 213 ILE   A CB  1 
ATOM   1471 C CG1 . ILE   A 1 195 ? -9.998  -18.144 20.866 1.00 148.04 ? 213 ILE   A CG1 1 
ATOM   1472 C CG2 . ILE   A 1 195 ? -10.481 -19.799 19.039 1.00 146.90 ? 213 ILE   A CG2 1 
ATOM   1473 C CD1 . ILE   A 1 195 ? -10.559 -17.587 22.160 1.00 134.11 ? 213 ILE   A CD1 1 
ATOM   1474 N N   . ASP   A 1 196 ? -11.998 -18.327 16.753 1.00 148.48 ? 214 ASP   A N   1 
ATOM   1475 C CA  . ASP   A 1 196 ? -12.759 -18.871 15.629 1.00 150.11 ? 214 ASP   A CA  1 
ATOM   1476 C C   . ASP   A 1 196 ? -12.791 -20.389 15.755 1.00 158.89 ? 214 ASP   A C   1 
ATOM   1477 O O   . ASP   A 1 196 ? -11.840 -21.077 15.377 1.00 160.33 ? 214 ASP   A O   1 
ATOM   1478 C CB  . ASP   A 1 196 ? -12.140 -18.439 14.304 1.00 158.64 ? 214 ASP   A CB  1 
ATOM   1479 C CG  . ASP   A 1 196 ? -12.928 -18.928 13.101 1.00 160.23 ? 214 ASP   A CG  1 
ATOM   1480 O OD1 . ASP   A 1 196 ? -13.984 -19.566 13.293 1.00 160.84 ? 214 ASP   A OD1 1 
ATOM   1481 O OD2 . ASP   A 1 196 ? -12.489 -18.673 11.959 1.00 144.28 ? 214 ASP   A OD2 1 
ATOM   1482 N N   . VAL   A 1 197 ? -13.889 -20.917 16.286 1.00 153.62 ? 215 VAL   A N   1 
ATOM   1483 C CA  . VAL   A 1 197 ? -14.052 -22.358 16.427 1.00 161.27 ? 215 VAL   A CA  1 
ATOM   1484 C C   . VAL   A 1 197 ? -14.609 -22.939 15.133 1.00 150.20 ? 215 VAL   A C   1 
ATOM   1485 O O   . VAL   A 1 197 ? -14.241 -24.042 14.728 1.00 144.54 ? 215 VAL   A O   1 
ATOM   1486 C CB  . VAL   A 1 197 ? -14.963 -22.709 17.621 1.00 147.99 ? 215 VAL   A CB  1 
ATOM   1487 C CG1 . VAL   A 1 197 ? -14.366 -22.184 18.919 1.00 147.83 ? 215 VAL   A CG1 1 
ATOM   1488 C CG2 . VAL   A 1 197 ? -16.371 -22.160 17.411 1.00 157.55 ? 215 VAL   A CG2 1 
ATOM   1489 N N   . LYS   A 1 207 ? 2.308   -16.066 10.783 1.00 120.55 ? 225 LYS   A N   1 
ATOM   1490 C CA  . LYS   A 1 207 ? 2.315   -14.611 10.687 1.00 122.75 ? 225 LYS   A CA  1 
ATOM   1491 C C   . LYS   A 1 207 ? 2.860   -13.987 11.968 1.00 132.48 ? 225 LYS   A C   1 
ATOM   1492 O O   . LYS   A 1 207 ? 2.414   -14.316 13.066 1.00 132.78 ? 225 LYS   A O   1 
ATOM   1493 C CB  . LYS   A 1 207 ? 0.906   -14.091 10.405 1.00 130.77 ? 225 LYS   A CB  1 
ATOM   1494 C CG  . LYS   A 1 207 ? 0.281   -14.681 9.155  1.00 135.51 ? 225 LYS   A CG  1 
ATOM   1495 C CD  . LYS   A 1 207 ? -1.065  -14.049 8.855  1.00 135.10 ? 225 LYS   A CD  1 
ATOM   1496 C CE  . LYS   A 1 207 ? -1.652  -14.591 7.564  1.00 132.12 ? 225 LYS   A CE  1 
ATOM   1497 N NZ  . LYS   A 1 207 ? -2.909  -13.892 7.186  1.00 134.17 ? 225 LYS   A NZ  1 
ATOM   1498 N N   . ILE   A 1 208 ? 3.822   -13.081 11.819 1.00 134.30 ? 226 ILE   A N   1 
ATOM   1499 C CA  . ILE   A 1 208 ? 4.470   -12.457 12.968 1.00 124.48 ? 226 ILE   A CA  1 
ATOM   1500 C C   . ILE   A 1 208 ? 3.587   -11.335 13.494 1.00 133.39 ? 226 ILE   A C   1 
ATOM   1501 O O   . ILE   A 1 208 ? 3.152   -10.460 12.736 1.00 128.41 ? 226 ILE   A O   1 
ATOM   1502 C CB  . ILE   A 1 208 ? 5.865   -11.933 12.590 1.00 114.89 ? 226 ILE   A CB  1 
ATOM   1503 C CG1 . ILE   A 1 208 ? 6.786   -13.100 12.222 1.00 125.78 ? 226 ILE   A CG1 1 
ATOM   1504 C CG2 . ILE   A 1 208 ? 6.455   -11.111 13.738 1.00 108.42 ? 226 ILE   A CG2 1 
ATOM   1505 C CD1 . ILE   A 1 208 ? 8.190   -12.683 11.828 1.00 132.74 ? 226 ILE   A CD1 1 
ATOM   1506 N N   . ASN   A 1 209 ? 3.323   -11.359 14.798 1.00 119.43 ? 227 ASN   A N   1 
ATOM   1507 C CA  . ASN   A 1 209 ? 2.622   -10.276 15.478 1.00 124.16 ? 227 ASN   A CA  1 
ATOM   1508 C C   . ASN   A 1 209 ? 3.673   -9.315  16.024 1.00 121.62 ? 227 ASN   A C   1 
ATOM   1509 O O   . ASN   A 1 209 ? 4.385   -9.640  16.980 1.00 122.33 ? 227 ASN   A O   1 
ATOM   1510 C CB  . ASN   A 1 209 ? 1.730   -10.829 16.587 1.00 122.55 ? 227 ASN   A CB  1 
ATOM   1511 C CG  . ASN   A 1 209 ? 0.759   -9.797  17.124 1.00 130.31 ? 227 ASN   A CG  1 
ATOM   1512 O OD1 . ASN   A 1 209 ? 0.763   -8.642  16.697 1.00 137.41 ? 227 ASN   A OD1 1 
ATOM   1513 N ND2 . ASN   A 1 209 ? -0.092  -10.213 18.055 1.00 128.16 ? 227 ASN   A ND2 1 
ATOM   1514 N N   . ILE   A 1 210 ? 3.772   -8.132  15.413 1.00 124.47 ? 228 ILE   A N   1 
ATOM   1515 C CA  . ILE   A 1 210 ? 4.893   -7.237  15.696 1.00 128.87 ? 228 ILE   A CA  1 
ATOM   1516 C C   . ILE   A 1 210 ? 4.884   -6.813  17.160 1.00 125.18 ? 228 ILE   A C   1 
ATOM   1517 O O   . ILE   A 1 210 ? 5.917   -6.844  17.839 1.00 125.57 ? 228 ILE   A O   1 
ATOM   1518 C CB  . ILE   A 1 210 ? 4.857   -6.016  14.759 1.00 117.49 ? 228 ILE   A CB  1 
ATOM   1519 C CG1 . ILE   A 1 210 ? 4.919   -6.470  13.297 1.00 129.55 ? 228 ILE   A CG1 1 
ATOM   1520 C CG2 . ILE   A 1 210 ? 6.010   -5.070  15.083 1.00 109.85 ? 228 ILE   A CG2 1 
ATOM   1521 C CD1 . ILE   A 1 210 ? 4.819   -5.339  12.293 1.00 146.81 ? 228 ILE   A CD1 1 
ATOM   1522 N N   . ASN   A 1 211 ? 3.720   -6.408  17.670 1.00 123.80 ? 229 ASN   A N   1 
ATOM   1523 C CA  . ASN   A 1 211 ? 3.656   -5.925  19.044 1.00 117.83 ? 229 ASN   A CA  1 
ATOM   1524 C C   . ASN   A 1 211 ? 4.074   -6.993  20.044 1.00 122.56 ? 229 ASN   A C   1 
ATOM   1525 O O   . ASN   A 1 211 ? 4.455   -6.658  21.171 1.00 124.53 ? 229 ASN   A O   1 
ATOM   1526 C CB  . ASN   A 1 211 ? 2.242   -5.444  19.368 1.00 134.32 ? 229 ASN   A CB  1 
ATOM   1527 C CG  . ASN   A 1 211 ? 1.330   -6.572  19.807 1.00 133.02 ? 229 ASN   A CG  1 
ATOM   1528 O OD1 . ASN   A 1 211 ? 0.780   -7.301  18.982 1.00 136.38 ? 229 ASN   A OD1 1 
ATOM   1529 N ND2 . ASN   A 1 211 ? 1.164   -6.722  21.117 1.00 134.82 ? 229 ASN   A ND2 1 
ATOM   1530 N N   . MET   A 1 212 ? 4.013   -8.269  19.659 1.00 133.27 ? 230 MET   A N   1 
ATOM   1531 C CA  . MET   A 1 212 ? 4.340   -9.345  20.586 1.00 124.12 ? 230 MET   A CA  1 
ATOM   1532 C C   . MET   A 1 212 ? 5.839   -9.502  20.797 1.00 123.66 ? 230 MET   A C   1 
ATOM   1533 O O   . MET   A 1 212 ? 6.262   -9.916  21.882 1.00 129.62 ? 230 MET   A O   1 
ATOM   1534 C CB  . MET   A 1 212 ? 3.751   -10.663 20.084 1.00 119.47 ? 230 MET   A CB  1 
ATOM   1535 C CG  . MET   A 1 212 ? 2.242   -10.749 20.216 1.00 117.26 ? 230 MET   A CG  1 
ATOM   1536 S SD  . MET   A 1 212 ? 1.688   -10.540 21.922 1.00 86.45  ? 230 MET   A SD  1 
ATOM   1537 C CE  . MET   A 1 212 ? -0.061  -10.874 21.754 1.00 117.02 ? 230 MET   A CE  1 
ATOM   1538 N N   . LEU   A 1 213 ? 6.656   -9.193  19.793 1.00 126.87 ? 231 LEU   A N   1 
ATOM   1539 C CA  . LEU   A 1 213 ? 8.099   -9.378  19.913 1.00 141.15 ? 231 LEU   A CA  1 
ATOM   1540 C C   . LEU   A 1 213 ? 8.685   -8.190  20.668 1.00 149.21 ? 231 LEU   A C   1 
ATOM   1541 O O   . LEU   A 1 213 ? 8.767   -7.077  20.136 1.00 106.22 ? 231 LEU   A O   1 
ATOM   1542 C CB  . LEU   A 1 213 ? 8.741   -9.551  18.539 1.00 112.00 ? 231 LEU   A CB  1 
ATOM   1543 C CG  . LEU   A 1 213 ? 8.723   -8.383  17.556 1.00 109.61 ? 231 LEU   A CG  1 
ATOM   1544 C CD1 . LEU   A 1 213 ? 10.074  -7.684  17.525 1.00 136.03 ? 231 LEU   A CD1 1 
ATOM   1545 C CD2 . LEU   A 1 213 ? 8.339   -8.877  16.171 1.00 114.95 ? 231 LEU   A CD2 1 
ATOM   1546 N N   . ASN   A 1 214 ? 9.068   -8.427  21.918 1.00 131.51 ? 232 ASN   A N   1 
ATOM   1547 C CA  . ASN   A 1 214 ? 9.724   -7.434  22.761 1.00 150.33 ? 232 ASN   A CA  1 
ATOM   1548 C C   . ASN   A 1 214 ? 10.324  -8.179  23.945 1.00 135.17 ? 232 ASN   A C   1 
ATOM   1549 O O   . ASN   A 1 214 ? 10.037  -9.358  24.168 1.00 116.43 ? 232 ASN   A O   1 
ATOM   1550 C CB  . ASN   A 1 214 ? 8.756   -6.338  23.216 1.00 140.66 ? 232 ASN   A CB  1 
ATOM   1551 C CG  . ASN   A 1 214 ? 7.529   -6.892  23.906 1.00 110.26 ? 232 ASN   A CG  1 
ATOM   1552 O OD1 . ASN   A 1 214 ? 7.508   -7.053  25.126 1.00 148.32 ? 232 ASN   A OD1 1 
ATOM   1553 N ND2 . ASN   A 1 214 ? 6.493   -7.182  23.128 1.00 136.92 ? 232 ASN   A ND2 1 
ATOM   1554 N N   . PHE   A 1 215 ? 11.168  -7.476  24.705 1.00 132.59 ? 233 PHE   A N   1 
ATOM   1555 C CA  . PHE   A 1 215 ? 11.934  -8.150  25.748 1.00 128.61 ? 233 PHE   A CA  1 
ATOM   1556 C C   . PHE   A 1 215 ? 11.054  -8.581  26.916 1.00 130.61 ? 233 PHE   A C   1 
ATOM   1557 O O   . PHE   A 1 215 ? 11.374  -9.562  27.593 1.00 134.42 ? 233 PHE   A O   1 
ATOM   1558 C CB  . PHE   A 1 215 ? 13.073  -7.249  26.235 1.00 150.87 ? 233 PHE   A CB  1 
ATOM   1559 C CG  . PHE   A 1 215 ? 12.661  -6.238  27.271 1.00 171.67 ? 233 PHE   A CG  1 
ATOM   1560 C CD1 . PHE   A 1 215 ? 12.096  -5.028  26.897 1.00 157.64 ? 233 PHE   A CD1 1 
ATOM   1561 C CD2 . PHE   A 1 215 ? 12.860  -6.491  28.619 1.00 158.54 ? 233 PHE   A CD2 1 
ATOM   1562 C CE1 . PHE   A 1 215 ? 11.725  -4.095  27.851 1.00 142.24 ? 233 PHE   A CE1 1 
ATOM   1563 C CE2 . PHE   A 1 215 ? 12.491  -5.563  29.577 1.00 155.05 ? 233 PHE   A CE2 1 
ATOM   1564 C CZ  . PHE   A 1 215 ? 11.924  -4.364  29.192 1.00 143.69 ? 233 PHE   A CZ  1 
ATOM   1565 N N   . LYS   A 1 216 ? 9.948   -7.878  27.167 1.00 128.39 ? 234 LYS   A N   1 
ATOM   1566 C CA  . LYS   A 1 216 ? 9.081   -8.245  28.285 1.00 131.68 ? 234 LYS   A CA  1 
ATOM   1567 C C   . LYS   A 1 216 ? 8.339   -9.549  28.004 1.00 137.58 ? 234 LYS   A C   1 
ATOM   1568 O O   . LYS   A 1 216 ? 8.288   -10.447 28.856 1.00 138.89 ? 234 LYS   A O   1 
ATOM   1569 C CB  . LYS   A 1 216 ? 8.101   -7.106  28.573 1.00 141.17 ? 234 LYS   A CB  1 
ATOM   1570 C CG  . LYS   A 1 216 ? 8.780   -5.786  28.913 1.00 134.18 ? 234 LYS   A CG  1 
ATOM   1571 C CD  . LYS   A 1 216 ? 7.774   -4.666  29.135 1.00 148.32 ? 234 LYS   A CD  1 
ATOM   1572 C CE  . LYS   A 1 216 ? 8.471   -3.351  29.455 1.00 152.95 ? 234 LYS   A CE  1 
ATOM   1573 N NZ  . LYS   A 1 216 ? 7.507   -2.234  29.657 1.00 138.67 ? 234 LYS   A NZ  1 
ATOM   1574 N N   . VAL   A 1 217 ? 7.757   -9.673  26.809 1.00 171.88 ? 235 VAL   A N   1 
ATOM   1575 C CA  . VAL   A 1 217 ? 7.082   -10.913 26.437 1.00 168.18 ? 235 VAL   A CA  1 
ATOM   1576 C C   . VAL   A 1 217 ? 8.079   -12.062 26.393 1.00 139.22 ? 235 VAL   A C   1 
ATOM   1577 O O   . VAL   A 1 217 ? 7.781   -13.185 26.819 1.00 140.78 ? 235 VAL   A O   1 
ATOM   1578 C CB  . VAL   A 1 217 ? 6.358   -10.739 25.089 1.00 104.32 ? 235 VAL   A CB  1 
ATOM   1579 C CG1 . VAL   A 1 217 ? 5.733   -12.048 24.648 1.00 128.82 ? 235 VAL   A CG1 1 
ATOM   1580 C CG2 . VAL   A 1 217 ? 5.306   -9.649  25.190 1.00 140.20 ? 235 VAL   A CG2 1 
ATOM   1581 N N   . TYR   A 1 218 ? 9.275   -11.802 25.865 1.00 131.02 ? 236 TYR   A N   1 
ATOM   1582 C CA  . TYR   A 1 218 ? 10.313  -12.825 25.826 1.00 123.39 ? 236 TYR   A CA  1 
ATOM   1583 C C   . TYR   A 1 218 ? 10.688  -13.277 27.232 1.00 116.76 ? 236 TYR   A C   1 
ATOM   1584 O O   . TYR   A 1 218 ? 10.847  -14.478 27.487 1.00 115.11 ? 236 TYR   A O   1 
ATOM   1585 C CB  . TYR   A 1 218 ? 11.531  -12.276 25.083 1.00 104.52 ? 236 TYR   A CB  1 
ATOM   1586 C CG  . TYR   A 1 218 ? 12.536  -13.311 24.636 1.00 100.65 ? 236 TYR   A CG  1 
ATOM   1587 C CD1 . TYR   A 1 218 ? 12.145  -14.412 23.885 1.00 108.75 ? 236 TYR   A CD1 1 
ATOM   1588 C CD2 . TYR   A 1 218 ? 13.883  -13.168 24.935 1.00 108.61 ? 236 TYR   A CD2 1 
ATOM   1589 C CE1 . TYR   A 1 218 ? 13.067  -15.354 23.466 1.00 119.44 ? 236 TYR   A CE1 1 
ATOM   1590 C CE2 . TYR   A 1 218 ? 14.812  -14.099 24.516 1.00 106.89 ? 236 TYR   A CE2 1 
ATOM   1591 C CZ  . TYR   A 1 218 ? 14.400  -15.191 23.780 1.00 105.33 ? 236 TYR   A CZ  1 
ATOM   1592 O OH  . TYR   A 1 218 ? 15.323  -16.125 23.369 1.00 127.55 ? 236 TYR   A OH  1 
ATOM   1593 N N   . GLN   A 1 219 ? 10.831  -12.327 28.160 1.00 125.25 ? 237 GLN   A N   1 
ATOM   1594 C CA  . GLN   A 1 219 ? 11.128  -12.681 29.543 1.00 109.55 ? 237 GLN   A CA  1 
ATOM   1595 C C   . GLN   A 1 219 ? 10.021  -13.538 30.136 1.00 95.95  ? 237 GLN   A C   1 
ATOM   1596 O O   . GLN   A 1 219 ? 10.294  -14.540 30.804 1.00 98.25  ? 237 GLN   A O   1 
ATOM   1597 C CB  . GLN   A 1 219 ? 11.325  -11.418 30.384 1.00 112.46 ? 237 GLN   A CB  1 
ATOM   1598 C CG  . GLN   A 1 219 ? 12.686  -10.754 30.229 1.00 140.88 ? 237 GLN   A CG  1 
ATOM   1599 C CD  . GLN   A 1 219 ? 12.841  -9.534  31.122 1.00 152.61 ? 237 GLN   A CD  1 
ATOM   1600 O OE1 . GLN   A 1 219 ? 11.977  -9.245  31.950 1.00 132.94 ? 237 GLN   A OE1 1 
ATOM   1601 N NE2 . GLN   A 1 219 ? 13.944  -8.813  30.955 1.00 135.13 ? 237 GLN   A NE2 1 
ATOM   1602 N N   . ASN   A 1 220 ? 8.763   -13.157 29.910 1.00 102.95 ? 238 ASN   A N   1 
ATOM   1603 C CA  . ASN   A 1 220 ? 7.653   -13.970 30.402 1.00 97.44  ? 238 ASN   A CA  1 
ATOM   1604 C C   . ASN   A 1 220 ? 7.749   -15.394 29.867 1.00 98.77  ? 238 ASN   A C   1 
ATOM   1605 O O   . ASN   A 1 220 ? 7.687   -16.373 30.630 1.00 101.09 ? 238 ASN   A O   1 
ATOM   1606 C CB  . ASN   A 1 220 ? 6.320   -13.340 29.994 1.00 110.41 ? 238 ASN   A CB  1 
ATOM   1607 C CG  . ASN   A 1 220 ? 6.019   -12.061 30.750 1.00 140.75 ? 238 ASN   A CG  1 
ATOM   1608 O OD1 . ASN   A 1 220 ? 6.547   -11.828 31.836 1.00 119.65 ? 238 ASN   A OD1 1 
ATOM   1609 N ND2 . ASN   A 1 220 ? 5.155   -11.228 30.179 1.00 130.82 ? 238 ASN   A ND2 1 
ATOM   1610 N N   . ILE   A 1 221 ? 7.911   -15.522 28.548 1.00 92.56  ? 239 ILE   A N   1 
ATOM   1611 C CA  . ILE   A 1 221 ? 7.934   -16.840 27.921 1.00 91.43  ? 239 ILE   A CA  1 
ATOM   1612 C C   . ILE   A 1 221 ? 9.048   -17.682 28.519 1.00 88.34  ? 239 ILE   A C   1 
ATOM   1613 O O   . ILE   A 1 221 ? 8.838   -18.835 28.901 1.00 89.76  ? 239 ILE   A O   1 
ATOM   1614 C CB  . ILE   A 1 221 ? 8.103   -16.716 26.397 1.00 108.29 ? 239 ILE   A CB  1 
ATOM   1615 C CG1 . ILE   A 1 221 ? 6.980   -15.892 25.773 1.00 92.08  ? 239 ILE   A CG1 1 
ATOM   1616 C CG2 . ILE   A 1 221 ? 8.134   -18.098 25.759 1.00 108.69 ? 239 ILE   A CG2 1 
ATOM   1617 C CD1 . ILE   A 1 221 ? 7.402   -15.240 24.478 1.00 108.20 ? 239 ILE   A CD1 1 
ATOM   1618 N N   . ILE   A 1 222 ? 10.254  -17.119 28.605 1.00 89.42  ? 240 ILE   A N   1 
ATOM   1619 C CA  . ILE   A 1 222 ? 11.388  -17.893 29.099 1.00 83.38  ? 240 ILE   A CA  1 
ATOM   1620 C C   . ILE   A 1 222 ? 11.169  -18.286 30.552 1.00 75.83  ? 240 ILE   A C   1 
ATOM   1621 O O   . ILE   A 1 222 ? 11.327  -19.453 30.929 1.00 85.26  ? 240 ILE   A O   1 
ATOM   1622 C CB  . ILE   A 1 222 ? 12.695  -17.102 28.935 1.00 104.15 ? 240 ILE   A CB  1 
ATOM   1623 C CG1 . ILE   A 1 222 ? 12.987  -16.878 27.453 1.00 106.07 ? 240 ILE   A CG1 1 
ATOM   1624 C CG2 . ILE   A 1 222 ? 13.827  -17.836 29.655 1.00 111.55 ? 240 ILE   A CG2 1 
ATOM   1625 C CD1 . ILE   A 1 222 ? 14.292  -16.182 27.187 1.00 129.07 ? 240 ILE   A CD1 1 
ATOM   1626 N N   . ILE   A 1 223 ? 10.803  -17.316 31.389 1.00 86.43  ? 241 ILE   A N   1 
ATOM   1627 C CA  . ILE   A 1 223 ? 10.709  -17.567 32.821 1.00 87.42  ? 241 ILE   A CA  1 
ATOM   1628 C C   . ILE   A 1 223 ? 9.716   -18.685 33.095 1.00 88.57  ? 241 ILE   A C   1 
ATOM   1629 O O   . ILE   A 1 223 ? 10.003  -19.623 33.848 1.00 82.52  ? 241 ILE   A O   1 
ATOM   1630 C CB  . ILE   A 1 223 ? 10.324  -16.275 33.561 1.00 97.52  ? 241 ILE   A CB  1 
ATOM   1631 C CG1 . ILE   A 1 223 ? 11.461  -15.256 33.451 1.00 112.02 ? 241 ILE   A CG1 1 
ATOM   1632 C CG2 . ILE   A 1 223 ? 9.993   -16.578 35.012 1.00 93.62  ? 241 ILE   A CG2 1 
ATOM   1633 C CD1 . ILE   A 1 223 ? 11.076  -13.851 33.864 1.00 98.09  ? 241 ILE   A CD1 1 
ATOM   1634 N N   . HIS   A 1 224 ? 8.535   -18.615 32.478 1.00 87.75  ? 242 HIS   A N   1 
ATOM   1635 C CA  . HIS   A 1 224 ? 7.547   -19.657 32.733 1.00 82.43  ? 242 HIS   A CA  1 
ATOM   1636 C C   . HIS   A 1 224 ? 7.925   -20.964 32.045 1.00 79.51  ? 242 HIS   A C   1 
ATOM   1637 O O   . HIS   A 1 224 ? 7.717   -22.049 32.600 1.00 81.19  ? 242 HIS   A O   1 
ATOM   1638 C CB  . HIS   A 1 224 ? 6.167   -19.183 32.291 1.00 85.71  ? 242 HIS   A CB  1 
ATOM   1639 C CG  . HIS   A 1 224 ? 5.596   -18.119 33.174 1.00 88.09  ? 242 HIS   A CG  1 
ATOM   1640 N ND1 . HIS   A 1 224 ? 6.105   -16.839 33.219 1.00 90.39  ? 242 HIS   A ND1 1 
ATOM   1641 C CD2 . HIS   A 1 224 ? 4.577   -18.151 34.065 1.00 94.25  ? 242 HIS   A CD2 1 
ATOM   1642 C CE1 . HIS   A 1 224 ? 5.415   -16.124 34.089 1.00 94.95  ? 242 HIS   A CE1 1 
ATOM   1643 N NE2 . HIS   A 1 224 ? 4.484   -16.898 34.618 1.00 93.76  ? 242 HIS   A NE2 1 
ATOM   1644 N N   . LYS   A 1 225 ? 8.504   -20.878 30.848 1.00 85.23  ? 243 LYS   A N   1 
ATOM   1645 C CA  . LYS   A 1 225 ? 8.774   -22.068 30.050 1.00 85.87  ? 243 LYS   A CA  1 
ATOM   1646 C C   . LYS   A 1 225 ? 9.930   -22.878 30.621 1.00 85.50  ? 243 LYS   A C   1 
ATOM   1647 O O   . LYS   A 1 225 ? 9.842   -24.107 30.729 1.00 94.05  ? 243 LYS   A O   1 
ATOM   1648 C CB  . LYS   A 1 225 ? 9.072   -21.650 28.608 1.00 89.44  ? 243 LYS   A CB  1 
ATOM   1649 C CG  . LYS   A 1 225 ? 9.585   -22.754 27.711 1.00 95.02  ? 243 LYS   A CG  1 
ATOM   1650 C CD  . LYS   A 1 225 ? 9.768   -22.253 26.286 1.00 103.12 ? 243 LYS   A CD  1 
ATOM   1651 C CE  . LYS   A 1 225 ? 10.381  -23.320 25.398 1.00 136.59 ? 243 LYS   A CE  1 
ATOM   1652 N NZ  . LYS   A 1 225 ? 10.429  -22.906 23.971 1.00 127.88 ? 243 LYS   A NZ  1 
ATOM   1653 N N   . THR   A 1 226 ? 11.019  -22.211 30.992 1.00 89.28  ? 244 THR   A N   1 
ATOM   1654 C CA  . THR   A 1 226 ? 12.273  -22.886 31.301 1.00 77.80  ? 244 THR   A CA  1 
ATOM   1655 C C   . THR   A 1 226 ? 12.738  -22.667 32.730 1.00 74.13  ? 244 THR   A C   1 
ATOM   1656 O O   . THR   A 1 226 ? 13.142  -23.625 33.398 1.00 77.43  ? 244 THR   A O   1 
ATOM   1657 C CB  . THR   A 1 226 ? 13.368  -22.407 30.332 1.00 83.25  ? 244 THR   A CB  1 
ATOM   1658 O OG1 . THR   A 1 226 ? 12.980  -22.699 28.984 1.00 88.82  ? 244 THR   A OG1 1 
ATOM   1659 C CG2 . THR   A 1 226 ? 14.698  -23.081 30.639 1.00 79.84  ? 244 THR   A CG2 1 
ATOM   1660 N N   . ALA   A 1 227 ? 12.681  -21.429 33.224 1.00 67.73  ? 245 ALA   A N   1 
ATOM   1661 C CA  . ALA   A 1 227 ? 13.380  -21.092 34.459 1.00 76.78  ? 245 ALA   A CA  1 
ATOM   1662 C C   . ALA   A 1 227 ? 12.947  -21.984 35.614 1.00 70.22  ? 245 ALA   A C   1 
ATOM   1663 O O   . ALA   A 1 227 ? 13.787  -22.469 36.381 1.00 68.22  ? 245 ALA   A O   1 
ATOM   1664 C CB  . ALA   A 1 227 ? 13.143  -19.622 34.804 1.00 77.66  ? 245 ALA   A CB  1 
ATOM   1665 N N   . TYR   A 1 228 ? 11.645  -22.226 35.751 1.00 77.87  ? 246 TYR   A N   1 
ATOM   1666 C CA  . TYR   A 1 228 ? 11.147  -22.886 36.952 1.00 72.76  ? 246 TYR   A CA  1 
ATOM   1667 C C   . TYR   A 1 228 ? 11.512  -24.365 36.972 1.00 79.66  ? 246 TYR   A C   1 
ATOM   1668 O O   . TYR   A 1 228 ? 12.210  -24.832 37.880 1.00 76.28  ? 246 TYR   A O   1 
ATOM   1669 C CB  . TYR   A 1 228 ? 9.638   -22.685 37.062 1.00 74.45  ? 246 TYR   A CB  1 
ATOM   1670 C CG  . TYR   A 1 228 ? 9.300   -21.294 37.532 1.00 80.32  ? 246 TYR   A CG  1 
ATOM   1671 C CD1 . TYR   A 1 228 ? 9.306   -20.980 38.884 1.00 85.42  ? 246 TYR   A CD1 1 
ATOM   1672 C CD2 . TYR   A 1 228 ? 9.006   -20.285 36.627 1.00 82.04  ? 246 TYR   A CD2 1 
ATOM   1673 C CE1 . TYR   A 1 228 ? 9.014   -19.706 39.322 1.00 78.51  ? 246 TYR   A CE1 1 
ATOM   1674 C CE2 . TYR   A 1 228 ? 8.711   -19.007 37.056 1.00 90.26  ? 246 TYR   A CE2 1 
ATOM   1675 C CZ  . TYR   A 1 228 ? 8.717   -18.724 38.405 1.00 83.13  ? 246 TYR   A CZ  1 
ATOM   1676 O OH  . TYR   A 1 228 ? 8.425   -17.452 38.840 1.00 85.99  ? 246 TYR   A OH  1 
ATOM   1677 N N   . TYR   A 1 229 ? 11.060  -25.124 35.973 1.00 89.79  ? 247 TYR   A N   1 
ATOM   1678 C CA  . TYR   A 1 229 ? 11.320  -26.558 35.996 1.00 79.95  ? 247 TYR   A CA  1 
ATOM   1679 C C   . TYR   A 1 229 ? 12.809  -26.860 35.876 1.00 62.80  ? 247 TYR   A C   1 
ATOM   1680 O O   . TYR   A 1 229 ? 13.290  -27.827 36.476 1.00 65.31  ? 247 TYR   A O   1 
ATOM   1681 C CB  . TYR   A 1 229 ? 10.530  -27.257 34.887 1.00 79.74  ? 247 TYR   A CB  1 
ATOM   1682 C CG  . TYR   A 1 229 ? 11.279  -27.428 33.586 1.00 84.63  ? 247 TYR   A CG  1 
ATOM   1683 C CD1 . TYR   A 1 229 ? 11.357  -26.395 32.663 1.00 94.66  ? 247 TYR   A CD1 1 
ATOM   1684 C CD2 . TYR   A 1 229 ? 11.898  -28.630 33.276 1.00 74.04  ? 247 TYR   A CD2 1 
ATOM   1685 C CE1 . TYR   A 1 229 ? 12.038  -26.554 31.472 1.00 87.80  ? 247 TYR   A CE1 1 
ATOM   1686 C CE2 . TYR   A 1 229 ? 12.581  -28.797 32.089 1.00 78.94  ? 247 TYR   A CE2 1 
ATOM   1687 C CZ  . TYR   A 1 229 ? 12.649  -27.756 31.191 1.00 83.12  ? 247 TYR   A CZ  1 
ATOM   1688 O OH  . TYR   A 1 229 ? 13.330  -27.919 30.006 1.00 98.51  ? 247 TYR   A OH  1 
ATOM   1689 N N   . SER   A 1 230 ? 13.555  -26.053 35.117 1.00 61.20  ? 248 SER   A N   1 
ATOM   1690 C CA  . SER   A 1 230 ? 14.974  -26.334 34.918 1.00 71.29  ? 248 SER   A CA  1 
ATOM   1691 C C   . SER   A 1 230 ? 15.812  -25.966 36.138 1.00 67.32  ? 248 SER   A C   1 
ATOM   1692 O O   . SER   A 1 230 ? 16.735  -26.704 36.502 1.00 57.45  ? 248 SER   A O   1 
ATOM   1693 C CB  . SER   A 1 230 ? 15.494  -25.587 33.688 1.00 66.69  ? 248 SER   A CB  1 
ATOM   1694 O OG  . SER   A 1 230 ? 14.873  -26.052 32.504 1.00 72.94  ? 248 SER   A OG  1 
ATOM   1695 N N   . PHE   A 1 231 ? 15.519  -24.833 36.775 1.00 73.75  ? 249 PHE   A N   1 
ATOM   1696 C CA  . PHE   A 1 231 ? 16.380  -24.297 37.822 1.00 62.08  ? 249 PHE   A CA  1 
ATOM   1697 C C   . PHE   A 1 231 ? 15.694  -24.196 39.173 1.00 60.37  ? 249 PHE   A C   1 
ATOM   1698 O O   . PHE   A 1 231 ? 16.223  -24.705 40.167 1.00 64.20  ? 249 PHE   A O   1 
ATOM   1699 C CB  . PHE   A 1 231 ? 16.907  -22.922 37.388 1.00 60.02  ? 249 PHE   A CB  1 
ATOM   1700 C CG  . PHE   A 1 231 ? 17.716  -22.969 36.123 1.00 78.89  ? 249 PHE   A CG  1 
ATOM   1701 C CD1 . PHE   A 1 231 ? 19.079  -23.207 36.166 1.00 72.38  ? 249 PHE   A CD1 1 
ATOM   1702 C CD2 . PHE   A 1 231 ? 17.109  -22.801 34.889 1.00 68.63  ? 249 PHE   A CD2 1 
ATOM   1703 C CE1 . PHE   A 1 231 ? 19.825  -23.264 35.004 1.00 68.95  ? 249 PHE   A CE1 1 
ATOM   1704 C CE2 . PHE   A 1 231 ? 17.849  -22.858 33.724 1.00 71.81  ? 249 PHE   A CE2 1 
ATOM   1705 C CZ  . PHE   A 1 231 ? 19.209  -23.089 33.782 1.00 71.58  ? 249 PHE   A CZ  1 
ATOM   1706 N N   . PHE   A 1 232 ? 14.529  -23.554 39.247 1.00 65.30  ? 250 PHE   A N   1 
ATOM   1707 C CA  . PHE   A 1 232 ? 13.880  -23.364 40.540 1.00 65.68  ? 250 PHE   A CA  1 
ATOM   1708 C C   . PHE   A 1 232 ? 13.496  -24.697 41.167 1.00 64.02  ? 250 PHE   A C   1 
ATOM   1709 O O   . PHE   A 1 232 ? 13.722  -24.920 42.361 1.00 62.21  ? 250 PHE   A O   1 
ATOM   1710 C CB  . PHE   A 1 232 ? 12.646  -22.478 40.385 1.00 60.69  ? 250 PHE   A CB  1 
ATOM   1711 C CG  . PHE   A 1 232 ? 12.014  -22.087 41.692 1.00 60.47  ? 250 PHE   A CG  1 
ATOM   1712 C CD1 . PHE   A 1 232 ? 12.771  -21.508 42.696 1.00 70.39  ? 250 PHE   A CD1 1 
ATOM   1713 C CD2 . PHE   A 1 232 ? 10.662  -22.286 41.913 1.00 66.48  ? 250 PHE   A CD2 1 
ATOM   1714 C CE1 . PHE   A 1 232 ? 12.195  -21.142 43.897 1.00 70.97  ? 250 PHE   A CE1 1 
ATOM   1715 C CE2 . PHE   A 1 232 ? 10.079  -21.919 43.113 1.00 68.87  ? 250 PHE   A CE2 1 
ATOM   1716 C CZ  . PHE   A 1 232 ? 10.848  -21.347 44.105 1.00 64.45  ? 250 PHE   A CZ  1 
ATOM   1717 N N   . LEU   A 1 233 ? 12.905  -25.593 40.379 1.00 69.73  ? 251 LEU   A N   1 
ATOM   1718 C CA  . LEU   A 1 233 ? 12.422  -26.856 40.932 1.00 75.88  ? 251 LEU   A CA  1 
ATOM   1719 C C   . LEU   A 1 233 ? 13.538  -27.693 41.537 1.00 71.90  ? 251 LEU   A C   1 
ATOM   1720 O O   . LEU   A 1 233 ? 13.391  -28.143 42.688 1.00 69.21  ? 251 LEU   A O   1 
ATOM   1721 C CB  . LEU   A 1 233 ? 11.675  -27.633 39.843 1.00 70.32  ? 251 LEU   A CB  1 
ATOM   1722 C CG  . LEU   A 1 233 ? 11.147  -29.016 40.229 1.00 66.00  ? 251 LEU   A CG  1 
ATOM   1723 C CD1 . LEU   A 1 233 ? 10.151  -28.922 41.374 1.00 68.12  ? 251 LEU   A CD1 1 
ATOM   1724 C CD2 . LEU   A 1 233 ? 10.515  -29.699 39.022 1.00 83.80  ? 251 LEU   A CD2 1 
ATOM   1725 N N   . PRO   A 1 234 ? 14.644  -27.967 40.839 1.00 68.64  ? 252 PRO   A N   1 
ATOM   1726 C CA  . PRO   A 1 234 ? 15.705  -28.770 41.468 1.00 62.97  ? 252 PRO   A CA  1 
ATOM   1727 C C   . PRO   A 1 234 ? 16.290  -28.126 42.713 1.00 69.34  ? 252 PRO   A C   1 
ATOM   1728 O O   . PRO   A 1 234 ? 16.547  -28.817 43.710 1.00 69.51  ? 252 PRO   A O   1 
ATOM   1729 C CB  . PRO   A 1 234 ? 16.746  -28.910 40.346 1.00 66.57  ? 252 PRO   A CB  1 
ATOM   1730 C CG  . PRO   A 1 234 ? 16.437  -27.819 39.382 1.00 65.28  ? 252 PRO   A CG  1 
ATOM   1731 C CD  . PRO   A 1 234 ? 14.960  -27.637 39.440 1.00 65.59  ? 252 PRO   A CD  1 
ATOM   1732 N N   . ILE   A 1 235 ? 16.495  -26.808 42.686 1.00 66.83  ? 253 ILE   A N   1 
ATOM   1733 C CA  . ILE   A 1 235 ? 17.047  -26.124 43.850 1.00 66.98  ? 253 ILE   A CA  1 
ATOM   1734 C C   . ILE   A 1 235 ? 16.096  -26.248 45.029 1.00 60.00  ? 253 ILE   A C   1 
ATOM   1735 O O   . ILE   A 1 235 ? 16.512  -26.524 46.161 1.00 58.13  ? 253 ILE   A O   1 
ATOM   1736 C CB  . ILE   A 1 235 ? 17.339  -24.650 43.514 1.00 76.78  ? 253 ILE   A CB  1 
ATOM   1737 C CG1 . ILE   A 1 235 ? 18.310  -24.550 42.335 1.00 74.72  ? 253 ILE   A CG1 1 
ATOM   1738 C CG2 . ILE   A 1 235 ? 17.913  -23.931 44.728 1.00 88.09  ? 253 ILE   A CG2 1 
ATOM   1739 C CD1 . ILE   A 1 235 ? 18.520  -23.140 41.833 1.00 70.65  ? 253 ILE   A CD1 1 
ATOM   1740 N N   . VAL   A 1 236 ? 14.803  -26.036 44.782 1.00 69.36  ? 254 VAL   A N   1 
ATOM   1741 C CA  . VAL   A 1 236 ? 13.812  -26.127 45.846 1.00 70.90  ? 254 VAL   A CA  1 
ATOM   1742 C C   . VAL   A 1 236 ? 13.778  -27.536 46.417 1.00 78.33  ? 254 VAL   A C   1 
ATOM   1743 O O   . VAL   A 1 236 ? 13.685  -27.724 47.634 1.00 72.26  ? 254 VAL   A O   1 
ATOM   1744 C CB  . VAL   A 1 236 ? 12.432  -25.694 45.322 1.00 77.04  ? 254 VAL   A CB  1 
ATOM   1745 C CG1 . VAL   A 1 236 ? 11.323  -26.233 46.219 1.00 83.56  ? 254 VAL   A CG1 1 
ATOM   1746 C CG2 . VAL   A 1 236 ? 12.358  -24.177 45.221 1.00 75.05  ? 254 VAL   A CG2 1 
ATOM   1747 N N   . CYS   A 1 237 ? 13.830  -28.548 45.550 1.00 87.34  ? 255 CYS   A N   1 
ATOM   1748 C CA  . CYS   A 1 237 ? 13.827  -29.924 46.036 1.00 81.74  ? 255 CYS   A CA  1 
ATOM   1749 C C   . CYS   A 1 237 ? 15.034  -30.185 46.927 1.00 81.62  ? 255 CYS   A C   1 
ATOM   1750 O O   . CYS   A 1 237 ? 14.907  -30.751 48.021 1.00 80.00  ? 255 CYS   A O   1 
ATOM   1751 C CB  . CYS   A 1 237 ? 13.808  -30.896 44.858 1.00 71.04  ? 255 CYS   A CB  1 
ATOM   1752 S SG  . CYS   A 1 237 ? 12.238  -30.926 43.973 1.00 76.57  ? 255 CYS   A SG  1 
ATOM   1753 N N   . GLY   A 1 238 ? 16.219  -29.768 46.476 1.00 68.90  ? 256 GLY   A N   1 
ATOM   1754 C CA  . GLY   A 1 238 ? 17.409  -29.961 47.287 1.00 70.58  ? 256 GLY   A CA  1 
ATOM   1755 C C   . GLY   A 1 238 ? 17.300  -29.276 48.635 1.00 80.03  ? 256 GLY   A C   1 
ATOM   1756 O O   . GLY   A 1 238 ? 17.598  -29.868 49.676 1.00 75.67  ? 256 GLY   A O   1 
ATOM   1757 N N   . MET   A 1 239 ? 16.857  -28.017 48.635 1.00 77.34  ? 257 MET   A N   1 
ATOM   1758 C CA  . MET   A 1 239 ? 16.749  -27.268 49.883 1.00 75.91  ? 257 MET   A CA  1 
ATOM   1759 C C   . MET   A 1 239 ? 15.742  -27.913 50.828 1.00 84.72  ? 257 MET   A C   1 
ATOM   1760 O O   . MET   A 1 239 ? 16.019  -28.095 52.019 1.00 101.38 ? 257 MET   A O   1 
ATOM   1761 C CB  . MET   A 1 239 ? 16.353  -25.821 49.591 1.00 90.93  ? 257 MET   A CB  1 
ATOM   1762 C CG  . MET   A 1 239 ? 17.407  -25.032 48.838 1.00 84.29  ? 257 MET   A CG  1 
ATOM   1763 S SD  . MET   A 1 239 ? 16.798  -23.438 48.263 1.00 68.21  ? 257 MET   A SD  1 
ATOM   1764 C CE  . MET   A 1 239 ? 16.321  -22.671 49.810 1.00 91.54  ? 257 MET   A CE  1 
ATOM   1765 N N   . GLN   A 1 240 ? 14.562  -28.267 50.313 1.00 85.29  ? 258 GLN   A N   1 
ATOM   1766 C CA  . GLN   A 1 240 ? 13.535  -28.860 51.161 1.00 89.03  ? 258 GLN   A CA  1 
ATOM   1767 C C   . GLN   A 1 240 ? 14.007  -30.180 51.751 1.00 97.53  ? 258 GLN   A C   1 
ATOM   1768 O O   . GLN   A 1 240 ? 13.797  -30.447 52.941 1.00 103.67 ? 258 GLN   A O   1 
ATOM   1769 C CB  . GLN   A 1 240 ? 12.248  -29.063 50.361 1.00 85.84  ? 258 GLN   A CB  1 
ATOM   1770 C CG  . GLN   A 1 240 ? 11.551  -27.773 49.969 1.00 97.57  ? 258 GLN   A CG  1 
ATOM   1771 C CD  . GLN   A 1 240 ? 10.341  -28.014 49.087 1.00 85.37  ? 258 GLN   A CD  1 
ATOM   1772 O OE1 . GLN   A 1 240 ? 10.041  -29.150 48.726 1.00 81.28  ? 258 GLN   A OE1 1 
ATOM   1773 N NE2 . GLN   A 1 240 ? 9.640   -26.943 48.736 1.00 101.22 ? 258 GLN   A NE2 1 
ATOM   1774 N N   . MET   A 1 241 ? 14.646  -31.025 50.938 1.00 95.33  ? 259 MET   A N   1 
ATOM   1775 C CA  . MET   A 1 241 ? 15.168  -32.278 51.469 1.00 84.71  ? 259 MET   A CA  1 
ATOM   1776 C C   . MET   A 1 241 ? 16.292  -32.033 52.468 1.00 81.39  ? 259 MET   A C   1 
ATOM   1777 O O   . MET   A 1 241 ? 16.490  -32.837 53.385 1.00 88.33  ? 259 MET   A O   1 
ATOM   1778 C CB  . MET   A 1 241 ? 15.650  -33.171 50.327 1.00 88.00  ? 259 MET   A CB  1 
ATOM   1779 C CG  . MET   A 1 241 ? 14.541  -33.975 49.669 1.00 82.65  ? 259 MET   A CG  1 
ATOM   1780 S SD  . MET   A 1 241 ? 13.935  -35.312 50.719 1.00 114.51 ? 259 MET   A SD  1 
ATOM   1781 C CE  . MET   A 1 241 ? 15.374  -36.379 50.786 1.00 78.22  ? 259 MET   A CE  1 
ATOM   1782 N N   . GLY   A 1 242 ? 17.029  -30.931 52.317 1.00 86.16  ? 260 GLY   A N   1 
ATOM   1783 C CA  . GLY   A 1 242 ? 18.097  -30.623 53.251 1.00 98.69  ? 260 GLY   A CA  1 
ATOM   1784 C C   . GLY   A 1 242 ? 17.615  -30.177 54.615 1.00 107.70 ? 260 GLY   A C   1 
ATOM   1785 O O   . GLY   A 1 242 ? 18.401  -30.180 55.568 1.00 128.92 ? 260 GLY   A O   1 
ATOM   1786 N N   . GLY   A 1 243 ? 16.349  -29.788 54.730 1.00 106.80 ? 261 GLY   A N   1 
ATOM   1787 C CA  . GLY   A 1 243 ? 15.786  -29.349 55.989 1.00 113.73 ? 261 GLY   A CA  1 
ATOM   1788 C C   . GLY   A 1 243 ? 15.481  -27.869 56.085 1.00 119.24 ? 261 GLY   A C   1 
ATOM   1789 O O   . GLY   A 1 243 ? 15.157  -27.395 57.181 1.00 118.37 ? 261 GLY   A O   1 
ATOM   1790 N N   . ILE   A 1 244 ? 15.572  -27.125 54.983 1.00 142.57 ? 262 ILE   A N   1 
ATOM   1791 C CA  . ILE   A 1 244 ? 15.243  -25.705 55.010 1.00 109.92 ? 262 ILE   A CA  1 
ATOM   1792 C C   . ILE   A 1 244 ? 13.730  -25.549 55.084 1.00 130.36 ? 262 ILE   A C   1 
ATOM   1793 O O   . ILE   A 1 244 ? 12.988  -26.145 54.291 1.00 145.86 ? 262 ILE   A O   1 
ATOM   1794 C CB  . ILE   A 1 244 ? 15.818  -24.992 53.776 1.00 104.20 ? 262 ILE   A CB  1 
ATOM   1795 C CG1 . ILE   A 1 244 ? 17.305  -25.322 53.594 1.00 101.98 ? 262 ILE   A CG1 1 
ATOM   1796 C CG2 . ILE   A 1 244 ? 15.625  -23.485 53.891 1.00 107.12 ? 262 ILE   A CG2 1 
ATOM   1797 C CD1 . ILE   A 1 244 ? 18.181  -24.947 54.775 1.00 113.87 ? 262 ILE   A CD1 1 
ATOM   1798 N N   . SER   A 1 245 ? 13.265  -24.755 56.043 1.00 171.76 ? 263 SER   A N   1 
ATOM   1799 C CA  . SER   A 1 245 ? 11.837  -24.512 56.185 1.00 167.02 ? 263 SER   A CA  1 
ATOM   1800 C C   . SER   A 1 245 ? 11.317  -23.681 55.017 1.00 191.98 ? 263 SER   A C   1 
ATOM   1801 O O   . SER   A 1 245 ? 12.027  -22.844 54.454 1.00 125.97 ? 263 SER   A O   1 
ATOM   1802 C CB  . SER   A 1 245 ? 11.546  -23.802 57.506 1.00 137.53 ? 263 SER   A CB  1 
ATOM   1803 O OG  . SER   A 1 245 ? 12.298  -22.607 57.620 1.00 152.29 ? 263 SER   A OG  1 
ATOM   1804 N N   . LEU   A 1 246 ? 10.052  -23.919 54.659 1.00 144.45 ? 264 LEU   A N   1 
ATOM   1805 C CA  . LEU   A 1 246 ? 9.488   -23.295 53.465 1.00 153.99 ? 264 LEU   A CA  1 
ATOM   1806 C C   . LEU   A 1 246 ? 9.451   -21.776 53.587 1.00 160.66 ? 264 LEU   A C   1 
ATOM   1807 O O   . LEU   A 1 246 ? 9.774   -21.063 52.629 1.00 156.68 ? 264 LEU   A O   1 
ATOM   1808 C CB  . LEU   A 1 246 ? 8.083   -23.839 53.207 1.00 153.09 ? 264 LEU   A CB  1 
ATOM   1809 C CG  . LEU   A 1 246 ? 7.965   -25.351 53.014 1.00 144.27 ? 264 LEU   A CG  1 
ATOM   1810 C CD1 . LEU   A 1 246 ? 6.515   -25.737 52.773 1.00 140.89 ? 264 LEU   A CD1 1 
ATOM   1811 C CD2 . LEU   A 1 246 ? 8.846   -25.823 51.866 1.00 123.74 ? 264 LEU   A CD2 1 
ATOM   1812 N N   . ASP   A 1 247 ? 9.059   -21.260 54.752 1.00 176.59 ? 265 ASP   A N   1 
ATOM   1813 C CA  . ASP   A 1 247 ? 8.911   -19.819 54.929 1.00 174.03 ? 265 ASP   A CA  1 
ATOM   1814 C C   . ASP   A 1 247 ? 10.241  -19.076 54.948 1.00 161.73 ? 265 ASP   A C   1 
ATOM   1815 O O   . ASP   A 1 247 ? 10.238  -17.854 55.132 1.00 157.86 ? 265 ASP   A O   1 
ATOM   1816 C CB  . ASP   A 1 247 ? 8.144   -19.526 56.221 1.00 187.25 ? 265 ASP   A CB  1 
ATOM   1817 C CG  . ASP   A 1 247 ? 6.675   -19.895 56.125 1.00 196.90 ? 265 ASP   A CG  1 
ATOM   1818 O OD1 . ASP   A 1 247 ? 6.247   -20.374 55.053 1.00 195.67 ? 265 ASP   A OD1 1 
ATOM   1819 O OD2 . ASP   A 1 247 ? 5.948   -19.702 57.122 1.00 204.46 ? 265 ASP   A OD2 1 
ATOM   1820 N N   . ASN   A 1 248 ? 11.365  -19.764 54.768 1.00 145.75 ? 266 ASN   A N   1 
ATOM   1821 C CA  . ASN   A 1 248 ? 12.655  -19.090 54.746 1.00 136.60 ? 266 ASN   A CA  1 
ATOM   1822 C C   . ASN   A 1 248 ? 12.742  -18.159 53.543 1.00 123.34 ? 266 ASN   A C   1 
ATOM   1823 O O   . ASN   A 1 248 ? 12.272  -18.483 52.449 1.00 113.80 ? 266 ASN   A O   1 
ATOM   1824 C CB  . ASN   A 1 248 ? 13.786  -20.116 54.708 1.00 129.98 ? 266 ASN   A CB  1 
ATOM   1825 C CG  . ASN   A 1 248 ? 15.143  -19.501 54.990 1.00 123.76 ? 266 ASN   A CG  1 
ATOM   1826 O OD1 . ASN   A 1 248 ? 15.448  -18.400 54.531 1.00 121.49 ? 266 ASN   A OD1 1 
ATOM   1827 N ND2 . ASN   A 1 248 ? 15.965  -20.210 55.755 1.00 127.66 ? 266 ASN   A ND2 1 
ATOM   1828 N N   . LEU   A 1 249 ? 13.353  -16.991 53.752 1.00 128.04 ? 267 LEU   A N   1 
ATOM   1829 C CA  . LEU   A 1 249 ? 13.434  -15.995 52.690 1.00 121.09 ? 267 LEU   A CA  1 
ATOM   1830 C C   . LEU   A 1 249 ? 14.246  -16.485 51.500 1.00 101.91 ? 267 LEU   A C   1 
ATOM   1831 O O   . LEU   A 1 249 ? 14.058  -15.981 50.387 1.00 103.40 ? 267 LEU   A O   1 
ATOM   1832 C CB  . LEU   A 1 249 ? 14.039  -14.702 53.235 1.00 116.62 ? 267 LEU   A CB  1 
ATOM   1833 C CG  . LEU   A 1 249 ? 13.771  -13.441 52.412 1.00 117.42 ? 267 LEU   A CG  1 
ATOM   1834 C CD1 . LEU   A 1 249 ? 12.277  -13.160 52.331 1.00 135.33 ? 267 LEU   A CD1 1 
ATOM   1835 C CD2 . LEU   A 1 249 ? 14.510  -12.250 53.003 1.00 116.08 ? 267 LEU   A CD2 1 
ATOM   1836 N N   . LEU   A 1 250 ? 15.134  -17.461 51.705 1.00 96.67  ? 268 LEU   A N   1 
ATOM   1837 C CA  . LEU   A 1 250 ? 15.917  -17.994 50.595 1.00 108.95 ? 268 LEU   A CA  1 
ATOM   1838 C C   . LEU   A 1 250 ? 15.019  -18.389 49.432 1.00 93.98  ? 268 LEU   A C   1 
ATOM   1839 O O   . LEU   A 1 250 ? 15.318  -18.087 48.271 1.00 90.73  ? 268 LEU   A O   1 
ATOM   1840 C CB  . LEU   A 1 250 ? 16.735  -19.197 51.066 1.00 99.28  ? 268 LEU   A CB  1 
ATOM   1841 C CG  . LEU   A 1 250 ? 17.901  -18.900 52.008 1.00 128.80 ? 268 LEU   A CG  1 
ATOM   1842 C CD1 . LEU   A 1 250 ? 18.474  -20.186 52.573 1.00 84.04  ? 268 LEU   A CD1 1 
ATOM   1843 C CD2 . LEU   A 1 250 ? 18.973  -18.117 51.274 1.00 118.85 ? 268 LEU   A CD2 1 
ATOM   1844 N N   . TYR   A 1 251 ? 13.891  -19.036 49.730 1.00 97.55  ? 269 TYR   A N   1 
ATOM   1845 C CA  . TYR   A 1 251 ? 13.016  -19.545 48.683 1.00 99.39  ? 269 TYR   A CA  1 
ATOM   1846 C C   . TYR   A 1 251 ? 12.506  -18.452 47.755 1.00 86.18  ? 269 TYR   A C   1 
ATOM   1847 O O   . TYR   A 1 251 ? 11.918  -18.772 46.715 1.00 89.82  ? 269 TYR   A O   1 
ATOM   1848 C CB  . TYR   A 1 251 ? 11.842  -20.291 49.316 1.00 108.09 ? 269 TYR   A CB  1 
ATOM   1849 C CG  . TYR   A 1 251 ? 12.230  -21.644 49.866 1.00 96.44  ? 269 TYR   A CG  1 
ATOM   1850 C CD1 . TYR   A 1 251 ? 12.251  -22.765 49.049 1.00 99.94  ? 269 TYR   A CD1 1 
ATOM   1851 C CD2 . TYR   A 1 251 ? 12.587  -21.798 51.197 1.00 107.68 ? 269 TYR   A CD2 1 
ATOM   1852 C CE1 . TYR   A 1 251 ? 12.612  -24.002 49.542 1.00 90.86  ? 269 TYR   A CE1 1 
ATOM   1853 C CE2 . TYR   A 1 251 ? 12.948  -23.031 51.699 1.00 112.52 ? 269 TYR   A CE2 1 
ATOM   1854 C CZ  . TYR   A 1 251 ? 12.958  -24.129 50.869 1.00 104.85 ? 269 TYR   A CZ  1 
ATOM   1855 O OH  . TYR   A 1 251 ? 13.318  -25.358 51.367 1.00 113.95 ? 269 TYR   A OH  1 
ATOM   1856 N N   . LYS   A 1 252 ? 12.714  -17.180 48.088 1.00 93.81  ? 270 LYS   A N   1 
ATOM   1857 C CA  . LYS   A 1 252 ? 12.443  -16.105 47.143 1.00 97.20  ? 270 LYS   A CA  1 
ATOM   1858 C C   . LYS   A 1 252 ? 13.710  -15.649 46.431 1.00 86.51  ? 270 LYS   A C   1 
ATOM   1859 O O   . LYS   A 1 252 ? 13.723  -15.539 45.200 1.00 81.16  ? 270 LYS   A O   1 
ATOM   1860 C CB  . LYS   A 1 252 ? 11.781  -14.915 47.849 1.00 100.13 ? 270 LYS   A CB  1 
ATOM   1861 C CG  . LYS   A 1 252 ? 11.159  -13.899 46.893 1.00 99.18  ? 270 LYS   A CG  1 
ATOM   1862 C CD  . LYS   A 1 252 ? 10.049  -14.516 46.042 1.00 100.75 ? 270 LYS   A CD  1 
ATOM   1863 C CE  . LYS   A 1 252 ? 9.384   -13.487 45.141 1.00 110.69 ? 270 LYS   A CE  1 
ATOM   1864 N NZ  . LYS   A 1 252 ? 8.312   -14.097 44.305 1.00 152.30 ? 270 LYS   A NZ  1 
ATOM   1865 N N   . LYS   A 1 253 ? 14.790  -15.410 47.178 1.00 77.83  ? 271 LYS   A N   1 
ATOM   1866 C CA  . LYS   A 1 253 ? 16.056  -15.073 46.538 1.00 75.68  ? 271 LYS   A CA  1 
ATOM   1867 C C   . LYS   A 1 253 ? 16.399  -16.114 45.485 1.00 83.44  ? 271 LYS   A C   1 
ATOM   1868 O O   . LYS   A 1 253 ? 16.630  -15.789 44.313 1.00 79.16  ? 271 LYS   A O   1 
ATOM   1869 C CB  . LYS   A 1 253 ? 17.167  -14.984 47.584 1.00 85.89  ? 271 LYS   A CB  1 
ATOM   1870 C CG  . LYS   A 1 253 ? 16.889  -14.011 48.709 1.00 108.16 ? 271 LYS   A CG  1 
ATOM   1871 C CD  . LYS   A 1 253 ? 17.973  -14.073 49.764 1.00 93.11  ? 271 LYS   A CD  1 
ATOM   1872 C CE  . LYS   A 1 253 ? 17.607  -13.234 50.968 1.00 108.13 ? 271 LYS   A CE  1 
ATOM   1873 N NZ  . LYS   A 1 253 ? 18.580  -13.414 52.072 1.00 118.56 ? 271 LYS   A NZ  1 
ATOM   1874 N N   . VAL   A 1 254 ? 16.355  -17.388 45.879 1.00 85.08  ? 272 VAL   A N   1 
ATOM   1875 C CA  . VAL   A 1 254 ? 16.622  -18.476 44.946 1.00 71.73  ? 272 VAL   A CA  1 
ATOM   1876 C C   . VAL   A 1 254 ? 15.746  -18.327 43.712 1.00 73.35  ? 272 VAL   A C   1 
ATOM   1877 O O   . VAL   A 1 254 ? 16.225  -18.392 42.573 1.00 81.95  ? 272 VAL   A O   1 
ATOM   1878 C CB  . VAL   A 1 254 ? 16.393  -19.831 45.638 1.00 83.59  ? 272 VAL   A CB  1 
ATOM   1879 C CG1 . VAL   A 1 254 ? 16.231  -20.943 44.613 1.00 82.27  ? 272 VAL   A CG1 1 
ATOM   1880 C CG2 . VAL   A 1 254 ? 17.538  -20.131 46.594 1.00 87.00  ? 272 VAL   A CG2 1 
ATOM   1881 N N   . GLU   A 1 255 ? 14.451  -18.079 43.924 1.00 72.96  ? 273 GLU   A N   1 
ATOM   1882 C CA  . GLU   A 1 255 ? 13.546  -17.919 42.795 1.00 69.68  ? 273 GLU   A CA  1 
ATOM   1883 C C   . GLU   A 1 255 ? 14.103  -16.896 41.816 1.00 69.97  ? 273 GLU   A C   1 
ATOM   1884 O O   . GLU   A 1 255 ? 14.298  -17.194 40.631 1.00 70.06  ? 273 GLU   A O   1 
ATOM   1885 C CB  . GLU   A 1 255 ? 12.160  -17.505 43.297 1.00 74.92  ? 273 GLU   A CB  1 
ATOM   1886 C CG  . GLU   A 1 255 ? 11.108  -17.345 42.209 1.00 79.34  ? 273 GLU   A CG  1 
ATOM   1887 C CD  . GLU   A 1 255 ? 9.732   -17.031 42.772 1.00 87.76  ? 273 GLU   A CD  1 
ATOM   1888 O OE1 . GLU   A 1 255 ? 9.548   -17.157 44.001 1.00 100.97 ? 273 GLU   A OE1 1 
ATOM   1889 O OE2 . GLU   A 1 255 ? 8.835   -16.660 41.988 1.00 78.55  ? 273 GLU   A OE2 1 
ATOM   1890 N N   . ASN   A 1 256 ? 14.449  -15.707 42.316 1.00 81.12  ? 274 ASN   A N   1 
ATOM   1891 C CA  . ASN   A 1 256 ? 15.010  -14.687 41.440 1.00 78.69  ? 274 ASN   A CA  1 
ATOM   1892 C C   . ASN   A 1 256 ? 16.202  -15.243 40.678 1.00 71.04  ? 274 ASN   A C   1 
ATOM   1893 O O   . ASN   A 1 256 ? 16.252  -15.183 39.444 1.00 72.11  ? 274 ASN   A O   1 
ATOM   1894 C CB  . ASN   A 1 256 ? 15.413  -13.455 42.251 1.00 86.19  ? 274 ASN   A CB  1 
ATOM   1895 C CG  . ASN   A 1 256 ? 14.223  -12.598 42.638 1.00 110.78 ? 274 ASN   A CG  1 
ATOM   1896 O OD1 . ASN   A 1 256 ? 13.948  -11.578 42.005 1.00 141.65 ? 274 ASN   A OD1 1 
ATOM   1897 N ND2 . ASN   A 1 256 ? 13.506  -13.012 43.676 1.00 110.92 ? 274 ASN   A ND2 1 
ATOM   1898 N N   . ILE   A 1 257 ? 17.148  -15.847 41.399 1.00 66.05  ? 275 ILE   A N   1 
ATOM   1899 C CA  . ILE   A 1 257 ? 18.326  -16.392 40.736 1.00 69.68  ? 275 ILE   A CA  1 
ATOM   1900 C C   . ILE   A 1 257 ? 17.895  -17.356 39.645 1.00 72.49  ? 275 ILE   A C   1 
ATOM   1901 O O   . ILE   A 1 257 ? 18.312  -17.240 38.485 1.00 75.89  ? 275 ILE   A O   1 
ATOM   1902 C CB  . ILE   A 1 257 ? 19.256  -17.066 41.759 1.00 71.94  ? 275 ILE   A CB  1 
ATOM   1903 C CG1 . ILE   A 1 257 ? 19.794  -16.009 42.726 1.00 83.07  ? 275 ILE   A CG1 1 
ATOM   1904 C CG2 . ILE   A 1 257 ? 20.387  -17.811 41.045 1.00 73.57  ? 275 ILE   A CG2 1 
ATOM   1905 C CD1 . ILE   A 1 257 ? 20.813  -16.515 43.718 1.00 92.88  ? 275 ILE   A CD1 1 
ATOM   1906 N N   . ALA   A 1 258 ? 16.993  -18.280 39.986 1.00 71.23  ? 276 ALA   A N   1 
ATOM   1907 C CA  . ALA   A 1 258 ? 16.522  -19.229 38.989 1.00 72.79  ? 276 ALA   A CA  1 
ATOM   1908 C C   . ALA   A 1 258 ? 16.054  -18.483 37.752 1.00 71.30  ? 276 ALA   A C   1 
ATOM   1909 O O   . ALA   A 1 258 ? 16.541  -18.726 36.640 1.00 72.02  ? 276 ALA   A O   1 
ATOM   1910 C CB  . ALA   A 1 258 ? 15.397  -20.087 39.568 1.00 72.21  ? 276 ALA   A CB  1 
ATOM   1911 N N   . ILE   A 1 259 ? 15.179  -17.494 37.951 1.00 73.66  ? 277 ILE   A N   1 
ATOM   1912 C CA  . ILE   A 1 259 ? 14.695  -16.691 36.833 1.00 77.49  ? 277 ILE   A CA  1 
ATOM   1913 C C   . ILE   A 1 259 ? 15.872  -16.241 35.984 1.00 78.93  ? 277 ILE   A C   1 
ATOM   1914 O O   . ILE   A 1 259 ? 15.995  -16.606 34.806 1.00 83.82  ? 277 ILE   A O   1 
ATOM   1915 C CB  . ILE   A 1 259 ? 13.878  -15.494 37.348 1.00 64.16  ? 277 ILE   A CB  1 
ATOM   1916 C CG1 . ILE   A 1 259 ? 12.532  -15.975 37.899 1.00 70.25  ? 277 ILE   A CG1 1 
ATOM   1917 C CG2 . ILE   A 1 259 ? 13.696  -14.462 36.247 1.00 77.06  ? 277 ILE   A CG2 1 
ATOM   1918 C CD1 . ILE   A 1 259 ? 11.789  -14.938 38.709 1.00 74.27  ? 277 ILE   A CD1 1 
ATOM   1919 N N   . LEU   A 1 260 ? 16.802  -15.508 36.600 1.00 69.00  ? 278 LEU   A N   1 
ATOM   1920 C CA  . LEU   A 1 260 ? 17.936  -14.996 35.845 1.00 71.53  ? 278 LEU   A CA  1 
ATOM   1921 C C   . LEU   A 1 260 ? 18.618  -16.129 35.099 1.00 73.94  ? 278 LEU   A C   1 
ATOM   1922 O O   . LEU   A 1 260 ? 18.746  -16.093 33.868 1.00 78.93  ? 278 LEU   A O   1 
ATOM   1923 C CB  . LEU   A 1 260 ? 18.917  -14.293 36.783 1.00 85.93  ? 278 LEU   A CB  1 
ATOM   1924 C CG  . LEU   A 1 260 ? 18.365  -13.094 37.556 1.00 87.27  ? 278 LEU   A CG  1 
ATOM   1925 C CD1 . LEU   A 1 260 ? 19.410  -12.556 38.523 1.00 101.15 ? 278 LEU   A CD1 1 
ATOM   1926 C CD2 . LEU   A 1 260 ? 17.906  -12.006 36.600 1.00 89.64  ? 278 LEU   A CD2 1 
ATOM   1927 N N   . MET   A 1 261 ? 18.978  -17.194 35.821 1.00 81.91  ? 279 MET   A N   1 
ATOM   1928 C CA  . MET   A 1 261 ? 19.664  -18.304 35.176 1.00 79.55  ? 279 MET   A CA  1 
ATOM   1929 C C   . MET   A 1 261 ? 18.844  -18.814 34.004 1.00 80.64  ? 279 MET   A C   1 
ATOM   1930 O O   . MET   A 1 261 ? 19.346  -18.917 32.878 1.00 86.13  ? 279 MET   A O   1 
ATOM   1931 C CB  . MET   A 1 261 ? 19.930  -19.422 36.183 1.00 70.48  ? 279 MET   A CB  1 
ATOM   1932 C CG  . MET   A 1 261 ? 20.873  -19.026 37.306 1.00 79.10  ? 279 MET   A CG  1 
ATOM   1933 S SD  . MET   A 1 261 ? 21.298  -20.402 38.390 1.00 81.17  ? 279 MET   A SD  1 
ATOM   1934 C CE  . MET   A 1 261 ? 22.304  -21.405 37.297 1.00 94.20  ? 279 MET   A CE  1 
ATOM   1935 N N   . GLY   A 1 262 ? 17.558  -19.077 34.240 1.00 78.32  ? 280 GLY   A N   1 
ATOM   1936 C CA  . GLY   A 1 262 ? 16.687  -19.514 33.174 1.00 81.95  ? 280 GLY   A CA  1 
ATOM   1937 C C   . GLY   A 1 262 ? 16.901  -18.615 31.982 1.00 77.17  ? 280 GLY   A C   1 
ATOM   1938 O O   . GLY   A 1 262 ? 17.390  -19.057 30.933 1.00 86.23  ? 280 GLY   A O   1 
ATOM   1939 N N   . GLU   A 1 263 ? 16.614  -17.326 32.177 1.00 86.58  ? 281 GLU   A N   1 
ATOM   1940 C CA  . GLU   A 1 263 ? 16.800  -16.344 31.120 1.00 96.96  ? 281 GLU   A CA  1 
ATOM   1941 C C   . GLU   A 1 263 ? 18.120  -16.608 30.413 1.00 95.37  ? 281 GLU   A C   1 
ATOM   1942 O O   . GLU   A 1 263 ? 18.150  -17.016 29.243 1.00 104.09 ? 281 GLU   A O   1 
ATOM   1943 C CB  . GLU   A 1 263 ? 16.758  -14.935 31.721 1.00 89.50  ? 281 GLU   A CB  1 
ATOM   1944 C CG  . GLU   A 1 263 ? 16.322  -13.845 30.761 1.00 108.24 ? 281 GLU   A CG  1 
ATOM   1945 C CD  . GLU   A 1 263 ? 16.232  -12.488 31.436 1.00 120.31 ? 281 GLU   A CD  1 
ATOM   1946 O OE1 . GLU   A 1 263 ? 15.988  -12.449 32.662 1.00 103.04 ? 281 GLU   A OE1 1 
ATOM   1947 O OE2 . GLU   A 1 263 ? 16.408  -11.462 30.743 1.00 102.14 ? 281 GLU   A OE2 1 
ATOM   1948 N N   . TYR   A 1 264 ? 19.216  -16.485 31.166 1.00 90.89  ? 282 TYR   A N   1 
ATOM   1949 C CA  . TYR   A 1 264 ? 20.548  -16.696 30.622 1.00 97.36  ? 282 TYR   A CA  1 
ATOM   1950 C C   . TYR   A 1 264 ? 20.559  -17.912 29.708 1.00 102.02 ? 282 TYR   A C   1 
ATOM   1951 O O   . TYR   A 1 264 ? 20.684  -17.789 28.480 1.00 105.00 ? 282 TYR   A O   1 
ATOM   1952 C CB  . TYR   A 1 264 ? 21.532  -16.861 31.790 1.00 93.59  ? 282 TYR   A CB  1 
ATOM   1953 C CG  . TYR   A 1 264 ? 22.957  -17.217 31.421 1.00 95.38  ? 282 TYR   A CG  1 
ATOM   1954 C CD1 . TYR   A 1 264 ? 23.354  -18.542 31.301 1.00 113.81 ? 282 TYR   A CD1 1 
ATOM   1955 C CD2 . TYR   A 1 264 ? 23.912  -16.229 31.230 1.00 114.53 ? 282 TYR   A CD2 1 
ATOM   1956 C CE1 . TYR   A 1 264 ? 24.658  -18.873 30.979 1.00 134.59 ? 282 TYR   A CE1 1 
ATOM   1957 C CE2 . TYR   A 1 264 ? 25.218  -16.550 30.909 1.00 108.98 ? 282 TYR   A CE2 1 
ATOM   1958 C CZ  . TYR   A 1 264 ? 25.585  -17.874 30.785 1.00 111.43 ? 282 TYR   A CZ  1 
ATOM   1959 O OH  . TYR   A 1 264 ? 26.884  -18.199 30.466 1.00 132.74 ? 282 TYR   A OH  1 
ATOM   1960 N N   . PHE   A 1 265 ? 20.310  -19.088 30.283 1.00 101.52 ? 283 PHE   A N   1 
ATOM   1961 C CA  . PHE   A 1 265 ? 20.510  -20.312 29.521 1.00 97.50  ? 283 PHE   A CA  1 
ATOM   1962 C C   . PHE   A 1 265 ? 19.584  -20.359 28.316 1.00 99.42  ? 283 PHE   A C   1 
ATOM   1963 O O   . PHE   A 1 265 ? 20.005  -20.742 27.217 1.00 106.29 ? 283 PHE   A O   1 
ATOM   1964 C CB  . PHE   A 1 265 ? 20.320  -21.530 30.423 1.00 84.64  ? 283 PHE   A CB  1 
ATOM   1965 C CG  . PHE   A 1 265 ? 21.545  -21.872 31.226 1.00 95.96  ? 283 PHE   A CG  1 
ATOM   1966 C CD1 . PHE   A 1 265 ? 22.541  -22.667 30.685 1.00 105.63 ? 283 PHE   A CD1 1 
ATOM   1967 C CD2 . PHE   A 1 265 ? 21.712  -21.382 32.511 1.00 92.06  ? 283 PHE   A CD2 1 
ATOM   1968 C CE1 . PHE   A 1 265 ? 23.675  -22.977 31.413 1.00 94.22  ? 283 PHE   A CE1 1 
ATOM   1969 C CE2 . PHE   A 1 265 ? 22.844  -21.691 33.245 1.00 83.56  ? 283 PHE   A CE2 1 
ATOM   1970 C CZ  . PHE   A 1 265 ? 23.826  -22.489 32.694 1.00 98.70  ? 283 PHE   A CZ  1 
ATOM   1971 N N   . GLN   A 1 266 ? 18.332  -19.924 28.480 1.00 98.22  ? 284 GLN   A N   1 
ATOM   1972 C CA  . GLN   A 1 266 ? 17.423  -19.988 27.344 1.00 89.23  ? 284 GLN   A CA  1 
ATOM   1973 C C   . GLN   A 1 266 ? 17.952  -19.141 26.198 1.00 94.56  ? 284 GLN   A C   1 
ATOM   1974 O O   . GLN   A 1 266 ? 17.969  -19.586 25.044 1.00 119.31 ? 284 GLN   A O   1 
ATOM   1975 C CB  . GLN   A 1 266 ? 16.020  -19.545 27.747 1.00 102.99 ? 284 GLN   A CB  1 
ATOM   1976 C CG  . GLN   A 1 266 ? 14.995  -19.660 26.623 1.00 106.28 ? 284 GLN   A CG  1 
ATOM   1977 C CD  . GLN   A 1 266 ? 14.981  -21.031 25.974 1.00 115.90 ? 284 GLN   A CD  1 
ATOM   1978 O OE1 . GLN   A 1 266 ? 14.880  -22.050 26.654 1.00 92.07  ? 284 GLN   A OE1 1 
ATOM   1979 N NE2 . GLN   A 1 266 ? 15.089  -21.063 24.650 1.00 137.33 ? 284 GLN   A NE2 1 
ATOM   1980 N N   . VAL   A 1 267 ? 18.443  -17.938 26.504 1.00 107.83 ? 285 VAL   A N   1 
ATOM   1981 C CA  . VAL   A 1 267 ? 19.054  -17.124 25.460 1.00 111.56 ? 285 VAL   A CA  1 
ATOM   1982 C C   . VAL   A 1 267 ? 20.189  -17.899 24.812 1.00 120.48 ? 285 VAL   A C   1 
ATOM   1983 O O   . VAL   A 1 267 ? 20.256  -18.031 23.583 1.00 120.02 ? 285 VAL   A O   1 
ATOM   1984 C CB  . VAL   A 1 267 ? 19.536  -15.780 26.033 1.00 104.86 ? 285 VAL   A CB  1 
ATOM   1985 C CG1 . VAL   A 1 267 ? 20.316  -15.004 24.985 1.00 108.18 ? 285 VAL   A CG1 1 
ATOM   1986 C CG2 . VAL   A 1 267 ? 18.352  -14.966 26.529 1.00 116.36 ? 285 VAL   A CG2 1 
ATOM   1987 N N   . HIS   A 1 268 ? 21.063  -18.479 25.637 1.00 119.57 ? 286 HIS   A N   1 
ATOM   1988 C CA  . HIS   A 1 268 ? 22.131  -19.315 25.107 1.00 116.42 ? 286 HIS   A CA  1 
ATOM   1989 C C   . HIS   A 1 268 ? 21.558  -20.365 24.168 1.00 112.26 ? 286 HIS   A C   1 
ATOM   1990 O O   . HIS   A 1 268 ? 22.039  -20.542 23.042 1.00 123.66 ? 286 HIS   A O   1 
ATOM   1991 C CB  . HIS   A 1 268 ? 22.899  -19.969 26.256 1.00 123.21 ? 286 HIS   A CB  1 
ATOM   1992 C CG  . HIS   A 1 268 ? 24.019  -20.856 25.809 1.00 126.30 ? 286 HIS   A CG  1 
ATOM   1993 N ND1 . HIS   A 1 268 ? 25.077  -20.397 25.054 1.00 109.01 ? 286 HIS   A ND1 1 
ATOM   1994 C CD2 . HIS   A 1 268 ? 24.247  -22.175 26.015 1.00 120.52 ? 286 HIS   A CD2 1 
ATOM   1995 C CE1 . HIS   A 1 268 ? 25.908  -21.395 24.813 1.00 105.66 ? 286 HIS   A CE1 1 
ATOM   1996 N NE2 . HIS   A 1 268 ? 25.428  -22.485 25.386 1.00 128.65 ? 286 HIS   A NE2 1 
ATOM   1997 N N   . ASP   A 1 269 ? 20.492  -21.041 24.600 1.00 116.60 ? 287 ASP   A N   1 
ATOM   1998 C CA  . ASP   A 1 269 ? 19.880  -22.061 23.760 1.00 122.55 ? 287 ASP   A CA  1 
ATOM   1999 C C   . ASP   A 1 269 ? 19.519  -21.484 22.399 1.00 133.41 ? 287 ASP   A C   1 
ATOM   2000 O O   . ASP   A 1 269 ? 19.878  -22.045 21.355 1.00 140.88 ? 287 ASP   A O   1 
ATOM   2001 C CB  . ASP   A 1 269 ? 18.647  -22.637 24.456 1.00 114.00 ? 287 ASP   A CB  1 
ATOM   2002 C CG  . ASP   A 1 269 ? 18.239  -23.986 23.899 1.00 126.11 ? 287 ASP   A CG  1 
ATOM   2003 O OD1 . ASP   A 1 269 ? 18.319  -24.175 22.666 1.00 140.92 ? 287 ASP   A OD1 1 
ATOM   2004 O OD2 . ASP   A 1 269 ? 17.846  -24.862 24.698 1.00 114.20 ? 287 ASP   A OD2 1 
ATOM   2005 N N   . ASP   A 1 270 ? 18.843  -20.332 22.390 1.00 129.19 ? 288 ASP   A N   1 
ATOM   2006 C CA  . ASP   A 1 270 ? 18.486  -19.712 21.120 1.00 131.15 ? 288 ASP   A CA  1 
ATOM   2007 C C   . ASP   A 1 270 ? 19.733  -19.371 20.319 1.00 133.32 ? 288 ASP   A C   1 
ATOM   2008 O O   . ASP   A 1 270 ? 19.776  -19.587 19.103 1.00 136.92 ? 288 ASP   A O   1 
ATOM   2009 C CB  . ASP   A 1 270 ? 17.636  -18.465 21.356 1.00 125.20 ? 288 ASP   A CB  1 
ATOM   2010 C CG  . ASP   A 1 270 ? 16.215  -18.798 21.771 1.00 127.05 ? 288 ASP   A CG  1 
ATOM   2011 O OD1 . ASP   A 1 270 ? 15.937  -19.984 22.044 1.00 129.58 ? 288 ASP   A OD1 1 
ATOM   2012 O OD2 . ASP   A 1 270 ? 15.376  -17.874 21.819 1.00 128.02 ? 288 ASP   A OD2 1 
ATOM   2013 N N   . TYR   A 1 271 ? 20.771  -18.861 20.990 1.00 129.63 ? 289 TYR   A N   1 
ATOM   2014 C CA  . TYR   A 1 271 ? 22.020  -18.576 20.294 1.00 131.34 ? 289 TYR   A CA  1 
ATOM   2015 C C   . TYR   A 1 271 ? 22.558  -19.828 19.615 1.00 130.71 ? 289 TYR   A C   1 
ATOM   2016 O O   . TYR   A 1 271 ? 23.119  -19.755 18.515 1.00 137.68 ? 289 TYR   A O   1 
ATOM   2017 C CB  . TYR   A 1 271 ? 23.047  -18.005 21.273 1.00 124.74 ? 289 TYR   A CB  1 
ATOM   2018 C CG  . TYR   A 1 271 ? 24.445  -17.901 20.705 1.00 127.50 ? 289 TYR   A CG  1 
ATOM   2019 C CD1 . TYR   A 1 271 ? 24.786  -16.881 19.828 1.00 130.95 ? 289 TYR   A CD1 1 
ATOM   2020 C CD2 . TYR   A 1 271 ? 25.425  -18.823 21.051 1.00 117.62 ? 289 TYR   A CD2 1 
ATOM   2021 C CE1 . TYR   A 1 271 ? 26.062  -16.782 19.307 1.00 125.55 ? 289 TYR   A CE1 1 
ATOM   2022 C CE2 . TYR   A 1 271 ? 26.704  -18.733 20.536 1.00 130.59 ? 289 TYR   A CE2 1 
ATOM   2023 C CZ  . TYR   A 1 271 ? 27.017  -17.710 19.665 1.00 134.93 ? 289 TYR   A CZ  1 
ATOM   2024 O OH  . TYR   A 1 271 ? 28.289  -17.615 19.149 1.00 136.02 ? 289 TYR   A OH  1 
ATOM   2025 N N   . ILE   A 1 272 ? 22.390  -20.989 20.252 1.00 133.83 ? 290 ILE   A N   1 
ATOM   2026 C CA  . ILE   A 1 272 ? 22.818  -22.234 19.625 1.00 125.55 ? 290 ILE   A CA  1 
ATOM   2027 C C   . ILE   A 1 272 ? 21.937  -22.553 18.424 1.00 158.70 ? 290 ILE   A C   1 
ATOM   2028 O O   . ILE   A 1 272 ? 22.426  -22.999 17.379 1.00 139.72 ? 290 ILE   A O   1 
ATOM   2029 C CB  . ILE   A 1 272 ? 22.812  -23.380 20.652 1.00 123.09 ? 290 ILE   A CB  1 
ATOM   2030 C CG1 . ILE   A 1 272 ? 23.802  -23.084 21.783 1.00 128.82 ? 290 ILE   A CG1 1 
ATOM   2031 C CG2 . ILE   A 1 272 ? 23.154  -24.703 19.975 1.00 167.36 ? 290 ILE   A CG2 1 
ATOM   2032 C CD1 . ILE   A 1 272 ? 23.772  -24.102 22.906 1.00 150.13 ? 290 ILE   A CD1 1 
ATOM   2033 N N   . ASP   A 1 273 ? 20.626  -22.331 18.550 1.00 134.75 ? 291 ASP   A N   1 
ATOM   2034 C CA  . ASP   A 1 273 ? 19.710  -22.690 17.471 1.00 141.72 ? 291 ASP   A CA  1 
ATOM   2035 C C   . ASP   A 1 273 ? 20.025  -21.906 16.203 1.00 142.74 ? 291 ASP   A C   1 
ATOM   2036 O O   . ASP   A 1 273 ? 20.116  -22.477 15.110 1.00 152.44 ? 291 ASP   A O   1 
ATOM   2037 C CB  . ASP   A 1 273 ? 18.265  -22.449 17.911 1.00 139.58 ? 291 ASP   A CB  1 
ATOM   2038 C CG  . ASP   A 1 273 ? 17.256  -22.791 16.828 1.00 136.98 ? 291 ASP   A CG  1 
ATOM   2039 O OD1 . ASP   A 1 273 ? 17.302  -22.174 15.743 1.00 129.25 ? 291 ASP   A OD1 1 
ATOM   2040 O OD2 . ASP   A 1 273 ? 16.418  -23.687 17.062 1.00 142.70 ? 291 ASP   A OD2 1 
ATOM   2041 N N   . THR   A 1 274 ? 20.198  -20.593 16.331 1.00 152.04 ? 292 THR   A N   1 
ATOM   2042 C CA  . THR   A 1 274 ? 20.501  -19.750 15.183 1.00 143.52 ? 292 THR   A CA  1 
ATOM   2043 C C   . THR   A 1 274 ? 21.981  -19.748 14.823 1.00 147.17 ? 292 THR   A C   1 
ATOM   2044 O O   . THR   A 1 274 ? 22.330  -19.315 13.719 1.00 144.19 ? 292 THR   A O   1 
ATOM   2045 C CB  . THR   A 1 274 ? 20.042  -18.316 15.457 1.00 139.67 ? 292 THR   A CB  1 
ATOM   2046 O OG1 . THR   A 1 274 ? 20.602  -17.862 16.696 1.00 142.15 ? 292 THR   A OG1 1 
ATOM   2047 C CG2 . THR   A 1 274 ? 18.522  -18.247 15.533 1.00 131.94 ? 292 THR   A CG2 1 
ATOM   2048 N N   . PHE   A 1 275 ? 22.848  -20.228 15.710 1.00 142.76 ? 293 PHE   A N   1 
ATOM   2049 C CA  . PHE   A 1 275 ? 24.287  -20.240 15.462 1.00 152.85 ? 293 PHE   A CA  1 
ATOM   2050 C C   . PHE   A 1 275 ? 24.787  -18.852 15.074 1.00 148.24 ? 293 PHE   A C   1 
ATOM   2051 O O   . PHE   A 1 275 ? 24.539  -17.873 15.778 1.00 139.52 ? 293 PHE   A O   1 
ATOM   2052 C CB  . PHE   A 1 275 ? 24.638  -21.248 14.365 1.00 148.30 ? 293 PHE   A CB  1 
ATOM   2053 C CG  . PHE   A 1 275 ? 24.326  -22.674 14.726 1.00 148.73 ? 293 PHE   A CG  1 
ATOM   2054 C CD1 . PHE   A 1 275 ? 25.153  -23.382 15.582 1.00 155.56 ? 293 PHE   A CD1 1 
ATOM   2055 C CD2 . PHE   A 1 275 ? 23.211  -23.308 14.203 1.00 152.00 ? 293 PHE   A CD2 1 
ATOM   2056 C CE1 . PHE   A 1 275 ? 24.871  -24.694 15.915 1.00 156.16 ? 293 PHE   A CE1 1 
ATOM   2057 C CE2 . PHE   A 1 275 ? 22.924  -24.620 14.531 1.00 156.32 ? 293 PHE   A CE2 1 
ATOM   2058 C CZ  . PHE   A 1 275 ? 23.756  -25.314 15.388 1.00 157.73 ? 293 PHE   A CZ  1 
ATOM   2059 N N   . SER   A 1 286 ? 15.798  -24.718 14.567 1.00 140.19 ? 304 SER   A N   1 
ATOM   2060 C CA  . SER   A 1 286 ? 14.730  -24.502 13.599 1.00 138.72 ? 304 SER   A CA  1 
ATOM   2061 C C   . SER   A 1 286 ? 13.662  -23.573 14.167 1.00 134.17 ? 304 SER   A C   1 
ATOM   2062 O O   . SER   A 1 286 ? 12.475  -23.724 13.874 1.00 130.84 ? 304 SER   A O   1 
ATOM   2063 C CB  . SER   A 1 286 ? 14.101  -25.835 13.188 1.00 144.49 ? 304 SER   A CB  1 
ATOM   2064 O OG  . SER   A 1 286 ? 13.543  -26.500 14.307 1.00 151.94 ? 304 SER   A OG  1 
ATOM   2065 N N   . ASP   A 1 287 ? 14.093  -22.608 14.983 1.00 191.54 ? 305 ASP   A N   1 
ATOM   2066 C CA  . ASP   A 1 287 ? 13.153  -21.643 15.545 1.00 131.17 ? 305 ASP   A CA  1 
ATOM   2067 C C   . ASP   A 1 287 ? 12.493  -20.820 14.447 1.00 153.61 ? 305 ASP   A C   1 
ATOM   2068 O O   . ASP   A 1 287 ? 11.294  -20.524 14.514 1.00 160.47 ? 305 ASP   A O   1 
ATOM   2069 C CB  . ASP   A 1 287 ? 13.871  -20.728 16.536 1.00 134.79 ? 305 ASP   A CB  1 
ATOM   2070 C CG  . ASP   A 1 287 ? 14.340  -21.462 17.778 1.00 165.20 ? 305 ASP   A CG  1 
ATOM   2071 O OD1 . ASP   A 1 287 ? 13.739  -22.502 18.120 1.00 209.35 ? 305 ASP   A OD1 1 
ATOM   2072 O OD2 . ASP   A 1 287 ? 15.307  -20.995 18.416 1.00 123.08 ? 305 ASP   A OD2 1 
ATOM   2073 N N   . ILE   A 1 288 ? 13.264  -20.437 13.430 1.00 164.73 ? 306 ILE   A N   1 
ATOM   2074 C CA  . ILE   A 1 288 ? 12.718  -19.640 12.338 1.00 134.26 ? 306 ILE   A CA  1 
ATOM   2075 C C   . ILE   A 1 288 ? 11.684  -20.442 11.554 1.00 161.03 ? 306 ILE   A C   1 
ATOM   2076 O O   . ILE   A 1 288 ? 10.646  -19.908 11.145 1.00 152.44 ? 306 ILE   A O   1 
ATOM   2077 C CB  . ILE   A 1 288 ? 13.858  -19.140 11.433 1.00 137.67 ? 306 ILE   A CB  1 
ATOM   2078 C CG1 . ILE   A 1 288 ? 14.842  -18.291 12.247 1.00 193.19 ? 306 ILE   A CG1 1 
ATOM   2079 C CG2 . ILE   A 1 288 ? 13.297  -18.345 10.265 1.00 142.59 ? 306 ILE   A CG2 1 
ATOM   2080 C CD1 . ILE   A 1 288 ? 16.133  -17.977 11.523 1.00 161.18 ? 306 ILE   A CD1 1 
ATOM   2081 N N   . GLN   A 1 289 ? 11.949  -21.733 11.332 1.00 142.43 ? 307 GLN   A N   1 
ATOM   2082 C CA  . GLN   A 1 289 ? 11.004  -22.565 10.594 1.00 127.24 ? 307 GLN   A CA  1 
ATOM   2083 C C   . GLN   A 1 289 ? 9.647   -22.596 11.282 1.00 129.15 ? 307 GLN   A C   1 
ATOM   2084 O O   . GLN   A 1 289 ? 8.605   -22.462 10.629 1.00 122.63 ? 307 GLN   A O   1 
ATOM   2085 C CB  . GLN   A 1 289 ? 11.547  -23.987 10.456 1.00 127.71 ? 307 GLN   A CB  1 
ATOM   2086 C CG  . GLN   A 1 289 ? 12.875  -24.092 9.736  1.00 186.71 ? 307 GLN   A CG  1 
ATOM   2087 C CD  . GLN   A 1 289 ? 13.332  -25.530 9.582  1.00 187.95 ? 307 GLN   A CD  1 
ATOM   2088 O OE1 . GLN   A 1 289 ? 12.805  -26.433 10.233 1.00 193.97 ? 307 GLN   A OE1 1 
ATOM   2089 N NE2 . GLN   A 1 289 ? 14.312  -25.752 8.715  1.00 184.54 ? 307 GLN   A NE2 1 
ATOM   2090 N N   . ASN   A 1 290 ? 9.641   -22.770 12.600 1.00 148.96 ? 308 ASN   A N   1 
ATOM   2091 C CA  . ASN   A 1 290 ? 8.413   -22.866 13.373 1.00 135.94 ? 308 ASN   A CA  1 
ATOM   2092 C C   . ASN   A 1 290 ? 7.907   -21.511 13.848 1.00 136.61 ? 308 ASN   A C   1 
ATOM   2093 O O   . ASN   A 1 290 ? 6.922   -21.460 14.590 1.00 138.23 ? 308 ASN   A O   1 
ATOM   2094 C CB  . ASN   A 1 290 ? 8.630   -23.791 14.575 1.00 132.69 ? 308 ASN   A CB  1 
ATOM   2095 C CG  . ASN   A 1 290 ? 9.063   -25.186 14.162 1.00 143.62 ? 308 ASN   A CG  1 
ATOM   2096 O OD1 . ASN   A 1 290 ? 10.139  -25.652 14.537 1.00 139.38 ? 308 ASN   A OD1 1 
ATOM   2097 N ND2 . ASN   A 1 290 ? 8.225   -25.858 13.380 1.00 126.04 ? 308 ASN   A ND2 1 
ATOM   2098 N N   . ASN   A 1 291 ? 8.557   -20.420 13.445 1.00 191.73 ? 309 ASN   A N   1 
ATOM   2099 C CA  . ASN   A 1 291 ? 8.109   -19.068 13.770 1.00 136.07 ? 309 ASN   A CA  1 
ATOM   2100 C C   . ASN   A 1 291 ? 8.076   -18.859 15.285 1.00 116.23 ? 309 ASN   A C   1 
ATOM   2101 O O   . ASN   A 1 291 ? 7.058   -18.485 15.872 1.00 128.70 ? 309 ASN   A O   1 
ATOM   2102 C CB  . ASN   A 1 291 ? 6.740   -18.790 13.141 1.00 120.38 ? 309 ASN   A CB  1 
ATOM   2103 C CG  . ASN   A 1 291 ? 6.323   -17.339 13.268 1.00 217.35 ? 309 ASN   A CG  1 
ATOM   2104 O OD1 . ASN   A 1 291 ? 7.161   -16.454 13.441 1.00 137.11 ? 309 ASN   A OD1 1 
ATOM   2105 N ND2 . ASN   A 1 291 ? 5.021   -17.087 13.182 1.00 126.95 ? 309 ASN   A ND2 1 
ATOM   2106 N N   . LYS   A 1 292 ? 9.221   -19.106 15.912 1.00 129.45 ? 310 LYS   A N   1 
ATOM   2107 C CA  . LYS   A 1 292 ? 9.376   -18.958 17.352 1.00 129.60 ? 310 LYS   A CA  1 
ATOM   2108 C C   . LYS   A 1 292 ? 9.974   -17.595 17.674 1.00 125.90 ? 310 LYS   A C   1 
ATOM   2109 O O   . LYS   A 1 292 ? 10.905  -17.138 17.004 1.00 130.45 ? 310 LYS   A O   1 
ATOM   2110 C CB  . LYS   A 1 292 ? 10.272  -20.059 17.922 1.00 137.84 ? 310 LYS   A CB  1 
ATOM   2111 C CG  . LYS   A 1 292 ? 9.704   -21.464 17.801 1.00 139.37 ? 310 LYS   A CG  1 
ATOM   2112 C CD  . LYS   A 1 292 ? 8.495   -21.664 18.699 1.00 127.47 ? 310 LYS   A CD  1 
ATOM   2113 C CE  . LYS   A 1 292 ? 8.042   -23.115 18.693 1.00 130.08 ? 310 LYS   A CE  1 
ATOM   2114 N NZ  . LYS   A 1 292 ? 6.869   -23.346 19.581 1.00 128.95 ? 310 LYS   A NZ  1 
ATOM   2115 N N   . LEU   A 1 293 ? 9.428   -16.946 18.700 1.00 134.76 ? 311 LEU   A N   1 
ATOM   2116 C CA  . LEU   A 1 293 ? 9.988   -15.688 19.178 1.00 167.93 ? 311 LEU   A CA  1 
ATOM   2117 C C   . LEU   A 1 293 ? 11.316  -15.966 19.871 1.00 161.21 ? 311 LEU   A C   1 
ATOM   2118 O O   . LEU   A 1 293 ? 11.355  -16.639 20.907 1.00 142.63 ? 311 LEU   A O   1 
ATOM   2119 C CB  . LEU   A 1 293 ? 9.011   -15.000 20.129 1.00 122.13 ? 311 LEU   A CB  1 
ATOM   2120 C CG  . LEU   A 1 293 ? 9.478   -13.690 20.769 1.00 104.14 ? 311 LEU   A CG  1 
ATOM   2121 C CD1 . LEU   A 1 293 ? 9.864   -12.670 19.711 1.00 114.98 ? 311 LEU   A CD1 1 
ATOM   2122 C CD2 . LEU   A 1 293 ? 8.397   -13.130 21.680 1.00 99.33  ? 311 LEU   A CD2 1 
ATOM   2123 N N   . THR   A 1 294 ? 12.403  -15.453 19.300 1.00 129.41 ? 312 THR   A N   1 
ATOM   2124 C CA  . THR   A 1 294 ? 13.745  -15.745 19.775 1.00 122.56 ? 312 THR   A CA  1 
ATOM   2125 C C   . THR   A 1 294 ? 14.501  -14.448 20.026 1.00 126.62 ? 312 THR   A C   1 
ATOM   2126 O O   . THR   A 1 294 ? 14.173  -13.393 19.479 1.00 159.98 ? 312 THR   A O   1 
ATOM   2127 C CB  . THR   A 1 294 ? 14.523  -16.612 18.773 1.00 129.54 ? 312 THR   A CB  1 
ATOM   2128 O OG1 . THR   A 1 294 ? 14.642  -15.918 17.524 1.00 112.77 ? 312 THR   A OG1 1 
ATOM   2129 C CG2 . THR   A 1 294 ? 13.818  -17.935 18.547 1.00 163.75 ? 312 THR   A CG2 1 
ATOM   2130 N N   . TRP   A 1 295 ? 15.523  -14.548 20.877 1.00 114.46 ? 313 TRP   A N   1 
ATOM   2131 C CA  . TRP   A 1 295 ? 16.362  -13.390 21.180 1.00 106.61 ? 313 TRP   A CA  1 
ATOM   2132 C C   . TRP   A 1 295 ? 16.978  -12.789 19.924 1.00 141.73 ? 313 TRP   A C   1 
ATOM   2133 O O   . TRP   A 1 295 ? 16.903  -11.556 19.750 1.00 140.27 ? 313 TRP   A O   1 
ATOM   2134 C CB  . TRP   A 1 295 ? 17.427  -13.811 22.200 1.00 129.68 ? 313 TRP   A CB  1 
ATOM   2135 C CG  . TRP   A 1 295 ? 18.213  -12.695 22.805 1.00 140.13 ? 313 TRP   A CG  1 
ATOM   2136 C CD1 . TRP   A 1 295 ? 17.889  -11.971 23.914 1.00 134.17 ? 313 TRP   A CD1 1 
ATOM   2137 C CD2 . TRP   A 1 295 ? 19.471  -12.188 22.348 1.00 160.02 ? 313 TRP   A CD2 1 
ATOM   2138 N NE1 . TRP   A 1 295 ? 18.864  -11.039 24.172 1.00 144.96 ? 313 TRP   A NE1 1 
ATOM   2139 C CE2 . TRP   A 1 295 ? 19.846  -11.150 23.223 1.00 158.45 ? 313 TRP   A CE2 1 
ATOM   2140 C CE3 . TRP   A 1 295 ? 20.314  -12.507 21.280 1.00 138.61 ? 313 TRP   A CE3 1 
ATOM   2141 C CZ2 . TRP   A 1 295 ? 21.027  -10.430 23.063 1.00 109.95 ? 313 TRP   A CZ2 1 
ATOM   2142 C CZ3 . TRP   A 1 295 ? 21.484  -11.790 21.123 1.00 133.54 ? 313 TRP   A CZ3 1 
ATOM   2143 C CH2 . TRP   A 1 295 ? 21.829  -10.764 22.009 1.00 159.72 ? 313 TRP   A CH2 1 
ATOM   2144 N N   . PRO   A 1 296 ? 17.582  -13.566 19.016 1.00 132.96 ? 314 PRO   A N   1 
ATOM   2145 C CA  . PRO   A 1 296 ? 18.111  -12.958 17.786 1.00 128.84 ? 314 PRO   A CA  1 
ATOM   2146 C C   . PRO   A 1 296 ? 17.062  -12.203 16.995 1.00 127.57 ? 314 PRO   A C   1 
ATOM   2147 O O   . PRO   A 1 296 ? 17.359  -11.137 16.449 1.00 149.36 ? 314 PRO   A O   1 
ATOM   2148 C CB  . PRO   A 1 296 ? 18.649  -14.163 17.001 1.00 126.20 ? 314 PRO   A CB  1 
ATOM   2149 C CG  . PRO   A 1 296 ? 18.898  -15.208 18.021 1.00 118.27 ? 314 PRO   A CG  1 
ATOM   2150 C CD  . PRO   A 1 296 ? 17.856  -15.013 19.073 1.00 118.28 ? 314 PRO   A CD  1 
ATOM   2151 N N   . LEU   A 1 297 ? 15.837  -12.726 16.919 1.00 143.66 ? 315 LEU   A N   1 
ATOM   2152 C CA  . LEU   A 1 297 ? 14.783  -12.031 16.187 1.00 121.20 ? 315 LEU   A CA  1 
ATOM   2153 C C   . LEU   A 1 297 ? 14.515  -10.659 16.790 1.00 145.24 ? 315 LEU   A C   1 
ATOM   2154 O O   . LEU   A 1 297 ? 14.471  -9.648  16.078 1.00 150.84 ? 315 LEU   A O   1 
ATOM   2155 C CB  . LEU   A 1 297 ? 13.507  -12.876 16.189 1.00 109.46 ? 315 LEU   A CB  1 
ATOM   2156 C CG  . LEU   A 1 297 ? 12.215  -12.164 15.777 1.00 140.91 ? 315 LEU   A CG  1 
ATOM   2157 C CD1 . LEU   A 1 297 ? 12.335  -11.598 14.372 1.00 120.81 ? 315 LEU   A CD1 1 
ATOM   2158 C CD2 . LEU   A 1 297 ? 11.026  -13.109 15.878 1.00 130.72 ? 315 LEU   A CD2 1 
ATOM   2159 N N   . ILE   A 1 298 ? 14.342  -10.606 18.112 1.00 136.43 ? 316 ILE   A N   1 
ATOM   2160 C CA  . ILE   A 1 298 ? 14.021  -9.344  18.769 1.00 123.50 ? 316 ILE   A CA  1 
ATOM   2161 C C   . ILE   A 1 298 ? 15.156  -8.349  18.588 1.00 126.82 ? 316 ILE   A C   1 
ATOM   2162 O O   . ILE   A 1 298 ? 14.926  -7.168  18.296 1.00 148.49 ? 316 ILE   A O   1 
ATOM   2163 C CB  . ILE   A 1 298 ? 13.709  -9.583  20.258 1.00 142.03 ? 316 ILE   A CB  1 
ATOM   2164 C CG1 . ILE   A 1 298 ? 12.483  -10.491 20.402 1.00 132.47 ? 316 ILE   A CG1 1 
ATOM   2165 C CG2 . ILE   A 1 298 ? 13.492  -8.254  20.976 1.00 123.82 ? 316 ILE   A CG2 1 
ATOM   2166 C CD1 . ILE   A 1 298 ? 12.146  -10.860 21.835 1.00 113.88 ? 316 ILE   A CD1 1 
ATOM   2167 N N   . LYS   A 1 299 ? 16.401  -8.802  18.755 1.00 121.44 ? 317 LYS   A N   1 
ATOM   2168 C CA  . LYS   A 1 299 ? 17.518  -7.865  18.675 1.00 132.73 ? 317 LYS   A CA  1 
ATOM   2169 C C   . LYS   A 1 299 ? 17.764  -7.409  17.241 1.00 130.92 ? 317 LYS   A C   1 
ATOM   2170 O O   . LYS   A 1 299 ? 18.113  -6.245  17.010 1.00 132.91 ? 317 LYS   A O   1 
ATOM   2171 C CB  . LYS   A 1 299 ? 18.772  -8.491  19.284 1.00 123.03 ? 317 LYS   A CB  1 
ATOM   2172 C CG  . LYS   A 1 299 ? 18.576  -8.983  20.722 1.00 127.79 ? 317 LYS   A CG  1 
ATOM   2173 C CD  . LYS   A 1 299 ? 17.940  -7.924  21.630 1.00 141.28 ? 317 LYS   A CD  1 
ATOM   2174 C CE  . LYS   A 1 299 ? 17.477  -8.520  22.950 1.00 142.93 ? 317 LYS   A CE  1 
ATOM   2175 N NZ  . LYS   A 1 299 ? 16.555  -7.603  23.678 1.00 144.34 ? 317 LYS   A NZ  1 
ATOM   2176 N N   . ALA   A 1 300 ? 17.570  -8.294  16.260 1.00 167.45 ? 318 ALA   A N   1 
ATOM   2177 C CA  . ALA   A 1 300 ? 17.652  -7.870  14.868 1.00 183.34 ? 318 ALA   A CA  1 
ATOM   2178 C C   . ALA   A 1 300 ? 16.575  -6.842  14.552 1.00 156.75 ? 318 ALA   A C   1 
ATOM   2179 O O   . ALA   A 1 300 ? 16.838  -5.844  13.872 1.00 149.70 ? 318 ALA   A O   1 
ATOM   2180 C CB  . ALA   A 1 300 ? 17.527  -9.078  13.942 1.00 127.24 ? 318 ALA   A CB  1 
ATOM   2181 N N   . PHE   A 1 301 ? 15.355  -7.065  15.046 1.00 153.62 ? 319 PHE   A N   1 
ATOM   2182 C CA  . PHE   A 1 301 ? 14.287  -6.095  14.835 1.00 133.47 ? 319 PHE   A CA  1 
ATOM   2183 C C   . PHE   A 1 301 ? 14.642  -4.751  15.457 1.00 149.94 ? 319 PHE   A C   1 
ATOM   2184 O O   . PHE   A 1 301 ? 14.432  -3.697  14.845 1.00 177.00 ? 319 PHE   A O   1 
ATOM   2185 C CB  . PHE   A 1 301 ? 12.980  -6.627  15.422 1.00 126.48 ? 319 PHE   A CB  1 
ATOM   2186 C CG  . PHE   A 1 301 ? 11.792  -6.439  14.527 1.00 122.04 ? 319 PHE   A CG  1 
ATOM   2187 C CD1 . PHE   A 1 301 ? 11.483  -7.383  13.561 1.00 118.91 ? 319 PHE   A CD1 1 
ATOM   2188 C CD2 . PHE   A 1 301 ? 10.981  -5.325  14.653 1.00 152.60 ? 319 PHE   A CD2 1 
ATOM   2189 C CE1 . PHE   A 1 301 ? 10.389  -7.216  12.736 1.00 123.60 ? 319 PHE   A CE1 1 
ATOM   2190 C CE2 . PHE   A 1 301 ? 9.885   -5.153  13.830 1.00 152.44 ? 319 PHE   A CE2 1 
ATOM   2191 C CZ  . PHE   A 1 301 ? 9.589   -6.100  12.871 1.00 173.19 ? 319 PHE   A CZ  1 
ATOM   2192 N N   . GLU   A 1 302 ? 15.186  -4.769  16.675 1.00 146.26 ? 320 GLU   A N   1 
ATOM   2193 C CA  . GLU   A 1 302 ? 15.574  -3.525  17.330 1.00 138.56 ? 320 GLU   A CA  1 
ATOM   2194 C C   . GLU   A 1 302 ? 16.656  -2.800  16.540 1.00 144.99 ? 320 GLU   A C   1 
ATOM   2195 O O   . GLU   A 1 302 ? 16.598  -1.577  16.369 1.00 149.66 ? 320 GLU   A O   1 
ATOM   2196 C CB  . GLU   A 1 302 ? 16.059  -3.815  18.752 1.00 139.79 ? 320 GLU   A CB  1 
ATOM   2197 C CG  . GLU   A 1 302 ? 16.542  -2.590  19.521 1.00 161.80 ? 320 GLU   A CG  1 
ATOM   2198 C CD  . GLU   A 1 302 ? 17.279  -2.955  20.795 1.00 162.91 ? 320 GLU   A CD  1 
ATOM   2199 O OE1 . GLU   A 1 302 ? 17.432  -4.164  21.069 1.00 144.91 ? 320 GLU   A OE1 1 
ATOM   2200 O OE2 . GLU   A 1 302 ? 17.710  -2.033  21.520 1.00 172.21 ? 320 GLU   A OE2 1 
ATOM   2201 N N   . LEU   A 1 303 ? 17.652  -3.540  16.050 1.00 179.40 ? 321 LEU   A N   1 
ATOM   2202 C CA  . LEU   A 1 303 ? 18.803  -2.915  15.409 1.00 218.44 ? 321 LEU   A CA  1 
ATOM   2203 C C   . LEU   A 1 303 ? 18.552  -2.578  13.945 1.00 210.86 ? 321 LEU   A C   1 
ATOM   2204 O O   . LEU   A 1 303 ? 19.109  -1.597  13.439 1.00 152.98 ? 321 LEU   A O   1 
ATOM   2205 C CB  . LEU   A 1 303 ? 20.021  -3.833  15.526 1.00 195.48 ? 321 LEU   A CB  1 
ATOM   2206 C CG  . LEU   A 1 303 ? 20.844  -3.719  16.811 1.00 130.57 ? 321 LEU   A CG  1 
ATOM   2207 C CD1 . LEU   A 1 303 ? 19.970  -3.787  18.055 1.00 147.55 ? 321 LEU   A CD1 1 
ATOM   2208 C CD2 . LEU   A 1 303 ? 21.905  -4.808  16.849 1.00 144.97 ? 321 LEU   A CD2 1 
ATOM   2209 N N   . CYS   A 1 304 ? 17.729  -3.358  13.252 1.00 154.17 ? 322 CYS   A N   1 
ATOM   2210 C CA  . CYS   A 1 304 ? 17.609  -3.208  11.811 1.00 148.83 ? 322 CYS   A CA  1 
ATOM   2211 C C   . CYS   A 1 304 ? 16.645  -2.081  11.449 1.00 167.00 ? 322 CYS   A C   1 
ATOM   2212 O O   . CYS   A 1 304 ? 15.797  -1.664  12.244 1.00 145.21 ? 322 CYS   A O   1 
ATOM   2213 C CB  . CYS   A 1 304 ? 17.147  -4.516  11.169 1.00 148.55 ? 322 CYS   A CB  1 
ATOM   2214 S SG  . CYS   A 1 304 ? 15.400  -4.906  11.426 1.00 140.20 ? 322 CYS   A SG  1 
ATOM   2215 N N   . SER   A 1 305 ? 16.794  -1.589  10.222 1.00 163.05 ? 323 SER   A N   1 
ATOM   2216 C CA  . SER   A 1 305 ? 15.950  -0.529  9.697  1.00 182.06 ? 323 SER   A CA  1 
ATOM   2217 C C   . SER   A 1 305 ? 14.581  -1.081  9.302  1.00 157.62 ? 323 SER   A C   1 
ATOM   2218 O O   . SER   A 1 305 ? 14.357  -2.293  9.251  1.00 152.80 ? 323 SER   A O   1 
ATOM   2219 C CB  . SER   A 1 305 ? 16.619  0.136   8.496  1.00 150.54 ? 323 SER   A CB  1 
ATOM   2220 O OG  . SER   A 1 305 ? 16.821  -0.797  7.448  1.00 171.74 ? 323 SER   A OG  1 
ATOM   2221 N N   . GLN   A 1 306 ? 13.657  -0.166  9.015  1.00 175.24 ? 324 GLN   A N   1 
ATOM   2222 C CA  . GLN   A 1 306 ? 12.297  -0.575  8.677  1.00 172.39 ? 324 GLN   A CA  1 
ATOM   2223 C C   . GLN   A 1 306 ? 12.236  -1.488  7.457  1.00 158.91 ? 324 GLN   A C   1 
ATOM   2224 O O   . GLN   A 1 306 ? 11.490  -2.483  7.504  1.00 168.99 ? 324 GLN   A O   1 
ATOM   2225 C CB  . GLN   A 1 306 ? 11.424  0.671   8.475  1.00 163.39 ? 324 GLN   A CB  1 
ATOM   2226 C CG  . GLN   A 1 306 ? 9.952   0.370   8.234  1.00 155.16 ? 324 GLN   A CG  1 
ATOM   2227 C CD  . GLN   A 1 306 ? 9.314   -0.384  9.386  1.00 146.42 ? 324 GLN   A CD  1 
ATOM   2228 O OE1 . GLN   A 1 306 ? 9.357   0.060   10.534 1.00 137.21 ? 324 GLN   A OE1 1 
ATOM   2229 N NE2 . GLN   A 1 306 ? 8.724   -1.535  9.085  1.00 165.25 ? 324 GLN   A NE2 1 
ATOM   2230 N N   . PRO   A 1 307 ? 12.947  -1.221  6.355  1.00 156.35 ? 325 PRO   A N   1 
ATOM   2231 C CA  . PRO   A 1 307 ? 12.930  -2.190  5.246  1.00 156.27 ? 325 PRO   A CA  1 
ATOM   2232 C C   . PRO   A 1 307 ? 13.378  -3.575  5.670  1.00 158.15 ? 325 PRO   A C   1 
ATOM   2233 O O   . PRO   A 1 307 ? 12.807  -4.577  5.223  1.00 157.60 ? 325 PRO   A O   1 
ATOM   2234 C CB  . PRO   A 1 307 ? 13.891  -1.567  4.222  1.00 157.68 ? 325 PRO   A CB  1 
ATOM   2235 C CG  . PRO   A 1 307 ? 13.901  -0.117  4.538  1.00 166.15 ? 325 PRO   A CG  1 
ATOM   2236 C CD  . PRO   A 1 307 ? 13.727  -0.016  6.024  1.00 163.22 ? 325 PRO   A CD  1 
ATOM   2237 N N   . GLU   A 1 308 ? 14.385  -3.661  6.542  1.00 166.35 ? 326 GLU   A N   1 
ATOM   2238 C CA  . GLU   A 1 308 ? 14.819  -4.965  7.029  1.00 151.88 ? 326 GLU   A CA  1 
ATOM   2239 C C   . GLU   A 1 308 ? 13.791  -5.582  7.968  1.00 141.73 ? 326 GLU   A C   1 
ATOM   2240 O O   . GLU   A 1 308 ? 13.655  -6.808  8.007  1.00 137.34 ? 326 GLU   A O   1 
ATOM   2241 C CB  . GLU   A 1 308 ? 16.177  -4.845  7.717  1.00 155.50 ? 326 GLU   A CB  1 
ATOM   2242 C CG  . GLU   A 1 308 ? 17.338  -5.243  6.821  1.00 158.01 ? 326 GLU   A CG  1 
ATOM   2243 C CD  . GLU   A 1 308 ? 18.679  -4.800  7.365  1.00 163.92 ? 326 GLU   A CD  1 
ATOM   2244 O OE1 . GLU   A 1 308 ? 18.733  -3.743  8.027  1.00 160.16 ? 326 GLU   A OE1 1 
ATOM   2245 O OE2 . GLU   A 1 308 ? 19.680  -5.511  7.134  1.00 173.02 ? 326 GLU   A OE2 1 
ATOM   2246 N N   . LYS   A 1 309 ? 13.057  -4.763  8.724  1.00 148.15 ? 327 LYS   A N   1 
ATOM   2247 C CA  . LYS   A 1 309 ? 11.945  -5.299  9.504  1.00 145.76 ? 327 LYS   A CA  1 
ATOM   2248 C C   . LYS   A 1 309 ? 10.907  -5.938  8.590  1.00 152.01 ? 327 LYS   A C   1 
ATOM   2249 O O   . LYS   A 1 309 ? 10.419  -7.043  8.861  1.00 150.79 ? 327 LYS   A O   1 
ATOM   2250 C CB  . LYS   A 1 309 ? 11.306  -4.190  10.342 1.00 131.85 ? 327 LYS   A CB  1 
ATOM   2251 C CG  . LYS   A 1 309 ? 12.219  -3.593  11.400 1.00 142.69 ? 327 LYS   A CG  1 
ATOM   2252 C CD  . LYS   A 1 309 ? 11.557  -2.415  12.101 1.00 157.07 ? 327 LYS   A CD  1 
ATOM   2253 C CE  . LYS   A 1 309 ? 12.517  -1.722  13.056 1.00 167.73 ? 327 LYS   A CE  1 
ATOM   2254 N NZ  . LYS   A 1 309 ? 11.903  -0.533  13.709 1.00 182.17 ? 327 LYS   A NZ  1 
ATOM   2255 N N   . GLU   A 1 310 ? 10.567  -5.258  7.492  1.00 154.57 ? 328 GLU   A N   1 
ATOM   2256 C CA  . GLU   A 1 310 ? 9.626   -5.829  6.534  1.00 140.61 ? 328 GLU   A CA  1 
ATOM   2257 C C   . GLU   A 1 310 ? 10.178  -7.109  5.922  1.00 152.87 ? 328 GLU   A C   1 
ATOM   2258 O O   . GLU   A 1 310 ? 9.443   -8.083  5.733  1.00 147.60 ? 328 GLU   A O   1 
ATOM   2259 C CB  . GLU   A 1 310 ? 9.307   -4.811  5.440  1.00 169.90 ? 328 GLU   A CB  1 
ATOM   2260 C CG  . GLU   A 1 310 ? 8.610   -3.560  5.940  1.00 179.01 ? 328 GLU   A CG  1 
ATOM   2261 C CD  . GLU   A 1 310 ? 8.311   -2.579  4.824  1.00 193.22 ? 328 GLU   A CD  1 
ATOM   2262 O OE1 . GLU   A 1 310 ? 8.722   -2.842  3.673  1.00 173.37 ? 328 GLU   A OE1 1 
ATOM   2263 O OE2 . GLU   A 1 310 ? 7.665   -1.546  5.096  1.00 172.92 ? 328 GLU   A OE2 1 
ATOM   2264 N N   . ASP   A 1 311 ? 11.472  -7.122  5.597  1.00 145.92 ? 329 ASP   A N   1 
ATOM   2265 C CA  . ASP   A 1 311 ? 12.082  -8.327  5.044  1.00 146.73 ? 329 ASP   A CA  1 
ATOM   2266 C C   . ASP   A 1 311 ? 11.998  -9.487  6.029  1.00 138.14 ? 329 ASP   A C   1 
ATOM   2267 O O   . ASP   A 1 311 ? 11.677  -10.617 5.644  1.00 140.91 ? 329 ASP   A O   1 
ATOM   2268 C CB  . ASP   A 1 311 ? 13.537  -8.051  4.667  1.00 144.65 ? 329 ASP   A CB  1 
ATOM   2269 C CG  . ASP   A 1 311 ? 13.670  -6.989  3.593  1.00 147.65 ? 329 ASP   A CG  1 
ATOM   2270 O OD1 . ASP   A 1 311 ? 12.629  -6.529  3.079  1.00 151.14 ? 329 ASP   A OD1 1 
ATOM   2271 O OD2 . ASP   A 1 311 ? 14.815  -6.615  3.265  1.00 138.85 ? 329 ASP   A OD2 1 
ATOM   2272 N N   . ILE   A 1 312 ? 12.281  -9.225  7.307  1.00 188.62 ? 330 ILE   A N   1 
ATOM   2273 C CA  . ILE   A 1 312 ? 12.178  -10.267 8.324  1.00 160.03 ? 330 ILE   A CA  1 
ATOM   2274 C C   . ILE   A 1 312 ? 10.748  -10.783 8.400  1.00 155.40 ? 330 ILE   A C   1 
ATOM   2275 O O   . ILE   A 1 312 ? 10.509  -11.995 8.458  1.00 137.29 ? 330 ILE   A O   1 
ATOM   2276 C CB  . ILE   A 1 312 ? 12.656  -9.736  9.689  1.00 158.21 ? 330 ILE   A CB  1 
ATOM   2277 C CG1 . ILE   A 1 312 ? 14.168  -9.493  9.670  1.00 154.37 ? 330 ILE   A CG1 1 
ATOM   2278 C CG2 . ILE   A 1 312 ? 12.276  -10.709 10.802 1.00 143.42 ? 330 ILE   A CG2 1 
ATOM   2279 C CD1 . ILE   A 1 312 ? 14.710  -8.877  10.949 1.00 161.13 ? 330 ILE   A CD1 1 
ATOM   2280 N N   . ILE   A 1 313 ? 9.775   -9.870  8.397  1.00 171.81 ? 331 ILE   A N   1 
ATOM   2281 C CA  . ILE   A 1 313 ? 8.377   -10.287 8.449  1.00 171.71 ? 331 ILE   A CA  1 
ATOM   2282 C C   . ILE   A 1 313 ? 8.042   -11.164 7.249  1.00 171.31 ? 331 ILE   A C   1 
ATOM   2283 O O   . ILE   A 1 313 ? 7.343   -12.177 7.376  1.00 151.91 ? 331 ILE   A O   1 
ATOM   2284 C CB  . ILE   A 1 313 ? 7.453   -9.057  8.528  1.00 172.62 ? 331 ILE   A CB  1 
ATOM   2285 C CG1 . ILE   A 1 313 ? 7.693   -8.293  9.833  1.00 149.38 ? 331 ILE   A CG1 1 
ATOM   2286 C CG2 . ILE   A 1 313 ? 5.993   -9.483  8.430  1.00 121.15 ? 331 ILE   A CG2 1 
ATOM   2287 C CD1 . ILE   A 1 313 ? 7.038   -6.926  9.876  1.00 129.13 ? 331 ILE   A CD1 1 
ATOM   2288 N N   . ARG   A 1 314 ? 8.539   -10.795 6.067  1.00 141.93 ? 332 ARG   A N   1 
ATOM   2289 C CA  . ARG   A 1 314 ? 8.251   -11.556 4.857  1.00 152.59 ? 332 ARG   A CA  1 
ATOM   2290 C C   . ARG   A 1 314 ? 8.901   -12.933 4.864  1.00 133.04 ? 332 ARG   A C   1 
ATOM   2291 O O   . ARG   A 1 314 ? 8.513   -13.790 4.063  1.00 121.09 ? 332 ARG   A O   1 
ATOM   2292 C CB  . ARG   A 1 314 ? 8.717   -10.775 3.627  1.00 145.06 ? 332 ARG   A CB  1 
ATOM   2293 C CG  . ARG   A 1 314 ? 7.940   -9.493  3.376  1.00 160.49 ? 332 ARG   A CG  1 
ATOM   2294 C CD  . ARG   A 1 314 ? 8.598   -8.637  2.305  1.00 171.76 ? 332 ARG   A CD  1 
ATOM   2295 N NE  . ARG   A 1 314 ? 7.907   -7.365  2.127  1.00 194.00 ? 332 ARG   A NE  1 
ATOM   2296 C CZ  . ARG   A 1 314 ? 8.277   -6.420  1.273  1.00 219.43 ? 332 ARG   A CZ  1 
ATOM   2297 N NH1 . ARG   A 1 314 ? 9.336   -6.568  0.493  1.00 190.28 ? 332 ARG   A NH1 1 
ATOM   2298 N NH2 . ARG   A 1 314 ? 7.568   -5.298  1.200  1.00 201.42 ? 332 ARG   A NH2 1 
ATOM   2299 N N   . ASN   A 1 315 ? 9.871   -13.165 5.743  1.00 185.42 ? 333 ASN   A N   1 
ATOM   2300 C CA  . ASN   A 1 315 ? 10.581  -14.436 5.786  1.00 123.69 ? 333 ASN   A CA  1 
ATOM   2301 C C   . ASN   A 1 315 ? 10.346  -15.145 7.116  1.00 157.49 ? 333 ASN   A C   1 
ATOM   2302 O O   . ASN   A 1 315 ? 10.389  -16.373 7.192  1.00 177.51 ? 333 ASN   A O   1 
ATOM   2303 C CB  . ASN   A 1 315 ? 12.078  -14.211 5.558  1.00 131.25 ? 333 ASN   A CB  1 
ATOM   2304 C CG  . ASN   A 1 315 ? 12.380  -13.667 4.173  1.00 158.33 ? 333 ASN   A CG  1 
ATOM   2305 O OD1 . ASN   A 1 315 ? 12.540  -14.424 3.217  1.00 128.71 ? 333 ASN   A OD1 1 
ATOM   2306 N ND2 . ASN   A 1 315 ? 12.455  -12.346 4.060  1.00 155.70 ? 333 ASN   A ND2 1 
ATOM   2307 N N   . LYS   A 1 318 ? 8.549   -19.923 8.553  1.00 146.95 ? 336 LYS   A N   1 
ATOM   2308 C CA  . LYS   A 1 318 ? 8.305   -20.415 7.201  1.00 169.69 ? 336 LYS   A CA  1 
ATOM   2309 C C   . LYS   A 1 318 ? 9.189   -21.620 6.892  1.00 198.69 ? 336 LYS   A C   1 
ATOM   2310 O O   . LYS   A 1 318 ? 10.374  -21.634 7.225  1.00 193.19 ? 336 LYS   A O   1 
ATOM   2311 C CB  . LYS   A 1 318 ? 8.555   -19.309 6.173  1.00 116.54 ? 336 LYS   A CB  1 
ATOM   2312 N N   . ASP   A 1 319 ? 8.604   -22.630 6.250  1.00 148.61 ? 337 ASP   A N   1 
ATOM   2313 C CA  . ASP   A 1 319 ? 9.330   -23.850 5.893  1.00 155.47 ? 337 ASP   A CA  1 
ATOM   2314 C C   . ASP   A 1 319 ? 9.890   -23.713 4.476  1.00 165.56 ? 337 ASP   A C   1 
ATOM   2315 O O   . ASP   A 1 319 ? 9.471   -24.382 3.529  1.00 174.71 ? 337 ASP   A O   1 
ATOM   2316 C CB  . ASP   A 1 319 ? 8.421   -25.066 6.021  1.00 156.01 ? 337 ASP   A CB  1 
ATOM   2317 C CG  . ASP   A 1 319 ? 7.872   -25.240 7.425  1.00 161.82 ? 337 ASP   A CG  1 
ATOM   2318 O OD1 . ASP   A 1 319 ? 8.556   -24.831 8.388  1.00 156.38 ? 337 ASP   A OD1 1 
ATOM   2319 O OD2 . ASP   A 1 319 ? 6.758   -25.788 7.565  1.00 168.52 ? 337 ASP   A OD2 1 
ATOM   2320 N N   . ASN   A 1 320 ? 10.865  -22.815 4.348  1.00 155.75 ? 338 ASN   A N   1 
ATOM   2321 C CA  . ASN   A 1 320 ? 11.528  -22.575 3.072  1.00 171.09 ? 338 ASN   A CA  1 
ATOM   2322 C C   . ASN   A 1 320 ? 12.969  -22.176 3.349  1.00 171.06 ? 338 ASN   A C   1 
ATOM   2323 O O   . ASN   A 1 320 ? 13.222  -21.288 4.168  1.00 177.79 ? 338 ASN   A O   1 
ATOM   2324 C CB  . ASN   A 1 320 ? 10.808  -21.485 2.271  1.00 151.78 ? 338 ASN   A CB  1 
ATOM   2325 C CG  . ASN   A 1 320 ? 11.210  -21.472 0.809  1.00 156.06 ? 338 ASN   A CG  1 
ATOM   2326 O OD1 . ASN   A 1 320 ? 11.770  -22.443 0.298  1.00 152.20 ? 338 ASN   A OD1 1 
ATOM   2327 N ND2 . ASN   A 1 320 ? 10.921  -20.371 0.126  1.00 175.67 ? 338 ASN   A ND2 1 
ATOM   2328 N N   . VAL   A 1 321 ? 13.907  -22.831 2.660  1.00 159.60 ? 339 VAL   A N   1 
ATOM   2329 C CA  . VAL   A 1 321 ? 15.325  -22.616 2.943  1.00 154.26 ? 339 VAL   A CA  1 
ATOM   2330 C C   . VAL   A 1 321 ? 15.722  -21.177 2.643  1.00 162.48 ? 339 VAL   A C   1 
ATOM   2331 O O   . VAL   A 1 321 ? 16.494  -20.563 3.390  1.00 163.79 ? 339 VAL   A O   1 
ATOM   2332 C CB  . VAL   A 1 321 ? 16.186  -23.615 2.149  1.00 157.41 ? 339 VAL   A CB  1 
ATOM   2333 C CG1 . VAL   A 1 321 ? 17.663  -23.393 2.442  1.00 156.27 ? 339 VAL   A CG1 1 
ATOM   2334 C CG2 . VAL   A 1 321 ? 15.784  -25.045 2.476  1.00 157.95 ? 339 VAL   A CG2 1 
ATOM   2335 N N   . THR   A 1 322 ? 15.216  -20.619 1.541  1.00 204.49 ? 340 THR   A N   1 
ATOM   2336 C CA  . THR   A 1 322 ? 15.626  -19.275 1.144  1.00 159.75 ? 340 THR   A CA  1 
ATOM   2337 C C   . THR   A 1 322 ? 15.275  -18.249 2.215  1.00 157.76 ? 340 THR   A C   1 
ATOM   2338 O O   . THR   A 1 322 ? 16.088  -17.376 2.537  1.00 151.83 ? 340 THR   A O   1 
ATOM   2339 C CB  . THR   A 1 322 ? 14.977  -18.901 -0.190 1.00 179.70 ? 340 THR   A CB  1 
ATOM   2340 O OG1 . THR   A 1 322 ? 13.556  -19.065 -0.098 1.00 190.52 ? 340 THR   A OG1 1 
ATOM   2341 C CG2 . THR   A 1 322 ? 15.519  -19.776 -1.313 1.00 213.89 ? 340 THR   A CG2 1 
ATOM   2342 N N   . CYS   A 1 323 ? 14.071  -18.341 2.784  1.00 167.40 ? 341 CYS   A N   1 
ATOM   2343 C CA  . CYS   A 1 323 ? 13.682  -17.417 3.845  1.00 148.33 ? 341 CYS   A CA  1 
ATOM   2344 C C   . CYS   A 1 323 ? 14.574  -17.578 5.070  1.00 150.69 ? 341 CYS   A C   1 
ATOM   2345 O O   . CYS   A 1 323 ? 14.972  -16.587 5.700  1.00 155.26 ? 341 CYS   A O   1 
ATOM   2346 C CB  . CYS   A 1 323 ? 12.217  -17.644 4.219  1.00 168.83 ? 341 CYS   A CB  1 
ATOM   2347 S SG  . CYS   A 1 323 ? 11.063  -17.491 2.838  1.00 152.21 ? 341 CYS   A SG  1 
ATOM   2348 N N   . ILE   A 1 324 ? 14.892  -18.823 5.426  1.00 163.53 ? 342 ILE   A N   1 
ATOM   2349 C CA  . ILE   A 1 324 ? 15.731  -19.073 6.594  1.00 170.09 ? 342 ILE   A CA  1 
ATOM   2350 C C   . ILE   A 1 324 ? 17.108  -18.457 6.396  1.00 171.01 ? 342 ILE   A C   1 
ATOM   2351 O O   . ILE   A 1 324 ? 17.653  -17.812 7.299  1.00 176.89 ? 342 ILE   A O   1 
ATOM   2352 C CB  . ILE   A 1 324 ? 15.823  -20.586 6.867  1.00 168.46 ? 342 ILE   A CB  1 
ATOM   2353 C CG1 . ILE   A 1 324 ? 14.430  -21.177 7.093  1.00 164.99 ? 342 ILE   A CG1 1 
ATOM   2354 C CG2 . ILE   A 1 324 ? 16.709  -20.854 8.075  1.00 166.55 ? 342 ILE   A CG2 1 
ATOM   2355 C CD1 . ILE   A 1 324 ? 14.380  -22.677 6.929  1.00 166.34 ? 342 ILE   A CD1 1 
ATOM   2356 N N   . LYS   A 1 325 ? 17.693  -18.643 5.211  1.00 160.71 ? 343 LYS   A N   1 
ATOM   2357 C CA  . LYS   A 1 325 ? 19.005  -18.064 4.945  1.00 163.24 ? 343 LYS   A CA  1 
ATOM   2358 C C   . LYS   A 1 325 ? 18.938  -16.546 4.866  1.00 158.74 ? 343 LYS   A C   1 
ATOM   2359 O O   . LYS   A 1 325 ? 19.894  -15.867 5.252  1.00 157.79 ? 343 LYS   A O   1 
ATOM   2360 C CB  . LYS   A 1 325 ? 19.589  -18.641 3.656  1.00 179.65 ? 343 LYS   A CB  1 
ATOM   2361 C CG  . LYS   A 1 325 ? 19.679  -20.164 3.638  1.00 178.49 ? 343 LYS   A CG  1 
ATOM   2362 C CD  . LYS   A 1 325 ? 20.500  -20.711 4.800  1.00 178.05 ? 343 LYS   A CD  1 
ATOM   2363 C CE  . LYS   A 1 325 ? 20.430  -22.228 4.860  1.00 185.18 ? 343 LYS   A CE  1 
ATOM   2364 N NZ  . LYS   A 1 325 ? 20.949  -22.871 3.622  1.00 200.77 ? 343 LYS   A NZ  1 
ATOM   2365 N N   . PHE   A 1 326 ? 17.824  -15.993 4.383  1.00 165.44 ? 344 PHE   A N   1 
ATOM   2366 C CA  . PHE   A 1 326 ? 17.659  -14.544 4.392  1.00 179.42 ? 344 PHE   A CA  1 
ATOM   2367 C C   . PHE   A 1 326 ? 17.691  -14.010 5.819  1.00 148.12 ? 344 PHE   A C   1 
ATOM   2368 O O   . PHE   A 1 326 ? 18.372  -13.020 6.115  1.00 145.21 ? 344 PHE   A O   1 
ATOM   2369 C CB  . PHE   A 1 326 ? 16.346  -14.170 3.704  1.00 150.71 ? 344 PHE   A CB  1 
ATOM   2370 C CG  . PHE   A 1 326 ? 16.333  -12.782 3.136  1.00 184.45 ? 344 PHE   A CG  1 
ATOM   2371 C CD1 . PHE   A 1 326 ? 16.055  -11.691 3.941  1.00 164.80 ? 344 PHE   A CD1 1 
ATOM   2372 C CD2 . PHE   A 1 326 ? 16.594  -12.568 1.793  1.00 192.74 ? 344 PHE   A CD2 1 
ATOM   2373 C CE1 . PHE   A 1 326 ? 16.042  -10.412 3.417  1.00 159.87 ? 344 PHE   A CE1 1 
ATOM   2374 C CE2 . PHE   A 1 326 ? 16.582  -11.292 1.263  1.00 173.96 ? 344 PHE   A CE2 1 
ATOM   2375 C CZ  . PHE   A 1 326 ? 16.305  -10.213 2.077  1.00 168.65 ? 344 PHE   A CZ  1 
ATOM   2376 N N   . ILE   A 1 327 ? 16.970  -14.672 6.725  1.00 182.39 ? 345 ILE   A N   1 
ATOM   2377 C CA  . ILE   A 1 327 ? 16.948  -14.221 8.114  1.00 210.57 ? 345 ILE   A CA  1 
ATOM   2378 C C   . ILE   A 1 327 ? 18.311  -14.427 8.767  1.00 202.93 ? 345 ILE   A C   1 
ATOM   2379 O O   . ILE   A 1 327 ? 18.749  -13.612 9.588  1.00 154.51 ? 345 ILE   A O   1 
ATOM   2380 C CB  . ILE   A 1 327 ? 15.824  -14.932 8.889  1.00 150.71 ? 345 ILE   A CB  1 
ATOM   2381 C CG1 . ILE   A 1 327 ? 14.469  -14.535 8.293  1.00 173.37 ? 345 ILE   A CG1 1 
ATOM   2382 C CG2 . ILE   A 1 327 ? 15.895  -14.590 10.379 1.00 129.09 ? 345 ILE   A CG2 1 
ATOM   2383 C CD1 . ILE   A 1 327 ? 13.275  -14.893 9.146  1.00 217.21 ? 345 ILE   A CD1 1 
ATOM   2384 N N   . ASN   A 1 328 ? 19.000  -15.518 8.427  1.00 171.19 ? 346 ASN   A N   1 
ATOM   2385 C CA  . ASN   A 1 328 ? 20.343  -15.730 8.961  1.00 168.55 ? 346 ASN   A CA  1 
ATOM   2386 C C   . ASN   A 1 328 ? 21.297  -14.640 8.490  1.00 165.21 ? 346 ASN   A C   1 
ATOM   2387 O O   . ASN   A 1 328 ? 22.134  -14.161 9.262  1.00 170.42 ? 346 ASN   A O   1 
ATOM   2388 C CB  . ASN   A 1 328 ? 20.865  -17.107 8.552  1.00 156.57 ? 346 ASN   A CB  1 
ATOM   2389 C CG  . ASN   A 1 328 ? 20.026  -18.239 9.110  1.00 160.05 ? 346 ASN   A CG  1 
ATOM   2390 O OD1 . ASN   A 1 328 ? 19.623  -19.145 8.381  1.00 163.60 ? 346 ASN   A OD1 1 
ATOM   2391 N ND2 . ASN   A 1 328 ? 19.756  -18.192 10.410 1.00 162.93 ? 346 ASN   A ND2 1 
ATOM   2392 N N   . ASP   A 1 329 ? 21.190  -14.241 7.221  1.00 162.95 ? 347 ASP   A N   1 
ATOM   2393 C CA  . ASP   A 1 329 ? 22.014  -13.149 6.716  1.00 174.04 ? 347 ASP   A CA  1 
ATOM   2394 C C   . ASP   A 1 329 ? 21.682  -11.842 7.422  1.00 179.39 ? 347 ASP   A C   1 
ATOM   2395 O O   . ASP   A 1 329 ? 22.578  -11.045 7.721  1.00 181.87 ? 347 ASP   A O   1 
ATOM   2396 C CB  . ASP   A 1 329 ? 21.827  -13.008 5.206  1.00 180.25 ? 347 ASP   A CB  1 
ATOM   2397 C CG  . ASP   A 1 329 ? 22.328  -14.217 4.441  1.00 170.50 ? 347 ASP   A CG  1 
ATOM   2398 O OD1 . ASP   A 1 329 ? 22.820  -15.167 5.086  1.00 172.47 ? 347 ASP   A OD1 1 
ATOM   2399 O OD2 . ASP   A 1 329 ? 22.231  -14.217 3.196  1.00 160.35 ? 347 ASP   A OD2 1 
ATOM   2400 N N   . ILE   A 1 330 ? 20.397  -11.599 7.692  1.00 164.06 ? 348 ILE   A N   1 
ATOM   2401 C CA  . ILE   A 1 330 ? 20.021  -10.402 8.440  1.00 175.40 ? 348 ILE   A CA  1 
ATOM   2402 C C   . ILE   A 1 330 ? 20.648  -10.428 9.829  1.00 184.72 ? 348 ILE   A C   1 
ATOM   2403 O O   . ILE   A 1 330 ? 21.170  -9.415  10.311 1.00 186.71 ? 348 ILE   A O   1 
ATOM   2404 C CB  . ILE   A 1 330 ? 18.489  -10.270 8.515  1.00 191.31 ? 348 ILE   A CB  1 
ATOM   2405 C CG1 . ILE   A 1 330 ? 17.915  -9.987  7.125  1.00 142.51 ? 348 ILE   A CG1 1 
ATOM   2406 C CG2 . ILE   A 1 330 ? 18.104  -9.167  9.494  1.00 164.89 ? 348 ILE   A CG2 1 
ATOM   2407 C CD1 . ILE   A 1 330 ? 16.401  -10.003 7.067  1.00 146.07 ? 348 ILE   A CD1 1 
ATOM   2408 N N   . TYR   A 1 331 ? 20.604  -11.584 10.496 1.00 197.24 ? 349 TYR   A N   1 
ATOM   2409 C CA  . TYR   A 1 331 ? 21.237  -11.708 11.805 1.00 160.58 ? 349 TYR   A CA  1 
ATOM   2410 C C   . TYR   A 1 331 ? 22.734  -11.436 11.718 1.00 177.77 ? 349 TYR   A C   1 
ATOM   2411 O O   . TYR   A 1 331 ? 23.296  -10.724 12.557 1.00 176.03 ? 349 TYR   A O   1 
ATOM   2412 C CB  . TYR   A 1 331 ? 21.000  -13.106 12.382 1.00 160.32 ? 349 TYR   A CB  1 
ATOM   2413 C CG  . TYR   A 1 331 ? 19.580  -13.411 12.821 1.00 163.96 ? 349 TYR   A CG  1 
ATOM   2414 C CD1 . TYR   A 1 331 ? 18.693  -12.397 13.163 1.00 144.95 ? 349 TYR   A CD1 1 
ATOM   2415 C CD2 . TYR   A 1 331 ? 19.135  -14.724 12.908 1.00 183.34 ? 349 TYR   A CD2 1 
ATOM   2416 C CE1 . TYR   A 1 331 ? 17.402  -12.685 13.569 1.00 123.25 ? 349 TYR   A CE1 1 
ATOM   2417 C CE2 . TYR   A 1 331 ? 17.849  -15.020 13.313 1.00 174.50 ? 349 TYR   A CE2 1 
ATOM   2418 C CZ  . TYR   A 1 331 ? 16.986  -13.998 13.642 1.00 137.98 ? 349 TYR   A CZ  1 
ATOM   2419 O OH  . TYR   A 1 331 ? 15.704  -14.293 14.046 1.00 153.38 ? 349 TYR   A OH  1 
ATOM   2420 N N   . GLU   A 1 332 ? 23.396  -11.998 10.705 1.00 177.54 ? 350 GLU   A N   1 
ATOM   2421 C CA  . GLU   A 1 332 ? 24.844  -11.877 10.592 1.00 166.87 ? 350 GLU   A CA  1 
ATOM   2422 C C   . GLU   A 1 332 ? 25.281  -10.490 10.136 1.00 175.53 ? 350 GLU   A C   1 
ATOM   2423 O O   . GLU   A 1 332 ? 26.447  -10.129 10.327 1.00 178.49 ? 350 GLU   A O   1 
ATOM   2424 C CB  . GLU   A 1 332 ? 25.375  -12.939 9.627  1.00 182.27 ? 350 GLU   A CB  1 
ATOM   2425 C CG  . GLU   A 1 332 ? 25.174  -14.369 10.114 1.00 171.99 ? 350 GLU   A CG  1 
ATOM   2426 C CD  . GLU   A 1 332 ? 25.378  -15.399 9.019  1.00 204.55 ? 350 GLU   A CD  1 
ATOM   2427 O OE1 . GLU   A 1 332 ? 25.739  -15.007 7.889  1.00 194.53 ? 350 GLU   A OE1 1 
ATOM   2428 O OE2 . GLU   A 1 332 ? 25.173  -16.602 9.288  1.00 194.44 ? 350 GLU   A OE2 1 
ATOM   2429 N N   . HIS   A 1 333 ? 24.379  -9.709  9.537  1.00 199.66 ? 351 HIS   A N   1 
ATOM   2430 C CA  . HIS   A 1 333 ? 24.738  -8.362  9.101  1.00 207.09 ? 351 HIS   A CA  1 
ATOM   2431 C C   . HIS   A 1 333 ? 24.981  -7.449  10.296 1.00 201.11 ? 351 HIS   A C   1 
ATOM   2432 O O   . HIS   A 1 333 ? 26.045  -6.828  10.414 1.00 201.96 ? 351 HIS   A O   1 
ATOM   2433 C CB  . HIS   A 1 333 ? 23.636  -7.793  8.203  1.00 212.22 ? 351 HIS   A CB  1 
ATOM   2434 C CG  . HIS   A 1 333 ? 23.622  -8.367  6.820  1.00 217.40 ? 351 HIS   A CG  1 
ATOM   2435 N ND1 . HIS   A 1 333 ? 24.727  -8.959  6.246  1.00 215.24 ? 351 HIS   A ND1 1 
ATOM   2436 C CD2 . HIS   A 1 333 ? 22.636  -8.436  5.894  1.00 222.70 ? 351 HIS   A CD2 1 
ATOM   2437 C CE1 . HIS   A 1 333 ? 24.422  -9.369  5.028  1.00 216.62 ? 351 HIS   A CE1 1 
ATOM   2438 N NE2 . HIS   A 1 333 ? 23.159  -9.064  4.790  1.00 224.25 ? 351 HIS   A NE2 1 
ATOM   2439 N N   . TYR   A 1 334 ? 24.006  -7.359  11.200 1.00 168.58 ? 352 TYR   A N   1 
ATOM   2440 C CA  . TYR   A 1 334 ? 24.150  -6.555  12.407 1.00 198.85 ? 352 TYR   A CA  1 
ATOM   2441 C C   . TYR   A 1 334 ? 24.917  -7.279  13.505 1.00 166.45 ? 352 TYR   A C   1 
ATOM   2442 O O   . TYR   A 1 334 ? 25.038  -6.743  14.611 1.00 152.09 ? 352 TYR   A O   1 
ATOM   2443 C CB  . TYR   A 1 334 ? 22.772  -6.132  12.925 1.00 166.00 ? 352 TYR   A CB  1 
ATOM   2444 C CG  . TYR   A 1 334 ? 22.046  -5.192  11.990 1.00 162.43 ? 352 TYR   A CG  1 
ATOM   2445 C CD1 . TYR   A 1 334 ? 21.247  -5.682  10.967 1.00 156.42 ? 352 TYR   A CD1 1 
ATOM   2446 C CD2 . TYR   A 1 334 ? 22.167  -3.815  12.125 1.00 163.48 ? 352 TYR   A CD2 1 
ATOM   2447 C CE1 . TYR   A 1 334 ? 20.585  -4.829  10.108 1.00 203.13 ? 352 TYR   A CE1 1 
ATOM   2448 C CE2 . TYR   A 1 334 ? 21.509  -2.953  11.269 1.00 183.04 ? 352 TYR   A CE2 1 
ATOM   2449 C CZ  . TYR   A 1 334 ? 20.723  -3.465  10.261 1.00 181.42 ? 352 TYR   A CZ  1 
ATOM   2450 O OH  . TYR   A 1 334 ? 20.062  -2.611  9.408  1.00 188.89 ? 352 TYR   A OH  1 
ATOM   2451 N N   . ASN   A 1 335 ? 25.427  -8.477  13.228 1.00 180.95 ? 353 ASN   A N   1 
ATOM   2452 C CA  . ASN   A 1 335 ? 26.294  -9.205  14.149 1.00 191.87 ? 353 ASN   A CA  1 
ATOM   2453 C C   . ASN   A 1 335 ? 25.642  -9.339  15.524 1.00 169.77 ? 353 ASN   A C   1 
ATOM   2454 O O   . ASN   A 1 335 ? 26.164  -8.885  16.544 1.00 134.08 ? 353 ASN   A O   1 
ATOM   2455 C CB  . ASN   A 1 335 ? 27.661  -8.524  14.249 1.00 162.12 ? 353 ASN   A CB  1 
ATOM   2456 C CG  . ASN   A 1 335 ? 28.388  -8.481  12.919 1.00 158.66 ? 353 ASN   A CG  1 
ATOM   2457 O OD1 . ASN   A 1 335 ? 29.109  -9.412  12.563 1.00 185.77 ? 353 ASN   A OD1 1 
ATOM   2458 N ND2 . ASN   A 1 335 ? 28.200  -7.396  12.177 1.00 238.58 ? 353 ASN   A ND2 1 
ATOM   2459 N N   . ILE   A 1 336 ? 24.473  -9.983  15.534 1.00 147.14 ? 354 ILE   A N   1 
ATOM   2460 C CA  . ILE   A 1 336 ? 23.799  -10.257 16.796 1.00 140.93 ? 354 ILE   A CA  1 
ATOM   2461 C C   . ILE   A 1 336 ? 24.580  -11.282 17.610 1.00 140.89 ? 354 ILE   A C   1 
ATOM   2462 O O   . ILE   A 1 336 ? 24.385  -11.389 18.829 1.00 145.35 ? 354 ILE   A O   1 
ATOM   2463 C CB  . ILE   A 1 336 ? 22.355  -10.747 16.563 1.00 139.89 ? 354 ILE   A CB  1 
ATOM   2464 C CG1 . ILE   A 1 336 ? 21.672  -9.985  15.420 1.00 148.54 ? 354 ILE   A CG1 1 
ATOM   2465 C CG2 . ILE   A 1 336 ? 21.534  -10.582 17.829 1.00 142.39 ? 354 ILE   A CG2 1 
ATOM   2466 C CD1 . ILE   A 1 336 ? 21.582  -8.485  15.624 1.00 146.45 ? 354 ILE   A CD1 1 
ATOM   2467 N N   . ARG   A 1 337 ? 25.470  -12.040 16.961 1.00 153.02 ? 355 ARG   A N   1 
ATOM   2468 C CA  . ARG   A 1 337 ? 26.232  -13.074 17.651 1.00 131.49 ? 355 ARG   A CA  1 
ATOM   2469 C C   . ARG   A 1 337 ? 27.181  -12.496 18.694 1.00 137.49 ? 355 ARG   A C   1 
ATOM   2470 O O   . ARG   A 1 337 ? 27.550  -13.204 19.637 1.00 130.45 ? 355 ARG   A O   1 
ATOM   2471 C CB  . ARG   A 1 337 ? 27.008  -13.909 16.629 1.00 140.00 ? 355 ARG   A CB  1 
ATOM   2472 C CG  . ARG   A 1 337 ? 26.112  -14.673 15.660 1.00 152.22 ? 355 ARG   A CG  1 
ATOM   2473 C CD  . ARG   A 1 337 ? 26.912  -15.498 14.662 1.00 153.95 ? 355 ARG   A CD  1 
ATOM   2474 N NE  . ARG   A 1 337 ? 26.045  -16.170 13.700 1.00 181.55 ? 355 ARG   A NE  1 
ATOM   2475 C CZ  . ARG   A 1 337 ? 26.476  -16.915 12.690 1.00 182.87 ? 355 ARG   A CZ  1 
ATOM   2476 N NH1 . ARG   A 1 337 ? 27.767  -17.115 12.478 1.00 178.58 ? 355 ARG   A NH1 1 
ATOM   2477 N NH2 . ARG   A 1 337 ? 25.589  -17.474 11.872 1.00 175.33 ? 355 ARG   A NH2 1 
ATOM   2478 N N   . ASP   A 1 338 ? 27.585  -11.234 18.548 1.00 124.34 ? 356 ASP   A N   1 
ATOM   2479 C CA  . ASP   A 1 338 ? 28.393  -10.569 19.564 1.00 152.99 ? 356 ASP   A CA  1 
ATOM   2480 C C   . ASP   A 1 338 ? 27.534  -9.866  20.605 1.00 132.59 ? 356 ASP   A C   1 
ATOM   2481 O O   . ASP   A 1 338 ? 27.944  -9.740  21.768 1.00 135.96 ? 356 ASP   A O   1 
ATOM   2482 C CB  . ASP   A 1 338 ? 29.333  -9.556  18.907 1.00 165.31 ? 356 ASP   A CB  1 
ATOM   2483 C CG  . ASP   A 1 338 ? 29.995  -10.104 17.660 1.00 143.33 ? 356 ASP   A CG  1 
ATOM   2484 O OD1 . ASP   A 1 338 ? 29.269  -10.424 16.696 1.00 143.94 ? 356 ASP   A OD1 1 
ATOM   2485 O OD2 . ASP   A 1 338 ? 31.239  -10.212 17.643 1.00 147.77 ? 356 ASP   A OD2 1 
ATOM   2486 N N   . HIS   A 1 339 ? 26.352  -9.394  20.208 1.00 121.64 ? 357 HIS   A N   1 
ATOM   2487 C CA  . HIS   A 1 339 ? 25.395  -8.921  21.197 1.00 144.27 ? 357 HIS   A CA  1 
ATOM   2488 C C   . HIS   A 1 339 ? 25.049  -10.030 22.175 1.00 133.51 ? 357 HIS   A C   1 
ATOM   2489 O O   . HIS   A 1 339 ? 24.832  -9.770  23.363 1.00 133.22 ? 357 HIS   A O   1 
ATOM   2490 C CB  . HIS   A 1 339 ? 24.134  -8.403  20.508 1.00 112.61 ? 357 HIS   A CB  1 
ATOM   2491 C CG  . HIS   A 1 339 ? 24.374  -7.215  19.629 1.00 137.20 ? 357 HIS   A CG  1 
ATOM   2492 N ND1 . HIS   A 1 339 ? 24.920  -7.320  18.368 1.00 166.43 ? 357 HIS   A ND1 1 
ATOM   2493 C CD2 . HIS   A 1 339 ? 24.150  -5.895  19.831 1.00 118.70 ? 357 HIS   A CD2 1 
ATOM   2494 C CE1 . HIS   A 1 339 ? 25.019  -6.118  17.830 1.00 146.25 ? 357 HIS   A CE1 1 
ATOM   2495 N NE2 . HIS   A 1 339 ? 24.559  -5.235  18.697 1.00 163.96 ? 357 HIS   A NE2 1 
ATOM   2496 N N   . TYR   A 1 340 ? 24.997  -11.277 21.700 1.00 131.33 ? 358 TYR   A N   1 
ATOM   2497 C CA  . TYR   A 1 340 ? 24.790  -12.383 22.627 1.00 125.39 ? 358 TYR   A CA  1 
ATOM   2498 C C   . TYR   A 1 340 ? 25.943  -12.495 23.612 1.00 120.95 ? 358 TYR   A C   1 
ATOM   2499 O O   . TYR   A 1 340 ? 25.731  -12.826 24.778 1.00 124.55 ? 358 TYR   A O   1 
ATOM   2500 C CB  . TYR   A 1 340 ? 24.626  -13.715 21.905 1.00 117.89 ? 358 TYR   A CB  1 
ATOM   2501 C CG  . TYR   A 1 340 ? 24.773  -14.862 22.885 1.00 128.45 ? 358 TYR   A CG  1 
ATOM   2502 C CD1 . TYR   A 1 340 ? 23.795  -15.107 23.840 1.00 122.14 ? 358 TYR   A CD1 1 
ATOM   2503 C CD2 . TYR   A 1 340 ? 25.908  -15.665 22.891 1.00 117.45 ? 358 TYR   A CD2 1 
ATOM   2504 C CE1 . TYR   A 1 340 ? 23.927  -16.134 24.753 1.00 114.73 ? 358 TYR   A CE1 1 
ATOM   2505 C CE2 . TYR   A 1 340 ? 26.048  -16.696 23.802 1.00 127.47 ? 358 TYR   A CE2 1 
ATOM   2506 C CZ  . TYR   A 1 340 ? 25.054  -16.924 24.731 1.00 123.05 ? 358 TYR   A CZ  1 
ATOM   2507 O OH  . TYR   A 1 340 ? 25.185  -17.946 25.642 1.00 127.29 ? 358 TYR   A OH  1 
ATOM   2508 N N   . VAL   A 1 341 ? 27.175  -12.265 23.156 1.00 125.98 ? 359 VAL   A N   1 
ATOM   2509 C CA  . VAL   A 1 341 ? 28.316  -12.321 24.067 1.00 125.17 ? 359 VAL   A CA  1 
ATOM   2510 C C   . VAL   A 1 341 ? 28.192  -11.242 25.133 1.00 125.51 ? 359 VAL   A C   1 
ATOM   2511 O O   . VAL   A 1 341 ? 28.421  -11.487 26.327 1.00 128.93 ? 359 VAL   A O   1 
ATOM   2512 C CB  . VAL   A 1 341 ? 29.630  -12.188 23.277 1.00 130.88 ? 359 VAL   A CB  1 
ATOM   2513 C CG1 . VAL   A 1 341 ? 30.822  -12.200 24.221 1.00 114.05 ? 359 VAL   A CG1 1 
ATOM   2514 C CG2 . VAL   A 1 341 ? 29.744  -13.299 22.242 1.00 118.94 ? 359 VAL   A CG2 1 
ATOM   2515 N N   . GLU   A 1 342 ? 27.834  -10.027 24.715 1.00 118.26 ? 360 GLU   A N   1 
ATOM   2516 C CA  . GLU   A 1 342 ? 27.641  -8.946  25.678 1.00 121.75 ? 360 GLU   A CA  1 
ATOM   2517 C C   . GLU   A 1 342 ? 26.542  -9.298  26.673 1.00 122.07 ? 360 GLU   A C   1 
ATOM   2518 O O   . GLU   A 1 342 ? 26.689  -9.084  27.886 1.00 128.62 ? 360 GLU   A O   1 
ATOM   2519 C CB  . GLU   A 1 342 ? 27.300  -7.648  24.945 1.00 136.22 ? 360 GLU   A CB  1 
ATOM   2520 C CG  . GLU   A 1 342 ? 28.335  -7.216  23.916 1.00 136.38 ? 360 GLU   A CG  1 
ATOM   2521 C CD  . GLU   A 1 342 ? 27.840  -6.084  23.037 1.00 141.42 ? 360 GLU   A CD  1 
ATOM   2522 O OE1 . GLU   A 1 342 ? 26.715  -5.595  23.276 1.00 143.14 ? 360 GLU   A OE1 1 
ATOM   2523 O OE2 . GLU   A 1 342 ? 28.573  -5.688  22.107 1.00 154.29 ? 360 GLU   A OE2 1 
ATOM   2524 N N   . TYR   A 1 343 ? 25.433  -9.845  26.173 1.00 145.77 ? 361 TYR   A N   1 
ATOM   2525 C CA  . TYR   A 1 343 ? 24.344  -10.261 27.046 1.00 125.05 ? 361 TYR   A CA  1 
ATOM   2526 C C   . TYR   A 1 343 ? 24.799  -11.348 28.007 1.00 106.95 ? 361 TYR   A C   1 
ATOM   2527 O O   . TYR   A 1 343 ? 24.414  -11.350 29.178 1.00 103.70 ? 361 TYR   A O   1 
ATOM   2528 C CB  . TYR   A 1 343 ? 23.163  -10.755 26.209 1.00 114.15 ? 361 TYR   A CB  1 
ATOM   2529 C CG  . TYR   A 1 343 ? 22.067  -11.373 27.041 1.00 111.36 ? 361 TYR   A CG  1 
ATOM   2530 C CD1 . TYR   A 1 343 ? 21.054  -10.592 27.577 1.00 96.66  ? 361 TYR   A CD1 1 
ATOM   2531 C CD2 . TYR   A 1 343 ? 22.053  -12.737 27.303 1.00 102.72 ? 361 TYR   A CD2 1 
ATOM   2532 C CE1 . TYR   A 1 343 ? 20.054  -11.151 28.346 1.00 134.56 ? 361 TYR   A CE1 1 
ATOM   2533 C CE2 . TYR   A 1 343 ? 21.059  -13.304 28.072 1.00 90.63  ? 361 TYR   A CE2 1 
ATOM   2534 C CZ  . TYR   A 1 343 ? 20.062  -12.507 28.590 1.00 103.64 ? 361 TYR   A CZ  1 
ATOM   2535 O OH  . TYR   A 1 343 ? 19.068  -13.066 29.356 1.00 109.54 ? 361 TYR   A OH  1 
ATOM   2536 N N   . GLU   A 1 344 ? 25.595  -12.298 27.519 1.00 102.64 ? 362 GLU   A N   1 
ATOM   2537 C CA  . GLU   A 1 344 ? 26.112  -13.356 28.376 1.00 104.40 ? 362 GLU   A CA  1 
ATOM   2538 C C   . GLU   A 1 344 ? 26.920  -12.762 29.516 1.00 98.35  ? 362 GLU   A C   1 
ATOM   2539 O O   . GLU   A 1 344 ? 26.725  -13.114 30.684 1.00 97.66  ? 362 GLU   A O   1 
ATOM   2540 C CB  . GLU   A 1 344 ? 26.967  -14.317 27.544 1.00 108.52 ? 362 GLU   A CB  1 
ATOM   2541 C CG  . GLU   A 1 344 ? 27.304  -15.641 28.222 1.00 131.83 ? 362 GLU   A CG  1 
ATOM   2542 C CD  . GLU   A 1 344 ? 28.354  -15.509 29.313 1.00 116.35 ? 362 GLU   A CD  1 
ATOM   2543 O OE1 . GLU   A 1 344 ? 29.156  -14.552 29.262 1.00 105.04 ? 362 GLU   A OE1 1 
ATOM   2544 O OE2 . GLU   A 1 344 ? 28.378  -16.365 30.222 1.00 121.11 ? 362 GLU   A OE2 1 
ATOM   2545 N N   . LYS   A 1 345 ? 27.819  -11.832 29.192 1.00 107.86 ? 363 LYS   A N   1 
ATOM   2546 C CA  . LYS   A 1 345 ? 28.623  -11.193 30.228 1.00 103.54 ? 363 LYS   A CA  1 
ATOM   2547 C C   . LYS   A 1 345 ? 27.736  -10.505 31.259 1.00 99.32  ? 363 LYS   A C   1 
ATOM   2548 O O   . LYS   A 1 345 ? 27.876  -10.726 32.468 1.00 104.35 ? 363 LYS   A O   1 
ATOM   2549 C CB  . LYS   A 1 345 ? 29.589  -10.191 29.597 1.00 117.43 ? 363 LYS   A CB  1 
ATOM   2550 C CG  . LYS   A 1 345 ? 30.643  -10.819 28.702 1.00 134.85 ? 363 LYS   A CG  1 
ATOM   2551 C CD  . LYS   A 1 345 ? 31.571  -9.763  28.127 1.00 142.01 ? 363 LYS   A CD  1 
ATOM   2552 C CE  . LYS   A 1 345 ? 32.631  -10.379 27.231 1.00 159.10 ? 363 LYS   A CE  1 
ATOM   2553 N NZ  . LYS   A 1 345 ? 33.547  -9.350  26.663 1.00 164.80 ? 363 LYS   A NZ  1 
ATOM   2554 N N   . LYS   A 1 346 ? 26.804  -9.671  30.795 1.00 106.93 ? 364 LYS   A N   1 
ATOM   2555 C CA  . LYS   A 1 346 ? 25.989  -8.891  31.724 1.00 95.75  ? 364 LYS   A CA  1 
ATOM   2556 C C   . LYS   A 1 346 ? 25.101  -9.792  32.578 1.00 104.60 ? 364 LYS   A C   1 
ATOM   2557 O O   . LYS   A 1 346 ? 24.985  -9.596  33.795 1.00 102.29 ? 364 LYS   A O   1 
ATOM   2558 C CB  . LYS   A 1 346 ? 25.146  -7.880  30.948 1.00 107.94 ? 364 LYS   A CB  1 
ATOM   2559 C CG  . LYS   A 1 346 ? 25.971  -6.852  30.185 1.00 128.11 ? 364 LYS   A CG  1 
ATOM   2560 C CD  . LYS   A 1 346 ? 25.098  -5.944  29.335 1.00 162.93 ? 364 LYS   A CD  1 
ATOM   2561 C CE  . LYS   A 1 346 ? 25.943  -4.968  28.527 1.00 159.28 ? 364 LYS   A CE  1 
ATOM   2562 N NZ  . LYS   A 1 346 ? 25.116  -4.087  27.657 1.00 164.00 ? 364 LYS   A NZ  1 
ATOM   2563 N N   . GLN   A 1 347 ? 24.461  -10.782 31.955 1.00 103.62 ? 365 GLN   A N   1 
ATOM   2564 C CA  . GLN   A 1 347 ? 23.572  -11.674 32.687 1.00 90.37  ? 365 GLN   A CA  1 
ATOM   2565 C C   . GLN   A 1 347 ? 24.346  -12.514 33.692 1.00 96.02  ? 365 GLN   A C   1 
ATOM   2566 O O   . GLN   A 1 347 ? 23.866  -12.752 34.805 1.00 87.29  ? 365 GLN   A O   1 
ATOM   2567 C CB  . GLN   A 1 347 ? 22.813  -12.567 31.706 1.00 90.12  ? 365 GLN   A CB  1 
ATOM   2568 C CG  . GLN   A 1 347 ? 21.574  -13.222 32.290 1.00 95.02  ? 365 GLN   A CG  1 
ATOM   2569 C CD  . GLN   A 1 347 ? 20.474  -12.224 32.590 1.00 89.27  ? 365 GLN   A CD  1 
ATOM   2570 O OE1 . GLN   A 1 347 ? 20.641  -11.021 32.391 1.00 97.18  ? 365 GLN   A OE1 1 
ATOM   2571 N NE2 . GLN   A 1 347 ? 19.339  -12.720 33.070 1.00 87.40  ? 365 GLN   A NE2 1 
ATOM   2572 N N   . LYS   A 1 348 ? 25.544  -12.978 33.322 1.00 94.02  ? 366 LYS   A N   1 
ATOM   2573 C CA  . LYS   A 1 348 ? 26.367  -13.714 34.273 1.00 89.40  ? 366 LYS   A CA  1 
ATOM   2574 C C   . LYS   A 1 348 ? 26.766  -12.824 35.440 1.00 88.48  ? 366 LYS   A C   1 
ATOM   2575 O O   . LYS   A 1 348 ? 26.788  -13.270 36.593 1.00 88.29  ? 366 LYS   A O   1 
ATOM   2576 C CB  . LYS   A 1 348 ? 27.604  -14.274 33.571 1.00 87.61  ? 366 LYS   A CB  1 
ATOM   2577 C CG  . LYS   A 1 348 ? 28.376  -15.294 34.391 1.00 120.15 ? 366 LYS   A CG  1 
ATOM   2578 C CD  . LYS   A 1 348 ? 29.475  -15.944 33.566 1.00 108.15 ? 366 LYS   A CD  1 
ATOM   2579 C CE  . LYS   A 1 348 ? 30.177  -17.047 34.338 1.00 114.31 ? 366 LYS   A CE  1 
ATOM   2580 N NZ  . LYS   A 1 348 ? 31.261  -17.677 33.538 1.00 122.33 ? 366 LYS   A NZ  1 
ATOM   2581 N N   . MET   A 1 349 ? 27.082  -11.557 35.162 1.00 94.88  ? 367 MET   A N   1 
ATOM   2582 C CA  . MET   A 1 349 ? 27.392  -10.623 36.239 1.00 97.35  ? 367 MET   A CA  1 
ATOM   2583 C C   . MET   A 1 349 ? 26.215  -10.488 37.195 1.00 91.29  ? 367 MET   A C   1 
ATOM   2584 O O   . MET   A 1 349 ? 26.380  -10.553 38.419 1.00 94.77  ? 367 MET   A O   1 
ATOM   2585 C CB  . MET   A 1 349 ? 27.763  -9.260  35.657 1.00 110.22 ? 367 MET   A CB  1 
ATOM   2586 C CG  . MET   A 1 349 ? 29.202  -9.155  35.185 1.00 116.87 ? 367 MET   A CG  1 
ATOM   2587 S SD  . MET   A 1 349 ? 30.384  -9.168  36.549 1.00 169.00 ? 367 MET   A SD  1 
ATOM   2588 C CE  . MET   A 1 349 ? 29.966  -7.632  37.374 1.00 153.99 ? 367 MET   A CE  1 
ATOM   2589 N N   . LYS   A 1 350 ? 25.014  -10.296 36.651 1.00 92.46  ? 368 LYS   A N   1 
ATOM   2590 C CA  . LYS   A 1 350 ? 23.842  -10.132 37.506 1.00 99.64  ? 368 LYS   A CA  1 
ATOM   2591 C C   . LYS   A 1 350 ? 23.565  -11.401 38.303 1.00 90.72  ? 368 LYS   A C   1 
ATOM   2592 O O   . LYS   A 1 350 ? 23.215  -11.339 39.489 1.00 96.31  ? 368 LYS   A O   1 
ATOM   2593 C CB  . LYS   A 1 350 ? 22.631  -9.743  36.659 1.00 105.47 ? 368 LYS   A CB  1 
ATOM   2594 C CG  . LYS   A 1 350 ? 21.478  -9.162  37.462 1.00 119.42 ? 368 LYS   A CG  1 
ATOM   2595 C CD  . LYS   A 1 350 ? 20.609  -8.247  36.610 1.00 123.87 ? 368 LYS   A CD  1 
ATOM   2596 C CE  . LYS   A 1 350 ? 19.970  -8.991  35.450 1.00 138.70 ? 368 LYS   A CE  1 
ATOM   2597 N NZ  . LYS   A 1 350 ? 19.110  -8.096  34.627 1.00 149.53 ? 368 LYS   A NZ  1 
ATOM   2598 N N   . ILE   A 1 351 ? 23.723  -12.564 37.669 1.00 84.22  ? 369 ILE   A N   1 
ATOM   2599 C CA  . ILE   A 1 351 ? 23.497  -13.829 38.359 1.00 88.99  ? 369 ILE   A CA  1 
ATOM   2600 C C   . ILE   A 1 351 ? 24.482  -13.992 39.506 1.00 86.95  ? 369 ILE   A C   1 
ATOM   2601 O O   . ILE   A 1 351 ? 24.107  -14.401 40.610 1.00 84.08  ? 369 ILE   A O   1 
ATOM   2602 C CB  . ILE   A 1 351 ? 23.592  -14.999 37.362 1.00 83.07  ? 369 ILE   A CB  1 
ATOM   2603 C CG1 . ILE   A 1 351 ? 22.399  -14.967 36.402 1.00 88.03  ? 369 ILE   A CG1 1 
ATOM   2604 C CG2 . ILE   A 1 351 ? 23.663  -16.329 38.104 1.00 89.13  ? 369 ILE   A CG2 1 
ATOM   2605 C CD1 . ILE   A 1 351 ? 22.536  -15.899 35.216 1.00 91.83  ? 369 ILE   A CD1 1 
ATOM   2606 N N   . LEU   A 1 352 ? 25.758  -13.688 39.265 1.00 91.97  ? 370 LEU   A N   1 
ATOM   2607 C CA  . LEU   A 1 352 ? 26.753  -13.806 40.325 1.00 88.40  ? 370 LEU   A CA  1 
ATOM   2608 C C   . LEU   A 1 352 ? 26.482  -12.813 41.447 1.00 89.66  ? 370 LEU   A C   1 
ATOM   2609 O O   . LEU   A 1 352 ? 26.672  -13.133 42.626 1.00 93.75  ? 370 LEU   A O   1 
ATOM   2610 C CB  . LEU   A 1 352 ? 28.153  -13.607 39.748 1.00 90.59  ? 370 LEU   A CB  1 
ATOM   2611 C CG  . LEU   A 1 352 ? 28.616  -14.716 38.800 1.00 90.43  ? 370 LEU   A CG  1 
ATOM   2612 C CD1 . LEU   A 1 352 ? 29.923  -14.340 38.128 1.00 92.80  ? 370 LEU   A CD1 1 
ATOM   2613 C CD2 . LEU   A 1 352 ? 28.759  -16.037 39.547 1.00 97.58  ? 370 LEU   A CD2 1 
ATOM   2614 N N   . GLU   A 1 353 ? 26.038  -11.602 41.103 1.00 88.76  ? 371 GLU   A N   1 
ATOM   2615 C CA  . GLU   A 1 353 ? 25.667  -10.638 42.133 1.00 90.15  ? 371 GLU   A CA  1 
ATOM   2616 C C   . GLU   A 1 353 ? 24.537  -11.177 42.997 1.00 89.40  ? 371 GLU   A C   1 
ATOM   2617 O O   . GLU   A 1 353 ? 24.572  -11.061 44.227 1.00 91.84  ? 371 GLU   A O   1 
ATOM   2618 C CB  . GLU   A 1 353 ? 25.259  -9.313  41.492 1.00 102.31 ? 371 GLU   A CB  1 
ATOM   2619 C CG  . GLU   A 1 353 ? 26.411  -8.538  40.880 1.00 127.09 ? 371 GLU   A CG  1 
ATOM   2620 C CD  . GLU   A 1 353 ? 25.955  -7.264  40.197 1.00 135.52 ? 371 GLU   A CD  1 
ATOM   2621 O OE1 . GLU   A 1 353 ? 24.740  -6.973  40.233 1.00 158.07 ? 371 GLU   A OE1 1 
ATOM   2622 O OE2 . GLU   A 1 353 ? 26.810  -6.556  39.625 1.00 115.96 ? 371 GLU   A OE2 1 
ATOM   2623 N N   . ALA   A 1 354 ? 23.521  -11.770 42.367 1.00 94.93  ? 372 ALA   A N   1 
ATOM   2624 C CA  . ALA   A 1 354 ? 22.432  -12.364 43.134 1.00 89.57  ? 372 ALA   A CA  1 
ATOM   2625 C C   . ALA   A 1 354 ? 22.938  -13.507 44.005 1.00 87.80  ? 372 ALA   A C   1 
ATOM   2626 O O   . ALA   A 1 354 ? 22.539  -13.638 45.168 1.00 90.85  ? 372 ALA   A O   1 
ATOM   2627 C CB  . ALA   A 1 354 ? 21.333  -12.853 42.192 1.00 85.35  ? 372 ALA   A CB  1 
ATOM   2628 N N   . ILE   A 1 355 ? 23.824  -14.340 43.459 1.00 87.89  ? 373 ILE   A N   1 
ATOM   2629 C CA  . ILE   A 1 355 ? 24.330  -15.488 44.204 1.00 89.77  ? 373 ILE   A CA  1 
ATOM   2630 C C   . ILE   A 1 355 ? 25.090  -15.026 45.439 1.00 93.50  ? 373 ILE   A C   1 
ATOM   2631 O O   . ILE   A 1 355 ? 24.929  -15.583 46.529 1.00 95.39  ? 373 ILE   A O   1 
ATOM   2632 C CB  . ILE   A 1 355 ? 25.205  -16.367 43.291 1.00 89.54  ? 373 ILE   A CB  1 
ATOM   2633 C CG1 . ILE   A 1 355 ? 24.338  -17.051 42.230 1.00 86.51  ? 373 ILE   A CG1 1 
ATOM   2634 C CG2 . ILE   A 1 355 ? 25.960  -17.402 44.110 1.00 92.21  ? 373 ILE   A CG2 1 
ATOM   2635 C CD1 . ILE   A 1 355 ? 25.126  -17.660 41.088 1.00 86.35  ? 373 ILE   A CD1 1 
ATOM   2636 N N   . ASN   A 1 356 ? 25.931  -14.003 45.292 1.00 95.01  ? 374 ASN   A N   1 
ATOM   2637 C CA  . ASN   A 1 356 ? 26.638  -13.475 46.451 1.00 99.10  ? 374 ASN   A CA  1 
ATOM   2638 C C   . ASN   A 1 356 ? 25.680  -12.907 47.490 1.00 100.03 ? 374 ASN   A C   1 
ATOM   2639 O O   . ASN   A 1 356 ? 26.035  -12.831 48.672 1.00 103.78 ? 374 ASN   A O   1 
ATOM   2640 C CB  . ASN   A 1 356 ? 27.639  -12.406 46.012 1.00 100.69 ? 374 ASN   A CB  1 
ATOM   2641 C CG  . ASN   A 1 356 ? 28.882  -13.000 45.382 1.00 101.73 ? 374 ASN   A CG  1 
ATOM   2642 O OD1 . ASN   A 1 356 ? 28.873  -14.143 44.922 1.00 100.28 ? 374 ASN   A OD1 1 
ATOM   2643 N ND2 . ASN   A 1 356 ? 29.962  -12.231 45.363 1.00 116.87 ? 374 ASN   A ND2 1 
ATOM   2644 N N   . GLN   A 1 357 ? 24.476  -12.508 47.078 1.00 98.73  ? 375 GLN   A N   1 
ATOM   2645 C CA  . GLN   A 1 357 ? 23.468  -12.019 48.010 1.00 98.13  ? 375 GLN   A CA  1 
ATOM   2646 C C   . GLN   A 1 357 ? 22.658  -13.141 48.648 1.00 97.95  ? 375 GLN   A C   1 
ATOM   2647 O O   . GLN   A 1 357 ? 21.830  -12.862 49.522 1.00 99.36  ? 375 GLN   A O   1 
ATOM   2648 C CB  . GLN   A 1 357 ? 22.522  -11.047 47.298 1.00 118.87 ? 375 GLN   A CB  1 
ATOM   2649 C CG  . GLN   A 1 357 ? 23.161  -9.716  46.922 1.00 96.55  ? 375 GLN   A CG  1 
ATOM   2650 C CD  . GLN   A 1 357 ? 22.177  -8.755  46.283 1.00 97.71  ? 375 GLN   A CD  1 
ATOM   2651 O OE1 . GLN   A 1 357 ? 21.060  -9.135  45.928 1.00 118.45 ? 375 GLN   A OE1 1 
ATOM   2652 N NE2 . GLN   A 1 357 ? 22.585  -7.498  46.138 1.00 113.52 ? 375 GLN   A NE2 1 
ATOM   2653 N N   . LEU   A 1 358 ? 22.870  -14.394 48.236 1.00 96.59  ? 376 LEU   A N   1 
ATOM   2654 C CA  . LEU   A 1 358 ? 22.150  -15.506 48.851 1.00 96.75  ? 376 LEU   A CA  1 
ATOM   2655 C C   . LEU   A 1 358 ? 22.524  -15.664 50.318 1.00 101.14 ? 376 LEU   A C   1 
ATOM   2656 O O   . LEU   A 1 358 ? 21.660  -15.930 51.162 1.00 102.32 ? 376 LEU   A O   1 
ATOM   2657 C CB  . LEU   A 1 358 ? 22.435  -16.805 48.097 1.00 96.45  ? 376 LEU   A CB  1 
ATOM   2658 C CG  . LEU   A 1 358 ? 21.386  -17.298 47.102 1.00 98.33  ? 376 LEU   A CG  1 
ATOM   2659 C CD1 . LEU   A 1 358 ? 21.855  -18.593 46.459 1.00 90.44  ? 376 LEU   A CD1 1 
ATOM   2660 C CD2 . LEU   A 1 358 ? 20.043  -17.495 47.784 1.00 109.00 ? 376 LEU   A CD2 1 
ATOM   2661 N N   . HIS   A 1 359 ? 23.808  -15.515 50.640 1.00 104.01 ? 377 HIS   A N   1 
ATOM   2662 C CA  . HIS   A 1 359 ? 24.305  -15.697 52.002 1.00 108.80 ? 377 HIS   A CA  1 
ATOM   2663 C C   . HIS   A 1 359 ? 24.076  -17.132 52.475 1.00 109.32 ? 377 HIS   A C   1 
ATOM   2664 O O   . HIS   A 1 359 ? 23.506  -17.385 53.538 1.00 111.74 ? 377 HIS   A O   1 
ATOM   2665 C CB  . HIS   A 1 359 ? 23.666  -14.686 52.956 1.00 111.35 ? 377 HIS   A CB  1 
ATOM   2666 C CG  . HIS   A 1 359 ? 24.057  -13.270 52.674 1.00 111.96 ? 377 HIS   A CG  1 
ATOM   2667 N ND1 . HIS   A 1 359 ? 23.186  -12.213 52.817 1.00 111.85 ? 377 HIS   A ND1 1 
ATOM   2668 C CD2 . HIS   A 1 359 ? 25.228  -12.739 52.251 1.00 112.98 ? 377 HIS   A CD2 1 
ATOM   2669 C CE1 . HIS   A 1 359 ? 23.803  -11.090 52.496 1.00 112.69 ? 377 HIS   A CE1 1 
ATOM   2670 N NE2 . HIS   A 1 359 ? 25.044  -11.381 52.149 1.00 113.40 ? 377 HIS   A NE2 1 
ATOM   2671 N N   . HIS   A 1 360 ? 24.533  -18.079 51.659 1.00 107.32 ? 378 HIS   A N   1 
ATOM   2672 C CA  . HIS   A 1 360 ? 24.531  -19.493 52.018 1.00 108.13 ? 378 HIS   A CA  1 
ATOM   2673 C C   . HIS   A 1 360 ? 25.671  -20.154 51.261 1.00 107.87 ? 378 HIS   A C   1 
ATOM   2674 O O   . HIS   A 1 360 ? 25.669  -20.170 50.027 1.00 104.52 ? 378 HIS   A O   1 
ATOM   2675 C CB  . HIS   A 1 360 ? 23.196  -20.158 51.684 1.00 105.04 ? 378 HIS   A CB  1 
ATOM   2676 C CG  . HIS   A 1 360 ? 23.055  -21.535 52.253 1.00 123.56 ? 378 HIS   A CG  1 
ATOM   2677 N ND1 . HIS   A 1 360 ? 23.683  -22.634 51.709 1.00 123.28 ? 378 HIS   A ND1 1 
ATOM   2678 C CD2 . HIS   A 1 360 ? 22.360  -21.991 53.323 1.00 108.77 ? 378 HIS   A CD2 1 
ATOM   2679 C CE1 . HIS   A 1 360 ? 23.381  -23.708 52.416 1.00 107.80 ? 378 HIS   A CE1 1 
ATOM   2680 N NE2 . HIS   A 1 360 ? 22.579  -23.345 53.401 1.00 109.49 ? 378 HIS   A NE2 1 
ATOM   2681 N N   . GLU   A 1 361 ? 26.637  -20.700 52.000 1.00 111.79 ? 379 GLU   A N   1 
ATOM   2682 C CA  . GLU   A 1 361 ? 27.899  -21.113 51.393 1.00 112.62 ? 379 GLU   A CA  1 
ATOM   2683 C C   . GLU   A 1 361 ? 27.688  -22.198 50.341 1.00 109.43 ? 379 GLU   A C   1 
ATOM   2684 O O   . GLU   A 1 361 ? 28.123  -22.058 49.189 1.00 107.44 ? 379 GLU   A O   1 
ATOM   2685 C CB  . GLU   A 1 361 ? 28.853  -21.605 52.485 1.00 117.89 ? 379 GLU   A CB  1 
ATOM   2686 C CG  . GLU   A 1 361 ? 29.073  -20.617 53.627 1.00 121.99 ? 379 GLU   A CG  1 
ATOM   2687 C CD  . GLU   A 1 361 ? 29.679  -21.269 54.858 1.00 136.46 ? 379 GLU   A CD  1 
ATOM   2688 O OE1 . GLU   A 1 361 ? 29.951  -22.487 54.818 1.00 138.45 ? 379 GLU   A OE1 1 
ATOM   2689 O OE2 . GLU   A 1 361 ? 29.879  -20.563 55.869 1.00 165.77 ? 379 GLU   A OE2 1 
ATOM   2690 N N   . GLY   A 1 362 ? 27.014  -23.286 50.717 1.00 109.28 ? 380 GLY   A N   1 
ATOM   2691 C CA  . GLY   A 1 362 ? 26.922  -24.432 49.825 1.00 107.23 ? 380 GLY   A CA  1 
ATOM   2692 C C   . GLY   A 1 362 ? 26.140  -24.133 48.560 1.00 102.72 ? 380 GLY   A C   1 
ATOM   2693 O O   . GLY   A 1 362 ? 26.564  -24.483 47.453 1.00 101.33 ? 380 GLY   A O   1 
ATOM   2694 N N   . ILE   A 1 363 ? 24.980  -23.492 48.706 1.00 100.78 ? 381 ILE   A N   1 
ATOM   2695 C CA  . ILE   A 1 363 ? 24.163  -23.180 47.539 1.00 96.85  ? 381 ILE   A CA  1 
ATOM   2696 C C   . ILE   A 1 363 ? 24.901  -22.205 46.633 1.00 95.84  ? 381 ILE   A C   1 
ATOM   2697 O O   . ILE   A 1 363 ? 24.849  -22.315 45.401 1.00 93.52  ? 381 ILE   A O   1 
ATOM   2698 C CB  . ILE   A 1 363 ? 22.791  -22.630 47.973 1.00 95.59  ? 381 ILE   A CB  1 
ATOM   2699 C CG1 . ILE   A 1 363 ? 22.088  -23.631 48.897 1.00 97.09  ? 381 ILE   A CG1 1 
ATOM   2700 C CG2 . ILE   A 1 363 ? 21.923  -22.337 46.752 1.00 91.90  ? 381 ILE   A CG2 1 
ATOM   2701 C CD1 . ILE   A 1 363 ? 20.729  -23.173 49.395 1.00 96.51  ? 381 ILE   A CD1 1 
ATOM   2702 N N   . GLU   A 1 364 ? 25.600  -21.235 47.226 1.00 97.95  ? 382 GLU   A N   1 
ATOM   2703 C CA  . GLU   A 1 364 ? 26.383  -20.299 46.429 1.00 97.55  ? 382 GLU   A CA  1 
ATOM   2704 C C   . GLU   A 1 364 ? 27.441  -21.033 45.618 1.00 98.20  ? 382 GLU   A C   1 
ATOM   2705 O O   . GLU   A 1 364 ? 27.616  -20.770 44.423 1.00 96.38  ? 382 GLU   A O   1 
ATOM   2706 C CB  . GLU   A 1 364 ? 27.031  -19.248 47.331 1.00 100.60 ? 382 GLU   A CB  1 
ATOM   2707 C CG  . GLU   A 1 364 ? 26.088  -18.140 47.774 1.00 99.82  ? 382 GLU   A CG  1 
ATOM   2708 C CD  . GLU   A 1 364 ? 26.796  -17.047 48.549 1.00 103.21 ? 382 GLU   A CD  1 
ATOM   2709 O OE1 . GLU   A 1 364 ? 28.022  -16.884 48.369 1.00 105.33 ? 382 GLU   A OE1 1 
ATOM   2710 O OE2 . GLU   A 1 364 ? 26.127  -16.353 49.343 1.00 104.14 ? 382 GLU   A OE2 1 
ATOM   2711 N N   . TYR   A 1 365 ? 28.156  -21.967 46.250 1.00 101.12 ? 383 TYR   A N   1 
ATOM   2712 C CA  . TYR   A 1 365 ? 29.162  -22.723 45.513 1.00 102.22 ? 383 TYR   A CA  1 
ATOM   2713 C C   . TYR   A 1 365 ? 28.530  -23.528 44.387 1.00 99.32  ? 383 TYR   A C   1 
ATOM   2714 O O   . TYR   A 1 365 ? 29.058  -23.568 43.269 1.00 98.86  ? 383 TYR   A O   1 
ATOM   2715 C CB  . TYR   A 1 365 ? 29.927  -23.657 46.448 1.00 106.09 ? 383 TYR   A CB  1 
ATOM   2716 C CG  . TYR   A 1 365 ? 30.675  -24.735 45.697 1.00 118.08 ? 383 TYR   A CG  1 
ATOM   2717 C CD1 . TYR   A 1 365 ? 31.872  -24.455 45.051 1.00 127.62 ? 383 TYR   A CD1 1 
ATOM   2718 C CD2 . TYR   A 1 365 ? 30.176  -26.029 45.617 1.00 121.93 ? 383 TYR   A CD2 1 
ATOM   2719 C CE1 . TYR   A 1 365 ? 32.557  -25.435 44.354 1.00 145.27 ? 383 TYR   A CE1 1 
ATOM   2720 C CE2 . TYR   A 1 365 ? 30.851  -27.015 44.923 1.00 124.67 ? 383 TYR   A CE2 1 
ATOM   2721 C CZ  . TYR   A 1 365 ? 32.041  -26.714 44.295 1.00 149.00 ? 383 TYR   A CZ  1 
ATOM   2722 O OH  . TYR   A 1 365 ? 32.717  -27.694 43.604 1.00 138.06 ? 383 TYR   A OH  1 
ATOM   2723 N N   . VAL   A 1 366 ? 27.403  -24.184 44.664 1.00 97.80  ? 384 VAL   A N   1 
ATOM   2724 C CA  . VAL   A 1 366 ? 26.771  -25.019 43.647 1.00 95.64  ? 384 VAL   A CA  1 
ATOM   2725 C C   . VAL   A 1 366 ? 26.352  -24.172 42.452 1.00 92.78  ? 384 VAL   A C   1 
ATOM   2726 O O   . VAL   A 1 366 ? 26.583  -24.542 41.294 1.00 92.21  ? 384 VAL   A O   1 
ATOM   2727 C CB  . VAL   A 1 366 ? 25.577  -25.783 44.249 1.00 94.92  ? 384 VAL   A CB  1 
ATOM   2728 C CG1 . VAL   A 1 366 ? 24.779  -26.472 43.153 1.00 92.76  ? 384 VAL   A CG1 1 
ATOM   2729 C CG2 . VAL   A 1 366 ? 26.058  -26.799 45.280 1.00 98.06  ? 384 VAL   A CG2 1 
ATOM   2730 N N   . LEU   A 1 367 ? 25.734  -23.019 42.713 1.00 91.30  ? 385 LEU   A N   1 
ATOM   2731 C CA  . LEU   A 1 367 ? 25.266  -22.177 41.616 1.00 88.74  ? 385 LEU   A CA  1 
ATOM   2732 C C   . LEU   A 1 367 ? 26.432  -21.564 40.849 1.00 89.62  ? 385 LEU   A C   1 
ATOM   2733 O O   . LEU   A 1 367 ? 26.368  -21.424 39.621 1.00 88.30  ? 385 LEU   A O   1 
ATOM   2734 C CB  . LEU   A 1 367 ? 24.336  -21.091 42.152 1.00 94.68  ? 385 LEU   A CB  1 
ATOM   2735 C CG  . LEU   A 1 367 ? 23.064  -21.611 42.828 1.00 86.65  ? 385 LEU   A CG  1 
ATOM   2736 C CD1 . LEU   A 1 367 ? 22.207  -20.456 43.316 1.00 93.02  ? 385 LEU   A CD1 1 
ATOM   2737 C CD2 . LEU   A 1 367 ? 22.269  -22.509 41.891 1.00 84.95  ? 385 LEU   A CD2 1 
ATOM   2738 N N   . LYS   A 1 368 ? 27.507  -21.188 41.548 1.00 92.25  ? 386 LYS   A N   1 
ATOM   2739 C CA  . LYS   A 1 368 ? 28.686  -20.684 40.853 1.00 95.52  ? 386 LYS   A CA  1 
ATOM   2740 C C   . LYS   A 1 368 ? 29.281  -21.757 39.950 1.00 96.33  ? 386 LYS   A C   1 
ATOM   2741 O O   . LYS   A 1 368 ? 29.692  -21.472 38.821 1.00 107.20 ? 386 LYS   A O   1 
ATOM   2742 C CB  . LYS   A 1 368 ? 29.723  -20.191 41.862 1.00 97.13  ? 386 LYS   A CB  1 
ATOM   2743 C CG  . LYS   A 1 368 ? 29.348  -18.883 42.551 1.00 98.55  ? 386 LYS   A CG  1 
ATOM   2744 C CD  . LYS   A 1 368 ? 30.376  -18.496 43.604 1.00 100.81 ? 386 LYS   A CD  1 
ATOM   2745 C CE  . LYS   A 1 368 ? 29.990  -17.211 44.320 1.00 101.09 ? 386 LYS   A CE  1 
ATOM   2746 N NZ  . LYS   A 1 368 ? 30.974  -16.840 45.377 1.00 120.19 ? 386 LYS   A NZ  1 
ATOM   2747 N N   . TYR   A 1 369 ? 29.328  -23.000 40.430 1.00 95.88  ? 387 TYR   A N   1 
ATOM   2748 C CA  . TYR   A 1 369 ? 29.793  -24.099 39.590 1.00 106.93 ? 387 TYR   A CA  1 
ATOM   2749 C C   . TYR   A 1 369 ? 28.901  -24.264 38.365 1.00 99.74  ? 387 TYR   A C   1 
ATOM   2750 O O   . TYR   A 1 369 ? 29.393  -24.408 37.237 1.00 110.59 ? 387 TYR   A O   1 
ATOM   2751 C CB  . TYR   A 1 369 ? 29.830  -25.386 40.416 1.00 103.52 ? 387 TYR   A CB  1 
ATOM   2752 C CG  . TYR   A 1 369 ? 30.324  -26.604 39.672 1.00 116.09 ? 387 TYR   A CG  1 
ATOM   2753 C CD1 . TYR   A 1 369 ? 31.680  -26.814 39.467 1.00 129.94 ? 387 TYR   A CD1 1 
ATOM   2754 C CD2 . TYR   A 1 369 ? 29.433  -27.555 39.192 1.00 114.41 ? 387 TYR   A CD2 1 
ATOM   2755 C CE1 . TYR   A 1 369 ? 32.137  -27.931 38.793 1.00 144.63 ? 387 TYR   A CE1 1 
ATOM   2756 C CE2 . TYR   A 1 369 ? 29.879  -28.675 38.517 1.00 127.99 ? 387 TYR   A CE2 1 
ATOM   2757 C CZ  . TYR   A 1 369 ? 31.232  -28.859 38.322 1.00 141.62 ? 387 TYR   A CZ  1 
ATOM   2758 O OH  . TYR   A 1 369 ? 31.679  -29.974 37.651 1.00 153.12 ? 387 TYR   A OH  1 
ATOM   2759 N N   . VAL   A 1 370 ? 27.583  -24.218 38.566 1.00 96.29  ? 388 VAL   A N   1 
ATOM   2760 C CA  . VAL   A 1 370 ? 26.655  -24.368 37.449 1.00 92.36  ? 388 VAL   A CA  1 
ATOM   2761 C C   . VAL   A 1 370 ? 26.896  -23.281 36.411 1.00 110.11 ? 388 VAL   A C   1 
ATOM   2762 O O   . VAL   A 1 370 ? 26.924  -23.548 35.204 1.00 110.49 ? 388 VAL   A O   1 
ATOM   2763 C CB  . VAL   A 1 370 ? 25.201  -24.345 37.955 1.00 87.37  ? 388 VAL   A CB  1 
ATOM   2764 C CG1 . VAL   A 1 370 ? 24.232  -24.336 36.780 1.00 102.39 ? 388 VAL   A CG1 1 
ATOM   2765 C CG2 . VAL   A 1 370 ? 24.931  -25.536 38.862 1.00 103.56 ? 388 VAL   A CG2 1 
ATOM   2766 N N   . MET   A 1 371 ? 27.064  -22.038 36.863 1.00 101.86 ? 389 MET   A N   1 
ATOM   2767 C CA  . MET   A 1 371 ? 27.327  -20.948 35.929 1.00 107.39 ? 389 MET   A CA  1 
ATOM   2768 C C   . MET   A 1 371 ? 28.666  -21.135 35.227 1.00 114.80 ? 389 MET   A C   1 
ATOM   2769 O O   . MET   A 1 371 ? 28.797  -20.829 34.036 1.00 119.58 ? 389 MET   A O   1 
ATOM   2770 C CB  . MET   A 1 371 ? 27.282  -19.608 36.663 1.00 107.31 ? 389 MET   A CB  1 
ATOM   2771 C CG  . MET   A 1 371 ? 25.878  -19.161 37.049 1.00 103.49 ? 389 MET   A CG  1 
ATOM   2772 S SD  . MET   A 1 371 ? 24.751  -19.035 35.643 1.00 93.64  ? 389 MET   A SD  1 
ATOM   2773 C CE  . MET   A 1 371 ? 25.641  -17.892 34.588 1.00 104.99 ? 389 MET   A CE  1 
ATOM   2774 N N   . ASP   A 1 372 ? 29.674  -21.633 35.946 1.00 135.78 ? 390 ASP   A N   1 
ATOM   2775 C CA  . ASP   A 1 372 ? 30.962  -21.909 35.324 1.00 136.72 ? 390 ASP   A CA  1 
ATOM   2776 C C   . ASP   A 1 372 ? 30.867  -23.006 34.274 1.00 137.90 ? 390 ASP   A C   1 
ATOM   2777 O O   . ASP   A 1 372 ? 31.717  -23.064 33.378 1.00 145.15 ? 390 ASP   A O   1 
ATOM   2778 C CB  . ASP   A 1 372 ? 31.990  -22.300 36.387 1.00 139.93 ? 390 ASP   A CB  1 
ATOM   2779 C CG  . ASP   A 1 372 ? 32.456  -21.117 37.212 1.00 143.39 ? 390 ASP   A CG  1 
ATOM   2780 O OD1 . ASP   A 1 372 ? 32.034  -19.978 36.915 1.00 149.07 ? 390 ASP   A OD1 1 
ATOM   2781 O OD2 . ASP   A 1 372 ? 33.246  -21.325 38.157 1.00 146.28 ? 390 ASP   A OD2 1 
ATOM   2782 N N   . ILE   A 1 373 ? 29.861  -23.880 34.363 1.00 131.75 ? 391 ILE   A N   1 
ATOM   2783 C CA  . ILE   A 1 373 ? 29.683  -24.893 33.324 1.00 129.09 ? 391 ILE   A CA  1 
ATOM   2784 C C   . ILE   A 1 373 ? 29.416  -24.232 31.976 1.00 125.84 ? 391 ILE   A C   1 
ATOM   2785 O O   . ILE   A 1 373 ? 29.984  -24.628 30.951 1.00 114.36 ? 391 ILE   A O   1 
ATOM   2786 C CB  . ILE   A 1 373 ? 28.555  -25.870 33.707 1.00 120.54 ? 391 ILE   A CB  1 
ATOM   2787 C CG1 . ILE   A 1 373 ? 28.960  -26.683 34.940 1.00 121.90 ? 391 ILE   A CG1 1 
ATOM   2788 C CG2 . ILE   A 1 373 ? 28.237  -26.800 32.539 1.00 125.76 ? 391 ILE   A CG2 1 
ATOM   2789 C CD1 . ILE   A 1 373 ? 27.870  -27.591 35.474 1.00 114.65 ? 391 ILE   A CD1 1 
ATOM   2790 N N   . LEU   A 1 374 ? 28.553  -23.220 31.954 1.00 133.81 ? 392 LEU   A N   1 
ATOM   2791 C CA  . LEU   A 1 374 ? 28.138  -22.581 30.706 1.00 128.68 ? 392 LEU   A CA  1 
ATOM   2792 C C   . LEU   A 1 374 ? 27.554  -23.615 29.748 1.00 125.21 ? 392 LEU   A C   1 
ATOM   2793 O O   . LEU   A 1 374 ? 26.585  -23.342 29.038 1.00 107.48 ? 392 LEU   A O   1 
ATOM   2794 C CB  . LEU   A 1 374 ? 29.307  -21.850 30.036 1.00 138.98 ? 392 LEU   A CB  1 
ATOM   2795 C CG  . LEU   A 1 374 ? 29.728  -20.510 30.645 1.00 148.38 ? 392 LEU   A CG  1 
ATOM   2796 C CD1 . LEU   A 1 374 ? 30.867  -20.692 31.633 1.00 141.98 ? 392 LEU   A CD1 1 
ATOM   2797 C CD2 . LEU   A 1 374 ? 30.116  -19.520 29.556 1.00 130.29 ? 392 LEU   A CD2 1 
HETATM 2798 C C15 . A1B0W B 2 .   ? 14.798  -26.147 27.154 1.00 89.54  ? 401 A1B0W A C15 1 
HETATM 2799 C C20 . A1B0W B 2 .   ? 9.160   -27.248 27.548 1.00 122.19 ? 401 A1B0W A C20 1 
HETATM 2800 C C21 . A1B0W B 2 .   ? 9.456   -27.938 26.207 1.00 129.98 ? 401 A1B0W A C21 1 
HETATM 2801 C C22 . A1B0W B 2 .   ? 10.926  -28.292 25.981 1.00 113.98 ? 401 A1B0W A C22 1 
HETATM 2802 C C26 . A1B0W B 2 .   ? 19.818  -26.103 32.156 1.00 72.26  ? 401 A1B0W A C26 1 
HETATM 2803 C C02 . A1B0W B 2 .   ? 21.136  -27.030 35.720 1.00 80.96  ? 401 A1B0W A C02 1 
HETATM 2804 C C03 . A1B0W B 2 .   ? 22.390  -26.626 33.483 1.00 81.40  ? 401 A1B0W A C03 1 
HETATM 2805 C C04 . A1B0W B 2 .   ? 22.376  -26.303 32.074 1.00 79.21  ? 401 A1B0W A C04 1 
HETATM 2806 C C05 . A1B0W B 2 .   ? 23.628  -26.253 31.381 1.00 70.15  ? 401 A1B0W A C05 1 
HETATM 2807 C C06 . A1B0W B 2 .   ? 24.852  -26.494 31.976 1.00 96.82  ? 401 A1B0W A C06 1 
HETATM 2808 C C07 . A1B0W B 2 .   ? 24.865  -26.808 33.339 1.00 114.34 ? 401 A1B0W A C07 1 
HETATM 2809 C C08 . A1B0W B 2 .   ? 23.688  -26.872 34.064 1.00 92.23  ? 401 A1B0W A C08 1 
HETATM 2810 C C09 . A1B0W B 2 .   ? 21.014  -26.059 31.520 1.00 86.54  ? 401 A1B0W A C09 1 
HETATM 2811 C C11 . A1B0W B 2 .   ? 18.972  -25.528 29.970 1.00 77.78  ? 401 A1B0W A C11 1 
HETATM 2812 C C12 . A1B0W B 2 .   ? 18.154  -25.163 28.688 1.00 82.14  ? 401 A1B0W A C12 1 
HETATM 2813 C C14 . A1B0W B 2 .   ? 15.799  -25.024 27.520 1.00 92.59  ? 401 A1B0W A C14 1 
HETATM 2814 C C16 . A1B0W B 2 .   ? 13.458  -25.544 26.790 1.00 110.22 ? 401 A1B0W A C16 1 
HETATM 2815 C C18 . A1B0W B 2 .   ? 11.336  -25.941 27.911 1.00 106.37 ? 401 A1B0W A C18 1 
HETATM 2816 C C19 . A1B0W B 2 .   ? 10.370  -26.984 28.435 1.00 113.95 ? 401 A1B0W A C19 1 
HETATM 2817 C C23 . A1B0W B 2 .   ? 11.880  -27.112 25.763 1.00 114.63 ? 401 A1B0W A C23 1 
HETATM 2818 C C25 . A1B0W B 2 .   ? 18.672  -25.799 31.259 1.00 73.07  ? 401 A1B0W A C25 1 
HETATM 2819 C C27 . A1B0W B 2 .   ? 19.817  -26.442 33.637 1.00 80.87  ? 401 A1B0W A C27 1 
HETATM 2820 N N01 . A1B0W B 2 .   ? 21.162  -26.691 34.228 1.00 80.01  ? 401 A1B0W A N01 1 
HETATM 2821 N N13 . A1B0W B 2 .   ? 16.722  -25.306 28.614 1.00 95.83  ? 401 A1B0W A N13 1 
HETATM 2822 N N17 . A1B0W B 2 .   ? 12.387  -26.617 27.071 1.00 112.14 ? 401 A1B0W A N17 1 
HETATM 2823 O O24 . A1B0W B 2 .   ? 18.712  -24.746 27.727 1.00 93.58  ? 401 A1B0W A O24 1 
HETATM 2824 O O28 . A1B0W B 2 .   ? 18.852  -26.518 34.341 1.00 90.56  ? 401 A1B0W A O28 1 
HETATM 2825 S S10 . A1B0W B 2 .   ? 20.724  -25.646 29.837 1.00 109.22 ? 401 A1B0W A S10 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   . ASP A 17  ? 1.2129 1.2309 1.7963 0.1634  -0.1000 -0.0343 35  ASP A N   
2    C CA  . ASP A 17  ? 1.7800 1.7729 2.2973 0.1430  -0.0761 -0.0301 35  ASP A CA  
3    C C   . ASP A 17  ? 1.7199 1.6787 2.2319 0.1556  -0.0668 -0.0407 35  ASP A C   
4    O O   . ASP A 17  ? 1.6546 1.6328 2.1851 0.1532  -0.0385 -0.0661 35  ASP A O   
5    C CB  . ASP A 17  ? 1.4007 1.4353 1.9157 0.1187  -0.0430 -0.0456 35  ASP A CB  
6    C CG  . ASP A 17  ? 1.2366 1.2443 1.6808 0.0984  -0.0260 -0.0392 35  ASP A CG  
7    O OD1 . ASP A 17  ? 1.3973 1.3837 1.7932 0.0863  -0.0382 -0.0171 35  ASP A OD1 
8    O OD2 . ASP A 17  ? 1.2561 1.2642 1.6948 0.0951  -0.0017 -0.0582 35  ASP A OD2 
9    N N   . TYR A 18  ? 1.6923 1.5974 2.1751 0.1666  -0.0893 -0.0220 36  TYR A N   
10   C CA  . TYR A 18  ? 1.4044 1.2687 1.8816 0.1781  -0.0837 -0.0299 36  TYR A CA  
11   C C   . TYR A 18  ? 1.4888 1.3253 1.9013 0.1566  -0.0665 -0.0251 36  TYR A C   
12   O O   . TYR A 18  ? 1.4005 1.1867 1.7766 0.1564  -0.0747 -0.0123 36  TYR A O   
13   C CB  . TYR A 18  ? 1.5046 1.3204 1.9846 0.2002  -0.1175 -0.0123 36  TYR A CB  
14   C CG  . TYR A 18  ? 1.8062 1.5820 2.3006 0.2179  -0.1148 -0.0241 36  TYR A CG  
15   C CD1 . TYR A 18  ? 1.8354 1.6365 2.4015 0.2400  -0.1090 -0.0518 36  TYR A CD1 
16   C CD2 . TYR A 18  ? 1.8781 1.5902 2.3173 0.2115  -0.1167 -0.0097 36  TYR A CD2 
17   C CE1 . TYR A 18  ? 1.5682 1.3287 2.1489 0.2571  -0.1070 -0.0641 36  TYR A CE1 
18   C CE2 . TYR A 18  ? 1.7654 1.4357 2.2163 0.2259  -0.1140 -0.0204 36  TYR A CE2 
19   C CZ  . TYR A 18  ? 1.7194 1.4122 2.2403 0.2496  -0.1102 -0.0472 36  TYR A CZ  
20   O OH  . TYR A 18  ? 1.9224 1.5698 2.4563 0.2647  -0.1078 -0.0594 36  TYR A OH  
21   N N   . PHE A 19  ? 1.4159 1.2858 1.8151 0.1372  -0.0426 -0.0367 37  PHE A N   
22   C CA  . PHE A 19  ? 1.2887 1.1420 1.6313 0.1166  -0.0308 -0.0332 37  PHE A CA  
23   C C   . PHE A 19  ? 1.2460 1.0909 1.5849 0.1148  -0.0090 -0.0569 37  PHE A C   
24   O O   . PHE A 19  ? 1.2695 1.0788 1.5773 0.1101  -0.0094 -0.0545 37  PHE A O   
25   C CB  . PHE A 19  ? 1.1791 1.0653 1.5010 0.0965  -0.0235 -0.0287 37  PHE A CB  
26   C CG  . PHE A 19  ? 1.1254 1.0013 1.3968 0.0776  -0.0129 -0.0296 37  PHE A CG  
27   C CD1 . PHE A 19  ? 1.0484 0.8894 1.2857 0.0737  -0.0226 -0.0185 37  PHE A CD1 
28   C CD2 . PHE A 19  ? 1.2390 1.1400 1.4966 0.0626  0.0060  -0.0423 37  PHE A CD2 
29   C CE1 . PHE A 19  ? 1.0627 0.8989 1.2626 0.0586  -0.0169 -0.0219 37  PHE A CE1 
30   C CE2 . PHE A 19  ? 1.1138 1.0026 1.3233 0.0472  0.0093  -0.0422 37  PHE A CE2 
31   C CZ  . PHE A 19  ? 1.0599 0.9188 1.2453 0.0468  -0.0039 -0.0328 37  PHE A CZ  
32   N N   . ARG A 20  ? 1.5020 1.3802 1.8732 0.1167  0.0117  -0.0823 38  ARG A N   
33   C CA  . ARG A 20  ? 1.5104 1.3818 1.8734 0.1126  0.0341  -0.1079 38  ARG A CA  
34   C C   . ARG A 20  ? 1.5052 1.3345 1.8842 0.1301  0.0277  -0.1136 38  ARG A C   
35   O O   . ARG A 20  ? 1.5709 1.3738 1.9218 0.1223  0.0358  -0.1229 38  ARG A O   
36   C CB  . ARG A 20  ? 1.6333 1.5484 2.0301 0.1107  0.0604  -0.1366 38  ARG A CB  
37   C CG  . ARG A 20  ? 1.7629 1.7064 2.1210 0.0844  0.0762  -0.1366 38  ARG A CG  
38   C CD  . ARG A 20  ? 1.9077 1.8314 2.2047 0.0661  0.0862  -0.1433 38  ARG A CD  
39   N NE  . ARG A 20  ? 1.9381 1.8587 2.2458 0.0690  0.1082  -0.1760 38  ARG A NE  
40   C CZ  . ARG A 20  ? 1.8166 1.7046 2.1301 0.0804  0.1036  -0.1845 38  ARG A CZ  
41   N NH1 . ARG A 20  ? 1.7717 1.6259 2.0794 0.0885  0.0795  -0.1624 38  ARG A NH1 
42   N NH2 . ARG A 20  ? 1.7898 1.6768 2.1132 0.0813  0.1259  -0.2174 38  ARG A NH2 
43   N N   . SER A 21  ? 1.2558 1.0756 1.6796 0.1536  0.0111  -0.1085 39  SER A N   
44   C CA  . SER A 21  ? 1.1828 0.9546 1.6207 0.1713  0.0034  -0.1126 39  SER A CA  
45   C C   . SER A 21  ? 1.4387 1.1583 1.8217 0.1593  -0.0060 -0.0925 39  SER A C   
46   O O   . SER A 21  ? 1.3973 1.0753 1.7753 0.1624  -0.0018 -0.1014 39  SER A O   
47   C CB  . SER A 21  ? 1.5869 1.3520 2.0753 0.1993  -0.0215 -0.1040 39  SER A CB  
48   O OG  . SER A 21  ? 1.8883 1.6535 2.3568 0.1960  -0.0459 -0.0732 39  SER A OG  
49   N N   . MET A 22  ? 1.3648 1.0858 1.7091 0.1444  -0.0168 -0.0678 40  MET A N   
50   C CA  . MET A 22  ? 1.3266 1.0046 1.6238 0.1304  -0.0221 -0.0521 40  MET A CA  
51   C C   . MET A 22  ? 1.1163 0.7970 1.3883 0.1115  -0.0027 -0.0702 40  MET A C   
52   O O   . MET A 22  ? 0.9956 0.6395 1.2424 0.1012  -0.0021 -0.0672 40  MET A O   
53   C CB  . MET A 22  ? 1.2917 0.9755 1.5601 0.1202  -0.0369 -0.0255 40  MET A CB  
54   C CG  . MET A 22  ? 1.5758 1.2526 1.8608 0.1364  -0.0609 -0.0059 40  MET A CG  
55   S SD  . MET A 22  ? 1.4911 1.0934 1.7663 0.1506  -0.0790 0.0086  40  MET A SD  
56   C CE  . MET A 22  ? 1.4586 1.0204 1.6682 0.1224  -0.0719 0.0231  40  MET A CE  
57   N N   . TYR A 23  ? 1.0680 0.7900 1.3447 0.1051  0.0127  -0.0896 41  TYR A N   
58   C CA  . TYR A 23  ? 0.9886 0.7155 1.2354 0.0866  0.0252  -0.1053 41  TYR A CA  
59   C C   . TYR A 23  ? 1.0638 0.7500 1.3074 0.0848  0.0307  -0.1188 41  TYR A C   
60   O O   . TYR A 23  ? 1.0278 0.6962 1.2457 0.0701  0.0279  -0.1150 41  TYR A O   
61   C CB  . TYR A 23  ? 0.9335 0.6990 1.1848 0.0826  0.0428  -0.1280 41  TYR A CB  
62   C CG  . TYR A 23  ? 1.1013 0.8654 1.3213 0.0663  0.0538  -0.1490 41  TYR A CG  
63   C CD1 . TYR A 23  ? 1.0061 0.7794 1.1863 0.0490  0.0458  -0.1412 41  TYR A CD1 
64   C CD2 . TYR A 23  ? 1.3407 1.0934 1.5724 0.0690  0.0696  -0.1781 41  TYR A CD2 
65   C CE1 . TYR A 23  ? 1.1266 0.8987 1.2782 0.0352  0.0501  -0.1606 41  TYR A CE1 
66   C CE2 . TYR A 23  ? 1.3966 1.1478 1.5969 0.0530  0.0771  -0.1987 41  TYR A CE2 
67   C CZ  . TYR A 23  ? 1.1167 0.8782 1.2764 0.0362  0.0657  -0.1893 41  TYR A CZ  
68   O OH  . TYR A 23  ? 1.1820 0.9420 1.3104 0.0213  0.0676  -0.2100 41  TYR A OH  
69   N N   . ASP A 24  ? 1.0755 0.7464 1.3494 0.0994  0.0393  -0.1368 42  ASP A N   
70   C CA  . ASP A 24  ? 0.9720 0.6005 1.2438 0.0966  0.0461  -0.1521 42  ASP A CA  
71   C C   . ASP A 24  ? 1.0389 0.6226 1.2890 0.0890  0.0343  -0.1292 42  ASP A C   
72   O O   . ASP A 24  ? 0.9904 0.5581 1.2195 0.0707  0.0398  -0.1366 42  ASP A O   
73   C CB  . ASP A 24  ? 1.3273 0.9372 1.6408 0.1188  0.0521  -0.1693 42  ASP A CB  
74   C CG  . ASP A 24  ? 1.3532 1.0119 1.6956 0.1270  0.0667  -0.1921 42  ASP A CG  
75   O OD1 . ASP A 24  ? 1.3868 1.0781 1.7474 0.1355  0.0598  -0.1793 42  ASP A OD1 
76   O OD2 . ASP A 24  ? 1.6983 1.3629 2.0448 0.1230  0.0865  -0.2244 42  ASP A OD2 
77   N N   . ARG A 25  ? 1.2407 0.8061 1.4940 0.1007  0.0181  -0.1021 43  ARG A N   
78   C CA  . ARG A 25  ? 1.2361 0.7513 1.4621 0.0919  0.0093  -0.0800 43  ARG A CA  
79   C C   . ARG A 25  ? 1.1496 0.6773 1.3451 0.0659  0.0148  -0.0785 43  ARG A C   
80   O O   . ARG A 25  ? 1.1318 0.6210 1.3083 0.0503  0.0199  -0.0765 43  ARG A O   
81   C CB  . ARG A 25  ? 1.3986 0.9019 1.6228 0.1056  -0.0118 -0.0500 43  ARG A CB  
82   C CG  . ARG A 25  ? 1.7966 1.2903 2.0601 0.1348  -0.0231 -0.0516 43  ARG A CG  
83   C CD  . ARG A 25  ? 1.8329 1.3210 2.0942 0.1475  -0.0490 -0.0228 43  ARG A CD  
84   N NE  . ARG A 25  ? 1.9964 1.4799 2.3044 0.1781  -0.0646 -0.0262 43  ARG A NE  
85   C CZ  . ARG A 25  ? 2.2030 1.6840 2.5213 0.1949  -0.0921 -0.0057 43  ARG A CZ  
86   N NH1 . ARG A 25  ? 2.1957 1.6758 2.4754 0.1827  -0.1055 0.0202  43  ARG A NH1 
87   N NH2 . ARG A 25  ? 2.0068 1.4871 2.3782 0.2250  -0.1075 -0.0137 43  ARG A NH2 
88   N N   . TYR A 26  ? 1.0494 0.6292 1.2418 0.0604  0.0141  -0.0806 44  TYR A N   
89   C CA  . TYR A 26  ? 1.0250 0.6202 1.1968 0.0394  0.0159  -0.0823 44  TYR A CA  
90   C C   . TYR A 26  ? 1.0075 0.6120 1.1816 0.0278  0.0268  -0.1117 44  TYR A C   
91   O O   . TYR A 26  ? 1.0940 0.6820 1.2620 0.0112  0.0318  -0.1199 44  TYR A O   
92   C CB  . TYR A 26  ? 1.0371 0.6765 1.2026 0.0394  0.0066  -0.0709 44  TYR A CB  
93   C CG  . TYR A 26  ? 1.0283 0.6614 1.1922 0.0495  -0.0056 -0.0444 44  TYR A CG  
94   C CD1 . TYR A 26  ? 1.0725 0.6635 1.2205 0.0460  -0.0102 -0.0268 44  TYR A CD1 
95   C CD2 . TYR A 26  ? 0.9409 0.6082 1.1161 0.0601  -0.0123 -0.0378 44  TYR A CD2 
96   C CE1 . TYR A 26  ? 1.0313 0.6139 1.1720 0.0544  -0.0246 -0.0031 44  TYR A CE1 
97   C CE2 . TYR A 26  ? 0.9562 0.6196 1.1324 0.0686  -0.0260 -0.0157 44  TYR A CE2 
98   C CZ  . TYR A 26  ? 0.9593 0.5801 1.1169 0.0666  -0.0339 0.0017  44  TYR A CZ  
99   O OH  . TYR A 26  ? 1.1898 0.8039 1.3424 0.0743  -0.0507 0.0233  44  TYR A OH  
100  N N   . ARG A 27  ? 1.0342 0.6644 1.2168 0.0346  0.0317  -0.1299 45  ARG A N   
101  C CA  . ARG A 27  ? 1.0002 0.6401 1.1777 0.0226  0.0392  -0.1586 45  ARG A CA  
102  C C   . ARG A 27  ? 1.1248 0.7221 1.3100 0.0154  0.0484  -0.1730 45  ARG A C   
103  O O   . ARG A 27  ? 1.1377 0.7321 1.3178 -0.0026 0.0493  -0.1843 45  ARG A O   
104  C CB  . ARG A 27  ? 0.9894 0.6540 1.1694 0.0303  0.0472  -0.1767 45  ARG A CB  
105  C CG  . ARG A 27  ? 1.1116 0.7806 1.2805 0.0182  0.0550  -0.2091 45  ARG A CG  
106  C CD  . ARG A 27  ? 1.1284 0.8018 1.3067 0.0276  0.0713  -0.2313 45  ARG A CD  
107  N NE  . ARG A 27  ? 1.1663 0.8059 1.3780 0.0439  0.0789  -0.2324 45  ARG A NE  
108  C CZ  . ARG A 27  ? 1.1733 0.8156 1.4096 0.0590  0.0919  -0.2482 45  ARG A CZ  
109  N NH1 . ARG A 27  ? 1.2961 0.9747 1.5248 0.0566  0.1041  -0.2656 45  ARG A NH1 
110  N NH2 . ARG A 27  ? 1.1929 0.7989 1.4621 0.0765  0.0931  -0.2473 45  ARG A NH2 
111  N N   . ASP A 28  ? 1.0189 0.5808 1.2195 0.0294  0.0544  -0.1728 46  ASP A N   
112  C CA  . ASP A 28  ? 1.1638 0.6755 1.3689 0.0223  0.0633  -0.1845 46  ASP A CA  
113  C C   . ASP A 28  ? 1.1570 0.6456 1.3471 0.0024  0.0624  -0.1711 46  ASP A C   
114  O O   . ASP A 28  ? 1.2200 0.6956 1.4100 -0.0172 0.0712  -0.1900 46  ASP A O   
115  C CB  . ASP A 28  ? 1.4440 0.9130 1.6664 0.0439  0.0635  -0.1774 46  ASP A CB  
116  C CG  . ASP A 28  ? 1.3060 0.8031 1.5531 0.0637  0.0682  -0.1953 46  ASP A CG  
117  O OD1 . ASP A 28  ? 1.2179 0.7494 1.4617 0.0555  0.0779  -0.2213 46  ASP A OD1 
118  O OD2 . ASP A 28  ? 1.2279 0.7129 1.4977 0.0867  0.0619  -0.1847 46  ASP A OD2 
119  N N   . VAL A 29  ? 1.0989 0.5861 1.2770 0.0049  0.0532  -0.1414 47  VAL A N   
120  C CA  . VAL A 29  ? 1.3442 0.8079 1.5059 -0.0159 0.0568  -0.1300 47  VAL A CA  
121  C C   . VAL A 29  ? 1.2474 0.7477 1.4156 -0.0371 0.0614  -0.1526 47  VAL A C   
122  O O   . VAL A 29  ? 1.2105 0.6891 1.3814 -0.0583 0.0732  -0.1664 47  VAL A O   
123  C CB  . VAL A 29  ? 1.0317 0.4977 1.1763 -0.0105 0.0457  -0.0981 47  VAL A CB  
124  C CG1 . VAL A 29  ? 1.2691 0.7387 1.4004 -0.0347 0.0519  -0.0949 47  VAL A CG1 
125  C CG2 . VAL A 29  ? 1.2853 0.6948 1.4175 0.0030  0.0396  -0.0748 47  VAL A CG2 
126  N N   . PHE A 30  ? 1.1938 0.7489 1.3662 -0.0319 0.0509  -0.1582 48  PHE A N   
127  C CA  . PHE A 30  ? 1.0794 0.6696 1.2605 -0.0483 0.0483  -0.1796 48  PHE A CA  
128  C C   . PHE A 30  ? 1.1571 0.7365 1.3494 -0.0594 0.0569  -0.2114 48  PHE A C   
129  O O   . PHE A 30  ? 1.1193 0.6977 1.3247 -0.0801 0.0627  -0.2287 48  PHE A O   
130  C CB  . PHE A 30  ? 1.0696 0.7100 1.2458 -0.0388 0.0319  -0.1784 48  PHE A CB  
131  C CG  . PHE A 30  ? 1.0084 0.6828 1.1931 -0.0511 0.0220  -0.2011 48  PHE A CG  
132  C CD1 . PHE A 30  ? 0.9559 0.6438 1.1563 -0.0638 0.0190  -0.2032 48  PHE A CD1 
133  C CD2 . PHE A 30  ? 1.0771 0.7701 1.2547 -0.0501 0.0146  -0.2223 48  PHE A CD2 
134  C CE1 . PHE A 30  ? 0.8983 0.6202 1.1152 -0.0723 0.0053  -0.2261 48  PHE A CE1 
135  C CE2 . PHE A 30  ? 1.1388 0.8609 1.3225 -0.0600 -0.0008 -0.2427 48  PHE A CE2 
136  C CZ  . PHE A 30  ? 1.0768 0.8147 1.2842 -0.0696 -0.0073 -0.2447 48  PHE A CZ  
137  N N   . ILE A 31  ? 1.2802 0.8513 1.4707 -0.0471 0.0597  -0.2220 49  ILE A N   
138  C CA  . ILE A 31  ? 1.3579 0.9162 1.5567 -0.0578 0.0682  -0.2546 49  ILE A CA  
139  C C   . ILE A 31  ? 1.3704 0.8756 1.5768 -0.0727 0.0834  -0.2564 49  ILE A C   
140  O O   . ILE A 31  ? 1.2542 0.7543 1.4724 -0.0931 0.0903  -0.2827 49  ILE A O   
141  C CB  . ILE A 31  ? 1.5590 1.1151 1.7543 -0.0412 0.0722  -0.2667 49  ILE A CB  
142  C CG1 . ILE A 31  ? 1.2653 0.8715 1.4451 -0.0330 0.0603  -0.2654 49  ILE A CG1 
143  C CG2 . ILE A 31  ? 1.8281 1.3664 2.0302 -0.0529 0.0822  -0.3028 49  ILE A CG2 
144  C CD1 . ILE A 31  ? 1.6739 1.2847 1.8484 -0.0207 0.0689  -0.2809 49  ILE A CD1 
145  N N   . ASN A 32  ? 1.6199 1.0823 1.8171 -0.0646 0.0877  -0.2283 50  ASN A N   
146  C CA  . ASN A 32  ? 1.6814 1.0832 1.8744 -0.0816 0.1021  -0.2254 50  ASN A CA  
147  C C   . ASN A 32  ? 1.6188 1.0352 1.8175 -0.1112 0.1097  -0.2337 50  ASN A C   
148  O O   . ASN A 32  ? 1.6284 1.0271 1.8292 -0.1321 0.1214  -0.2471 50  ASN A O   
149  C CB  . ASN A 32  ? 1.8315 1.1839 2.0041 -0.0677 0.0996  -0.1894 50  ASN A CB  
150  C CG  . ASN A 32  ? 1.8761 1.2013 2.0551 -0.0403 0.0947  -0.1876 50  ASN A CG  
151  O OD1 . ASN A 32  ? 1.8808 1.1986 2.0734 -0.0385 0.1011  -0.2135 50  ASN A OD1 
152  N ND2 . ASN A 32  ? 1.9262 1.2407 2.0973 -0.0183 0.0819  -0.1585 50  ASN A ND2 
153  N N   . HIS A 33  ? 1.2833 0.7452 1.4826 -0.1110 0.1004  -0.2227 51  HIS A N   
154  C CA  . HIS A 33  ? 1.2317 0.7175 1.4476 -0.1370 0.1076  -0.2366 51  HIS A CA  
155  C C   . HIS A 33  ? 1.1098 0.6258 1.3552 -0.1507 0.1066  -0.2764 51  HIS A C   
156  O O   . HIS A 33  ? 1.0393 0.5579 1.2984 -0.1744 0.1184  -0.2909 51  HIS A O   
157  C CB  . HIS A 33  ? 1.4472 0.9820 1.6650 -0.1296 0.0942  -0.2230 51  HIS A CB  
158  C CG  . HIS A 33  ? 1.2270 0.8042 1.4765 -0.1499 0.0959  -0.2464 51  HIS A CG  
159  N ND1 . HIS A 33  ? 1.2950 0.8530 1.5566 -0.1792 0.1188  -0.2574 51  HIS A ND1 
160  C CD2 . HIS A 33  ? 1.1364 0.7736 1.4107 -0.1451 0.0768  -0.2624 51  HIS A CD2 
161  C CE1 . HIS A 33  ? 0.9556 0.5669 1.2567 -0.1906 0.1148  -0.2821 51  HIS A CE1 
162  N NE2 . HIS A 33  ? 1.1058 0.7640 1.4151 -0.1685 0.0867  -0.2847 51  HIS A NE2 
163  N N   . ILE A 34  ? 1.2529 0.8016 1.4998 -0.1342 0.0897  -0.2890 52  ILE A N   
164  C CA  . ILE A 34  ? 1.1422 0.7162 1.4099 -0.1465 0.0846  -0.3272 52  ILE A CA  
165  C C   . ILE A 34  ? 1.1865 0.7176 1.4503 -0.1564 0.1009  -0.3387 52  ILE A C   
166  O O   . ILE A 34  ? 1.2929 0.8403 1.5729 -0.1742 0.1026  -0.3628 52  ILE A O   
167  C CB  . ILE A 34  ? 1.1633 0.7777 1.4184 -0.1275 0.0621  -0.3334 52  ILE A CB  
168  C CG1 . ILE A 34  ? 1.0325 0.6881 1.2830 -0.1155 0.0438  -0.3121 52  ILE A CG1 
169  C CG2 . ILE A 34  ? 1.0281 0.6682 1.2976 -0.1410 0.0518  -0.3729 52  ILE A CG2 
170  C CD1 . ILE A 34  ? 1.0268 0.7191 1.2588 -0.1020 0.0204  -0.3169 52  ILE A CD1 
171  N N   . ASN A 35  ? 1.3951 0.8752 1.6375 -0.1425 0.1099  -0.3192 53  ASN A N   
172  C CA  . ASN A 35  ? 1.2946 0.7316 1.5298 -0.1488 0.1221  -0.3248 53  ASN A CA  
173  C C   . ASN A 35  ? 1.3275 0.7445 1.5631 -0.1750 0.1364  -0.3189 53  ASN A C   
174  O O   . ASN A 35  ? 1.3874 0.7925 1.6294 -0.1911 0.1448  -0.3367 53  ASN A O   
175  C CB  . ASN A 35  ? 1.4057 0.7919 1.6220 -0.1250 0.1242  -0.3032 53  ASN A CB  
176  C CG  . ASN A 35  ? 1.3763 0.7774 1.5972 -0.1040 0.1186  -0.3216 53  ASN A CG  
177  O OD1 . ASN A 35  ? 1.3988 0.8453 1.6271 -0.1074 0.1115  -0.3470 53  ASN A OD1 
178  N ND2 . ASN A 35  ? 1.6131 0.9759 1.8283 -0.0822 0.1209  -0.3100 53  ASN A ND2 
179  N N   . ASP A 36  ? 1.2604 0.6728 1.4878 -0.1811 0.1409  -0.2951 54  ASP A N   
180  C CA  . ASP A 36  ? 1.2665 0.6609 1.4904 -0.2084 0.1585  -0.2901 54  ASP A CA  
181  C C   . ASP A 36  ? 1.1153 0.5646 1.3774 -0.2315 0.1625  -0.3227 54  ASP A C   
182  O O   . ASP A 36  ? 1.1390 0.5769 1.4050 -0.2568 0.1809  -0.3267 54  ASP A O   
183  C CB  . ASP A 36  ? 1.3539 0.7356 1.5570 -0.2101 0.1630  -0.2599 54  ASP A CB  
184  C CG  . ASP A 36  ? 1.5484 0.8722 1.7134 -0.1883 0.1564  -0.2256 54  ASP A CG  
185  O OD1 . ASP A 36  ? 1.6393 0.9309 1.7982 -0.1722 0.1505  -0.2261 54  ASP A OD1 
186  O OD2 . ASP A 36  ? 1.6867 0.9988 1.8298 -0.1864 0.1560  -0.1995 54  ASP A OD2 
187  N N   . TYR A 37  ? 1.0799 0.5873 1.3696 -0.2235 0.1446  -0.3461 55  TYR A N   
188  C CA  . TYR A 37  ? 1.0469 0.6089 1.3772 -0.2416 0.1417  -0.3783 55  TYR A CA  
189  C C   . TYR A 37  ? 1.1377 0.6780 1.4729 -0.2595 0.1543  -0.3968 55  TYR A C   
190  O O   . TYR A 37  ? 1.2450 0.7340 1.5540 -0.2532 0.1592  -0.3899 55  TYR A O   
191  C CB  . TYR A 37  ? 1.0986 0.7148 1.4470 -0.2268 0.1131  -0.3993 55  TYR A CB  
192  C CG  . TYR A 37  ? 1.1914 0.8444 1.5490 -0.2148 0.0977  -0.3897 55  TYR A CG  
193  C CD1 . TYR A 37  ? 1.0336 0.6716 1.3832 -0.2166 0.1110  -0.3640 55  TYR A CD1 
194  C CD2 . TYR A 37  ? 1.1773 0.8768 1.5475 -0.2024 0.0680  -0.4067 55  TYR A CD2 
195  C CE1 . TYR A 37  ? 0.9464 0.6167 1.3059 -0.2056 0.0969  -0.3567 55  TYR A CE1 
196  C CE2 . TYR A 37  ? 0.8730 0.6023 1.2518 -0.1908 0.0513  -0.3980 55  TYR A CE2 
197  C CZ  . TYR A 37  ? 0.9191 0.6348 1.2955 -0.1921 0.0667  -0.3737 55  TYR A CZ  
198  O OH  . TYR A 37  ? 1.1160 0.8625 1.4992 -0.1788 0.0496  -0.3631 55  TYR A OH  
199  N N   . VAL A 38  ? 1.2995 0.8810 1.6731 -0.2813 0.1590  -0.4223 56  VAL A N   
200  C CA  . VAL A 38  ? 1.3169 0.8832 1.7011 -0.3019 0.1722  -0.4426 56  VAL A CA  
201  C C   . VAL A 38  ? 1.2716 0.8637 1.6667 -0.2937 0.1504  -0.4712 56  VAL A C   
202  O O   . VAL A 38  ? 1.2669 0.9167 1.6997 -0.3007 0.1360  -0.4995 56  VAL A O   
203  C CB  . VAL A 38  ? 1.3937 0.9951 1.8182 -0.3300 0.1895  -0.4598 56  VAL A CB  
204  C CG1 . VAL A 38  ? 1.2296 0.8092 1.6627 -0.3532 0.2058  -0.4793 56  VAL A CG1 
205  C CG2 . VAL A 38  ? 1.4884 1.0677 1.8962 -0.3390 0.2119  -0.4332 56  VAL A CG2 
206  N N   . LEU A 39  ? 1.3047 0.8539 1.6664 -0.2782 0.1471  -0.4650 57  LEU A N   
207  C CA  . LEU A 39  ? 1.4614 1.0280 1.8220 -0.2701 0.1290  -0.4912 57  LEU A CA  
208  C C   . LEU A 39  ? 1.6678 1.1757 2.0063 -0.2710 0.1425  -0.4936 57  LEU A C   
209  O O   . LEU A 39  ? 1.6696 1.1204 1.9901 -0.2726 0.1607  -0.4708 57  LEU A O   
210  C CB  . LEU A 39  ? 1.3922 0.9780 1.7339 -0.2441 0.1075  -0.4851 57  LEU A CB  
211  C CG  . LEU A 39  ? 1.3630 1.0020 1.7234 -0.2393 0.0898  -0.4812 57  LEU A CG  
212  C CD1 . LEU A 39  ? 1.3243 0.9630 1.6570 -0.2141 0.0754  -0.4668 57  LEU A CD1 
213  C CD2 . LEU A 39  ? 1.4357 1.1342 1.8291 -0.2497 0.0677  -0.5135 57  LEU A CD2 
214  N N   . GLU A 40  ? 1.9730 1.4929 2.3107 -0.2697 0.1314  -0.5220 58  GLU A N   
215  C CA  . GLU A 40  ? 2.0257 1.4932 2.3439 -0.2670 0.1421  -0.5284 58  GLU A CA  
216  C C   . GLU A 40  ? 1.9851 1.4248 2.2734 -0.2376 0.1399  -0.5123 58  GLU A C   
217  O O   . GLU A 40  ? 1.9340 1.4057 2.2147 -0.2217 0.1261  -0.5079 58  GLU A O   
218  C CB  . GLU A 40  ? 2.0896 1.5815 2.4172 -0.2785 0.1323  -0.5674 58  GLU A CB  
219  C CG  . GLU A 40  ? 2.2502 1.7688 2.6140 -0.3076 0.1356  -0.5867 58  GLU A CG  
220  C CD  . GLU A 40  ? 2.2520 1.8311 2.6332 -0.3139 0.1103  -0.6207 58  GLU A CD  
221  O OE1 . GLU A 40  ? 2.3346 1.9125 2.6910 -0.3044 0.0974  -0.6379 58  GLU A OE1 
222  O OE2 . GLU A 40  ? 2.1878 1.8152 2.6066 -0.3278 0.1025  -0.6307 58  GLU A OE2 
223  N N   . ASP A 41  ? 1.9015 1.2808 2.1750 -0.2301 0.1533  -0.5048 59  ASP A N   
224  C CA  . ASP A 41  ? 1.9267 1.2780 2.1804 -0.2005 0.1533  -0.4884 59  ASP A CA  
225  C C   . ASP A 41  ? 1.7735 1.1631 2.0190 -0.1864 0.1424  -0.5112 59  ASP A C   
226  O O   . ASP A 41  ? 1.7669 1.1645 2.0022 -0.1646 0.1388  -0.4983 59  ASP A O   
227  C CB  . ASP A 41  ? 2.0235 1.3052 2.2682 -0.1941 0.1657  -0.4830 59  ASP A CB  
228  C CG  . ASP A 41  ? 2.2434 1.4757 2.4831 -0.2062 0.1749  -0.4547 59  ASP A CG  
229  O OD1 . ASP A 41  ? 2.3113 1.5458 2.5614 -0.2348 0.1825  -0.4639 59  ASP A OD1 
230  O OD2 . ASP A 41  ? 2.4862 1.6772 2.7103 -0.1879 0.1742  -0.4238 59  ASP A OD2 
231  N N   . ASP A 42  ? 2.1976 1.6099 2.4443 -0.2001 0.1374  -0.5456 60  ASP A N   
232  C CA  . ASP A 42  ? 1.7319 1.1758 1.9599 -0.1905 0.1273  -0.5686 60  ASP A CA  
233  C C   . ASP A 42  ? 1.8683 1.3625 2.0904 -0.1870 0.1089  -0.5615 60  ASP A C   
234  O O   . ASP A 42  ? 1.6572 1.1616 1.8595 -0.1694 0.1062  -0.5579 60  ASP A O   
235  C CB  . ASP A 42  ? 1.9519 1.4072 2.1773 -0.2089 0.1226  -0.6062 60  ASP A CB  
236  C CG  . ASP A 42  ? 1.7563 1.2074 1.9548 -0.1977 0.1259  -0.6301 60  ASP A CG  
237  O OD1 . ASP A 42  ? 1.8728 1.3354 2.0529 -0.1793 0.1256  -0.6232 60  ASP A OD1 
238  O OD2 . ASP A 42  ? 1.8964 1.3330 2.0920 -0.2084 0.1305  -0.6572 60  ASP A OD2 
239  N N   . ILE A 43  ? 1.8651 1.3916 2.1066 -0.2037 0.0964  -0.5607 61  ILE A N   
240  C CA  . ILE A 43  ? 1.7981 1.3700 2.0381 -0.1995 0.0759  -0.5533 61  ILE A CA  
241  C C   . ILE A 43  ? 1.8614 1.4180 2.0976 -0.1805 0.0837  -0.5195 61  ILE A C   
242  O O   . ILE A 43  ? 1.4331 1.0123 1.6535 -0.1679 0.0718  -0.5143 61  ILE A O   
243  C CB  . ILE A 43  ? 1.8325 1.4420 2.1056 -0.2189 0.0629  -0.5587 61  ILE A CB  
244  C CG1 . ILE A 43  ? 1.2398 0.8749 1.5161 -0.2351 0.0471  -0.5944 61  ILE A CG1 
245  C CG2 . ILE A 43  ? 2.1108 1.7603 2.3890 -0.2111 0.0431  -0.5450 61  ILE A CG2 
246  C CD1 . ILE A 43  ? 2.4512 2.0613 2.7489 -0.2538 0.0651  -0.6072 61  ILE A CD1 
247  N N   . LYS A 44  ? 1.4677 0.9833 1.7150 -0.1792 0.1021  -0.4958 62  LYS A N   
248  C CA  . LYS A 44  ? 1.5181 1.0144 1.7600 -0.1608 0.1077  -0.4626 62  LYS A CA  
249  C C   . LYS A 44  ? 1.5750 1.0632 1.7981 -0.1370 0.1099  -0.4641 62  LYS A C   
250  O O   . LYS A 44  ? 1.6896 1.1951 1.9062 -0.1228 0.1037  -0.4508 62  LYS A O   
251  C CB  . LYS A 44  ? 1.4289 0.8726 1.6751 -0.1640 0.1245  -0.4384 62  LYS A CB  
252  C CG  . LYS A 44  ? 1.6002 1.0520 1.8630 -0.1884 0.1282  -0.4325 62  LYS A CG  
253  C CD  . LYS A 44  ? 1.4607 0.8536 1.7135 -0.1916 0.1442  -0.4038 62  LYS A CD  
254  C CE  . LYS A 44  ? 1.5185 0.9226 1.7845 -0.2176 0.1525  -0.3980 62  LYS A CE  
255  N NZ  . LYS A 44  ? 1.4075 0.7516 1.6515 -0.2218 0.1665  -0.3661 62  LYS A NZ  
256  N N   . ILE A 45  ? 1.5929 1.0569 1.8098 -0.1330 0.1200  -0.4824 63  ILE A N   
257  C CA  . ILE A 45  ? 1.5896 1.0497 1.7943 -0.1112 0.1267  -0.4886 63  ILE A CA  
258  C C   . ILE A 45  ? 1.5599 1.0670 1.7428 -0.1121 0.1148  -0.5056 63  ILE A C   
259  O O   . ILE A 45  ? 1.6165 1.1346 1.7911 -0.0959 0.1166  -0.4967 63  ILE A O   
260  C CB  . ILE A 45  ? 1.6201 1.0501 1.8244 -0.1098 0.1397  -0.5113 63  ILE A CB  
261  C CG1 . ILE A 45  ? 1.7259 1.0996 1.9455 -0.1048 0.1491  -0.4907 63  ILE A CG1 
262  C CG2 . ILE A 45  ? 1.8162 1.2550 2.0099 -0.0909 0.1487  -0.5268 63  ILE A CG2 
263  C CD1 . ILE A 45  ? 1.4903 0.8301 1.7122 -0.1086 0.1592  -0.5139 63  ILE A CD1 
264  N N   . ILE A 46  ? 1.5546 1.0890 1.7257 -0.1316 0.1009  -0.5302 64  ILE A N   
265  C CA  . ILE A 46  ? 1.5213 1.0927 1.6591 -0.1341 0.0857  -0.5474 64  ILE A CA  
266  C C   . ILE A 46  ? 1.5494 1.1456 1.6872 -0.1286 0.0707  -0.5254 64  ILE A C   
267  O O   . ILE A 46  ? 1.4471 1.0638 1.5539 -0.1164 0.0670  -0.5121 64  ILE A O   
268  C CB  . ILE A 46  ? 1.9342 1.5270 2.0583 -0.1554 0.0672  -0.5763 64  ILE A CB  
269  C CG1 . ILE A 46  ? 1.5860 1.1519 1.7108 -0.1617 0.0828  -0.5993 64  ILE A CG1 
270  C CG2 . ILE A 46  ? 1.5565 1.1795 1.6329 -0.1582 0.0479  -0.5919 64  ILE A CG2 
271  C CD1 . ILE A 46  ? 1.7340 1.2825 1.8360 -0.1482 0.1035  -0.6117 64  ILE A CD1 
272  N N   . ILE A 47  ? 1.5985 1.2015 1.7650 -0.1354 0.0610  -0.5080 65  ILE A N   
273  C CA  . ILE A 47  ? 1.3874 1.0223 1.5509 -0.1270 0.0434  -0.4761 65  ILE A CA  
274  C C   . ILE A 47  ? 1.4027 1.0238 1.5632 -0.1050 0.0571  -0.4406 65  ILE A C   
275  O O   . ILE A 47  ? 1.3629 1.0106 1.5034 -0.0936 0.0458  -0.4173 65  ILE A O   
276  C CB  . ILE A 47  ? 1.2561 0.9027 1.4567 -0.1410 0.0340  -0.4722 65  ILE A CB  
277  C CG1 . ILE A 47  ? 1.4658 1.0701 1.6934 -0.1440 0.0591  -0.4576 65  ILE A CG1 
278  C CG2 . ILE A 47  ? 1.4534 1.1242 1.6631 -0.1610 0.0161  -0.5069 65  ILE A CG2 
279  C CD1 . ILE A 47  ? 1.5661 1.1847 1.8242 -0.1601 0.0568  -0.4503 65  ILE A CD1 
280  N N   . SER A 48  ? 1.4398 1.0173 1.6205 -0.0987 0.0792  -0.4357 66  SER A N   
281  C CA  . SER A 48  ? 1.3031 0.8683 1.4848 -0.0761 0.0880  -0.4047 66  SER A CA  
282  C C   . SER A 48  ? 1.4077 0.9927 1.5660 -0.0626 0.0920  -0.4116 66  SER A C   
283  O O   . SER A 48  ? 1.3298 0.9370 1.4784 -0.0495 0.0875  -0.3863 66  SER A O   
284  C CB  . SER A 48  ? 1.3820 0.8902 1.5873 -0.0707 0.1061  -0.4009 66  SER A CB  
285  O OG  . SER A 48  ? 1.7830 1.2689 1.9896 -0.0737 0.1183  -0.4318 66  SER A OG  
286  N N   . LYS A 49  ? 1.5114 1.0891 1.6592 -0.0684 0.1023  -0.4479 67  LYS A N   
287  C CA  . LYS A 49  ? 1.3936 0.9918 1.5140 -0.0611 0.1105  -0.4596 67  LYS A CA  
288  C C   . LYS A 49  ? 1.4511 1.0913 1.5316 -0.0668 0.0905  -0.4452 67  LYS A C   
289  O O   . LYS A 49  ? 1.2970 0.9558 1.3629 -0.0563 0.0942  -0.4274 67  LYS A O   
290  C CB  . LYS A 49  ? 1.3819 0.9664 1.4896 -0.0721 0.1238  -0.5056 67  LYS A CB  
291  C CG  . LYS A 49  ? 1.6187 1.1582 1.7631 -0.0621 0.1470  -0.5233 67  LYS A CG  
292  C CD  . LYS A 49  ? 1.8306 1.3692 1.9540 -0.0712 0.1578  -0.5597 67  LYS A CD  
293  C CE  . LYS A 49  ? 1.9049 1.4092 2.0607 -0.0564 0.1753  -0.5636 67  LYS A CE  
294  N NZ  . LYS A 49  ? 2.0022 1.5069 2.1391 -0.0641 0.1885  -0.6011 67  LYS A NZ  
295  N N   . TYR A 50  ? 1.4130 1.0673 1.4779 -0.0836 0.0676  -0.4533 68  TYR A N   
296  C CA  . TYR A 50  ? 1.2985 0.9853 1.3206 -0.0886 0.0437  -0.4424 68  TYR A CA  
297  C C   . TYR A 50  ? 1.2922 0.9943 1.3227 -0.0760 0.0346  -0.4005 68  TYR A C   
298  O O   . TYR A 50  ? 1.2691 0.9878 1.2653 -0.0722 0.0304  -0.3848 68  TYR A O   
299  C CB  . TYR A 50  ? 1.1944 0.8929 1.2102 -0.1057 0.0158  -0.4605 68  TYR A CB  
300  C CG  . TYR A 50  ? 1.2450 0.9702 1.2156 -0.1090 -0.0157 -0.4491 68  TYR A CG  
301  C CD1 . TYR A 50  ? 1.4288 1.1559 1.3366 -0.1185 -0.0225 -0.4666 68  TYR A CD1 
302  C CD2 . TYR A 50  ? 1.2504 0.9943 1.2371 -0.1032 -0.0387 -0.4209 68  TYR A CD2 
303  C CE1 . TYR A 50  ? 1.5267 1.2686 1.3851 -0.1217 -0.0545 -0.4531 68  TYR A CE1 
304  C CE2 . TYR A 50  ? 1.3399 1.1016 1.2858 -0.1041 -0.0704 -0.4094 68  TYR A CE2 
305  C CZ  . TYR A 50  ? 1.4195 1.1777 1.2993 -0.1132 -0.0798 -0.4239 68  TYR A CZ  
306  O OH  . TYR A 50  ? 1.4077 1.1745 1.2391 -0.1144 -0.1147 -0.4095 68  TYR A OH  
307  N N   . TYR A 51  ? 1.2837 0.9779 1.3561 -0.0719 0.0328  -0.3827 69  TYR A N   
308  C CA  . TYR A 51  ? 1.1746 0.8825 1.2536 -0.0617 0.0234  -0.3455 69  TYR A CA  
309  C C   . TYR A 51  ? 1.1933 0.8947 1.2765 -0.0449 0.0418  -0.3258 69  TYR A C   
310  O O   . TYR A 51  ? 1.2798 0.9994 1.3499 -0.0380 0.0347  -0.3007 69  TYR A O   
311  C CB  . TYR A 51  ? 1.0362 0.7366 1.1538 -0.0656 0.0188  -0.3355 69  TYR A CB  
312  C CG  . TYR A 51  ? 0.9005 0.6228 1.0244 -0.0799 -0.0048 -0.3497 69  TYR A CG  
313  C CD1 . TYR A 51  ? 0.9186 0.6653 1.0092 -0.0836 -0.0293 -0.3593 69  TYR A CD1 
314  C CD2 . TYR A 51  ? 0.9369 0.6544 1.1000 -0.0902 -0.0032 -0.3541 69  TYR A CD2 
315  C CE1 . TYR A 51  ? 1.0684 0.8369 1.1717 -0.0935 -0.0561 -0.3737 69  TYR A CE1 
316  C CE2 . TYR A 51  ? 0.8872 0.6314 1.0679 -0.1024 -0.0246 -0.3713 69  TYR A CE2 
317  C CZ  . TYR A 51  ? 0.8998 0.6708 1.0539 -0.1020 -0.0534 -0.3813 69  TYR A CZ  
318  O OH  . TYR A 51  ? 1.0045 0.8039 1.1823 -0.1110 -0.0801 -0.3999 69  TYR A OH  
319  N N   . LYS A 52  ? 1.2281 0.9040 1.3326 -0.0376 0.0640  -0.3383 70  LYS A N   
320  C CA  . LYS A 52  ? 1.1929 0.8689 1.3077 -0.0202 0.0792  -0.3261 70  LYS A CA  
321  C C   . LYS A 52  ? 1.1952 0.8989 1.2737 -0.0230 0.0841  -0.3338 70  LYS A C   
322  O O   . LYS A 52  ? 1.0240 0.7456 1.1006 -0.0148 0.0862  -0.3131 70  LYS A O   
323  C CB  . LYS A 52  ? 1.2337 0.8758 1.3805 -0.0104 0.0993  -0.3440 70  LYS A CB  
324  C CG  . LYS A 52  ? 1.3571 1.0024 1.5266 0.0104  0.1131  -0.3369 70  LYS A CG  
325  C CD  . LYS A 52  ? 1.2191 0.8272 1.4248 0.0233  0.1288  -0.3563 70  LYS A CD  
326  C CE  . LYS A 52  ? 1.3541 0.9718 1.5927 0.0466  0.1400  -0.3539 70  LYS A CE  
327  N NZ  . LYS A 52  ? 1.1878 0.8469 1.4096 0.0419  0.1560  -0.3741 70  LYS A NZ  
328  N N   . LEU A 53  ? 1.2183 0.9240 1.2639 -0.0373 0.0865  -0.3641 71  LEU A N   
329  C CA  . LEU A 53  ? 1.2432 0.9691 1.2402 -0.0455 0.0920  -0.3715 71  LEU A CA  
330  C C   . LEU A 53  ? 1.2639 1.0089 1.2280 -0.0500 0.0682  -0.3411 71  LEU A C   
331  O O   . LEU A 53  ? 1.2532 1.0126 1.1956 -0.0496 0.0755  -0.3276 71  LEU A O   
332  C CB  . LEU A 53  ? 1.3645 1.0835 1.3224 -0.0628 0.0939  -0.4089 71  LEU A CB  
333  C CG  . LEU A 53  ? 1.3634 1.0958 1.2518 -0.0776 0.0958  -0.4162 71  LEU A CG  
334  C CD1 . LEU A 53  ? 1.4319 1.1746 1.3247 -0.0720 0.1299  -0.4204 71  LEU A CD1 
335  C CD2 . LEU A 53  ? 1.6068 1.3284 1.4521 -0.0960 0.0920  -0.4530 71  LEU A CD2 
336  N N   . LEU A 54  ? 1.2153 0.9604 1.1787 -0.0549 0.0401  -0.3321 72  LEU A N   
337  C CA  . LEU A 54  ? 1.1546 0.9143 1.0925 -0.0567 0.0144  -0.3047 72  LEU A CA  
338  C C   . LEU A 54  ? 1.2299 0.9974 1.1896 -0.0438 0.0214  -0.2728 72  LEU A C   
339  O O   . LEU A 54  ? 1.3152 1.0930 1.2424 -0.0461 0.0194  -0.2565 72  LEU A O   
340  C CB  . LEU A 54  ? 1.1555 0.9170 1.1123 -0.0599 -0.0137 -0.3039 72  LEU A CB  
341  C CG  . LEU A 54  ? 1.1546 0.9295 1.1052 -0.0568 -0.0415 -0.2761 72  LEU A CG  
342  C CD1 . LEU A 54  ? 1.2445 1.0226 1.1306 -0.0650 -0.0623 -0.2737 72  LEU A CD1 
343  C CD2 . LEU A 54  ? 1.0223 0.8028 1.0131 -0.0583 -0.0606 -0.2814 72  LEU A CD2 
344  N N   . PHE A 55  ? 1.1590 0.9183 1.1701 -0.0318 0.0291  -0.2637 73  PHE A N   
345  C CA  . PHE A 55  ? 1.0536 0.8192 1.0860 -0.0196 0.0317  -0.2342 73  PHE A CA  
346  C C   . PHE A 55  ? 1.1884 0.9646 1.2170 -0.0150 0.0536  -0.2361 73  PHE A C   
347  O O   . PHE A 55  ? 1.2277 1.0194 1.2433 -0.0149 0.0515  -0.2162 73  PHE A O   
348  C CB  . PHE A 55  ? 1.0177 0.7648 1.0968 -0.0094 0.0352  -0.2261 73  PHE A CB  
349  C CG  . PHE A 55  ? 1.0843 0.8286 1.1718 -0.0146 0.0167  -0.2148 73  PHE A CG  
350  C CD1 . PHE A 55  ? 1.1363 0.8776 1.2225 -0.0267 0.0079  -0.2354 73  PHE A CD1 
351  C CD2 . PHE A 55  ? 0.9215 0.6682 1.0211 -0.0085 0.0091  -0.1867 73  PHE A CD2 
352  C CE1 . PHE A 55  ? 1.0962 0.8406 1.1992 -0.0323 -0.0061 -0.2296 73  PHE A CE1 
353  C CE2 . PHE A 55  ? 0.9624 0.7087 1.0724 -0.0146 -0.0036 -0.1804 73  PHE A CE2 
354  C CZ  . PHE A 55  ? 1.0451 0.7919 1.1598 -0.0264 -0.0102 -0.2027 73  PHE A CZ  
355  N N   . ASP A 56  ? 1.2022 0.9713 1.2457 -0.0119 0.0761  -0.2626 74  ASP A N   
356  C CA  . ASP A 56  ? 1.1082 0.8924 1.1605 -0.0070 0.1005  -0.2705 74  ASP A CA  
357  C C   . ASP A 56  ? 1.1370 0.9378 1.1322 -0.0248 0.1067  -0.2755 74  ASP A C   
358  O O   . ASP A 56  ? 1.1654 0.9849 1.1640 -0.0251 0.1255  -0.2744 74  ASP A O   
359  C CB  . ASP A 56  ? 1.1579 0.9295 1.2419 0.0008  0.1233  -0.3029 74  ASP A CB  
360  C CG  . ASP A 56  ? 1.2054 0.9512 1.3408 0.0183  0.1178  -0.2957 74  ASP A CG  
361  O OD1 . ASP A 56  ? 1.1171 0.8576 1.2619 0.0232  0.0991  -0.2656 74  ASP A OD1 
362  O OD2 . ASP A 56  ? 1.2086 0.9354 1.3715 0.0262  0.1325  -0.3205 74  ASP A OD2 
363  N N   . TYR A 57  ? 1.2525 1.0451 1.1944 -0.0407 0.0907  -0.2813 75  TYR A N   
364  C CA  . TYR A 57  ? 1.3672 1.1643 1.2402 -0.0602 0.0937  -0.2852 75  TYR A CA  
365  C C   . TYR A 57  ? 1.2688 1.0705 1.1126 -0.0644 0.0723  -0.2502 75  TYR A C   
366  O O   . TYR A 57  ? 1.3934 1.2027 1.2055 -0.0749 0.0859  -0.2426 75  TYR A O   
367  C CB  . TYR A 57  ? 1.1519 0.9335 0.9767 -0.0746 0.0809  -0.3084 75  TYR A CB  
368  C CG  . TYR A 57  ? 1.3129 1.0901 1.0552 -0.0971 0.0868  -0.3181 75  TYR A CG  
369  C CD1 . TYR A 57  ? 1.4645 1.2337 1.1456 -0.1082 0.0585  -0.2940 75  TYR A CD1 
370  C CD2 . TYR A 57  ? 1.5851 1.3618 1.3070 -0.1080 0.1205  -0.3522 75  TYR A CD2 
371  C CE1 . TYR A 57  ? 1.6382 1.3942 1.2320 -0.1311 0.0623  -0.3000 75  TYR A CE1 
372  C CE2 . TYR A 57  ? 1.4925 1.2606 1.1287 -0.1325 0.1286  -0.3614 75  TYR A CE2 
373  C CZ  . TYR A 57  ? 1.4008 1.1561 0.9690 -0.1449 0.0986  -0.3336 75  TYR A CZ  
374  O OH  . TYR A 57  ? 1.4692 1.2072 0.9409 -0.1715 0.1053  -0.3401 75  TYR A OH  
375  N N   . ASN A 58  ? 1.2538 1.0500 1.1097 -0.0576 0.0408  -0.2304 76  ASN A N   
376  C CA  . ASN A 58  ? 1.2414 1.0373 1.0682 -0.0610 0.0168  -0.2003 76  ASN A CA  
377  C C   . ASN A 58  ? 1.2619 1.0688 1.1341 -0.0481 0.0179  -0.1738 76  ASN A C   
378  O O   . ASN A 58  ? 1.4256 1.2320 1.2746 -0.0517 0.0040  -0.1498 76  ASN A O   
379  C CB  . ASN A 58  ? 1.3119 1.0980 1.1255 -0.0614 -0.0205 -0.1977 76  ASN A CB  
380  C CG  . ASN A 58  ? 1.2643 1.0386 1.0212 -0.0760 -0.0306 -0.2203 76  ASN A CG  
381  O OD1 . ASN A 58  ? 1.4136 1.1760 1.1030 -0.0886 -0.0440 -0.2122 76  ASN A OD1 
382  N ND2 . ASN A 58  ? 1.1692 0.9422 0.9484 -0.0758 -0.0250 -0.2487 76  ASN A ND2 
383  N N   . CYS A 59  ? 1.2959 1.1085 1.2280 -0.0336 0.0320  -0.1774 77  CYS A N   
384  C CA  . CYS A 59  ? 1.3060 1.1271 1.2778 -0.0217 0.0309  -0.1536 77  CYS A CA  
385  C C   . CYS A 59  ? 1.4784 1.3161 1.4783 -0.0168 0.0576  -0.1579 77  CYS A C   
386  O O   . CYS A 59  ? 1.0838 0.9299 1.1199 -0.0061 0.0556  -0.1406 77  CYS A O   
387  C CB  . CYS A 59  ? 1.0506 0.8613 1.0668 -0.0088 0.0212  -0.1497 77  CYS A CB  
388  S SG  . CYS A 59  ? 1.1667 0.9674 1.1691 -0.0143 -0.0081 -0.1475 77  CYS A SG  
389  N N   . LEU A 60  ? 1.3536 1.1977 1.3397 -0.0247 0.0821  -0.1830 78  LEU A N   
390  C CA  . LEU A 60  ? 1.4264 1.2922 1.4484 -0.0201 0.1100  -0.1940 78  LEU A CA  
391  C C   . LEU A 60  ? 1.4297 1.3069 1.4024 -0.0425 0.1313  -0.2039 78  LEU A C   
392  O O   . LEU A 60  ? 1.4352 1.2966 1.3425 -0.0600 0.1270  -0.2094 78  LEU A O   
393  C CB  . LEU A 60  ? 1.3846 1.2474 1.4529 -0.0060 0.1270  -0.2225 78  LEU A CB  
394  C CG  . LEU A 60  ? 1.1455 0.9880 1.2565 0.0134  0.1093  -0.2135 78  LEU A CG  
395  C CD1 . LEU A 60  ? 1.4258 1.2578 1.5766 0.0262  0.1262  -0.2425 78  LEU A CD1 
396  C CD2 . LEU A 60  ? 1.2456 1.0958 1.3926 0.0268  0.0961  -0.1851 78  LEU A CD2 
397  N N   . GLY A 61  ? 1.4502 1.3540 1.4538 -0.0432 0.1540  -0.2066 79  GLY A N   
398  C CA  . GLY A 61  ? 1.5559 1.4721 1.5175 -0.0679 0.1808  -0.2161 79  GLY A CA  
399  C C   . GLY A 61  ? 1.5880 1.5058 1.5199 -0.0817 0.1713  -0.1856 79  GLY A C   
400  O O   . GLY A 61  ? 1.8623 1.7938 1.7724 -0.1028 0.1979  -0.1915 79  GLY A O   
401  N N   . GLY A 62  ? 1.8595 1.7624 1.7902 -0.0722 0.1362  -0.1552 80  GLY A N   
402  C CA  . GLY A 62  ? 1.6573 1.5580 1.5650 -0.0830 0.1248  -0.1265 80  GLY A CA  
403  C C   . GLY A 62  ? 1.6240 1.5541 1.6014 -0.0716 0.1301  -0.1189 80  GLY A C   
404  O O   . GLY A 62  ? 1.2082 1.1597 1.2528 -0.0532 0.1394  -0.1342 80  GLY A O   
405  N N   . LYS A 63  ? 1.3211 1.2493 1.2810 -0.0827 0.1211  -0.0947 81  LYS A N   
406  C CA  . LYS A 63  ? 1.2851 1.2410 1.3060 -0.0749 0.1223  -0.0865 81  LYS A CA  
407  C C   . LYS A 63  ? 1.1388 1.0876 1.1971 -0.0505 0.0905  -0.0687 81  LYS A C   
408  O O   . LYS A 63  ? 1.1409 1.1116 1.2549 -0.0393 0.0876  -0.0648 81  LYS A O   
409  C CB  . LYS A 63  ? 1.4018 1.3560 1.3872 -0.0998 0.1276  -0.0697 81  LYS A CB  
410  C CG  . LYS A 63  ? 1.5433 1.4908 1.4669 -0.1307 0.1578  -0.0820 81  LYS A CG  
411  C CD  . LYS A 63  ? 1.7785 1.7624 1.7445 -0.1329 0.1976  -0.1185 81  LYS A CD  
412  C CE  . LYS A 63  ? 1.8755 1.8469 1.7679 -0.1659 0.2299  -0.1337 81  LYS A CE  
413  N NZ  . LYS A 63  ? 1.9400 1.9024 1.7854 -0.1986 0.2429  -0.1175 81  LYS A NZ  
414  N N   . ASN A 64  ? 1.1769 1.0962 1.2059 -0.0435 0.0671  -0.0596 82  ASN A N   
415  C CA  . ASN A 64  ? 1.1298 1.0392 1.1874 -0.0244 0.0416  -0.0452 82  ASN A CA  
416  C C   . ASN A 64  ? 1.0621 0.9764 1.1302 -0.0260 0.0283  -0.0227 82  ASN A C   
417  O O   . ASN A 64  ? 1.0087 0.9307 1.1195 -0.0117 0.0188  -0.0164 82  ASN A O   
418  C CB  . ASN A 64  ? 1.0623 0.9809 1.1764 -0.0038 0.0467  -0.0594 82  ASN A CB  
419  C CG  . ASN A 64  ? 1.3159 1.2307 1.4248 -0.0032 0.0637  -0.0856 82  ASN A CG  
420  O OD1 . ASN A 64  ? 1.1214 1.0137 1.2085 -0.0013 0.0540  -0.0891 82  ASN A OD1 
421  N ND2 . ASN A 64  ? 1.4481 1.3870 1.5805 -0.0058 0.0905  -0.1073 82  ASN A ND2 
422  N N   . ASN A 65  ? 1.0728 0.9777 1.0967 -0.0444 0.0262  -0.0104 83  ASN A N   
423  C CA  . ASN A 65  ? 0.9787 0.8862 1.0100 -0.0490 0.0156  0.0088  83  ASN A CA  
424  C C   . ASN A 65  ? 1.0183 0.9091 1.0582 -0.0348 -0.0117 0.0236  83  ASN A C   
425  O O   . ASN A 65  ? 0.9658 0.8661 1.0374 -0.0285 -0.0194 0.0321  83  ASN A O   
426  C CB  . ASN A 65  ? 1.1111 1.0015 1.0859 -0.0728 0.0182  0.0197  83  ASN A CB  
427  C CG  . ASN A 65  ? 1.1161 1.0245 1.0815 -0.0931 0.0509  0.0057  83  ASN A CG  
428  O OD1 . ASN A 65  ? 0.9604 0.9047 0.9797 -0.0901 0.0704  -0.0090 83  ASN A OD1 
429  N ND2 . ASN A 65  ? 1.1805 1.0631 1.0770 -0.1144 0.0567  0.0091  83  ASN A ND2 
430  N N   . ARG A 66  ? 1.0258 0.8931 1.0385 -0.0307 -0.0261 0.0245  84  ARG A N   
431  C CA  . ARG A 66  ? 0.9811 0.8340 1.0011 -0.0209 -0.0478 0.0352  84  ARG A CA  
432  C C   . ARG A 66  ? 1.0391 0.8999 1.1020 -0.0062 -0.0477 0.0328  84  ARG A C   
433  O O   . ARG A 66  ? 1.0796 0.9383 1.1559 -0.0026 -0.0581 0.0441  84  ARG A O   
434  C CB  . ARG A 66  ? 1.0295 0.8627 1.0234 -0.0191 -0.0614 0.0306  84  ARG A CB  
435  C CG  . ARG A 66  ? 0.9566 0.7711 0.9025 -0.0305 -0.0737 0.0386  84  ARG A CG  
436  C CD  . ARG A 66  ? 1.0428 0.8560 0.9513 -0.0437 -0.0594 0.0306  84  ARG A CD  
437  N NE  . ARG A 66  ? 0.9532 0.7383 0.8053 -0.0538 -0.0769 0.0397  84  ARG A NE  
438  C CZ  . ARG A 66  ? 1.1833 0.9560 0.9831 -0.0708 -0.0678 0.0386  84  ARG A CZ  
439  N NH1 . ARG A 66  ? 1.3433 1.1344 1.1447 -0.0804 -0.0371 0.0253  84  ARG A NH1 
440  N NH2 . ARG A 66  ? 1.3964 1.1352 1.1395 -0.0784 -0.0903 0.0503  84  ARG A NH2 
441  N N   . GLY A 67  ? 0.9218 0.7863 1.0019 0.0019  -0.0370 0.0182  85  GLY A N   
442  C CA  . GLY A 67  ? 0.8648 0.7265 0.9782 0.0159  -0.0395 0.0181  85  GLY A CA  
443  C C   . GLY A 67  ? 0.8449 0.7242 0.9891 0.0206  -0.0401 0.0248  85  GLY A C   
444  O O   . GLY A 67  ? 0.9231 0.7937 1.0799 0.0282  -0.0528 0.0350  85  GLY A O   
445  N N   . ILE A 68  ? 0.8447 0.7493 1.0011 0.0145  -0.0263 0.0175  86  ILE A N   
446  C CA  . ILE A 68  ? 0.9207 0.8495 1.1150 0.0177  -0.0277 0.0203  86  ILE A CA  
447  C C   . ILE A 68  ? 0.9749 0.8983 1.1559 0.0102  -0.0440 0.0388  86  ILE A C   
448  O O   . ILE A 68  ? 0.9563 0.8856 1.1621 0.0174  -0.0572 0.0458  86  ILE A O   
449  C CB  . ILE A 68  ? 0.9435 0.9041 1.1549 0.0078  -0.0045 0.0048  86  ILE A CB  
450  C CG1 . ILE A 68  ? 0.9230 0.8899 1.1559 0.0180  0.0121  -0.0175 86  ILE A CG1 
451  C CG2 . ILE A 68  ? 1.0882 1.0799 1.3439 0.0077  -0.0068 0.0059  86  ILE A CG2 
452  C CD1 . ILE A 68  ? 1.0547 1.0504 1.2957 0.0047  0.0415  -0.0379 86  ILE A CD1 
453  N N   . LEU A 69  ? 0.9815 0.8914 1.1223 -0.0039 -0.0453 0.0462  87  LEU A N   
454  C CA  . LEU A 69  ? 0.9368 0.8367 1.0644 -0.0104 -0.0605 0.0616  87  LEU A CA  
455  C C   . LEU A 69  ? 0.9703 0.8514 1.0997 0.0011  -0.0766 0.0683  87  LEU A C   
456  O O   . LEU A 69  ? 1.0412 0.9229 1.1796 0.0016  -0.0883 0.0767  87  LEU A O   
457  C CB  . LEU A 69  ? 0.9192 0.8000 1.0031 -0.0237 -0.0622 0.0674  87  LEU A CB  
458  C CG  . LEU A 69  ? 1.1664 1.0326 1.2357 -0.0309 -0.0768 0.0811  87  LEU A CG  
459  C CD1 . LEU A 69  ? 0.9731 0.8593 1.0624 -0.0411 -0.0730 0.0847  87  LEU A CD1 
460  C CD2 . LEU A 69  ? 1.0518 0.8932 1.0790 -0.0401 -0.0821 0.0863  87  LEU A CD2 
461  N N   . VAL A 70  ? 1.0379 0.9012 1.1564 0.0078  -0.0761 0.0633  88  VAL A N   
462  C CA  . VAL A 70  ? 0.9726 0.8151 1.0884 0.0146  -0.0860 0.0679  88  VAL A CA  
463  C C   . VAL A 70  ? 1.0004 0.8458 1.1395 0.0242  -0.0924 0.0723  88  VAL A C   
464  O O   . VAL A 70  ? 1.1273 0.9613 1.2596 0.0238  -0.1050 0.0822  88  VAL A O   
465  C CB  . VAL A 70  ? 0.8985 0.7249 1.0062 0.0182  -0.0802 0.0583  88  VAL A CB  
466  C CG1 . VAL A 70  ? 0.8509 0.6536 0.9535 0.0207  -0.0853 0.0622  88  VAL A CG1 
467  C CG2 . VAL A 70  ? 0.9740 0.7979 1.0613 0.0108  -0.0806 0.0533  88  VAL A CG2 
468  N N   . ILE A 71  ? 0.9699 0.8290 1.1359 0.0334  -0.0854 0.0638  89  ILE A N   
469  C CA  . ILE A 71  ? 1.0662 0.9241 1.2583 0.0470  -0.0963 0.0669  89  ILE A CA  
470  C C   . ILE A 71  ? 1.0155 0.8936 1.2237 0.0445  -0.1095 0.0744  89  ILE A C   
471  O O   . ILE A 71  ? 1.0860 0.9501 1.2913 0.0497  -0.1284 0.0849  89  ILE A O   
472  C CB  . ILE A 71  ? 1.0408 0.9121 1.2672 0.0593  -0.0856 0.0520  89  ILE A CB  
473  C CG1 . ILE A 71  ? 0.9466 0.7939 1.1555 0.0607  -0.0742 0.0436  89  ILE A CG1 
474  C CG2 . ILE A 71  ? 1.2692 1.1390 1.5289 0.0769  -0.1023 0.0551  89  ILE A CG2 
475  C CD1 . ILE A 71  ? 1.2819 1.1435 1.5188 0.0686  -0.0585 0.0242  89  ILE A CD1 
476  N N   . LEU A 72  ? 0.9545 0.8636 1.1767 0.0342  -0.0997 0.0688  90  LEU A N   
477  C CA  . LEU A 72  ? 1.0426 0.9747 1.2856 0.0289  -0.1104 0.0728  90  LEU A CA  
478  C C   . LEU A 72  ? 0.9934 0.9028 1.2027 0.0206  -0.1259 0.0869  90  LEU A C   
479  O O   . LEU A 72  ? 1.0660 0.9771 1.2843 0.0232  -0.1449 0.0930  90  LEU A O   
480  C CB  . LEU A 72  ? 1.0590 1.0223 1.3145 0.0134  -0.0917 0.0641  90  LEU A CB  
481  C CG  . LEU A 72  ? 0.9285 0.9208 1.2208 0.0178  -0.0716 0.0455  90  LEU A CG  
482  C CD1 . LEU A 72  ? 0.8124 0.8256 1.0984 -0.0045 -0.0487 0.0385  90  LEU A CD1 
483  C CD2 . LEU A 72  ? 0.8688 0.8884 1.2217 0.0343  -0.0831 0.0373  90  LEU A CD2 
484  N N   . ILE A 73  ? 0.8144 0.7027 0.9860 0.0110  -0.1193 0.0901  91  ILE A N   
485  C CA  . ILE A 73  ? 0.9294 0.7977 1.0731 0.0029  -0.1307 0.0990  91  ILE A CA  
486  C C   . ILE A 73  ? 1.1271 0.9698 1.2563 0.0108  -0.1435 0.1050  91  ILE A C   
487  O O   . ILE A 73  ? 1.3399 1.1749 1.4583 0.0069  -0.1582 0.1115  91  ILE A O   
488  C CB  . ILE A 73  ? 0.9844 0.8364 1.0993 -0.0056 -0.1224 0.0981  91  ILE A CB  
489  C CG1 . ILE A 73  ? 1.0517 0.9194 1.1685 -0.0172 -0.1140 0.0969  91  ILE A CG1 
490  C CG2 . ILE A 73  ? 1.1000 0.9293 1.1911 -0.0111 -0.1318 0.1026  91  ILE A CG2 
491  C CD1 . ILE A 73  ? 1.0584 0.9079 1.1470 -0.0225 -0.1102 0.0966  91  ILE A CD1 
492  N N   . TYR A 74  ? 1.1788 1.0044 1.3028 0.0200  -0.1378 0.1027  92  TYR A N   
493  C CA  . TYR A 74  ? 1.2289 1.0225 1.3312 0.0244  -0.1482 0.1101  92  TYR A CA  
494  C C   . TYR A 74  ? 1.2057 1.0040 1.3244 0.0337  -0.1697 0.1172  92  TYR A C   
495  O O   . TYR A 74  ? 1.1478 0.9233 1.2393 0.0307  -0.1859 0.1268  92  TYR A O   
496  C CB  . TYR A 74  ? 1.3812 1.1537 1.4781 0.0311  -0.1373 0.1060  92  TYR A CB  
497  C CG  . TYR A 74  ? 1.3170 1.0488 1.3852 0.0330  -0.1467 0.1156  92  TYR A CG  
498  C CD1 . TYR A 74  ? 1.1903 0.8936 1.2181 0.0195  -0.1421 0.1183  92  TYR A CD1 
499  C CD2 . TYR A 74  ? 1.3410 1.0599 1.4208 0.0477  -0.1601 0.1215  92  TYR A CD2 
500  C CE1 . TYR A 74  ? 1.4108 1.0710 1.4018 0.0166  -0.1478 0.1280  92  TYR A CE1 
501  C CE2 . TYR A 74  ? 1.4731 1.1448 1.5161 0.0479  -0.1709 0.1336  92  TYR A CE2 
502  C CZ  . TYR A 74  ? 1.4383 1.0794 1.4325 0.0304  -0.1634 0.1376  92  TYR A CZ  
503  O OH  . TYR A 74  ? 1.2950 0.8835 1.2425 0.0261  -0.1711 0.1504  92  TYR A OH  
504  N N   . GLU A 75  ? 1.2078 1.0358 1.3715 0.0450  -0.1709 0.1109  93  GLU A N   
505  C CA  . GLU A 75  ? 1.2909 1.1279 1.4816 0.0574  -0.1952 0.1148  93  GLU A CA  
506  C C   . GLU A 75  ? 1.1951 1.0476 1.3846 0.0468  -0.2111 0.1189  93  GLU A C   
507  O O   . GLU A 75  ? 1.1808 1.0186 1.3592 0.0510  -0.2376 0.1278  93  GLU A O   
508  C CB  . GLU A 75  ? 1.2412 1.1155 1.4921 0.0709  -0.1895 0.1012  93  GLU A CB  
509  C CG  . GLU A 75  ? 1.5453 1.4338 1.8379 0.0880  -0.2177 0.1015  93  GLU A CG  
510  C CD  . GLU A 75  ? 1.8794 1.8024 2.2376 0.1045  -0.2096 0.0837  93  GLU A CD  
511  O OE1 . GLU A 75  ? 1.7043 1.6357 2.0669 0.1008  -0.1805 0.0719  93  GLU A OE1 
512  O OE2 . GLU A 75  ? 1.9482 1.8903 2.3549 0.1213  -0.2332 0.0796  93  GLU A OE2 
513  N N   . TYR A 76  ? 1.1240 1.0021 1.3209 0.0319  -0.1967 0.1127  94  TYR A N   
514  C CA  . TYR A 76  ? 1.3624 1.2569 1.5640 0.0203  -0.2101 0.1141  94  TYR A CA  
515  C C   . TYR A 76  ? 1.2802 1.1388 1.4278 0.0091  -0.2187 0.1229  94  TYR A C   
516  O O   . TYR A 76  ? 1.2218 1.0818 1.3645 0.0037  -0.2391 0.1258  94  TYR A O   
517  C CB  . TYR A 76  ? 1.1855 1.1128 1.4100 0.0060  -0.1908 0.1052  94  TYR A CB  
518  C CG  . TYR A 76  ? 1.1280 1.1014 1.4142 0.0114  -0.1875 0.0932  94  TYR A CG  
519  C CD1 . TYR A 76  ? 1.1546 1.1595 1.4802 0.0091  -0.2052 0.0887  94  TYR A CD1 
520  C CD2 . TYR A 76  ? 1.1285 1.1163 1.4370 0.0182  -0.1662 0.0833  94  TYR A CD2 
521  C CE1 . TYR A 76  ? 1.3737 1.4269 1.7658 0.0136  -0.2002 0.0732  94  TYR A CE1 
522  C CE2 . TYR A 76  ? 1.4148 1.4476 1.7841 0.0222  -0.1590 0.0678  94  TYR A CE2 
523  C CZ  . TYR A 76  ? 1.6163 1.6835 2.0305 0.0201  -0.1754 0.0622  94  TYR A CZ  
524  O OH  . TYR A 76  ? 1.5847 1.7027 2.0690 0.0236  -0.1662 0.0425  94  TYR A OH  
525  N N   . VAL A 77  ? 1.2705 1.0990 1.3798 0.0046  -0.2031 0.1244  95  VAL A N   
526  C CA  . VAL A 77  ? 1.1920 0.9869 1.2529 -0.0060 -0.2074 0.1287  95  VAL A CA  
527  C C   . VAL A 77  ? 1.4301 1.1926 1.4598 -0.0005 -0.2257 0.1383  95  VAL A C   
528  O O   . VAL A 77  ? 1.4848 1.2200 1.4705 -0.0116 -0.2322 0.1415  95  VAL A O   
529  C CB  . VAL A 77  ? 1.2521 1.0285 1.2898 -0.0123 -0.1849 0.1235  95  VAL A CB  
530  C CG1 . VAL A 77  ? 1.1278 0.9260 1.1849 -0.0183 -0.1728 0.1170  95  VAL A CG1 
531  C CG2 . VAL A 77  ? 1.4474 1.2100 1.4835 -0.0024 -0.1741 0.1232  95  VAL A CG2 
532  N N   . LYS A 78  ? 1.4742 1.2348 1.5218 0.0158  -0.2342 0.1426  96  LYS A N   
533  C CA  . LYS A 78  ? 1.2456 0.9671 1.2591 0.0223  -0.2558 0.1549  96  LYS A CA  
534  C C   . LYS A 78  ? 1.2196 0.9582 1.2569 0.0315  -0.2908 0.1592  96  LYS A C   
535  O O   . LYS A 78  ? 1.7051 1.4217 1.7032 0.0239  -0.3127 0.1666  96  LYS A O   
536  C CB  . LYS A 78  ? 1.3752 1.0758 1.3931 0.0362  -0.2485 0.1576  96  LYS A CB  
537  C CG  . LYS A 78  ? 1.3351 1.0008 1.3114 0.0247  -0.2224 0.1565  96  LYS A CG  
538  C CD  . LYS A 78  ? 1.5385 1.1528 1.4454 0.0108  -0.2290 0.1672  96  LYS A CD  
539  C CE  . LYS A 78  ? 1.8285 1.4109 1.7011 -0.0024 -0.1999 0.1628  96  LYS A CE  
540  N NZ  . LYS A 78  ? 2.2148 1.7475 2.0158 -0.0210 -0.2001 0.1705  96  LYS A NZ  
541  N N   . ASP A 81  ? 1.5828 1.2928 1.7431 0.1302  -0.3815 0.1743  99  ASP A N   
542  C CA  . ASP A 81  ? 1.8477 1.4894 1.9506 0.1367  -0.3952 0.1907  99  ASP A CA  
543  C C   . ASP A 81  ? 1.7657 1.3610 1.8103 0.1201  -0.3616 0.1972  99  ASP A C   
544  O O   . ASP A 81  ? 1.7245 1.2905 1.7030 0.0970  -0.3526 0.2057  99  ASP A O   
545  C CB  . ASP A 81  ? 1.9685 1.5812 2.0130 0.1282  -0.4258 0.2034  99  ASP A CB  
546  C CG  . ASP A 81  ? 1.8991 1.5581 2.0031 0.1435  -0.4613 0.1949  99  ASP A CG  
547  O OD1 . ASP A 81  ? 2.0007 1.6957 2.1822 0.1667  -0.4669 0.1818  99  ASP A OD1 
548  O OD2 . ASP A 81  ? 1.7573 1.4180 1.8332 0.1314  -0.4826 0.1989  99  ASP A OD2 
549  N N   . ILE A 82  ? 2.1600 1.7508 2.2327 0.1312  -0.3419 0.1900  100 ILE A N   
550  C CA  . ILE A 82  ? 1.8056 1.3663 1.8385 0.1148  -0.3052 0.1888  100 ILE A CA  
551  C C   . ILE A 82  ? 1.5780 1.0946 1.6052 0.1282  -0.3047 0.1920  100 ILE A C   
552  O O   . ILE A 82  ? 1.9259 1.4630 2.0109 0.1522  -0.3154 0.1831  100 ILE A O   
553  C CB  . ILE A 82  ? 1.9814 1.5998 2.0576 0.1067  -0.2683 0.1672  100 ILE A CB  
554  C CG1 . ILE A 82  ? 2.1064 1.7654 2.1832 0.0910  -0.2660 0.1634  100 ILE A CG1 
555  C CG2 . ILE A 82  ? 1.8363 1.4273 1.8789 0.0918  -0.2349 0.1633  100 ILE A CG2 
556  C CD1 . ILE A 82  ? 1.5818 1.2962 1.7025 0.0854  -0.2381 0.1449  100 ILE A CD1 
557  N N   . ASN A 83  ? 1.6314 1.0921 1.5912 0.1104  -0.2878 0.2013  101 ASN A N   
558  C CA  . ASN A 83  ? 1.6061 1.0210 1.5503 0.1177  -0.2836 0.2049  101 ASN A CA  
559  C C   . ASN A 83  ? 1.5119 0.9343 1.4938 0.1204  -0.2545 0.1889  101 ASN A C   
560  O O   . ASN A 83  ? 1.8295 1.2980 1.8502 0.1172  -0.2375 0.1740  101 ASN A O   
561  C CB  . ASN A 83  ? 1.6066 0.9564 1.4608 0.0944  -0.2781 0.2217  101 ASN A CB  
562  C CG  . ASN A 83  ? 1.9483 1.2855 1.7656 0.0651  -0.2432 0.2175  101 ASN A CG  
563  O OD1 . ASN A 83  ? 1.9906 1.3618 1.8481 0.0636  -0.2242 0.2029  101 ASN A OD1 
564  N ND2 . ASN A 83  ? 1.6257 0.9130 1.3665 0.0408  -0.2347 0.2289  101 ASN A ND2 
565  N N   . CYS A 84  ? 1.3486 1.2045 1.7640 0.0938  -0.3305 0.2649  102 CYS A N   
566  C CA  . CYS A 84  ? 1.3206 1.1738 1.7794 0.1087  -0.2772 0.2492  102 CYS A CA  
567  C C   . CYS A 84  ? 1.1428 0.9483 1.5380 0.1031  -0.2501 0.2085  102 CYS A C   
568  O O   . CYS A 84  ? 1.2515 1.0579 1.6689 0.1003  -0.2225 0.1858  102 CYS A O   
569  C CB  . CYS A 84  ? 1.2826 1.1351 1.7805 0.1382  -0.2517 0.2744  102 CYS A CB  
570  S SG  . CYS A 84  ? 1.5291 1.4484 2.1202 0.1561  -0.2753 0.3248  102 CYS A SG  
571  N N   . ASN A 85  ? 1.2024 0.9724 1.5194 0.1031  -0.2563 0.2010  103 ASN A N   
572  C CA  . ASN A 85  ? 1.2431 0.9806 1.5062 0.1012  -0.2300 0.1664  103 ASN A CA  
573  C C   . ASN A 85  ? 1.3501 1.0804 1.5920 0.0853  -0.2444 0.1373  103 ASN A C   
574  O O   . ASN A 85  ? 1.2874 1.0089 1.5294 0.0841  -0.2170 0.1117  103 ASN A O   
575  C CB  . ASN A 85  ? 1.2900 1.0039 1.4741 0.1070  -0.2342 0.1686  103 ASN A CB  
576  C CG  . ASN A 85  ? 1.3632 1.0778 1.5642 0.1194  -0.2182 0.2010  103 ASN A CG  
577  O OD1 . ASN A 85  ? 1.3495 1.0647 1.6091 0.1262  -0.1900 0.2087  103 ASN A OD1 
578  N ND2 . ASN A 85  ? 1.4909 1.1996 1.6351 0.1230  -0.2373 0.2202  103 ASN A ND2 
579  N N   . GLU A 86  ? 1.3828 1.1131 1.6044 0.0711  -0.2907 0.1424  104 GLU A N   
580  C CA  . GLU A 86  ? 1.2852 0.9986 1.4870 0.0528  -0.3102 0.1190  104 GLU A CA  
581  C C   . GLU A 86  ? 1.2084 0.9552 1.4890 0.0440  -0.2906 0.1213  104 GLU A C   
582  O O   . GLU A 86  ? 1.1779 0.9085 1.4464 0.0376  -0.2779 0.0971  104 GLU A O   
583  C CB  . GLU A 86  ? 1.3784 1.0807 1.5470 0.0337  -0.3695 0.1283  104 GLU A CB  
584  C CG  . GLU A 86  ? 1.5370 1.1947 1.6030 0.0430  -0.3907 0.1156  104 GLU A CG  
585  C CD  . GLU A 86  ? 1.7132 1.3573 1.7432 0.0223  -0.4540 0.1263  104 GLU A CD  
586  O OE1 . GLU A 86  ? 1.5467 1.2370 1.6374 0.0116  -0.4763 0.1624  104 GLU A OE1 
587  O OE2 . GLU A 86  ? 2.1880 1.7740 2.1277 0.0177  -0.4830 0.0982  104 GLU A OE2 
588  N N   . TRP A 87  ? 1.1775 0.9740 1.5378 0.0464  -0.2869 0.1515  105 TRP A N   
589  C CA  . TRP A 87  ? 1.1606 0.9965 1.5936 0.0431  -0.2623 0.1546  105 TRP A CA  
590  C C   . TRP A 87  ? 1.0777 0.8961 1.5070 0.0584  -0.2111 0.1292  105 TRP A C   
591  O O   . TRP A 87  ? 1.0196 0.8439 1.4611 0.0501  -0.1945 0.1137  105 TRP A O   
592  C CB  . TRP A 87  ? 1.0729 0.9701 1.5915 0.0532  -0.2622 0.1921  105 TRP A CB  
593  C CG  . TRP A 87  ? 1.3963 1.3337 1.9441 0.0292  -0.3126 0.2211  105 TRP A CG  
594  C CD1 . TRP A 87  ? 1.4783 1.4476 2.0515 0.0320  -0.3447 0.2554  105 TRP A CD1 
595  C CD2 . TRP A 87  ? 1.4643 1.4151 2.0199 -0.0055 -0.3408 0.2217  105 TRP A CD2 
596  N NE1 . TRP A 87  ? 1.3909 1.3968 1.9893 -0.0009 -0.3925 0.2764  105 TRP A NE1 
597  C CE2 . TRP A 87  ? 1.4970 1.4893 2.0849 -0.0259 -0.3910 0.2567  105 TRP A CE2 
598  C CE3 . TRP A 87  ? 1.3911 1.3218 1.9293 -0.0233 -0.3309 0.1992  105 TRP A CE3 
599  C CZ2 . TRP A 87  ? 1.7299 1.7418 2.3341 -0.0676 -0.4321 0.2695  105 TRP A CZ2 
600  C CZ3 . TRP A 87  ? 1.6727 1.6185 2.2248 -0.0616 -0.3700 0.2129  105 TRP A CZ3 
601  C CH2 . TRP A 87  ? 1.7143 1.6992 2.2996 -0.0855 -0.4203 0.2477  105 TRP A CH2 
602  N N   . GLU A 88  ? 1.0557 0.8530 1.4677 0.0777  -0.1881 0.1272  106 GLU A N   
603  C CA  . GLU A 88  ? 1.0207 0.7986 1.4266 0.0864  -0.1451 0.1040  106 GLU A CA  
604  C C   . GLU A 88  ? 1.0370 0.7899 1.3874 0.0748  -0.1445 0.0734  106 GLU A C   
605  O O   . GLU A 88  ? 1.0638 0.8192 1.4244 0.0711  -0.1216 0.0549  106 GLU A O   
606  C CB  . GLU A 88  ? 1.0878 0.8429 1.4797 0.1016  -0.1287 0.1127  106 GLU A CB  
607  C CG  . GLU A 88  ? 1.0306 0.7637 1.4218 0.1056  -0.0885 0.0932  106 GLU A CG  
608  C CD  . GLU A 88  ? 1.1590 0.8655 1.5357 0.1137  -0.0770 0.1074  106 GLU A CD  
609  O OE1 . GLU A 88  ? 1.2260 0.9291 1.5669 0.1138  -0.0974 0.1239  106 GLU A OE1 
610  O OE2 . GLU A 88  ? 1.1541 0.8394 1.5511 0.1186  -0.0490 0.1028  106 GLU A OE2 
611  N N   . LYS A 89  ? 1.1272 0.8558 1.4152 0.0721  -0.1701 0.0677  107 LYS A N   
612  C CA  . LYS A 89  ? 1.0978 0.8015 1.3320 0.0689  -0.1703 0.0395  107 LYS A CA  
613  C C   . LYS A 89  ? 1.0732 0.7793 1.3222 0.0528  -0.1842 0.0319  107 LYS A C   
614  O O   . LYS A 89  ? 1.0442 0.7442 1.2843 0.0513  -0.1675 0.0125  107 LYS A O   
615  C CB  . LYS A 89  ? 1.1346 0.8092 1.2942 0.0751  -0.1964 0.0342  107 LYS A CB  
616  C CG  . LYS A 89  ? 1.0483 0.7238 1.1826 0.0897  -0.1806 0.0440  107 LYS A CG  
617  C CD  . LYS A 89  ? 1.2152 0.8671 1.2726 0.0971  -0.2103 0.0422  107 LYS A CD  
618  C CE  . LYS A 89  ? 0.9743 0.6339 1.0040 0.1100  -0.1943 0.0583  107 LYS A CE  
619  N NZ  . LYS A 89  ? 1.2896 0.9601 1.3095 0.1184  -0.1544 0.0469  107 LYS A NZ  
620  N N   . VAL A 90  ? 1.1237 0.8421 1.3969 0.0380  -0.2169 0.0509  108 VAL A N   
621  C CA  . VAL A 90  ? 1.0145 0.7346 1.3006 0.0164  -0.2348 0.0503  108 VAL A CA  
622  C C   . VAL A 90  ? 0.9348 0.6937 1.2794 0.0150  -0.1985 0.0524  108 VAL A C   
623  O O   . VAL A 90  ? 0.7758 0.5274 1.1115 0.0050  -0.1937 0.0406  108 VAL A O   
624  C CB  . VAL A 90  ? 0.9871 0.7194 1.2922 -0.0051 -0.2810 0.0758  108 VAL A CB  
625  C CG1 . VAL A 90  ? 1.2584 0.9999 1.5885 -0.0337 -0.2982 0.0834  108 VAL A CG1 
626  C CG2 . VAL A 90  ? 1.1101 0.7917 1.3385 -0.0049 -0.3208 0.0670  108 VAL A CG2 
627  N N   . ALA A 91  ? 1.0106 0.8081 1.4114 0.0273  -0.1730 0.0674  109 ALA A N   
628  C CA  . ALA A 91  ? 0.7678 0.5973 1.2138 0.0315  -0.1353 0.0648  109 ALA A CA  
629  C C   . ALA A 91  ? 0.7562 0.5573 1.1647 0.0388  -0.1057 0.0343  109 ALA A C   
630  O O   . ALA A 91  ? 0.6821 0.4947 1.0975 0.0331  -0.0870 0.0240  109 ALA A O   
631  C CB  . ALA A 91  ? 0.7262 0.5914 1.2318 0.0511  -0.1142 0.0838  109 ALA A CB  
632  N N   . CYS A 92  ? 0.8742 0.6438 1.2428 0.0494  -0.1023 0.0225  110 CYS A N   
633  C CA  . CYS A 92  ? 0.9623 0.7138 1.2983 0.0521  -0.0797 -0.0027 110 CYS A CA  
634  C C   . CYS A 92  ? 1.1593 0.8989 1.4603 0.0419  -0.0946 -0.0164 110 CYS A C   
635  O O   . CYS A 92  ? 1.4237 1.1684 1.7218 0.0384  -0.0767 -0.0306 110 CYS A O   
636  C CB  . CYS A 92  ? 0.9354 0.6663 1.2380 0.0623  -0.0762 -0.0058 110 CYS A CB  
637  S SG  . CYS A 92  ? 0.7756 0.4979 1.0377 0.0621  -0.0583 -0.0312 110 CYS A SG  
638  N N   . ILE A 93  ? 1.0333 0.7516 1.3029 0.0376  -0.1298 -0.0124 111 ILE A N   
639  C CA  . ILE A 93  ? 0.8740 0.5676 1.1064 0.0309  -0.1477 -0.0244 111 ILE A CA  
640  C C   . ILE A 93  ? 0.7844 0.4994 1.0520 0.0121  -0.1461 -0.0148 111 ILE A C   
641  O O   . ILE A 93  ? 0.8842 0.5932 1.1359 0.0089  -0.1398 -0.0253 111 ILE A O   
642  C CB  . ILE A 93  ? 0.9403 0.5928 1.1253 0.0302  -0.1895 -0.0237 111 ILE A CB  
643  C CG1 . ILE A 93  ? 0.9326 0.5682 1.0711 0.0528  -0.1854 -0.0352 111 ILE A CG1 
644  C CG2 . ILE A 93  ? 0.8748 0.4890 1.0231 0.0229  -0.2126 -0.0336 111 ILE A CG2 
645  C CD1 . ILE A 93  ? 0.9047 0.4963 0.9852 0.0564  -0.2247 -0.0382 111 ILE A CD1 
646  N N   . ALA A 94  ? 0.7621 0.5085 1.0791 0.0002  -0.1518 0.0086  112 ALA A N   
647  C CA  . ALA A 94  ? 0.7598 0.5394 1.1144 -0.0182 -0.1471 0.0235  112 ALA A CA  
648  C C   . ALA A 94  ? 0.8287 0.6320 1.1950 -0.0096 -0.1044 0.0102  112 ALA A C   
649  O O   . ALA A 94  ? 0.8259 0.6341 1.1836 -0.0208 -0.0999 0.0086  112 ALA A O   
650  C CB  . ALA A 94  ? 0.7891 0.6154 1.2046 -0.0278 -0.1555 0.0544  112 ALA A CB  
651  N N   . TRP A 95  ? 0.9673 0.7795 1.3475 0.0091  -0.0752 0.0005  113 TRP A N   
652  C CA  . TRP A 95  ? 0.9120 0.7367 1.2946 0.0154  -0.0383 -0.0163 113 TRP A CA  
653  C C   . TRP A 95  ? 0.8636 0.6610 1.1973 0.0144  -0.0374 -0.0395 113 TRP A C   
654  O O   . TRP A 95  ? 0.7527 0.5603 1.0782 0.0105  -0.0189 -0.0512 113 TRP A O   
655  C CB  . TRP A 95  ? 0.8106 0.6389 1.2181 0.0342  -0.0114 -0.0204 113 TRP A CB  
656  C CG  . TRP A 95  ? 0.7187 0.5893 1.1807 0.0419  0.0029  -0.0012 113 TRP A CG  
657  C CD1 . TRP A 95  ? 0.7671 0.6534 1.2697 0.0554  -0.0008 0.0189  113 TRP A CD1 
658  C CD2 . TRP A 95  ? 0.6694 0.5807 1.1529 0.0394  0.0242  0.0028  113 TRP A CD2 
659  N NE1 . TRP A 95  ? 0.7136 0.6520 1.2673 0.0642  0.0181  0.0351  113 TRP A NE1 
660  C CE2 . TRP A 95  ? 0.7722 0.7277 1.3135 0.0544  0.0355  0.0252  113 TRP A CE2 
661  C CE3 . TRP A 95  ? 0.7271 0.6461 1.1856 0.0273  0.0354  -0.0081 113 TRP A CE3 
662  C CZ2 . TRP A 95  ? 0.8929 0.9048 1.4685 0.0595  0.0614  0.0362  113 TRP A CZ2 
663  C CZ3 . TRP A 95  ? 0.7330 0.7025 1.2193 0.0293  0.0595  0.0029  113 TRP A CZ3 
664  C CH2 . TRP A 95  ? 0.8626 0.8801 1.4074 0.0460  0.0742  0.0244  113 TRP A CH2 
665  N N   . CYS A 96  ? 0.8543 0.6220 1.1542 0.0194  -0.0573 -0.0454 114 CYS A N   
666  C CA  . CYS A 96  ? 0.9119 0.6650 1.1716 0.0220  -0.0583 -0.0630 114 CYS A CA  
667  C C   . CYS A 96  ? 0.8973 0.6452 1.1409 0.0113  -0.0750 -0.0591 114 CYS A C   
668  O O   . CYS A 96  ? 1.0405 0.7950 1.2683 0.0097  -0.0660 -0.0691 114 CYS A O   
669  C CB  . CYS A 96  ? 0.9395 0.6691 1.1668 0.0357  -0.0729 -0.0679 114 CYS A CB  
670  S SG  . CYS A 96  ? 1.4529 1.1903 1.6884 0.0449  -0.0487 -0.0721 114 CYS A SG  
671  N N   . ILE A 97  ? 0.8635 0.5984 1.1104 0.0010  -0.1023 -0.0419 115 ILE A N   
672  C CA  . ILE A 97  ? 0.9865 0.7106 1.2200 -0.0140 -0.1203 -0.0324 115 ILE A CA  
673  C C   . ILE A 97  ? 0.9198 0.6879 1.1833 -0.0274 -0.0951 -0.0232 115 ILE A C   
674  O O   . ILE A 97  ? 0.8287 0.5968 1.0739 -0.0354 -0.0959 -0.0214 115 ILE A O   
675  C CB  . ILE A 97  ? 0.9360 0.6302 1.1658 -0.0288 -0.1599 -0.0141 115 ILE A CB  
676  C CG1 . ILE A 97  ? 0.9297 0.5737 1.1139 -0.0110 -0.1837 -0.0289 115 ILE A CG1 
677  C CG2 . ILE A 97  ? 0.8896 0.5647 1.1053 -0.0490 -0.1808 0.0002  115 ILE A CG2 
678  C CD1 . ILE A 97  ? 0.9419 0.5350 1.1006 -0.0256 -0.2302 -0.0187 115 ILE A CD1 
679  N N   . GLU A 98  ? 0.8842 0.6902 1.1907 -0.0266 -0.0718 -0.0166 116 GLU A N   
680  C CA  . GLU A 98  ? 0.8564 0.7056 1.1841 -0.0319 -0.0415 -0.0124 116 GLU A CA  
681  C C   . GLU A 98  ? 0.8454 0.6908 1.1419 -0.0239 -0.0187 -0.0389 116 GLU A C   
682  O O   . GLU A 98  ? 0.8443 0.7088 1.1285 -0.0324 -0.0070 -0.0381 116 GLU A O   
683  C CB  . GLU A 98  ? 0.7111 0.5982 1.0889 -0.0229 -0.0187 -0.0033 116 GLU A CB  
684  C CG  . GLU A 98  ? 0.8375 0.7515 1.2580 -0.0367 -0.0400 0.0303  116 GLU A CG  
685  C CD  . GLU A 98  ? 0.9447 0.8875 1.3735 -0.0624 -0.0473 0.0556  116 GLU A CD  
686  O OE1 . GLU A 98  ? 0.7721 0.7425 1.1944 -0.0616 -0.0182 0.0517  116 GLU A OE1 
687  O OE2 . GLU A 98  ? 0.9086 0.8434 1.3462 -0.0856 -0.0839 0.0802  116 GLU A OE2 
688  N N   . ILE A 99  ? 0.8521 0.6763 1.1349 -0.0104 -0.0137 -0.0599 117 ILE A N   
689  C CA  . ILE A 99  ? 0.9143 0.7368 1.1698 -0.0087 0.0013  -0.0830 117 ILE A CA  
690  C C   . ILE A 99  ? 0.9616 0.7760 1.1832 -0.0139 -0.0192 -0.0824 117 ILE A C   
691  O O   . ILE A 99  ? 1.0875 0.9149 1.2888 -0.0196 -0.0109 -0.0914 117 ILE A O   
692  C CB  . ILE A 99  ? 0.9970 0.8029 1.2517 0.0015  0.0083  -0.0986 117 ILE A CB  
693  C CG1 . ILE A 99  ? 0.8135 0.6200 1.0992 0.0094  0.0294  -0.0986 117 ILE A CG1 
694  C CG2 . ILE A 99  ? 0.8821 0.6903 1.1112 -0.0036 0.0165  -0.1188 117 ILE A CG2 
695  C CD1 . ILE A 99  ? 0.9682 0.7528 1.2565 0.0170  0.0309  -0.1040 117 ILE A CD1 
696  N N   . LEU A 100 ? 0.8980 0.6868 1.1086 -0.0097 -0.0479 -0.0728 118 LEU A N   
697  C CA  . LEU A 100 ? 0.9861 0.7593 1.1644 -0.0090 -0.0692 -0.0698 118 LEU A CA  
698  C C   . LEU A 100 ? 1.0024 0.7884 1.1789 -0.0272 -0.0708 -0.0522 118 LEU A C   
699  O O   . LEU A 100 ? 1.0127 0.8054 1.1653 -0.0295 -0.0726 -0.0530 118 LEU A O   
700  C CB  . LEU A 100 ? 0.9990 0.7294 1.1595 0.0019  -0.1002 -0.0648 118 LEU A CB  
701  C CG  . LEU A 100 ? 0.9683 0.6682 1.0910 0.0121  -0.1246 -0.0636 118 LEU A CG  
702  C CD1 . LEU A 100 ? 1.1806 0.9043 1.2909 0.0295  -0.1127 -0.0795 118 LEU A CD1 
703  C CD2 . LEU A 100 ? 1.0865 0.7309 1.1837 0.0249  -0.1552 -0.0629 118 LEU A CD2 
704  N N   . GLN A 101 ? 1.1303 0.9266 1.3342 -0.0412 -0.0704 -0.0325 119 GLN A N   
705  C CA  . GLN A 101 ? 1.0762 0.8979 1.2843 -0.0611 -0.0660 -0.0103 119 GLN A CA  
706  C C   . GLN A 101 ? 1.1032 0.9624 1.3019 -0.0602 -0.0327 -0.0242 119 GLN A C   
707  O O   . GLN A 101 ? 1.1190 0.9894 1.2930 -0.0704 -0.0333 -0.0153 119 GLN A O   
708  C CB  . GLN A 101 ? 1.0042 0.8494 1.2559 -0.0754 -0.0654 0.0148  119 GLN A CB  
709  C CG  . GLN A 101 ? 1.1073 1.0018 1.3753 -0.0950 -0.0487 0.0409  119 GLN A CG  
710  C CD  . GLN A 101 ? 1.2092 1.0831 1.4603 -0.1201 -0.0801 0.0717  119 GLN A CD  
711  O OE1 . GLN A 101 ? 1.3457 1.1619 1.5613 -0.1172 -0.1115 0.0668  119 GLN A OE1 
712  N NE2 . GLN A 101 ? 1.3687 1.2898 1.6455 -0.1438 -0.0712 0.1057  119 GLN A NE2 
713  N N   . ALA A 102 ? 1.0068 0.8799 1.2198 -0.0485 -0.0054 -0.0459 120 ALA A N   
714  C CA  . ALA A 102 ? 0.9927 0.8891 1.1878 -0.0476 0.0242  -0.0647 120 ALA A CA  
715  C C   . ALA A 102 ? 0.9652 0.8516 1.1192 -0.0496 0.0134  -0.0800 120 ALA A C   
716  O O   . ALA A 102 ? 1.0840 0.9895 1.2089 -0.0581 0.0221  -0.0823 120 ALA A O   
717  C CB  . ALA A 102 ? 0.9161 0.8104 1.1299 -0.0334 0.0501  -0.0868 120 ALA A CB  
718  N N   . SER A 103 ? 0.9732 0.8363 1.1241 -0.0409 -0.0052 -0.0890 121 SER A N   
719  C CA  . SER A 103 ? 0.8841 0.7503 1.0060 -0.0406 -0.0167 -0.0996 121 SER A CA  
720  C C   . SER A 103 ? 1.0295 0.8966 1.1278 -0.0458 -0.0378 -0.0782 121 SER A C   
721  O O   . SER A 103 ? 0.9247 0.8112 0.9955 -0.0529 -0.0384 -0.0806 121 SER A O   
722  C CB  . SER A 103 ? 0.8675 0.7196 0.9974 -0.0263 -0.0294 -0.1078 121 SER A CB  
723  O OG  . SER A 103 ? 0.9300 0.7553 1.0649 -0.0152 -0.0503 -0.0925 121 SER A OG  
724  N N   . PHE A 104 ? 1.0614 0.9031 1.1667 -0.0442 -0.0583 -0.0559 122 PHE A N   
725  C CA  . PHE A 104 ? 1.0223 0.8530 1.1042 -0.0512 -0.0806 -0.0312 122 PHE A CA  
726  C C   . PHE A 104 ? 1.1390 1.0035 1.2114 -0.0718 -0.0632 -0.0171 122 PHE A C   
727  O O   . PHE A 104 ? 1.2059 1.0785 1.2478 -0.0783 -0.0727 -0.0045 122 PHE A O   
728  C CB  . PHE A 104 ? 1.0529 0.8387 1.1419 -0.0515 -0.1077 -0.0105 122 PHE A CB  
729  C CG  . PHE A 104 ? 1.0636 0.8085 1.1432 -0.0263 -0.1292 -0.0229 122 PHE A CG  
730  C CD1 . PHE A 104 ? 1.0294 0.7827 1.0924 -0.0049 -0.1319 -0.0378 122 PHE A CD1 
731  C CD2 . PHE A 104 ? 1.1162 0.8186 1.2020 -0.0236 -0.1472 -0.0187 122 PHE A CD2 
732  C CE1 . PHE A 104 ? 1.1320 0.8564 1.1858 0.0234  -0.1468 -0.0481 122 PHE A CE1 
733  C CE2 . PHE A 104 ? 1.1332 0.7966 1.2004 0.0034  -0.1646 -0.0325 122 PHE A CE2 
734  C CZ  . PHE A 104 ? 1.1461 0.8225 1.1977 0.0293  -0.1617 -0.0472 122 PHE A CZ  
735  N N   . LEU A 105 ? 1.0191 0.9072 1.1163 -0.0793 -0.0367 -0.0170 123 LEU A N   
736  C CA  . LEU A 105 ? 1.0673 0.9956 1.1555 -0.0943 -0.0138 -0.0031 123 LEU A CA  
737  C C   . LEU A 105 ? 1.1152 1.0648 1.1631 -0.0930 0.0029  -0.0269 123 LEU A C   
738  O O   . LEU A 105 ? 1.2785 1.2493 1.2926 -0.1048 0.0039  -0.0121 123 LEU A O   
739  C CB  . LEU A 105 ? 1.0653 1.0199 1.1947 -0.0936 0.0138  -0.0007 123 LEU A CB  
740  C CG  . LEU A 105 ? 1.4488 1.4555 1.5746 -0.0970 0.0523  0.0028  123 LEU A CG  
741  C CD1 . LEU A 105 ? 1.6634 1.7019 1.8443 -0.0990 0.0654  0.0271  123 LEU A CD1 
742  C CD2 . LEU A 105 ? 1.4277 1.4354 1.5300 -0.0805 0.0811  -0.0402 123 LEU A CD2 
743  N N   . VAL A 106 ? 1.0699 1.0121 1.1175 -0.0819 0.0133  -0.0623 124 VAL A N   
744  C CA  . VAL A 106 ? 1.1383 1.0937 1.1445 -0.0858 0.0229  -0.0877 124 VAL A CA  
745  C C   . VAL A 106 ? 1.2069 1.1638 1.1846 -0.0903 -0.0081 -0.0782 124 VAL A C   
746  O O   . VAL A 106 ? 1.2795 1.2573 1.2145 -0.1007 -0.0082 -0.0791 124 VAL A O   
747  C CB  . VAL A 106 ? 1.0895 1.0288 1.1051 -0.0783 0.0359  -0.1242 124 VAL A CB  
748  C CG1 . VAL A 106 ? 1.1088 1.0543 1.0775 -0.0886 0.0393  -0.1516 124 VAL A CG1 
749  C CG2 . VAL A 106 ? 1.2877 1.2237 1.3312 -0.0683 0.0663  -0.1312 124 VAL A CG2 
750  N N   . ALA A 107 ? 1.2255 1.1611 1.2233 -0.0796 -0.0350 -0.0687 125 ALA A N   
751  C CA  . ALA A 107 ? 1.1380 1.0769 1.1143 -0.0760 -0.0645 -0.0562 125 ALA A CA  
752  C C   . ALA A 107 ? 1.2654 1.2074 1.2144 -0.0867 -0.0753 -0.0226 125 ALA A C   
753  O O   . ALA A 107 ? 1.1307 1.0922 1.0455 -0.0917 -0.0882 -0.0151 125 ALA A O   
754  C CB  . ALA A 107 ? 1.2943 1.2063 1.2951 -0.0546 -0.0870 -0.0521 125 ALA A CB  
755  N N   . ASP A 108 ? 1.3021 1.2279 1.2669 -0.0932 -0.0726 0.0016  126 ASP A N   
756  C CA  . ASP A 108 ? 1.3842 1.3128 1.3260 -0.1090 -0.0828 0.0400  126 ASP A CA  
757  C C   . ASP A 108 ? 1.3631 1.3390 1.2710 -0.1247 -0.0556 0.0387  126 ASP A C   
758  O O   . ASP A 108 ? 1.5255 1.5147 1.3953 -0.1355 -0.0664 0.0633  126 ASP A O   
759  C CB  . ASP A 108 ? 1.3231 1.2279 1.2954 -0.1190 -0.0875 0.0681  126 ASP A CB  
760  C CG  . ASP A 108 ? 1.7482 1.6472 1.7000 -0.1398 -0.1046 0.1149  126 ASP A CG  
761  O OD1 . ASP A 108 ? 1.7135 1.6567 1.6395 -0.1552 -0.0855 0.1285  126 ASP A OD1 
762  O OD2 . ASP A 108 ? 1.9303 1.7761 1.8868 -0.1410 -0.1381 0.1385  126 ASP A OD2 
763  N N   . ASP A 109 ? 1.2494 1.2475 1.1653 -0.1237 -0.0201 0.0105  127 ASP A N   
764  C CA  . ASP A 109 ? 1.2773 1.3140 1.1496 -0.1324 0.0080  0.0009  127 ASP A CA  
765  C C   . ASP A 109 ? 1.2932 1.3362 1.1153 -0.1350 -0.0086 -0.0162 127 ASP A C   
766  O O   . ASP A 109 ? 1.3540 1.4233 1.1249 -0.1467 -0.0063 -0.0042 127 ASP A O   
767  C CB  . ASP A 109 ? 1.3654 1.4111 1.2525 -0.1227 0.0472  -0.0329 127 ASP A CB  
768  C CG  . ASP A 109 ? 1.6088 1.6695 1.5442 -0.1214 0.0674  -0.0099 127 ASP A CG  
769  O OD1 . ASP A 109 ? 1.5634 1.6426 1.5049 -0.1363 0.0606  0.0334  127 ASP A OD1 
770  O OD2 . ASP A 109 ? 1.3970 1.4526 1.3660 -0.1072 0.0881  -0.0320 127 ASP A OD2 
771  N N   . ILE A 110 ? 1.3045 1.3299 1.1410 -0.1258 -0.0263 -0.0413 128 ILE A N   
772  C CA  . ILE A 110 ? 1.1952 1.2357 0.9942 -0.1310 -0.0477 -0.0534 128 ILE A CA  
773  C C   . ILE A 110 ? 1.3833 1.4302 1.1648 -0.1319 -0.0807 -0.0130 128 ILE A C   
774  O O   . ILE A 110 ? 1.4022 1.4749 1.1339 -0.1430 -0.0908 -0.0056 128 ILE A O   
775  C CB  . ILE A 110 ? 1.2215 1.2522 1.0520 -0.1227 -0.0595 -0.0811 128 ILE A CB  
776  C CG1 . ILE A 110 ? 1.3687 1.3853 1.2086 -0.1243 -0.0293 -0.1195 128 ILE A CG1 
777  C CG2 . ILE A 110 ? 1.3187 1.3771 1.1217 -0.1306 -0.0873 -0.0858 128 ILE A CG2 
778  C CD1 . ILE A 110 ? 1.5689 1.5737 1.4479 -0.1187 -0.0382 -0.1389 128 ILE A CD1 
779  N N   . MET A 111 ? 1.4735 1.4912 1.2908 -0.1191 -0.0999 0.0134  129 MET A N   
780  C CA  . MET A 111 ? 1.4152 1.4241 1.2180 -0.1131 -0.1357 0.0498  129 MET A CA  
781  C C   . MET A 111 ? 1.4636 1.4813 1.2272 -0.1322 -0.1343 0.0880  129 MET A C   
782  O O   . MET A 111 ? 1.5065 1.5412 1.2303 -0.1363 -0.1551 0.1091  129 MET A O   
783  C CB  . MET A 111 ? 1.4128 1.3731 1.2554 -0.0918 -0.1561 0.0631  129 MET A CB  
784  C CG  . MET A 111 ? 1.3422 1.3014 1.2173 -0.0683 -0.1623 0.0341  129 MET A CG  
785  S SD  . MET A 111 ? 1.2947 1.1918 1.1996 -0.0375 -0.1853 0.0461  129 MET A SD  
786  C CE  . MET A 111 ? 1.5876 1.4632 1.5247 -0.0482 -0.1570 0.0281  129 MET A CE  
787  N N   . ASP A 112 ? 1.6712 1.6842 1.4475 -0.1448 -0.1104 0.1013  130 ASP A N   
788  C CA  . ASP A 112 ? 1.7421 1.7676 1.4905 -0.1658 -0.1073 0.1459  130 ASP A CA  
789  C C   . ASP A 112 ? 1.6924 1.7724 1.3902 -0.1802 -0.0754 0.1367  130 ASP A C   
790  O O   . ASP A 112 ? 1.8048 1.9080 1.4752 -0.1983 -0.0662 0.1748  130 ASP A O   
791  C CB  . ASP A 112 ? 1.8154 1.8215 1.6071 -0.1760 -0.0976 0.1698  130 ASP A CB  
792  C CG  . ASP A 112 ? 1.8315 1.7715 1.6562 -0.1648 -0.1345 0.1833  130 ASP A CG  
793  O OD1 . ASP A 112 ? 1.9130 1.8257 1.7275 -0.1439 -0.1639 0.1763  130 ASP A OD1 
794  O OD2 . ASP A 112 ? 1.7839 1.7006 1.6433 -0.1757 -0.1348 0.2008  130 ASP A OD2 
795  N N   . LYS A 113 ? 1.7078 1.8058 1.3883 -0.1734 -0.0588 0.0877  131 LYS A N   
796  C CA  . LYS A 113 ? 1.5600 1.6982 1.1808 -0.1833 -0.0286 0.0695  131 LYS A CA  
797  C C   . LYS A 113 ? 1.6307 1.7944 1.2600 -0.1883 0.0149  0.0827  131 LYS A C   
798  O O   . LYS A 113 ? 1.7265 1.9294 1.3060 -0.1996 0.0349  0.1024  131 LYS A O   
799  C CB  . LYS A 113 ? 1.5278 1.6889 1.0816 -0.1958 -0.0517 0.0952  131 LYS A CB  
800  C CG  . LYS A 113 ? 1.8502 2.0039 1.3960 -0.1897 -0.0929 0.0814  131 LYS A CG  
801  C CD  . LYS A 113 ? 1.6658 1.8481 1.1434 -0.2020 -0.1172 0.1089  131 LYS A CD  
802  C CE  . LYS A 113 ? 1.7544 1.9436 1.2310 -0.1958 -0.1588 0.0965  131 LYS A CE  
803  N NZ  . LYS A 113 ? 1.9107 2.1322 1.3207 -0.2075 -0.1865 0.1251  131 LYS A NZ  
804  N N   . GLY A 114 ? 1.5738 1.7220 1.2679 -0.1789 0.0298  0.0745  132 GLY A N   
805  C CA  . GLY A 114 ? 1.6012 1.7837 1.3182 -0.1807 0.0703  0.0887  132 GLY A CA  
806  C C   . GLY A 114 ? 1.6299 1.8391 1.3114 -0.1669 0.1159  0.0444  132 GLY A C   
807  O O   . GLY A 114 ? 1.6404 1.8270 1.2870 -0.1581 0.1136  -0.0036 132 GLY A O   
808  N N   . GLU A 115 ? 1.7700 2.0274 1.4612 -0.1646 0.1577  0.0619  133 GLU A N   
809  C CA  . GLU A 115 ? 1.8213 2.1058 1.4719 -0.1447 0.2070  0.0232  133 GLU A CA  
810  C C   . GLU A 115 ? 1.7046 1.9936 1.4203 -0.1209 0.2395  0.0054  133 GLU A C   
811  O O   . GLU A 115 ? 1.5970 1.8547 1.2981 -0.0983 0.2563  -0.0481 133 GLU A O   
812  C CB  . GLU A 115 ? 1.8484 2.1997 1.4464 -0.1532 0.2376  0.0567  133 GLU A CB  
813  C CG  . GLU A 115 ? 1.8066 2.1561 1.3272 -0.1743 0.2078  0.0728  133 GLU A CG  
814  C CD  . GLU A 115 ? 2.0931 2.5111 1.5533 -0.1824 0.2409  0.1063  133 GLU A CD  
815  O OE1 . GLU A 115 ? 2.0100 2.4826 1.4905 -0.1693 0.2908  0.1152  133 GLU A OE1 
816  O OE2 . GLU A 115 ? 2.2746 2.6975 1.6676 -0.2005 0.2177  0.1263  133 GLU A OE2 
817  N N   . THR A 116 ? 1.8327 2.1578 1.6203 -0.1271 0.2459  0.0511  134 THR A N   
818  C CA  . THR A 116 ? 1.4843 1.8259 1.3408 -0.1049 0.2744  0.0432  134 THR A CA  
819  C C   . THR A 116 ? 1.5600 1.8726 1.4969 -0.1178 0.2364  0.0680  134 THR A C   
820  O O   . THR A 116 ? 1.9290 2.2428 1.8837 -0.1465 0.2045  0.1150  134 THR A O   
821  C CB  . THR A 116 ? 1.7967 2.2287 1.6699 -0.0983 0.3233  0.0770  134 THR A CB  
822  O OG1 . THR A 116 ? 1.5735 2.0462 1.4715 -0.1348 0.3043  0.1449  134 THR A OG1 
823  C CG2 . THR A 116 ? 1.6800 2.1384 1.4632 -0.0788 0.3658  0.0466  134 THR A CG2 
824  N N   . ARG A 117 ? 1.4087 1.6888 1.3875 -0.0963 0.2385  0.0360  135 ARG A N   
825  C CA  . ARG A 117 ? 1.5743 1.8293 1.6252 -0.1036 0.2075  0.0544  135 ARG A CA  
826  C C   . ARG A 117 ? 1.5330 1.8196 1.6451 -0.0790 0.2392  0.0495  135 ARG A C   
827  O O   . ARG A 117 ? 1.7100 1.9837 1.8056 -0.0482 0.2686  0.0061  135 ARG A O   
828  C CB  . ARG A 117 ? 1.6094 1.7873 1.6479 -0.1018 0.1695  0.0220  135 ARG A CB  
829  C CG  . ARG A 117 ? 1.5096 1.6558 1.6084 -0.1071 0.1362  0.0378  135 ARG A CG  
830  C CD  . ARG A 117 ? 1.4215 1.5615 1.5282 -0.1363 0.0991  0.0853  135 ARG A CD  
831  N NE  . ARG A 117 ? 1.5313 1.6320 1.5848 -0.1436 0.0695  0.0805  135 ARG A NE  
832  C CZ  . ARG A 117 ? 1.8119 1.8850 1.8594 -0.1627 0.0315  0.1146  135 ARG A CZ  
833  N NH1 . ARG A 117 ? 1.6690 1.7420 1.7561 -0.1827 0.0148  0.1552  135 ARG A NH1 
834  N NH2 . ARG A 117 ? 1.5867 1.6292 1.5874 -0.1620 0.0072  0.1088  135 ARG A NH2 
835  N N   . ARG A 118 ? 1.6110 1.9358 1.7931 -0.0932 0.2303  0.0949  136 ARG A N   
836  C CA  . ARG A 118 ? 1.5809 1.9556 1.8308 -0.0711 0.2595  0.1019  136 ARG A CA  
837  C C   . ARG A 118 ? 1.5999 2.0406 1.8296 -0.0419 0.3196  0.0920  136 ARG A C   
838  O O   . ARG A 118 ? 1.5954 2.0478 1.8479 -0.0034 0.3526  0.0671  136 ARG A O   
839  C CB  . ARG A 118 ? 1.5051 1.8204 1.7786 -0.0474 0.2482  0.0644  136 ARG A CB  
840  C CG  . ARG A 118 ? 1.5109 1.7800 1.8186 -0.0703 0.1954  0.0813  136 ARG A CG  
841  C CD  . ARG A 118 ? 1.4698 1.6839 1.7927 -0.0472 0.1866  0.0460  136 ARG A CD  
842  N NE  . ARG A 118 ? 1.5673 1.7423 1.9172 -0.0657 0.1393  0.0621  136 ARG A NE  
843  C CZ  . ARG A 118 ? 1.5325 1.6573 1.8909 -0.0524 0.1230  0.0390  136 ARG A CZ  
844  N NH1 . ARG A 118 ? 1.5282 1.6311 1.8753 -0.0241 0.1469  0.0017  136 ARG A NH1 
845  N NH2 . ARG A 118 ? 1.4955 1.5870 1.8692 -0.0685 0.0808  0.0542  136 ARG A NH2 
846  N N   . ASN A 119 ? 1.4941 1.9761 1.6763 -0.0577 0.3342  0.1122  137 ASN A N   
847  C CA  . ASN A 119 ? 1.5260 2.0784 1.6777 -0.0308 0.3935  0.1069  137 ASN A CA  
848  C C   . ASN A 119 ? 1.5224 2.0202 1.6090 0.0114  0.4209  0.0360  137 ASN A C   
849  O O   . ASN A 119 ? 1.3941 1.9326 1.4735 0.0517  0.4728  0.0180  137 ASN A O   
850  C CB  . ASN A 119 ? 1.5334 2.1873 1.7726 -0.0168 0.4278  0.1476  137 ASN A CB  
851  C CG  . ASN A 119 ? 1.6490 2.3714 1.9414 -0.0652 0.4070  0.2231  137 ASN A CG  
852  O OD1 . ASN A 119 ? 1.6442 2.3681 1.8892 -0.0990 0.3930  0.2485  137 ASN A OD1 
853  N ND2 . ASN A 119 ? 1.4931 2.2703 1.8839 -0.0712 0.4015  0.2617  137 ASN A ND2 
854  N N   . LYS A 120 ? 1.6059 2.0107 1.6439 0.0028  0.3857  -0.0042 138 LYS A N   
855  C CA  . LYS A 120 ? 1.4302 1.7739 1.3956 0.0306  0.4027  -0.0696 138 LYS A CA  
856  C C   . LYS A 120 ? 1.3937 1.6754 1.2906 0.0014  0.3616  -0.0896 138 LYS A C   
857  O O   . LYS A 120 ? 1.4356 1.7091 1.3527 -0.0313 0.3189  -0.0580 138 LYS A O   
858  C CB  . LYS A 120 ? 1.2562 1.5478 1.2626 0.0613  0.4058  -0.1038 138 LYS A CB  
859  C CG  . LYS A 120 ? 1.2352 1.4819 1.2996 0.0403  0.3569  -0.0917 138 LYS A CG  
860  C CD  . LYS A 120 ? 1.1496 1.3506 1.2501 0.0719  0.3642  -0.1211 138 LYS A CD  
861  C CE  . LYS A 120 ? 1.2624 1.4266 1.4171 0.0532  0.3190  -0.1064 138 LYS A CE  
862  N NZ  . LYS A 120 ? 1.1613 1.2825 1.3491 0.0823  0.3252  -0.1295 138 LYS A NZ  
863  N N   . HIS A 121 ? 1.5448 1.7820 1.3589 0.0147  0.3735  -0.1425 139 HIS A N   
864  C CA  . HIS A 121 ? 1.5368 1.7290 1.2837 -0.0131 0.3358  -0.1605 139 HIS A CA  
865  C C   . HIS A 121 ? 1.4502 1.5900 1.2425 -0.0315 0.2866  -0.1600 139 HIS A C   
866  O O   . HIS A 121 ? 1.2684 1.3737 1.1098 -0.0167 0.2857  -0.1757 139 HIS A O   
867  C CB  . HIS A 121 ? 1.3797 1.5238 1.0339 0.0025  0.3527  -0.2226 139 HIS A CB  
868  C CG  . HIS A 121 ? 1.4726 1.6637 1.0604 0.0227  0.4007  -0.2288 139 HIS A CG  
869  N ND1 . HIS A 121 ? 1.5156 1.7660 1.0606 0.0024  0.4020  -0.1937 139 HIS A ND1 
870  C CD2 . HIS A 121 ? 1.5503 1.7375 1.1030 0.0646  0.4505  -0.2656 139 HIS A CD2 
871  C CE1 . HIS A 121 ? 1.5929 1.8807 1.0784 0.0295  0.4525  -0.2080 139 HIS A CE1 
872  N NE2 . HIS A 121 ? 1.6247 1.8743 1.1130 0.0699  0.4835  -0.2536 139 HIS A NE2 
873  N N   . CYS A 122 ? 1.4476 1.5838 1.2215 -0.0610 0.2466  -0.1398 140 CYS A N   
874  C CA  . CYS A 122 ? 1.4258 1.5200 1.2373 -0.0742 0.2022  -0.1382 140 CYS A CA  
875  C C   . CYS A 122 ? 1.2433 1.2797 1.0313 -0.0686 0.1954  -0.1906 140 CYS A C   
876  O O   . CYS A 122 ? 1.2702 1.2894 0.9895 -0.0671 0.2077  -0.2278 140 CYS A O   
877  C CB  . CYS A 122 ? 1.3518 1.4546 1.1406 -0.0999 0.1634  -0.1082 140 CYS A CB  
878  S SG  . CYS A 122 ? 1.5017 1.6574 1.3172 -0.1149 0.1624  -0.0402 140 CYS A SG  
879  N N   . TRP A 123 ? 1.3732 1.3775 1.2157 -0.0678 0.1742  -0.1924 141 TRP A N   
880  C CA  . TRP A 123 ? 1.3088 1.2599 1.1409 -0.0660 0.1681  -0.2347 141 TRP A CA  
881  C C   . TRP A 123 ? 1.3849 1.3224 1.1511 -0.0881 0.1449  -0.2584 141 TRP A C   
882  O O   . TRP A 123 ? 1.4400 1.3365 1.1650 -0.0902 0.1498  -0.3004 141 TRP A O   
883  C CB  . TRP A 123 ? 1.1683 1.0994 1.0665 -0.0661 0.1448  -0.2227 141 TRP A CB  
884  C CG  . TRP A 123 ? 1.1326 1.0137 1.0295 -0.0678 0.1385  -0.2573 141 TRP A CG  
885  C CD1 . TRP A 123 ? 1.1524 1.0204 1.0508 -0.0863 0.1069  -0.2627 141 TRP A CD1 
886  C CD2 . TRP A 123 ? 1.1795 1.0181 1.0757 -0.0508 0.1642  -0.2874 141 TRP A CD2 
887  N NE1 . TRP A 123 ? 1.1531 0.9744 1.0524 -0.0879 0.1102  -0.2919 141 TRP A NE1 
888  C CE2 . TRP A 123 ? 1.2340 1.0289 1.1291 -0.0656 0.1439  -0.3085 141 TRP A CE2 
889  C CE3 . TRP A 123 ? 1.1889 1.0238 1.0872 -0.0223 0.2027  -0.2962 141 TRP A CE3 
890  C CZ2 . TRP A 123 ? 1.4162 1.1522 1.3075 -0.0565 0.1579  -0.3378 141 TRP A CZ2 
891  C CZ3 . TRP A 123 ? 1.1682 0.9448 1.0627 -0.0063 0.2179  -0.3279 141 TRP A CZ3 
892  C CH2 . TRP A 123 ? 1.2373 0.9592 1.1260 -0.0250 0.1942  -0.3484 141 TRP A CH2 
893  N N   . TYR A 124 ? 1.5282 1.4969 1.2829 -0.1055 0.1166  -0.2309 142 TYR A N   
894  C CA  . TYR A 124 ? 1.3554 1.3228 1.0543 -0.1273 0.0892  -0.2469 142 TYR A CA  
895  C C   . TYR A 124 ? 1.3478 1.3242 0.9608 -0.1315 0.1068  -0.2661 142 TYR A C   
896  O O   . TYR A 124 ? 1.3426 1.3134 0.8989 -0.1516 0.0840  -0.2861 142 TYR A O   
897  C CB  . TYR A 124 ? 1.4190 1.4172 1.1378 -0.1383 0.0516  -0.2080 142 TYR A CB  
898  C CG  . TYR A 124 ? 1.3703 1.4055 1.0637 -0.1405 0.0535  -0.1709 142 TYR A CG  
899  C CD1 . TYR A 124 ? 1.3503 1.3990 1.0853 -0.1306 0.0682  -0.1359 142 TYR A CD1 
900  C CD2 . TYR A 124 ? 1.3904 1.4483 1.0182 -0.1560 0.0375  -0.1672 142 TYR A CD2 
901  C CE1 . TYR A 124 ? 1.3617 1.4433 1.0751 -0.1381 0.0683  -0.0965 142 TYR A CE1 
902  C CE2 . TYR A 124 ? 1.3696 1.4604 0.9718 -0.1600 0.0387  -0.1282 142 TYR A CE2 
903  C CZ  . TYR A 124 ? 1.4457 1.5473 1.0919 -0.1520 0.0548  -0.0920 142 TYR A CZ  
904  O OH  . TYR A 124 ? 1.4770 1.6104 1.0994 -0.1612 0.0546  -0.0479 142 TYR A OH  
905  N N   . LEU A 125 ? 1.4056 1.4010 1.0063 -0.1133 0.1462  -0.2593 143 LEU A N   
906  C CA  . LEU A 125 ? 1.5783 1.5868 1.0911 -0.1120 0.1693  -0.2772 143 LEU A CA  
907  C C   . LEU A 125 ? 1.7456 1.7040 1.2120 -0.0939 0.2002  -0.3336 143 LEU A C   
908  O O   . LEU A 125 ? 1.8561 1.8117 1.2332 -0.0915 0.2170  -0.3602 143 LEU A O   
909  C CB  . LEU A 125 ? 1.4127 1.4805 0.9339 -0.1012 0.1990  -0.2347 143 LEU A CB  
910  C CG  . LEU A 125 ? 1.4546 1.5639 0.9947 -0.1214 0.1692  -0.1780 143 LEU A CG  
911  C CD1 . LEU A 125 ? 1.4660 1.6317 1.0166 -0.1156 0.2011  -0.1347 143 LEU A CD1 
912  C CD2 . LEU A 125 ? 1.4748 1.5877 0.9413 -0.1440 0.1362  -0.1819 143 LEU A CD2 
913  N N   . LEU A 126 ? 1.5633 1.4773 1.0815 -0.0797 0.2075  -0.3525 144 LEU A N   
914  C CA  . LEU A 126 ? 1.6264 1.4806 1.1019 -0.0579 0.2364  -0.4046 144 LEU A CA  
915  C C   . LEU A 126 ? 1.9704 1.7673 1.3611 -0.0836 0.2094  -0.4520 144 LEU A C   
916  O O   . LEU A 126 ? 1.5731 1.3722 0.9703 -0.1185 0.1642  -0.4444 144 LEU A O   
917  C CB  . LEU A 126 ? 1.6230 1.4392 1.1765 -0.0395 0.2439  -0.4077 144 LEU A CB  
918  C CG  . LEU A 126 ? 1.8397 1.6918 1.4486 -0.0007 0.2872  -0.3852 144 LEU A CG  
919  C CD1 . LEU A 126 ? 1.6453 1.5821 1.2989 -0.0086 0.2854  -0.3271 144 LEU A CD1 
920  C CD2 . LEU A 126 ? 2.0108 1.8241 1.6945 0.0146  0.2869  -0.3857 144 LEU A CD2 
921  N N   . LYS A 127 ? 1.9839 1.7298 1.2934 -0.0650 0.2370  -0.5015 145 LYS A N   
922  C CA  . LYS A 127 ? 2.0001 1.6780 1.2192 -0.0917 0.2096  -0.5522 145 LYS A CA  
923  C C   . LYS A 127 ? 1.9573 1.5808 1.2245 -0.1198 0.1709  -0.5619 145 LYS A C   
924  O O   . LYS A 127 ? 1.9938 1.6097 1.2352 -0.1626 0.1254  -0.5691 145 LYS A O   
925  C CB  . LYS A 127 ? 2.1568 1.7699 1.2831 -0.0584 0.2494  -0.6085 145 LYS A CB  
926  C CG  . LYS A 127 ? 2.3944 1.8991 1.4395 -0.0816 0.2218  -0.6703 145 LYS A CG  
927  C CD  . LYS A 127 ? 2.4144 1.8440 1.3618 -0.0396 0.2643  -0.7288 145 LYS A CD  
928  C CE  . LYS A 127 ? 2.7333 2.0400 1.6142 -0.0608 0.2302  -0.7857 145 LYS A CE  
929  N NZ  . LYS A 127 ? 2.4493 1.7027 1.4204 -0.0722 0.2098  -0.7776 145 LYS A NZ  
930  N N   . ASP A 128 ? 1.8811 1.4733 1.2204 -0.0974 0.1877  -0.5582 146 ASP A N   
931  C CA  . ASP A 128 ? 1.9956 1.5368 1.3816 -0.1220 0.1566  -0.5636 146 ASP A CA  
932  C C   . ASP A 128 ? 1.8512 1.4595 1.3279 -0.1437 0.1263  -0.5122 146 ASP A C   
933  O O   . ASP A 128 ? 1.9159 1.4990 1.4340 -0.1671 0.0997  -0.5101 146 ASP A O   
934  C CB  . ASP A 128 ? 2.0914 1.5678 1.5111 -0.0862 0.1874  -0.5791 146 ASP A CB  
935  C CG  . ASP A 128 ? 2.2519 1.6405 1.5771 -0.0615 0.2138  -0.6372 146 ASP A CG  
936  O OD1 . ASP A 128 ? 2.2556 1.6720 1.5365 -0.0258 0.2525  -0.6453 146 ASP A OD1 
937  O OD2 . ASP A 128 ? 2.4663 1.7564 1.7593 -0.0774 0.1961  -0.6743 146 ASP A OD2 
938  N N   . VAL A 129 ? 1.9575 1.6472 1.4629 -0.1359 0.1300  -0.4705 147 VAL A N   
939  C CA  . VAL A 129 ? 1.7177 1.4631 1.3009 -0.1489 0.1029  -0.4243 147 VAL A CA  
940  C C   . VAL A 129 ? 1.6610 1.4721 1.2186 -0.1624 0.0842  -0.3973 147 VAL A C   
941  O O   . VAL A 129 ? 1.8180 1.6697 1.3744 -0.1440 0.1055  -0.3726 147 VAL A O   
942  C CB  . VAL A 129 ? 1.5851 1.3493 1.2507 -0.1184 0.1260  -0.3925 147 VAL A CB  
943  C CG1 . VAL A 129 ? 1.6496 1.4528 1.3853 -0.1297 0.0962  -0.3532 147 VAL A CG1 
944  C CG2 . VAL A 129 ? 1.5187 1.2184 1.2021 -0.0984 0.1488  -0.4175 147 VAL A CG2 
945  N N   . GLU A 130 ? 1.4818 1.3071 1.0217 -0.1955 0.0432  -0.3977 148 GLU A N   
946  C CA  . GLU A 130 ? 1.7257 1.6138 1.2503 -0.2070 0.0190  -0.3662 148 GLU A CA  
947  C C   . GLU A 130 ? 1.4977 1.4277 1.1082 -0.2019 -0.0007 -0.3212 148 GLU A C   
948  O O   . GLU A 130 ? 1.3764 1.2906 1.0519 -0.1881 0.0091  -0.3144 148 GLU A O   
949  C CB  . GLU A 130 ? 1.8556 1.7439 1.3140 -0.2428 -0.0171 -0.3886 148 GLU A CB  
950  C CG  . GLU A 130 ? 1.6466 1.5163 0.9981 -0.2444 -0.0022 -0.4193 148 GLU A CG  
951  C CD  . GLU A 130 ? 1.9384 1.7293 1.2473 -0.2308 0.0310  -0.4704 148 GLU A CD  
952  O OE1 . GLU A 130 ? 2.2988 2.0352 1.6259 -0.2454 0.0185  -0.4961 148 GLU A OE1 
953  O OE2 . GLU A 130 ? 2.5216 2.3056 1.7795 -0.2039 0.0703  -0.4828 148 GLU A OE2 
954  N N   . ILE A 131 ? 1.3182 1.2991 0.9246 -0.2104 -0.0293 -0.2903 149 ILE A N   
955  C CA  . ILE A 131 ? 1.3644 1.3786 1.0420 -0.2013 -0.0505 -0.2516 149 ILE A CA  
956  C C   . ILE A 131 ? 1.5005 1.5096 1.2264 -0.2122 -0.0677 -0.2623 149 ILE A C   
957  O O   . ILE A 131 ? 1.4142 1.4270 1.2051 -0.1957 -0.0665 -0.2441 149 ILE A O   
958  C CB  . ILE A 131 ? 1.3728 1.4368 1.0292 -0.2070 -0.0817 -0.2194 149 ILE A CB  
959  C CG1 . ILE A 131 ? 1.4680 1.5389 1.0738 -0.2002 -0.0637 -0.2032 149 ILE A CG1 
960  C CG2 . ILE A 131 ? 1.4758 1.5654 1.2002 -0.1898 -0.1026 -0.1823 149 ILE A CG2 
961  C CD1 . ILE A 131 ? 1.7172 1.8225 1.2568 -0.2181 -0.0901 -0.1935 149 ILE A CD1 
962  N N   . LYS A 132 ? 1.4797 1.4806 1.1712 -0.2426 -0.0850 -0.2909 150 LYS A N   
963  C CA  . LYS A 132 ? 1.3875 1.3905 1.1247 -0.2610 -0.1029 -0.2969 150 LYS A CA  
964  C C   . LYS A 132 ? 1.4707 1.4292 1.2551 -0.2444 -0.0750 -0.3036 150 LYS A C   
965  O O   . LYS A 132 ? 1.3139 1.2930 1.1618 -0.2388 -0.0813 -0.2845 150 LYS A O   
966  C CB  . LYS A 132 ? 1.4142 1.3977 1.0970 -0.3026 -0.1241 -0.3312 150 LYS A CB  
967  C CG  . LYS A 132 ? 1.3974 1.3042 1.0060 -0.3044 -0.0981 -0.3759 150 LYS A CG  
968  C CD  . LYS A 132 ? 1.4760 1.3493 1.0244 -0.3488 -0.1254 -0.4132 150 LYS A CD  
969  C CE  . LYS A 132 ? 1.6873 1.4673 1.1611 -0.3436 -0.0973 -0.4632 150 LYS A CE  
970  N NZ  . LYS A 132 ? 1.8357 1.5615 1.2485 -0.3896 -0.1275 -0.5038 150 LYS A NZ  
971  N N   . ASN A 133 ? 1.5153 1.4158 1.2677 -0.2332 -0.0431 -0.3295 151 ASN A N   
972  C CA  . ASN A 133 ? 1.4545 1.3137 1.2507 -0.2142 -0.0173 -0.3328 151 ASN A CA  
973  C C   . ASN A 133 ? 1.4112 1.2960 1.2579 -0.1814 -0.0039 -0.2986 151 ASN A C   
974  O O   . ASN A 133 ? 1.4138 1.2888 1.3135 -0.1691 0.0024  -0.2878 151 ASN A O   
975  C CB  . ASN A 133 ? 1.5671 1.3591 1.3151 -0.2064 0.0126  -0.3700 151 ASN A CB  
976  C CG  . ASN A 133 ? 1.6010 1.3311 1.3302 -0.2322 0.0041  -0.4034 151 ASN A CG  
977  O OD1 . ASN A 133 ? 1.5710 1.3090 1.3441 -0.2531 -0.0167 -0.3924 151 ASN A OD1 
978  N ND2 . ASN A 133 ? 1.7366 1.4024 1.3983 -0.2303 0.0207  -0.4438 151 ASN A ND2 
979  N N   . ALA A 134 ? 1.3382 1.2523 1.1652 -0.1698 -0.0015 -0.2802 152 ALA A N   
980  C CA  . ALA A 134 ? 1.3926 1.3203 1.2611 -0.1440 0.0083  -0.2486 152 ALA A CA  
981  C C   . ALA A 134 ? 1.4231 1.3749 1.3434 -0.1375 -0.0151 -0.2228 152 ALA A C   
982  O O   . ALA A 134 ? 1.3067 1.2471 1.2699 -0.1192 -0.0075 -0.2095 152 ALA A O   
983  C CB  . ALA A 134 ? 1.5530 1.5061 1.3866 -0.1400 0.0116  -0.2299 152 ALA A CB  
984  N N   . VAL A 135 ? 1.3027 1.2907 1.2182 -0.1501 -0.0439 -0.2155 153 VAL A N   
985  C CA  . VAL A 135 ? 1.2716 1.2883 1.2341 -0.1367 -0.0630 -0.1921 153 VAL A CA  
986  C C   . VAL A 135 ? 1.1610 1.1630 1.1648 -0.1363 -0.0541 -0.2011 153 VAL A C   
987  O O   . VAL A 135 ? 1.0795 1.0765 1.1195 -0.1139 -0.0500 -0.1865 153 VAL A O   
988  C CB  . VAL A 135 ? 1.2344 1.3037 1.1883 -0.1486 -0.0943 -0.1819 153 VAL A CB  
989  C CG1 . VAL A 135 ? 1.2257 1.3310 1.2296 -0.1279 -0.1095 -0.1593 153 VAL A CG1 
990  C CG2 . VAL A 135 ? 1.2605 1.3427 1.1710 -0.1475 -0.1049 -0.1672 153 VAL A CG2 
991  N N   . ASN A 136 ? 1.2086 1.1987 1.2021 -0.1630 -0.0530 -0.2248 154 ASN A N   
992  C CA  . ASN A 136 ? 1.0749 1.0498 1.1049 -0.1685 -0.0461 -0.2294 154 ASN A CA  
993  C C   . ASN A 136 ? 1.1373 1.0649 1.1825 -0.1463 -0.0200 -0.2309 154 ASN A C   
994  O O   . ASN A 136 ? 1.1718 1.0988 1.2552 -0.1344 -0.0162 -0.2187 154 ASN A O   
995  C CB  . ASN A 136 ? 1.1821 1.1367 1.1890 -0.2066 -0.0523 -0.2553 154 ASN A CB  
996  C CG  . ASN A 136 ? 1.1724 1.1160 1.2178 -0.2199 -0.0503 -0.2534 154 ASN A CG  
997  O OD1 . ASN A 136 ? 1.0341 1.0322 1.1153 -0.2310 -0.0666 -0.2345 154 ASN A OD1 
998  N ND2 . ASN A 136 ? 1.4047 1.2814 1.4443 -0.2179 -0.0296 -0.2699 154 ASN A ND2 
999  N N   . ASP A 137 ? 1.1607 1.0552 1.1767 -0.1392 -0.0016 -0.2434 155 ASP A N   
1000 C CA  . ASP A 137 ? 1.1671 1.0269 1.2033 -0.1177 0.0220  -0.2418 155 ASP A CA  
1001 C C   . ASP A 137 ? 1.1259 1.0048 1.1930 -0.0942 0.0172  -0.2128 155 ASP A C   
1002 O O   . ASP A 137 ? 1.0987 0.9607 1.1969 -0.0799 0.0248  -0.2046 155 ASP A O   
1003 C CB  . ASP A 137 ? 1.2133 1.0471 1.2136 -0.1131 0.0449  -0.2599 155 ASP A CB  
1004 C CG  . ASP A 137 ? 1.3523 1.1438 1.3145 -0.1309 0.0516  -0.2952 155 ASP A CG  
1005 O OD1 . ASP A 137 ? 1.2370 1.0165 1.2078 -0.1520 0.0368  -0.3023 155 ASP A OD1 
1006 O OD2 . ASP A 137 ? 1.3777 1.1469 1.2993 -0.1241 0.0715  -0.3155 155 ASP A OD2 
1007 N N   . VAL A 138 ? 1.0753 0.9833 1.1300 -0.0905 0.0022  -0.1966 156 VAL A N   
1008 C CA  . VAL A 138 ? 1.1039 1.0157 1.1803 -0.0700 -0.0075 -0.1712 156 VAL A CA  
1009 C C   . VAL A 138 ? 1.0149 0.9343 1.1196 -0.0595 -0.0184 -0.1649 156 VAL A C   
1010 O O   . VAL A 138 ? 1.0975 0.9997 1.2222 -0.0425 -0.0176 -0.1549 156 VAL A O   
1011 C CB  . VAL A 138 ? 1.0750 1.0070 1.1284 -0.0687 -0.0250 -0.1534 156 VAL A CB  
1012 C CG1 . VAL A 138 ? 1.0323 0.9501 1.1013 -0.0494 -0.0379 -0.1293 156 VAL A CG1 
1013 C CG2 . VAL A 138 ? 1.4714 1.4047 1.4917 -0.0806 -0.0111 -0.1572 156 VAL A CG2 
1014 N N   . PHE A 139 ? 1.0370 0.9874 1.1428 -0.0701 -0.0290 -0.1693 157 PHE A N   
1015 C CA  . PHE A 139 ? 1.0155 0.9855 1.1500 -0.0591 -0.0341 -0.1609 157 PHE A CA  
1016 C C   . PHE A 139 ? 0.9779 0.9198 1.1316 -0.0630 -0.0168 -0.1677 157 PHE A C   
1017 O O   . PHE A 139 ? 0.9421 0.8830 1.1139 -0.0451 -0.0156 -0.1570 157 PHE A O   
1018 C CB  . PHE A 139 ? 0.9559 0.9793 1.0960 -0.0732 -0.0482 -0.1595 157 PHE A CB  
1019 C CG  . PHE A 139 ? 1.3499 1.4081 1.4811 -0.0571 -0.0685 -0.1444 157 PHE A CG  
1020 C CD1 . PHE A 139 ? 1.4509 1.5211 1.5954 -0.0222 -0.0761 -0.1281 157 PHE A CD1 
1021 C CD2 . PHE A 139 ? 1.4133 1.4866 1.5173 -0.0738 -0.0805 -0.1468 157 PHE A CD2 
1022 C CE1 . PHE A 139 ? 1.5083 1.6012 1.6432 -0.0022 -0.0957 -0.1135 157 PHE A CE1 
1023 C CE2 . PHE A 139 ? 1.4655 1.5682 1.5615 -0.0571 -0.1012 -0.1288 157 PHE A CE2 
1024 C CZ  . PHE A 139 ? 1.5153 1.6255 1.6287 -0.0202 -0.1089 -0.1116 157 PHE A CZ  
1025 N N   . LEU A 140 ? 0.9613 0.8752 1.1057 -0.0838 -0.0039 -0.1854 158 LEU A N   
1026 C CA  . LEU A 140 ? 0.9098 0.7880 1.0709 -0.0850 0.0114  -0.1895 158 LEU A CA  
1027 C C   . LEU A 140 ? 0.9502 0.8052 1.1232 -0.0596 0.0190  -0.1786 158 LEU A C   
1028 O O   . LEU A 140 ? 1.0152 0.8608 1.2076 -0.0501 0.0219  -0.1688 158 LEU A O   
1029 C CB  . LEU A 140 ? 1.0187 0.8577 1.1599 -0.1053 0.0234  -0.2133 158 LEU A CB  
1030 C CG  . LEU A 140 ? 0.9874 0.7774 1.1428 -0.1029 0.0393  -0.2174 158 LEU A CG  
1031 C CD1 . LEU A 140 ? 0.9737 0.7597 1.1402 -0.1287 0.0330  -0.2162 158 LEU A CD1 
1032 C CD2 . LEU A 140 ? 1.1323 0.8761 1.2637 -0.0996 0.0571  -0.2398 158 LEU A CD2 
1033 N N   . LEU A 141 ? 1.0368 0.8857 1.1982 -0.0515 0.0209  -0.1775 159 LEU A N   
1034 C CA  . LEU A 141 ? 1.1393 0.9728 1.3161 -0.0335 0.0233  -0.1637 159 LEU A CA  
1035 C C   . LEU A 141 ? 0.9816 0.8227 1.1641 -0.0178 0.0050  -0.1476 159 LEU A C   
1036 O O   . LEU A 141 ? 0.9514 0.7765 1.1477 -0.0060 0.0041  -0.1389 159 LEU A O   
1037 C CB  . LEU A 141 ? 0.9122 0.7495 1.0780 -0.0334 0.0271  -0.1601 159 LEU A CB  
1038 C CG  . LEU A 141 ? 0.8936 0.7232 1.0457 -0.0411 0.0498  -0.1781 159 LEU A CG  
1039 C CD1 . LEU A 141 ? 1.0909 0.9401 1.2259 -0.0429 0.0536  -0.1704 159 LEU A CD1 
1040 C CD2 . LEU A 141 ? 1.1176 0.9223 1.2944 -0.0297 0.0689  -0.1811 159 LEU A CD2 
1041 N N   . TYR A 142 ? 1.0122 0.8757 1.1801 -0.0146 -0.0105 -0.1441 160 TYR A N   
1042 C CA  . TYR A 142 ? 0.9718 0.8356 1.1366 0.0073  -0.0268 -0.1329 160 TYR A CA  
1043 C C   . TYR A 142 ? 1.0254 0.8976 1.2029 0.0149  -0.0206 -0.1325 160 TYR A C   
1044 O O   . TYR A 142 ? 1.0024 0.8576 1.1764 0.0333  -0.0263 -0.1258 160 TYR A O   
1045 C CB  . TYR A 142 ? 1.0005 0.8887 1.1492 0.0145  -0.0427 -0.1290 160 TYR A CB  
1046 C CG  . TYR A 142 ? 1.0456 0.9203 1.1820 0.0443  -0.0600 -0.1201 160 TYR A CG  
1047 C CD1 . TYR A 142 ? 0.9931 0.8226 1.1152 0.0521  -0.0741 -0.1125 160 TYR A CD1 
1048 C CD2 . TYR A 142 ? 1.0869 0.9934 1.2245 0.0650  -0.0625 -0.1192 160 TYR A CD2 
1049 C CE1 . TYR A 142 ? 1.0513 0.8524 1.1515 0.0800  -0.0929 -0.1088 160 TYR A CE1 
1050 C CE2 . TYR A 142 ? 1.0736 0.9608 1.1916 0.0995  -0.0762 -0.1153 160 TYR A CE2 
1051 C CZ  . TYR A 142 ? 1.2005 1.0273 1.2953 0.1070  -0.0925 -0.1125 160 TYR A CZ  
1052 O OH  . TYR A 142 ? 1.2372 1.0292 1.3022 0.1418  -0.1091 -0.1129 160 TYR A OH  
1053 N N   . ASN A 143 ? 1.3540 1.2514 1.5430 -0.0019 -0.0103 -0.1383 161 ASN A N   
1054 C CA  . ASN A 143 ? 1.3377 1.2476 1.5410 -0.0001 -0.0025 -0.1322 161 ASN A CA  
1055 C C   . ASN A 143 ? 1.3297 1.2003 1.5416 -0.0017 0.0079  -0.1301 161 ASN A C   
1056 O O   . ASN A 143 ? 1.3245 1.1946 1.5388 0.0101  0.0097  -0.1196 161 ASN A O   
1057 C CB  . ASN A 143 ? 1.3454 1.2922 1.5621 -0.0257 0.0020  -0.1345 161 ASN A CB  
1058 C CG  . ASN A 143 ? 1.4402 1.4458 1.6592 -0.0176 -0.0090 -0.1280 161 ASN A CG  
1059 O OD1 . ASN A 143 ? 1.4492 1.4809 1.6695 0.0102  -0.0107 -0.1172 161 ASN A OD1 
1060 N ND2 . ASN A 143 ? 1.4764 1.5042 1.6933 -0.0386 -0.0169 -0.1347 161 ASN A ND2 
1061 N N   . ALA A 144 ? 1.1410 0.9819 1.3561 -0.0132 0.0156  -0.1387 162 ALA A N   
1062 C CA  . ALA A 144 ? 1.2756 1.0829 1.5040 -0.0099 0.0250  -0.1343 162 ALA A CA  
1063 C C   . ALA A 144 ? 0.8434 0.6411 1.0707 0.0109  0.0137  -0.1213 162 ALA A C   
1064 O O   . ALA A 144 ? 0.8916 0.6742 1.1276 0.0177  0.0152  -0.1109 162 ALA A O   
1065 C CB  . ALA A 144 ? 1.2971 1.0811 1.5284 -0.0179 0.0376  -0.1467 162 ALA A CB  
1066 N N   . ILE A 145 ? 1.0145 0.8160 1.2280 0.0188  -0.0009 -0.1204 163 ILE A N   
1067 C CA  . ILE A 145 ? 0.9237 0.7077 1.1286 0.0341  -0.0185 -0.1098 163 ILE A CA  
1068 C C   . ILE A 145 ? 0.9524 0.7373 1.1443 0.0488  -0.0219 -0.1048 163 ILE A C   
1069 O O   . ILE A 145 ? 0.7682 0.5373 0.9628 0.0540  -0.0248 -0.0956 163 ILE A O   
1070 C CB  . ILE A 145 ? 0.7216 0.5012 0.9059 0.0389  -0.0374 -0.1096 163 ILE A CB  
1071 C CG1 . ILE A 145 ? 0.9051 0.6886 1.1003 0.0230  -0.0326 -0.1086 163 ILE A CG1 
1072 C CG2 . ILE A 145 ? 0.8540 0.6030 1.0199 0.0521  -0.0610 -0.1016 163 ILE A CG2 
1073 C CD1 . ILE A 145 ? 1.0382 0.8211 1.2117 0.0229  -0.0487 -0.1059 163 ILE A CD1 
1074 N N   . TYR A 146 ? 0.9039 0.7141 1.0816 0.0572  -0.0210 -0.1088 164 TYR A N   
1075 C CA  . TYR A 146 ? 0.8071 0.6284 0.9684 0.0753  -0.0201 -0.1031 164 TYR A CA  
1076 C C   . TYR A 146 ? 0.8084 0.6404 0.9892 0.0622  -0.0028 -0.0935 164 TYR A C   
1077 O O   . TYR A 146 ? 0.9394 0.7707 1.1065 0.0743  -0.0020 -0.0833 164 TYR A O   
1078 C CB  . TYR A 146 ? 0.8364 0.6950 0.9852 0.0913  -0.0199 -0.1068 164 TYR A CB  
1079 C CG  . TYR A 146 ? 0.8169 0.6530 0.9402 0.1094  -0.0400 -0.1138 164 TYR A CG  
1080 C CD1 . TYR A 146 ? 0.7632 0.5669 0.8472 0.1389  -0.0557 -0.1168 164 TYR A CD1 
1081 C CD2 . TYR A 146 ? 0.8631 0.7026 0.9954 0.0963  -0.0452 -0.1173 164 TYR A CD2 
1082 C CE1 . TYR A 146 ? 0.8103 0.5790 0.8673 0.1542  -0.0775 -0.1225 164 TYR A CE1 
1083 C CE2 . TYR A 146 ? 0.8511 0.6643 0.9594 0.1108  -0.0654 -0.1189 164 TYR A CE2 
1084 C CZ  . TYR A 146 ? 0.8510 0.6251 0.9230 0.1393  -0.0823 -0.1212 164 TYR A CZ  
1085 O OH  . TYR A 146 ? 0.7882 0.5223 0.8325 0.1527  -0.1057 -0.1222 164 TYR A OH  
1086 N N   . LYS A 147 ? 0.7805 0.6161 0.9875 0.0375  0.0099  -0.0961 165 LYS A N   
1087 C CA  . LYS A 147 ? 0.8702 0.6995 1.0938 0.0230  0.0232  -0.0855 165 LYS A CA  
1088 C C   . LYS A 147 ? 0.8129 0.6064 1.0378 0.0322  0.0192  -0.0752 165 LYS A C   
1089 O O   . LYS A 147 ? 0.7305 0.5236 0.9498 0.0371  0.0212  -0.0590 165 LYS A O   
1090 C CB  . LYS A 147 ? 0.9556 0.7757 1.1981 -0.0042 0.0332  -0.0955 165 LYS A CB  
1091 C CG  . LYS A 147 ? 0.8575 0.6566 1.1143 -0.0221 0.0442  -0.0847 165 LYS A CG  
1092 C CD  . LYS A 147 ? 0.9316 0.7718 1.1904 -0.0314 0.0482  -0.0668 165 LYS A CD  
1093 C CE  . LYS A 147 ? 1.1089 0.9213 1.3789 -0.0490 0.0562  -0.0481 165 LYS A CE  
1094 N NZ  . LYS A 147 ? 1.1999 1.0623 1.4756 -0.0636 0.0620  -0.0251 165 LYS A NZ  
1095 N N   . LEU A 148 ? 0.8737 0.6439 1.1074 0.0343  0.0131  -0.0810 166 LEU A N   
1096 C CA  . LEU A 148 ? 0.7662 0.5134 1.0092 0.0431  0.0062  -0.0680 166 LEU A CA  
1097 C C   . LEU A 148 ? 0.8956 0.6426 1.1097 0.0595  -0.0130 -0.0592 166 LEU A C   
1098 O O   . LEU A 148 ? 0.8793 0.6161 1.0908 0.0654  -0.0181 -0.0433 166 LEU A O   
1099 C CB  . LEU A 148 ? 0.8460 0.5851 1.1093 0.0419  0.0042  -0.0729 166 LEU A CB  
1100 C CG  . LEU A 148 ? 0.7077 0.4409 0.9891 0.0310  0.0248  -0.0857 166 LEU A CG  
1101 C CD1 . LEU A 148 ? 0.9230 0.6632 1.2173 0.0324  0.0255  -0.0901 166 LEU A CD1 
1102 C CD2 . LEU A 148 ? 0.8948 0.6021 1.1950 0.0321  0.0380  -0.0780 166 LEU A CD2 
1103 N N   . LEU A 149 ? 0.7879 0.5402 0.9747 0.0684  -0.0258 -0.0698 167 LEU A N   
1104 C CA  . LEU A 149 ? 0.7308 0.4707 0.8774 0.0869  -0.0454 -0.0674 167 LEU A CA  
1105 C C   . LEU A 149 ? 0.9023 0.6591 1.0290 0.0966  -0.0340 -0.0580 167 LEU A C   
1106 O O   . LEU A 149 ? 0.8734 0.6165 0.9753 0.1063  -0.0450 -0.0478 167 LEU A O   
1107 C CB  . LEU A 149 ? 0.8276 0.5616 0.9437 0.0990  -0.0588 -0.0825 167 LEU A CB  
1108 C CG  . LEU A 149 ? 0.9001 0.6129 1.0259 0.0885  -0.0760 -0.0861 167 LEU A CG  
1109 C CD1 . LEU A 149 ? 0.9579 0.6590 1.0508 0.1021  -0.0886 -0.0984 167 LEU A CD1 
1110 C CD2 . LEU A 149 ? 1.0297 0.7143 1.1542 0.0835  -0.1003 -0.0755 167 LEU A CD2 
1111 N N   . ASP A 150 ? 0.9807 0.7719 1.1175 0.0916  -0.0129 -0.0584 168 ASP A N   
1112 C CA  . ASP A 150 ? 0.9417 0.7605 1.0668 0.0958  0.0016  -0.0431 168 ASP A CA  
1113 C C   . ASP A 150 ? 0.8649 0.6660 1.0073 0.0824  0.0056  -0.0222 168 ASP A C   
1114 O O   . ASP A 150 ? 0.9212 0.7250 1.0380 0.0920  0.0048  -0.0056 168 ASP A O   
1115 C CB  . ASP A 150 ? 0.9048 0.7715 1.0508 0.0843  0.0211  -0.0428 168 ASP A CB  
1116 C CG  . ASP A 150 ? 0.9458 0.8567 1.0814 0.0885  0.0376  -0.0229 168 ASP A CG  
1117 O OD1 . ASP A 150 ? 1.0040 0.9074 1.1037 0.1077  0.0344  -0.0138 168 ASP A OD1 
1118 O OD2 . ASP A 150 ? 0.8239 0.7807 0.9864 0.0706  0.0529  -0.0145 168 ASP A OD2 
1119 N N   . VAL A 151 ? 0.8895 0.6701 1.0712 0.0634  0.0101  -0.0224 169 VAL A N   
1120 C CA  . VAL A 151 ? 0.9517 0.7093 1.1530 0.0542  0.0149  -0.0019 169 VAL A CA  
1121 C C   . VAL A 151 ? 0.9810 0.7195 1.1674 0.0700  -0.0044 0.0108  169 VAL A C   
1122 O O   . VAL A 151 ? 0.8159 0.5484 0.9954 0.0715  -0.0046 0.0348  169 VAL A O   
1123 C CB  . VAL A 151 ? 0.8680 0.6001 1.1079 0.0388  0.0237  -0.0107 169 VAL A CB  
1124 C CG1 . VAL A 151 ? 0.8359 0.5334 1.0959 0.0407  0.0239  0.0085  169 VAL A CG1 
1125 C CG2 . VAL A 151 ? 0.8835 0.6279 1.1331 0.0159  0.0393  -0.0178 169 VAL A CG2 
1126 N N   . TYR A 152 ? 0.9505 0.6800 1.1314 0.0788  -0.0237 -0.0019 170 TYR A N   
1127 C CA  . TYR A 152 ? 0.9640 0.6772 1.1416 0.0866  -0.0470 0.0114  170 TYR A CA  
1128 C C   . TYR A 152 ? 1.0068 0.7161 1.1272 0.1006  -0.0700 0.0092  170 TYR A C   
1129 O O   . TYR A 152 ? 1.0293 0.7279 1.1365 0.1048  -0.0904 0.0252  170 TYR A O   
1130 C CB  . TYR A 152 ? 0.9604 0.6678 1.1741 0.0819  -0.0570 0.0046  170 TYR A CB  
1131 C CG  . TYR A 152 ? 0.9283 0.6323 1.1936 0.0767  -0.0375 0.0101  170 TYR A CG  
1132 C CD1 . TYR A 152 ? 0.8686 0.5657 1.1626 0.0835  -0.0417 0.0330  170 TYR A CD1 
1133 C CD2 . TYR A 152 ? 1.0341 0.7392 1.3152 0.0677  -0.0160 -0.0083 170 TYR A CD2 
1134 C CE1 . TYR A 152 ? 0.8972 0.5837 1.2337 0.0864  -0.0223 0.0356  170 TYR A CE1 
1135 C CE2 . TYR A 152 ? 1.0497 0.7413 1.3666 0.0668  0.0021  -0.0084 170 TYR A CE2 
1136 C CZ  . TYR A 152 ? 0.9529 0.6330 1.2972 0.0785  0.0002  0.0126  170 TYR A CZ  
1137 O OH  . TYR A 152 ? 1.0298 0.6894 1.4055 0.0849  0.0196  0.0101  170 TYR A OH  
1138 N N   . LEU A 153 ? 1.2130 0.9281 1.2957 0.1102  -0.0687 -0.0106 171 LEU A N   
1139 C CA  . LEU A 153 ? 1.2660 0.9621 1.2860 0.1278  -0.0932 -0.0204 171 LEU A CA  
1140 C C   . LEU A 153 ? 1.1886 0.9037 1.1581 0.1494  -0.0776 -0.0286 171 LEU A C   
1141 O O   . LEU A 153 ? 1.1828 0.8753 1.0916 0.1706  -0.0948 -0.0446 171 LEU A O   
1142 C CB  . LEU A 153 ? 1.1303 0.7995 1.1463 0.1254  -0.1168 -0.0395 171 LEU A CB  
1143 C CG  . LEU A 153 ? 1.3262 0.9834 1.3826 0.1065  -0.1389 -0.0280 171 LEU A CG  
1144 C CD1 . LEU A 153 ? 1.0910 0.7676 1.2103 0.0917  -0.1190 -0.0283 171 LEU A CD1 
1145 C CD2 . LEU A 153 ? 1.2489 0.8677 1.2667 0.1050  -0.1786 -0.0381 171 LEU A CD2 
1146 N N   . ARG A 154 ? 1.2500 0.5248 0.9763 0.0123  -0.0748 0.0683  172 ARG A N   
1147 C CA  . ARG A 154 ? 1.2529 0.5493 0.9965 0.0034  -0.0406 0.1060  172 ARG A CA  
1148 C C   . ARG A 154 ? 1.3196 0.6095 1.0084 0.0242  -0.0178 0.1180  172 ARG A C   
1149 O O   . ARG A 154 ? 1.5366 0.8564 1.2248 0.0306  0.0147  0.1280  172 ARG A O   
1150 C CB  . ARG A 154 ? 1.2157 0.5001 0.9985 -0.0220 -0.0458 0.1437  172 ARG A CB  
1151 C CG  . ARG A 154 ? 1.5096 0.8307 1.3291 -0.0345 -0.0099 0.1797  172 ARG A CG  
1152 C CD  . ARG A 154 ? 1.2907 0.5962 1.1326 -0.0553 -0.0060 0.2261  172 ARG A CD  
1153 N NE  . ARG A 154 ? 1.5179 0.8199 1.4204 -0.0819 -0.0314 0.2305  172 ARG A NE  
1154 C CZ  . ARG A 154 ? 1.3005 0.6410 1.2653 -0.0998 -0.0214 0.2424  172 ARG A CZ  
1155 N NH1 . ARG A 154 ? 1.1444 0.5310 1.1222 -0.0939 0.0146  0.2516  172 ARG A NH1 
1156 N NH2 . ARG A 154 ? 1.5532 0.8854 1.5684 -0.1223 -0.0503 0.2432  172 ARG A NH2 
1157 N N   . ASN A 155 ? 1.3744 0.6250 1.0144 0.0372  -0.0353 0.1161  173 ASN A N   
1158 C CA  . ASN A 155 ? 1.3608 0.6015 0.9408 0.0592  -0.0168 0.1282  173 ASN A CA  
1159 C C   . ASN A 155 ? 1.5298 0.7853 1.0746 0.0854  -0.0132 0.0886  173 ASN A C   
1160 O O   . ASN A 155 ? 1.6535 0.9107 1.1515 0.1056  0.0069  0.0950  173 ASN A O   
1161 C CB  . ASN A 155 ? 1.8346 1.0245 1.3725 0.0654  -0.0401 0.1409  173 ASN A CB  
1162 C CG  . ASN A 155 ? 1.7783 0.9482 1.3482 0.0391  -0.0415 0.1857  173 ASN A CG  
1163 O OD1 . ASN A 155 ? 1.4556 0.6530 1.0649 0.0207  -0.0141 0.2178  173 ASN A OD1 
1164 N ND2 . ASN A 155 ? 1.9581 1.0800 1.5149 0.0373  -0.0748 0.1877  173 ASN A ND2 
1165 N N   . ASP A 156 ? 1.5303 0.7967 1.0964 0.0856  -0.0321 0.0484  174 ASP A N   
1166 C CA  . ASP A 156 ? 1.5832 0.8632 1.1245 0.1070  -0.0308 0.0108  174 ASP A CA  
1167 C C   . ASP A 156 ? 1.5508 0.8654 1.1060 0.1090  0.0034  0.0162  174 ASP A C   
1168 O O   . ASP A 156 ? 1.4071 0.7447 1.0091 0.0906  0.0203  0.0373  174 ASP A O   
1169 C CB  . ASP A 156 ? 1.5525 0.8388 1.1198 0.1034  -0.0573 -0.0294 174 ASP A CB  
1170 C CG  . ASP A 156 ? 1.6675 0.9603 1.2079 0.1250  -0.0636 -0.0694 174 ASP A CG  
1171 O OD1 . ASP A 156 ? 1.9797 1.2856 1.5031 0.1371  -0.0419 -0.0716 174 ASP A OD1 
1172 O OD2 . ASP A 156 ? 1.4219 0.7076 0.9603 0.1304  -0.0910 -0.0998 174 ASP A OD2 
1173 N N   . ASN A 157 ? 1.6623 0.9800 1.1771 0.1335  0.0113  -0.0053 175 ASN A N   
1174 C CA  . ASN A 157 ? 1.5874 0.9328 1.1062 0.1415  0.0431  -0.0020 175 ASN A CA  
1175 C C   . ASN A 157 ? 1.4420 0.8151 1.0182 0.1275  0.0465  -0.0179 175 ASN A C   
1176 O O   . ASN A 157 ? 1.5172 0.9144 1.1103 0.1300  0.0728  -0.0094 175 ASN A O   
1177 C CB  . ASN A 157 ? 1.6051 0.9427 1.0656 0.1729  0.0443  -0.0282 175 ASN A CB  
1178 C CG  . ASN A 157 ? 2.0402 1.3502 1.4354 0.1907  0.0418  -0.0110 175 ASN A CG  
1179 O OD1 . ASN A 157 ? 2.0725 1.3872 1.4416 0.1984  0.0696  0.0208  175 ASN A OD1 
1180 N ND2 . ASN A 157 ? 2.0440 1.3264 1.4122 0.1983  0.0090  -0.0312 175 ASN A ND2 
1181 N N   . CYS A 158 ? 1.3241 0.6949 0.9289 0.1146  0.0213  -0.0399 176 CYS A N   
1182 C CA  . CYS A 158 ? 1.3931 0.7876 1.0463 0.1024  0.0229  -0.0548 176 CYS A CA  
1183 C C   . CYS A 158 ? 1.2301 0.6342 0.9329 0.0767  0.0176  -0.0350 176 CYS A C   
1184 O O   . CYS A 158 ? 1.1919 0.6096 0.9290 0.0657  0.0093  -0.0499 176 CYS A O   
1185 C CB  . CYS A 158 ? 1.4577 0.8487 1.1070 0.1083  0.0010  -0.0966 176 CYS A CB  
1186 S SG  . CYS A 158 ? 1.1833 0.5580 0.8338 0.1001  -0.0342 -0.1101 176 CYS A SG  
1187 N N   . TYR A 159 ? 1.2337 0.6305 0.9407 0.0667  0.0214  -0.0013 177 TYR A N   
1188 C CA  . TYR A 159 ? 1.2327 0.6358 0.9874 0.0425  0.0115  0.0152  177 TYR A CA  
1189 C C   . TYR A 159 ? 1.1422 0.5786 0.9443 0.0327  0.0284  0.0223  177 TYR A C   
1190 O O   . TYR A 159 ? 1.0557 0.5019 0.8909 0.0202  0.0146  0.0120  177 TYR A O   
1191 C CB  . TYR A 159 ? 1.1601 0.5478 0.9140 0.0326  0.0134  0.0523  177 TYR A CB  
1192 C CG  . TYR A 159 ? 1.1804 0.5714 0.9853 0.0073  -0.0005 0.0687  177 TYR A CG  
1193 C CD1 . TYR A 159 ? 1.1769 0.5547 0.9921 0.0000  -0.0325 0.0464  177 TYR A CD1 
1194 C CD2 . TYR A 159 ? 1.0953 0.5044 0.9389 -0.0083 0.0175  0.1051  177 TYR A CD2 
1195 C CE1 . TYR A 159 ? 1.0366 0.4155 0.8950 -0.0209 -0.0483 0.0580  177 TYR A CE1 
1196 C CE2 . TYR A 159 ? 1.1111 0.5226 1.0039 -0.0316 0.0009  0.1178  177 TYR A CE2 
1197 C CZ  . TYR A 159 ? 1.0086 0.4029 0.9062 -0.0372 -0.0331 0.0932  177 TYR A CZ  
1198 O OH  . TYR A 159 ? 1.2563 0.6513 1.1997 -0.0581 -0.0526 0.1026  177 TYR A OH  
1199 N N   . LEU A 160 ? 0.9941 0.4490 0.7980 0.0405  0.0583  0.0397  178 LEU A N   
1200 C CA  . LEU A 160 ? 0.9749 0.4615 0.8247 0.0342  0.0741  0.0472  178 LEU A CA  
1201 C C   . LEU A 160 ? 1.1331 0.6243 0.9866 0.0403  0.0677  0.0148  178 LEU A C   
1202 O O   . LEU A 160 ? 1.0608 0.5680 0.9539 0.0287  0.0635  0.0146  178 LEU A O   
1203 C CB  . LEU A 160 ? 1.0266 0.5336 0.8747 0.0459  0.1083  0.0693  178 LEU A CB  
1204 C CG  . LEU A 160 ? 1.2626 0.7706 1.1101 0.0389  0.1215  0.1074  178 LEU A CG  
1205 C CD1 . LEU A 160 ? 1.3654 0.9108 1.2396 0.0439  0.1568  0.1322  178 LEU A CD1 
1206 C CD2 . LEU A 160 ? 1.3920 0.8906 1.2744 0.0121  0.0988  0.1246  178 LEU A CD2 
1207 N N   . ASP A 161 ? 1.1535 0.6302 0.9666 0.0582  0.0659  -0.0120 179 ASP A N   
1208 C CA  . ASP A 161 ? 1.0690 0.5481 0.8890 0.0615  0.0590  -0.0419 179 ASP A CA  
1209 C C   . ASP A 161 ? 0.9844 0.4629 0.8262 0.0444  0.0351  -0.0523 179 ASP A C   
1210 O O   . ASP A 161 ? 1.0705 0.5622 0.9416 0.0367  0.0344  -0.0578 179 ASP A O   
1211 C CB  . ASP A 161 ? 1.3471 0.8089 1.1223 0.0816  0.0554  -0.0705 179 ASP A CB  
1212 C CG  . ASP A 161 ? 1.5570 1.0182 1.3008 0.1026  0.0780  -0.0627 179 ASP A CG  
1213 O OD1 . ASP A 161 ? 1.5893 1.0696 1.3544 0.1032  0.1009  -0.0407 179 ASP A OD1 
1214 O OD2 . ASP A 161 ? 1.7279 1.1715 1.4251 0.1203  0.0726  -0.0794 179 ASP A OD2 
1215 N N   . LEU A 162 ? 1.0821 0.5449 0.9081 0.0399  0.0154  -0.0545 180 LEU A N   
1216 C CA  . LEU A 162 ? 1.0439 0.5074 0.8857 0.0277  -0.0075 -0.0678 180 LEU A CA  
1217 C C   . LEU A 162 ? 1.0955 0.5746 0.9783 0.0103  -0.0089 -0.0475 180 LEU A C   
1218 O O   . LEU A 162 ? 1.0924 0.5842 0.9955 0.0029  -0.0157 -0.0570 180 LEU A O   
1219 C CB  . LEU A 162 ? 1.0543 0.4951 0.8689 0.0305  -0.0295 -0.0759 180 LEU A CB  
1220 C CG  . LEU A 162 ? 1.0263 0.4545 0.8034 0.0481  -0.0362 -0.1035 180 LEU A CG  
1221 C CD1 . LEU A 162 ? 1.2524 0.6548 0.9996 0.0543  -0.0562 -0.1048 180 LEU A CD1 
1222 C CD2 . LEU A 162 ? 1.1307 0.5730 0.9211 0.0468  -0.0449 -0.1337 180 LEU A CD2 
1223 N N   . ILE A 163 ? 0.9861 0.4655 0.8822 0.0033  -0.0030 -0.0186 181 ILE A N   
1224 C CA  . ILE A 163 ? 1.0160 0.5108 0.9547 -0.0134 -0.0087 -0.0011 181 ILE A CA  
1225 C C   . ILE A 163 ? 0.9641 0.4840 0.9305 -0.0130 0.0073  0.0022  181 ILE A C   
1226 O O   . ILE A 163 ? 0.9456 0.4780 0.9384 -0.0226 -0.0031 0.0024  181 ILE A O   
1227 C CB  . ILE A 163 ? 0.9147 0.4068 0.8698 -0.0232 -0.0056 0.0306  181 ILE A CB  
1228 C CG1 . ILE A 163 ? 1.0746 0.5779 1.0257 -0.0138 0.0258  0.0504  181 ILE A CG1 
1229 C CG2 . ILE A 163 ? 1.1384 0.5993 1.0681 -0.0251 -0.0267 0.0280  181 ILE A CG2 
1230 C CD1 . ILE A 163 ? 1.0981 0.6018 1.0657 -0.0245 0.0331  0.0851  181 ILE A CD1 
1231 N N   . THR A 164 ? 1.0016 0.5273 0.9596 0.0002  0.0311  0.0037  182 THR A N   
1232 C CA  . THR A 164 ? 1.0526 0.5975 1.0366 0.0031  0.0446  0.0056  182 THR A CA  
1233 C C   . THR A 164 ? 0.9928 0.5334 0.9705 0.0041  0.0354  -0.0194 182 THR A C   
1234 O O   . THR A 164 ? 0.9841 0.5374 0.9876 -0.0006 0.0357  -0.0157 182 THR A O   
1235 C CB  . THR A 164 ? 1.0156 0.5666 0.9918 0.0197  0.0717  0.0120  182 THR A CB  
1236 O OG1 . THR A 164 ? 1.2785 0.8094 1.2097 0.0345  0.0733  -0.0097 182 THR A OG1 
1237 C CG2 . THR A 164 ? 1.1551 0.7193 1.1461 0.0165  0.0855  0.0425  182 THR A CG2 
1238 N N   . SER A 165 ? 0.9642 0.4883 0.9097 0.0098  0.0269  -0.0435 183 SER A N   
1239 C CA  . SER A 165 ? 0.9813 0.5052 0.9262 0.0071  0.0177  -0.0653 183 SER A CA  
1240 C C   . SER A 165 ? 0.8216 0.3553 0.7837 -0.0071 0.0010  -0.0614 183 SER A C   
1241 O O   . SER A 165 ? 0.9691 0.5131 0.9466 -0.0122 0.0010  -0.0626 183 SER A O   
1242 C CB  . SER A 165 ? 0.9192 0.4283 0.8318 0.0150  0.0089  -0.0918 183 SER A CB  
1243 O OG  . SER A 165 ? 1.1851 0.6834 1.0754 0.0305  0.0214  -0.0964 183 SER A OG  
1244 N N   . PHE A 166 ? 0.9623 0.4911 0.9202 -0.0127 -0.0142 -0.0565 184 PHE A N   
1245 C CA  . PHE A 166 ? 0.9181 0.4551 0.8899 -0.0236 -0.0326 -0.0547 184 PHE A CA  
1246 C C   . PHE A 166 ? 0.9681 0.5222 0.9733 -0.0305 -0.0276 -0.0330 184 PHE A C   
1247 O O   . PHE A 166 ? 0.9212 0.4863 0.9353 -0.0352 -0.0354 -0.0348 184 PHE A O   
1248 C CB  . PHE A 166 ? 1.1096 0.6326 1.0730 -0.0273 -0.0518 -0.0535 184 PHE A CB  
1249 C CG  . PHE A 166 ? 1.0334 0.5435 0.9676 -0.0208 -0.0667 -0.0796 184 PHE A CG  
1250 C CD1 . PHE A 166 ? 0.8897 0.3862 0.7981 -0.0097 -0.0608 -0.0909 184 PHE A CD1 
1251 C CD2 . PHE A 166 ? 0.9690 0.4825 0.9009 -0.0236 -0.0875 -0.0943 184 PHE A CD2 
1252 C CE1 . PHE A 166 ? 0.9179 0.4053 0.8032 -0.0023 -0.0764 -0.1157 184 PHE A CE1 
1253 C CE2 . PHE A 166 ? 0.9603 0.4660 0.8687 -0.0154 -0.1009 -0.1197 184 PHE A CE2 
1254 C CZ  . PHE A 166 ? 0.9924 0.4855 0.8797 -0.0051 -0.0958 -0.1301 184 PHE A CZ  
1255 N N   . ARG A 167 ? 1.0169 0.5755 1.0404 -0.0298 -0.0142 -0.0118 185 ARG A N   
1256 C CA  . ARG A 167 ? 1.0128 0.5911 1.0730 -0.0342 -0.0095 0.0085  185 ARG A CA  
1257 C C   . ARG A 167 ? 1.1303 0.7154 1.1943 -0.0294 -0.0013 0.0033  185 ARG A C   
1258 O O   . ARG A 167 ? 1.2633 0.8592 1.3425 -0.0346 -0.0112 0.0089  185 ARG A O   
1259 C CB  . ARG A 167 ? 1.0264 0.6135 1.1057 -0.0307 0.0100  0.0298  185 ARG A CB  
1260 C CG  . ARG A 167 ? 1.2569 0.8448 1.3522 -0.0413 0.0019  0.0475  185 ARG A CG  
1261 C CD  . ARG A 167 ? 1.5449 1.1392 1.6450 -0.0353 0.0271  0.0660  185 ARG A CD  
1262 N NE  . ARG A 167 ? 1.2754 0.8965 1.4079 -0.0287 0.0479  0.0806  185 ARG A NE  
1263 C CZ  . ARG A 167 ? 1.2676 0.8906 1.3876 -0.0119 0.0675  0.0719  185 ARG A CZ  
1264 N NH1 . ARG A 167 ? 1.3567 0.9577 1.4359 -0.0020 0.0680  0.0480  185 ARG A NH1 
1265 N NH2 . ARG A 167 ? 1.3458 0.9938 1.4982 -0.0042 0.0856  0.0862  185 ARG A NH2 
1266 N N   . GLU A 168 ? 0.9272 0.5037 0.9762 -0.0189 0.0153  -0.0072 186 GLU A N   
1267 C CA  . GLU A 168 ? 0.9155 0.4932 0.9719 -0.0149 0.0236  -0.0099 186 GLU A CA  
1268 C C   . GLU A 168 ? 0.9490 0.5252 0.9942 -0.0224 0.0109  -0.0223 186 GLU A C   
1269 O O   . GLU A 168 ? 1.1495 0.7320 1.2072 -0.0252 0.0101  -0.0141 186 GLU A O   
1270 C CB  . GLU A 168 ? 1.1080 0.6729 1.1513 -0.0018 0.0410  -0.0217 186 GLU A CB  
1271 C CG  . GLU A 168 ? 1.1797 0.7518 1.2375 0.0098  0.0589  -0.0073 186 GLU A CG  
1272 C CD  . GLU A 168 ? 1.3958 0.9839 1.4900 0.0102  0.0625  0.0118  186 GLU A CD  
1273 O OE1 . GLU A 168 ? 1.1885 0.7753 1.2902 0.0042  0.0532  0.0120  186 GLU A OE1 
1274 O OE2 . GLU A 168 ? 1.3033 0.9070 1.4186 0.0173  0.0749  0.0275  186 GLU A OE2 
1275 N N   . ALA A 169 ? 0.9057 0.4751 0.9268 -0.0245 0.0018  -0.0414 187 ALA A N   
1276 C CA  . ALA A 169 ? 0.9418 0.5163 0.9534 -0.0307 -0.0078 -0.0532 187 ALA A CA  
1277 C C   . ALA A 169 ? 1.1307 0.7185 1.1506 -0.0373 -0.0221 -0.0409 187 ALA A C   
1278 O O   . ALA A 169 ? 1.2577 0.8540 1.2786 -0.0406 -0.0227 -0.0374 187 ALA A O   
1279 C CB  . ALA A 169 ? 1.2678 0.8368 1.2555 -0.0293 -0.0168 -0.0766 187 ALA A CB  
1280 N N   . THR A 170 ? 1.2430 0.8319 1.2691 -0.0394 -0.0345 -0.0335 188 THR A N   
1281 C CA  . THR A 170 ? 1.2595 0.8599 1.2946 -0.0447 -0.0524 -0.0246 188 THR A CA  
1282 C C   . THR A 170 ? 1.2707 0.8819 1.3298 -0.0445 -0.0465 -0.0038 188 THR A C   
1283 O O   . THR A 170 ? 1.2936 0.9143 1.3504 -0.0460 -0.0567 0.0004  188 THR A O   
1284 C CB  . THR A 170 ? 1.1849 0.7808 1.2285 -0.0486 -0.0684 -0.0208 188 THR A CB  
1285 O OG1 . THR A 170 ? 1.0771 0.6585 1.0966 -0.0467 -0.0748 -0.0395 188 THR A OG1 
1286 C CG2 . THR A 170 ? 1.4309 1.0364 1.4823 -0.0534 -0.0924 -0.0173 188 THR A CG2 
1287 N N   . LEU A 171 ? 1.3176 0.9284 1.3982 -0.0404 -0.0306 0.0092  189 LEU A N   
1288 C CA  . LEU A 171 ? 1.1306 0.7517 1.2368 -0.0374 -0.0260 0.0281  189 LEU A CA  
1289 C C   . LEU A 171 ? 1.0945 0.7108 1.1885 -0.0354 -0.0199 0.0266  189 LEU A C   
1290 O O   . LEU A 171 ? 1.3313 0.9553 1.4310 -0.0356 -0.0280 0.0390  189 LEU A O   
1291 C CB  . LEU A 171 ? 1.2072 0.8301 1.3368 -0.0299 -0.0072 0.0387  189 LEU A CB  
1292 C CG  . LEU A 171 ? 1.6542 1.2955 1.8193 -0.0321 -0.0115 0.0569  189 LEU A CG  
1293 C CD1 . LEU A 171 ? 1.3913 1.0373 1.5732 -0.0225 0.0123  0.0647  189 LEU A CD1 
1294 C CD2 . LEU A 171 ? 1.3808 1.0382 1.5713 -0.0327 -0.0250 0.0715  189 LEU A CD2 
1295 N N   . LYS A 172 ? 1.1887 0.7914 1.2667 -0.0338 -0.0065 0.0125  190 LYS A N   
1296 C CA  . LYS A 172 ? 1.0435 0.6398 1.1149 -0.0349 0.0004  0.0129  190 LYS A CA  
1297 C C   . LYS A 172 ? 1.1059 0.7124 1.1575 -0.0420 -0.0116 0.0104  190 LYS A C   
1298 O O   . LYS A 172 ? 1.1390 0.7475 1.1890 -0.0434 -0.0110 0.0234  190 LYS A O   
1299 C CB  . LYS A 172 ? 0.9407 0.5211 1.0041 -0.0332 0.0144  -0.0041 190 LYS A CB  
1300 C CG  . LYS A 172 ? 1.2541 0.8230 1.3336 -0.0224 0.0281  -0.0011 190 LYS A CG  
1301 C CD  . LYS A 172 ? 1.0425 0.5938 1.1117 -0.0190 0.0378  -0.0218 190 LYS A CD  
1302 C CE  . LYS A 172 ? 1.0657 0.6046 1.1470 -0.0047 0.0507  -0.0208 190 LYS A CE  
1303 N NZ  . LYS A 172 ? 1.2514 0.8031 1.3393 0.0038  0.0544  -0.0116 190 LYS A NZ  
1304 N N   . THR A 173 ? 1.2893 0.9019 1.3235 -0.0447 -0.0227 -0.0056 191 THR A N   
1305 C CA  . THR A 173 ? 1.1522 0.7779 1.1652 -0.0479 -0.0343 -0.0105 191 THR A CA  
1306 C C   . THR A 173 ? 1.0978 0.7335 1.1144 -0.0463 -0.0499 0.0063  191 THR A C   
1307 O O   . THR A 173 ? 1.1433 0.7883 1.1435 -0.0462 -0.0533 0.0125  191 THR A O   
1308 C CB  . THR A 173 ? 1.0746 0.7028 1.0703 -0.0476 -0.0457 -0.0335 191 THR A CB  
1309 O OG1 . THR A 173 ? 1.1061 0.7266 1.0978 -0.0477 -0.0334 -0.0500 191 THR A OG1 
1310 C CG2 . THR A 173 ? 1.1622 0.8065 1.1341 -0.0472 -0.0574 -0.0415 191 THR A CG2 
1311 N N   . ILE A 174 ? 1.1630 0.7989 1.2015 -0.0447 -0.0596 0.0145  192 ILE A N   
1312 C CA  . ILE A 174 ? 1.2324 0.8793 1.2805 -0.0430 -0.0779 0.0290  192 ILE A CA  
1313 C C   . ILE A 174 ? 1.2285 0.8758 1.2844 -0.0391 -0.0694 0.0498  192 ILE A C   
1314 O O   . ILE A 174 ? 1.3306 0.9859 1.3731 -0.0364 -0.0814 0.0591  192 ILE A O   
1315 C CB  . ILE A 174 ? 1.2569 0.9066 1.3368 -0.0445 -0.0881 0.0344  192 ILE A CB  
1316 C CG1 . ILE A 174 ? 1.1700 0.8168 1.2385 -0.0488 -0.1061 0.0167  192 ILE A CG1 
1317 C CG2 . ILE A 174 ? 1.2240 0.8870 1.3284 -0.0419 -0.1026 0.0531  192 ILE A CG2 
1318 C CD1 . ILE A 174 ? 1.4424 1.0889 1.5435 -0.0538 -0.1137 0.0235  192 ILE A CD1 
1319 N N   . VAL A 175 ? 1.2436 0.8803 1.3189 -0.0368 -0.0499 0.0571  193 VAL A N   
1320 C CA  . VAL A 175 ? 1.1860 0.8170 1.2700 -0.0317 -0.0427 0.0765  193 VAL A CA  
1321 C C   . VAL A 175 ? 1.1272 0.7534 1.1812 -0.0356 -0.0373 0.0783  193 VAL A C   
1322 O O   . VAL A 175 ? 1.1740 0.8011 1.2205 -0.0325 -0.0425 0.0966  193 VAL A O   
1323 C CB  . VAL A 175 ? 1.3037 0.9211 1.4124 -0.0265 -0.0234 0.0788  193 VAL A CB  
1324 C CG1 . VAL A 175 ? 1.1250 0.7296 1.2411 -0.0206 -0.0168 0.0967  193 VAL A CG1 
1325 C CG2 . VAL A 175 ? 0.9570 0.5859 1.0970 -0.0216 -0.0259 0.0823  193 VAL A CG2 
1326 N N   . GLY A 176 ? 1.2436 0.8664 1.2811 -0.0422 -0.0267 0.0606  194 GLY A N   
1327 C CA  . GLY A 176 ? 1.1472 0.7714 1.1612 -0.0479 -0.0188 0.0629  194 GLY A CA  
1328 C C   . GLY A 176 ? 1.2463 0.8894 1.2313 -0.0461 -0.0338 0.0663  194 GLY A C   
1329 O O   . GLY A 176 ? 1.4163 1.0620 1.3837 -0.0467 -0.0297 0.0827  194 GLY A O   
1330 N N   . GLN A 177 ? 1.3375 0.9925 1.3150 -0.0433 -0.0517 0.0507  195 GLN A N   
1331 C CA  . GLN A 177 ? 1.3145 0.9862 1.2625 -0.0384 -0.0700 0.0497  195 GLN A CA  
1332 C C   . GLN A 177 ? 1.3440 1.0165 1.2946 -0.0316 -0.0833 0.0735  195 GLN A C   
1333 O O   . GLN A 177 ? 1.5042 1.1857 1.4243 -0.0269 -0.0883 0.0840  195 GLN A O   
1334 C CB  . GLN A 177 ? 1.2727 0.9504 1.2179 -0.0364 -0.0902 0.0264  195 GLN A CB  
1335 C CG  . GLN A 177 ? 1.5986 1.2920 1.5095 -0.0291 -0.1113 0.0172  195 GLN A CG  
1336 C CD  . GLN A 177 ? 1.6974 1.4050 1.5730 -0.0280 -0.0975 0.0080  195 GLN A CD  
1337 O OE1 . GLN A 177 ? 1.5669 1.2731 1.4489 -0.0350 -0.0743 0.0052  195 GLN A OE1 
1338 N NE2 . GLN A 177 ? 1.9530 1.6768 1.7922 -0.0184 -0.1121 0.0024  195 GLN A NE2 
1339 N N   . HIS A 178 ? 1.3508 1.0163 1.3375 -0.0295 -0.0887 0.0828  196 HIS A N   
1340 C CA  . HIS A 178 ? 1.2671 0.9345 1.2632 -0.0216 -0.1021 0.1053  196 HIS A CA  
1341 C C   . HIS A 178 ? 1.3048 0.9617 1.2855 -0.0198 -0.0874 0.1278  196 HIS A C   
1342 O O   . HIS A 178 ? 1.3770 1.0387 1.3345 -0.0126 -0.0994 0.1439  196 HIS A O   
1343 C CB  . HIS A 178 ? 1.5151 1.1802 1.5597 -0.0197 -0.1039 0.1111  196 HIS A CB  
1344 C CG  . HIS A 178 ? 1.3365 1.0040 1.3992 -0.0099 -0.1150 0.1342  196 HIS A CG  
1345 N ND1 . HIS A 178 ? 1.3326 1.0160 1.3983 -0.0039 -0.1443 0.1379  196 HIS A ND1 
1346 C CD2 . HIS A 178 ? 1.2022 0.8573 1.2822 -0.0037 -0.1032 0.1535  196 HIS A CD2 
1347 C CE1 . HIS A 178 ? 1.1936 0.8770 1.2780 0.0060  -0.1497 0.1593  196 HIS A CE1 
1348 N NE2 . HIS A 178 ? 1.4442 1.1094 1.5371 0.0068  -0.1247 0.1694  196 HIS A NE2 
1349 N N   . LEU A 179 ? 1.5033 1.1435 1.4960 -0.0261 -0.0627 0.1297  197 LEU A N   
1350 C CA  . LEU A 179 ? 1.2408 0.8657 1.2230 -0.0273 -0.0483 0.1520  197 LEU A CA  
1351 C C   . LEU A 179 ? 1.2813 0.9186 1.2192 -0.0311 -0.0449 0.1556  197 LEU A C   
1352 O O   . LEU A 179 ? 1.4214 1.0569 1.3364 -0.0264 -0.0479 0.1798  197 LEU A O   
1353 C CB  . LEU A 179 ? 1.3052 0.9087 1.3108 -0.0348 -0.0252 0.1475  197 LEU A CB  
1354 C CG  . LEU A 179 ? 1.4797 1.0698 1.5255 -0.0278 -0.0238 0.1464  197 LEU A CG  
1355 C CD1 . LEU A 179 ? 1.4953 1.0624 1.5561 -0.0335 -0.0030 0.1381  197 LEU A CD1 
1356 C CD2 . LEU A 179 ? 1.2778 0.8612 1.3371 -0.0156 -0.0344 0.1715  197 LEU A CD2 
1357 N N   . ASP A 180 ? 1.3874 1.0389 1.3112 -0.0379 -0.0386 0.1321  198 ASP A N   
1358 C CA  . ASP A 180 ? 1.4431 1.1128 1.3264 -0.0401 -0.0320 0.1328  198 ASP A CA  
1359 C C   . ASP A 180 ? 1.3476 1.0329 1.1949 -0.0271 -0.0542 0.1401  198 ASP A C   
1360 O O   . ASP A 180 ? 1.4428 1.1405 1.2513 -0.0249 -0.0479 0.1527  198 ASP A O   
1361 C CB  . ASP A 180 ? 1.4918 1.1775 1.3710 -0.0456 -0.0259 0.1015  198 ASP A CB  
1362 C CG  . ASP A 180 ? 1.8022 1.5145 1.6409 -0.0446 -0.0192 0.0983  198 ASP A CG  
1363 O OD1 . ASP A 180 ? 1.8381 1.5531 1.6703 -0.0532 0.0030  0.1159  198 ASP A OD1 
1364 O OD2 . ASP A 180 ? 2.2557 1.9865 2.0702 -0.0352 -0.0359 0.0782  198 ASP A OD2 
1365 N N   . THR A 181 ? 1.4125 1.0988 1.2722 -0.0184 -0.0803 0.1324  199 THR A N   
1366 C CA  . THR A 181 ? 1.3350 1.0357 1.1624 -0.0051 -0.1069 0.1341  199 THR A CA  
1367 C C   . THR A 181 ? 1.3176 1.0089 1.1431 0.0039  -0.1172 0.1653  199 THR A C   
1368 O O   . THR A 181 ? 1.3677 1.0686 1.1498 0.0145  -0.1285 0.1768  199 THR A O   
1369 C CB  . THR A 181 ? 1.9268 1.6341 1.7716 -0.0016 -0.1343 0.1086  199 THR A CB  
1370 O OG1 . THR A 181 ? 1.8847 1.5988 1.7240 -0.0071 -0.1280 0.0799  199 THR A OG1 
1371 C CG2 . THR A 181 ? 2.2798 1.9998 2.0948 0.0127  -0.1669 0.1072  199 THR A CG2 
1372 N N   . ASN A 182 ? 1.4552 1.1285 1.3244 0.0025  -0.1143 0.1789  200 ASN A N   
1373 C CA  . ASN A 182 ? 1.4342 1.1008 1.3101 0.0146  -0.1317 0.2035  200 ASN A CA  
1374 C C   . ASN A 182 ? 1.4495 1.0911 1.3316 0.0139  -0.1128 0.2342  200 ASN A C   
1375 O O   . ASN A 182 ? 1.5265 1.1590 1.4211 0.0254  -0.1267 0.2547  200 ASN A O   
1376 C CB  . ASN A 182 ? 1.4222 1.0929 1.3494 0.0182  -0.1508 0.1941  200 ASN A CB  
1377 C CG  . ASN A 182 ? 1.3941 1.0849 1.3193 0.0186  -0.1754 0.1677  200 ASN A CG  
1378 O OD1 . ASN A 182 ? 1.3522 1.0552 1.2601 0.0292  -0.2049 0.1677  200 ASN A OD1 
1379 N ND2 . ASN A 182 ? 1.4349 1.1269 1.3772 0.0077  -0.1657 0.1445  200 ASN A ND2 
1380 N N   . ILE A 183 ? 1.5036 1.1330 1.3799 0.0010  -0.0835 0.2379  201 ILE A N   
1381 C CA  . ILE A 183 ? 1.6251 1.2243 1.5154 -0.0014 -0.0675 0.2653  201 ILE A CA  
1382 C C   . ILE A 183 ? 1.6068 1.1991 1.4567 0.0074  -0.0737 0.2996  201 ILE A C   
1383 O O   . ILE A 183 ? 1.5485 1.1159 1.4118 0.0151  -0.0777 0.3251  201 ILE A O   
1384 C CB  . ILE A 183 ? 1.3959 0.9833 1.2963 -0.0195 -0.0372 0.2584  201 ILE A CB  
1385 C CG1 . ILE A 183 ? 1.6214 1.1979 1.5710 -0.0225 -0.0322 0.2369  201 ILE A CG1 
1386 C CG2 . ILE A 183 ? 1.4564 1.0163 1.3491 -0.0253 -0.0209 0.2918  201 ILE A CG2 
1387 C CD1 . ILE A 183 ? 1.7657 1.3344 1.7272 -0.0385 -0.0085 0.2215  201 ILE A CD1 
1388 N N   . PHE A 184 ? 1.6101 1.2238 1.4080 0.0085  -0.0745 0.3011  202 PHE A N   
1389 C CA  . PHE A 184 ? 1.7836 1.3928 1.5341 0.0185  -0.0797 0.3350  202 PHE A CA  
1390 C C   . PHE A 184 ? 1.6435 1.2626 1.3788 0.0403  -0.1167 0.3375  202 PHE A C   
1391 O O   . PHE A 184 ? 1.7629 1.3767 1.4564 0.0525  -0.1258 0.3663  202 PHE A O   
1392 C CB  . PHE A 184 ? 1.8933 1.5252 1.5899 0.0127  -0.0624 0.3368  202 PHE A CB  
1393 C CG  . PHE A 184 ? 1.9891 1.6113 1.6968 -0.0089 -0.0255 0.3469  202 PHE A CG  
1394 C CD1 . PHE A 184 ? 1.6808 1.2656 1.4279 -0.0192 -0.0124 0.3667  202 PHE A CD1 
1395 C CD2 . PHE A 184 ? 1.9473 1.5988 1.6284 -0.0182 -0.0054 0.3353  202 PHE A CD2 
1396 C CE1 . PHE A 184 ? 1.6383 1.2133 1.3999 -0.0405 0.0182  0.3746  202 PHE A CE1 
1397 C CE2 . PHE A 184 ? 2.0386 1.6856 1.7365 -0.0394 0.0272  0.3443  202 PHE A CE2 
1398 C CZ  . PHE A 184 ? 1.9568 1.5647 1.6960 -0.0517 0.0382  0.3641  202 PHE A CZ  
1399 N N   . SER A 185 ? 1.5939 1.2272 1.3626 0.0452  -0.1388 0.3095  203 SER A N   
1400 C CA  . SER A 185 ? 1.7249 1.3713 1.4858 0.0640  -0.1769 0.3085  203 SER A CA  
1401 C C   . SER A 185 ? 1.7647 1.3893 1.5441 0.0769  -0.1886 0.3395  203 SER A C   
1402 O O   . SER A 185 ? 1.7168 1.3136 1.5216 0.0713  -0.1682 0.3581  203 SER A O   
1403 C CB  . SER A 185 ? 1.6306 1.2956 1.4347 0.0622  -0.1958 0.2739  203 SER A CB  
1404 O OG  . SER A 185 ? 1.8043 1.4570 1.6709 0.0537  -0.1822 0.2702  203 SER A OG  
1405 N N   . ASP A 186 ? 1.8164 1.4531 1.5835 0.0959  -0.2246 0.3433  204 ASP A N   
1406 C CA  . ASP A 186 ? 1.8686 1.4879 1.6525 0.1121  -0.2410 0.3714  204 ASP A CA  
1407 C C   . ASP A 186 ? 1.8048 1.4175 1.6677 0.1098  -0.2378 0.3643  204 ASP A C   
1408 O O   . ASP A 186 ? 1.8841 1.4704 1.7685 0.1164  -0.2314 0.3879  204 ASP A O   
1409 C CB  . ASP A 186 ? 1.9189 1.5576 1.6771 0.1337  -0.2844 0.3716  204 ASP A CB  
1410 C CG  . ASP A 186 ? 2.1642 1.8072 1.8354 0.1420  -0.2879 0.3833  204 ASP A CG  
1411 O OD1 . ASP A 186 ? 2.1355 1.7714 1.7708 0.1291  -0.2544 0.3906  204 ASP A OD1 
1412 O OD2 . ASP A 186 ? 2.2646 1.9203 1.9037 0.1623  -0.3243 0.3849  204 ASP A OD2 
1413 N N   . LYS A 187 ? 1.7517 1.3874 1.6574 0.1014  -0.2418 0.3324  205 LYS A N   
1414 C CA  . LYS A 187 ? 1.8288 1.4652 1.8078 0.1014  -0.2384 0.3256  205 LYS A CA  
1415 C C   . LYS A 187 ? 1.8455 1.4508 1.8414 0.0926  -0.2026 0.3344  205 LYS A C   
1416 O O   . LYS A 187 ? 1.6697 1.2616 1.7084 0.1019  -0.2002 0.3444  205 LYS A O   
1417 C CB  . LYS A 187 ? 1.7752 1.4405 1.7906 0.0907  -0.2443 0.2926  205 LYS A CB  
1418 C CG  . LYS A 187 ? 1.7964 1.4559 1.8114 0.0707  -0.2125 0.2731  205 LYS A CG  
1419 C CD  . LYS A 187 ? 1.5954 1.2799 1.6405 0.0612  -0.2216 0.2436  205 LYS A CD  
1420 C CE  . LYS A 187 ? 1.8745 1.5762 1.8794 0.0618  -0.2480 0.2287  205 LYS A CE  
1421 N NZ  . LYS A 187 ? 1.6451 1.3378 1.5863 0.0565  -0.2316 0.2259  205 LYS A NZ  
1422 N N   . TYR A 188 ? 1.7778 1.3721 1.7425 0.0757  -0.1760 0.3291  206 TYR A N   
1423 C CA  . TYR A 188 ? 1.6923 1.2570 1.6747 0.0652  -0.1445 0.3332  206 TYR A CA  
1424 C C   . TYR A 188 ? 1.7300 1.2579 1.6982 0.0726  -0.1396 0.3682  206 TYR A C   
1425 O O   . TYR A 188 ? 1.8089 1.3065 1.7963 0.0654  -0.1176 0.3728  206 TYR A O   
1426 C CB  . TYR A 188 ? 1.7363 1.3037 1.6928 0.0448  -0.1204 0.3169  206 TYR A CB  
1427 C CG  . TYR A 188 ? 1.5825 1.1639 1.5749 0.0349  -0.1112 0.2841  206 TYR A CG  
1428 C CD1 . TYR A 188 ? 1.5378 1.1496 1.5411 0.0367  -0.1302 0.2626  206 TYR A CD1 
1429 C CD2 . TYR A 188 ? 1.5361 1.0981 1.5511 0.0242  -0.0853 0.2752  206 TYR A CD2 
1430 C CE1 . TYR A 188 ? 1.6214 1.2433 1.6551 0.0276  -0.1214 0.2366  206 TYR A CE1 
1431 C CE2 . TYR A 188 ? 1.5548 1.1286 1.5969 0.0173  -0.0774 0.2469  206 TYR A CE2 
1432 C CZ  . TYR A 188 ? 1.5202 1.1236 1.5705 0.0189  -0.0945 0.2294  206 TYR A CZ  
1433 O OH  . TYR A 188 ? 1.3989 1.0114 1.4736 0.0119  -0.0862 0.2051  206 TYR A OH  
1434 N N   . SER A 189 ? 2.3626 1.8898 2.2970 0.0872  -0.1612 0.3927  207 SER A N   
1435 C CA  . SER A 189 ? 2.3597 1.8487 2.2756 0.0953  -0.1592 0.4303  207 SER A CA  
1436 C C   . SER A 189 ? 1.8929 1.3720 1.8515 0.1181  -0.1807 0.4403  207 SER A C   
1437 O O   . SER A 189 ? 2.3832 1.8913 2.3534 0.1334  -0.2097 0.4336  207 SER A O   
1438 C CB  . SER A 189 ? 2.2106 1.7034 2.0560 0.0998  -0.1688 0.4546  207 SER A CB  
1439 O OG  . SER A 189 ? 2.2638 1.7732 2.0716 0.0814  -0.1487 0.4429  207 SER A OG  
1440 N N   . HIS A 190 ? 2.1169 1.5559 2.1019 0.1207  -0.1677 0.4546  208 HIS A N   
1441 C CA  . HIS A 190 ? 2.3236 1.7432 2.3443 0.1449  -0.1850 0.4697  208 HIS A CA  
1442 C C   . HIS A 190 ? 2.2522 1.6979 2.3405 0.1549  -0.1897 0.4414  208 HIS A C   
1443 O O   . HIS A 190 ? 2.2663 1.7045 2.3904 0.1778  -0.2048 0.4503  208 HIS A O   
1444 C CB  . HIS A 190 ? 2.4391 1.8643 2.4279 0.1664  -0.2182 0.4956  208 HIS A CB  
1445 C CG  . HIS A 190 ? 2.4920 1.8942 2.4088 0.1604  -0.2140 0.5280  208 HIS A CG  
1446 N ND1 . HIS A 190 ? 2.5167 1.8663 2.4169 0.1612  -0.2040 0.5636  208 HIS A ND1 
1447 C CD2 . HIS A 190 ? 2.5219 1.9471 2.3784 0.1540  -0.2175 0.5310  208 HIS A CD2 
1448 C CE1 . HIS A 190 ? 2.5746 1.9180 2.4077 0.1541  -0.1993 0.5900  208 HIS A CE1 
1449 N NE2 . HIS A 190 ? 2.6235 2.0140 2.4274 0.1511  -0.2069 0.5698  208 HIS A NE2 
1450 N N   . ILE A 191 ? 2.0921 1.5688 2.1996 0.1399  -0.1770 0.4093  209 ILE A N   
1451 C CA  . ILE A 191 ? 2.2989 1.8000 2.4695 0.1476  -0.1756 0.3856  209 ILE A CA  
1452 C C   . ILE A 191 ? 2.6349 2.1689 2.8363 0.1695  -0.2077 0.3900  209 ILE A C   
1453 O O   . ILE A 191 ? 2.7657 2.3403 2.9692 0.1654  -0.2245 0.3775  209 ILE A O   
1454 C CB  . ILE A 191 ? 1.9013 1.3658 2.1051 0.1547  -0.1561 0.3848  209 ILE A CB  
1455 C CG1 . ILE A 191 ? 1.6762 1.1086 1.8542 0.1317  -0.1276 0.3788  209 ILE A CG1 
1456 C CG2 . ILE A 191 ? 1.7352 1.2302 2.0003 0.1649  -0.1513 0.3604  209 ILE A CG2 
1457 C CD1 . ILE A 191 ? 2.5563 1.9385 2.7534 0.1385  -0.1144 0.3845  209 ILE A CD1 
1458 N N   . ASP A 194 ? 1.7757 1.4649 2.0960 0.1775  -0.2739 0.3456  212 ASP A N   
1459 C CA  . ASP A 194 ? 1.7335 1.4694 2.0813 0.1721  -0.2999 0.3313  212 ASP A CA  
1460 C C   . ASP A 194 ? 1.7141 1.4466 1.9976 0.1579  -0.3135 0.3247  212 ASP A C   
1461 O O   . ASP A 194 ? 1.9365 1.6357 2.1546 0.1560  -0.3051 0.3359  212 ASP A O   
1462 C CB  . ASP A 194 ? 1.8338 1.5961 2.2237 0.1956  -0.3355 0.3427  212 ASP A CB  
1463 C CG  . ASP A 194 ? 1.7678 1.5397 2.2257 0.2131  -0.3226 0.3471  212 ASP A CG  
1464 O OD1 . ASP A 194 ? 1.8487 1.6035 2.3158 0.2078  -0.2865 0.3410  212 ASP A OD1 
1465 O OD2 . ASP A 194 ? 1.7784 1.5761 2.2805 0.2339  -0.3497 0.3552  212 ASP A OD2 
1466 N N   . ILE A 195 ? 1.7750 1.5428 2.0794 0.1483  -0.3345 0.3064  213 ILE A N   
1467 C CA  . ILE A 195 ? 1.8994 1.6672 2.1484 0.1364  -0.3492 0.2935  213 ILE A CA  
1468 C C   . ILE A 195 ? 1.8032 1.5979 2.0588 0.1481  -0.3979 0.2918  213 ILE A C   
1469 O O   . ILE A 195 ? 1.7537 1.5809 2.0792 0.1534  -0.4173 0.2892  213 ILE A O   
1470 C CB  . ILE A 195 ? 2.0614 1.8396 2.3242 0.1125  -0.3317 0.2683  213 ILE A CB  
1471 C CG1 . ILE A 195 ? 1.8763 1.6261 2.1222 0.1020  -0.2868 0.2679  213 ILE A CG1 
1472 C CG2 . ILE A 195 ? 1.8622 1.6440 2.0754 0.1041  -0.3540 0.2515  213 ILE A CG2 
1473 C CD1 . ILE A 195 ? 1.6777 1.4324 1.9856 0.1046  -0.2624 0.2701  213 ILE A CD1 
1474 N N   . ASP A 196 ? 1.8917 1.6749 2.0751 0.1529  -0.4177 0.2926  214 ASP A N   
1475 C CA  . ASP A 196 ? 1.9076 1.7122 2.0838 0.1662  -0.4676 0.2881  214 ASP A CA  
1476 C C   . ASP A 196 ? 2.0041 1.8326 2.2006 0.1491  -0.4858 0.2570  214 ASP A C   
1477 O O   . ASP A 196 ? 2.0449 1.8626 2.1841 0.1407  -0.4844 0.2417  214 ASP A O   
1478 C CB  . ASP A 196 ? 2.0543 1.8357 2.1375 0.1812  -0.4797 0.3024  214 ASP A CB  
1479 C CG  . ASP A 196 ? 2.0729 1.8743 2.1407 0.1991  -0.5342 0.2970  214 ASP A CG  
1480 O OD1 . ASP A 196 ? 2.0470 1.8806 2.1836 0.1985  -0.5642 0.2823  214 ASP A OD1 
1481 O OD2 . ASP A 196 ? 1.9030 1.6892 1.8899 0.2140  -0.5473 0.3078  214 ASP A OD2 
1482 N N   . VAL A 197 ? 1.8981 1.7597 2.1789 0.1442  -0.5031 0.2481  215 VAL A N   
1483 C CA  . VAL A 197 ? 1.9782 1.8605 2.2889 0.1265  -0.5240 0.2211  215 VAL A CA  
1484 C C   . VAL A 197 ? 1.8394 1.7355 2.1319 0.1392  -0.5808 0.2101  215 VAL A C   
1485 O O   . VAL A 197 ? 1.7765 1.6717 2.0435 0.1306  -0.6024 0.1858  215 VAL A O   
1486 C CB  . VAL A 197 ? 1.7653 1.6788 2.1787 0.1122  -0.5145 0.2186  215 VAL A CB  
1487 C CG1 . VAL A 197 ? 1.7650 1.6636 2.1882 0.1020  -0.4595 0.2262  215 VAL A CG1 
1488 C CG2 . VAL A 197 ? 1.8536 1.7991 2.3334 0.1291  -0.5402 0.2322  215 VAL A CG2 
1489 N N   . LYS A 207 ? 1.8147 1.4975 1.2682 0.0903  -0.1385 0.3914  225 LYS A N   
1490 C CA  . LYS A 207 ? 1.8528 1.5025 1.3086 0.0843  -0.1196 0.4386  225 LYS A CA  
1491 C C   . LYS A 207 ? 1.9616 1.5899 1.4823 0.0582  -0.0891 0.4382  225 LYS A C   
1492 O O   . LYS A 207 ? 1.9472 1.5704 1.5272 0.0527  -0.0973 0.4112  225 LYS A O   
1493 C CB  . LYS A 207 ? 1.9594 1.5858 1.4235 0.1034  -0.1538 0.4582  225 LYS A CB  
1494 C CG  . LYS A 207 ? 2.0337 1.6796 1.4356 0.1311  -0.1898 0.4570  225 LYS A CG  
1495 C CD  . LYS A 207 ? 2.0325 1.6557 1.4449 0.1505  -0.2235 0.4797  225 LYS A CD  
1496 C CE  . LYS A 207 ? 2.0105 1.6525 1.3570 0.1793  -0.2620 0.4785  225 LYS A CE  
1497 N NZ  . LYS A 207 ? 2.0412 1.6620 1.3945 0.2001  -0.2955 0.5040  225 LYS A NZ  
1498 N N   . ILE A 208 ? 1.9926 1.6088 1.5015 0.0423  -0.0544 0.4686  226 ILE A N   
1499 C CA  . ILE A 208 ? 1.8555 1.4513 1.4229 0.0169  -0.0263 0.4670  226 ILE A CA  
1500 C C   . ILE A 208 ? 1.9699 1.5183 1.5800 0.0183  -0.0350 0.4899  226 ILE A C   
1501 O O   . ILE A 208 ? 1.9241 1.4475 1.5074 0.0281  -0.0412 0.5301  226 ILE A O   
1502 C CB  . ILE A 208 ? 1.7389 1.3423 1.2839 -0.0027 0.0132  0.4903  226 ILE A CB  
1503 C CG1 . ILE A 208 ? 1.8710 1.5260 1.3821 -0.0025 0.0236  0.4610  226 ILE A CG1 
1504 C CG2 . ILE A 208 ? 1.6451 1.2204 1.2539 -0.0289 0.0377  0.4921  226 ILE A CG2 
1505 C CD1 . ILE A 208 ? 1.9589 1.6327 1.4518 -0.0212 0.0644  0.4818  226 ILE A CD1 
1506 N N   . ASN A 209 ? 1.7760 1.3115 1.4503 0.0106  -0.0359 0.4641  227 ASN A N   
1507 C CA  . ASN A 209 ? 1.8351 1.3263 1.5560 0.0117  -0.0400 0.4798  227 ASN A CA  
1508 C C   . ASN A 209 ? 1.8040 1.2675 1.5495 -0.0130 -0.0076 0.4936  227 ASN A C   
1509 O O   . ASN A 209 ? 1.7988 1.2713 1.5779 -0.0295 0.0084  0.4645  227 ASN A O   
1510 C CB  . ASN A 209 ? 1.7953 1.2908 1.5701 0.0192  -0.0578 0.4441  227 ASN A CB  
1511 C CG  . ASN A 209 ? 1.8927 1.3489 1.7097 0.0293  -0.0678 0.4590  227 ASN A CG  
1512 O OD1 . ASN A 209 ? 1.9979 1.4178 1.8055 0.0303  -0.0634 0.4955  227 ASN A OD1 
1513 N ND2 . ASN A 209 ? 1.8473 1.3108 1.7113 0.0377  -0.0812 0.4317  227 ASN A ND2 
1514 N N   . ILE A 210 ? 1.8571 1.2856 1.5866 -0.0158 0.0003  0.5386  228 ILE A N   
1515 C CA  . ILE A 210 ? 1.9147 1.3193 1.6626 -0.0425 0.0312  0.5568  228 ILE A CA  
1516 C C   . ILE A 210 ? 1.8546 1.2304 1.6711 -0.0525 0.0346  0.5317  228 ILE A C   
1517 O O   . ILE A 210 ? 1.8487 1.2304 1.6919 -0.0748 0.0561  0.5140  228 ILE A O   
1518 C CB  . ILE A 210 ? 1.7930 1.1586 1.5123 -0.0427 0.0357  0.6138  228 ILE A CB  
1519 C CG1 . ILE A 210 ? 1.9607 1.3580 1.6035 -0.0307 0.0338  0.6382  228 ILE A CG1 
1520 C CG2 . ILE A 210 ? 1.6961 1.0347 1.4430 -0.0738 0.0668  0.6336  228 ILE A CG2 
1521 C CD1 . ILE A 210 ? 2.2044 1.5643 1.8094 -0.0280 0.0368  0.6982  228 ILE A CD1 
1522 N N   . ASN A 211 ? 1.8373 1.1836 1.6831 -0.0343 0.0129  0.5285  229 ASN A N   
1523 C CA  . ASN A 211 ? 1.7513 1.0684 1.6573 -0.0395 0.0159  0.5052  229 ASN A CA  
1524 C C   . ASN A 211 ? 1.7915 1.1446 1.7205 -0.0470 0.0223  0.4564  229 ASN A C   
1525 O O   . ASN A 211 ? 1.8088 1.1432 1.7798 -0.0573 0.0317  0.4353  229 ASN A O   
1526 C CB  . ASN A 211 ? 1.9612 1.2504 1.8919 -0.0135 -0.0088 0.5073  229 ASN A CB  
1527 C CG  . ASN A 211 ? 1.9276 1.2563 1.8702 0.0044  -0.0268 0.4724  229 ASN A CG  
1528 O OD1 . ASN A 211 ? 1.9705 1.3301 1.8812 0.0177  -0.0436 0.4761  229 ASN A OD1 
1529 N ND2 . ASN A 211 ? 1.9355 1.2629 1.9242 0.0048  -0.0240 0.4385  229 ASN A ND2 
1530 N N   . MET A 212 ? 1.9203 1.3219 1.8212 -0.0408 0.0155  0.4376  230 MET A N   
1531 C CA  . MET A 212 ? 1.7876 1.2205 1.7080 -0.0459 0.0187  0.3931  230 MET A CA  
1532 C C   . MET A 212 ? 1.7770 1.2243 1.6973 -0.0705 0.0440  0.3819  230 MET A C   
1533 O O   . MET A 212 ? 1.8401 1.2945 1.7903 -0.0780 0.0500  0.3481  230 MET A O   
1534 C CB  . MET A 212 ? 1.7236 1.1988 1.6167 -0.0311 -0.0003 0.3767  230 MET A CB  
1535 C CG  . MET A 212 ? 1.6913 1.1621 1.6020 -0.0084 -0.0268 0.3754  230 MET A CG  
1536 S SD  . MET A 212 ? 1.2854 0.7385 1.2609 -0.0054 -0.0253 0.3477  230 MET A SD  
1537 C CE  . MET A 212 ? 1.6628 1.1289 1.6545 0.0213  -0.0559 0.3491  230 MET A CE  
1538 N N   . LEU A 213 ? 1.8260 1.2806 1.7140 -0.0824 0.0593  0.4099  231 LEU A N   
1539 C CA  . LEU A 213 ? 1.9982 1.4751 1.8898 -0.1055 0.0843  0.4000  231 LEU A CA  
1540 C C   . LEU A 213 ? 2.0985 1.5348 2.0360 -0.1256 0.0988  0.4079  231 LEU A C   
1541 O O   . LEU A 213 ? 1.5655 0.9688 1.5017 -0.1338 0.1060  0.4471  231 LEU A O   
1542 C CB  . LEU A 213 ? 1.6362 1.1434 1.4761 -0.1096 0.0975  0.4268  231 LEU A CB  
1543 C CG  . LEU A 213 ? 1.6228 1.1016 1.4403 -0.1140 0.1061  0.4805  231 LEU A CG  
1544 C CD1 . LEU A 213 ? 1.9517 1.4296 1.7873 -0.1440 0.1377  0.4988  231 LEU A CD1 
1545 C CD2 . LEU A 213 ? 1.7039 1.2095 1.4541 -0.0958 0.0979  0.5013  231 LEU A CD2 
1546 N N   . ASN A 214 ? 1.8612 1.2972 1.8385 -0.1326 0.1010  0.3706  232 ASN A N   
1547 C CA  . ASN A 214 ? 2.0960 1.4966 2.1195 -0.1515 0.1117  0.3683  232 ASN A CA  
1548 C C   . ASN A 214 ? 1.8880 1.3097 1.9382 -0.1565 0.1136  0.3205  232 ASN A C   
1549 O O   . ASN A 214 ? 1.6448 1.0994 1.6796 -0.1433 0.1049  0.2931  232 ASN A O   
1550 C CB  . ASN A 214 ? 1.9846 1.3270 2.0327 -0.1407 0.0981  0.3809  232 ASN A CB  
1551 C CG  . ASN A 214 ? 1.5977 0.9409 1.6508 -0.1141 0.0779  0.3551  232 ASN A CG  
1552 O OD1 . ASN A 214 ? 2.0716 1.4091 2.1546 -0.1113 0.0753  0.3207  232 ASN A OD1 
1553 N ND2 . ASN A 214 ? 1.9420 1.2940 1.9662 -0.0944 0.0634  0.3722  232 ASN A ND2 
1554 N N   . PHE A 215 ? 1.8488 1.2493 1.9396 -0.1756 0.1231  0.3111  233 PHE A N   
1555 C CA  . PHE A 215 ? 1.7834 1.2065 1.8966 -0.1817 0.1254  0.2676  233 PHE A CA  
1556 C C   . PHE A 215 ? 1.8098 1.2204 1.9324 -0.1605 0.1083  0.2340  233 PHE A C   
1557 O O   . PHE A 215 ? 1.8487 1.2874 1.9711 -0.1570 0.1062  0.1994  233 PHE A O   
1558 C CB  . PHE A 215 ? 2.0571 1.4611 2.2140 -0.2079 0.1371  0.2657  233 PHE A CB  
1559 C CG  . PHE A 215 ? 2.3276 1.6740 2.5212 -0.2049 0.1257  0.2558  233 PHE A CG  
1560 C CD1 . PHE A 215 ? 2.1643 1.4596 2.3658 -0.2051 0.1222  0.2896  233 PHE A CD1 
1561 C CD2 . PHE A 215 ? 2.1547 1.4966 2.3724 -0.2001 0.1176  0.2120  233 PHE A CD2 
1562 C CE1 . PHE A 215 ? 1.9765 1.2236 2.2045 -0.1981 0.1082  0.2739  233 PHE A CE1 
1563 C CE2 . PHE A 215 ? 2.1181 1.4076 2.3656 -0.1942 0.1066  0.1998  233 PHE A CE2 
1564 C CZ  . PHE A 215 ? 1.9880 1.2361 2.2356 -0.1915 0.1000  0.2273  233 PHE A CZ  
1565 N N   . LYS A 216 ? 1.7925 1.1627 1.9230 -0.1451 0.0967  0.2445  234 LYS A N   
1566 C CA  . LYS A 216 ? 1.8334 1.1959 1.9741 -0.1241 0.0840  0.2148  234 LYS A CA  
1567 C C   . LYS A 216 ? 1.9046 1.3065 2.0165 -0.1076 0.0755  0.2069  234 LYS A C   
1568 O O   . LYS A 216 ? 1.9141 1.3350 2.0280 -0.1005 0.0719  0.1754  234 LYS A O   
1569 C CB  . LYS A 216 ? 1.9641 1.2764 2.1235 -0.1101 0.0749  0.2283  234 LYS A CB  
1570 C CG  . LYS A 216 ? 1.8806 1.1456 2.0718 -0.1257 0.0792  0.2339  234 LYS A CG  
1571 C CD  . LYS A 216 ? 2.0718 1.2909 2.2727 -0.1077 0.0666  0.2435  234 LYS A CD  
1572 C CE  . LYS A 216 ? 2.1370 1.3210 2.3534 -0.1218 0.0647  0.2403  234 LYS A CE  
1573 N NZ  . LYS A 216 ? 1.9696 1.1125 2.1867 -0.1016 0.0508  0.2449  234 LYS A NZ  
1574 N N   . VAL A 217 ? 2.3444 1.7572 2.4289 -0.1015 0.0707  0.2358  235 VAL A N   
1575 C CA  . VAL A 217 ? 2.2939 1.7432 2.3531 -0.0875 0.0595  0.2282  235 VAL A CA  
1576 C C   . VAL A 217 ? 1.9191 1.4089 1.9618 -0.0974 0.0657  0.2054  235 VAL A C   
1577 O O   . VAL A 217 ? 1.9330 1.4456 1.9704 -0.0885 0.0569  0.1811  235 VAL A O   
1578 C CB  . VAL A 217 ? 1.4939 0.9455 1.5245 -0.0787 0.0507  0.2632  235 VAL A CB  
1579 C CG1 . VAL A 217 ? 1.7998 1.2891 1.8059 -0.0659 0.0359  0.2527  235 VAL A CG1 
1580 C CG2 . VAL A 217 ? 1.9553 1.3668 2.0047 -0.0653 0.0417  0.2837  235 VAL A CG2 
1581 N N   . TYR A 218 ? 1.8140 1.3138 1.8505 -0.1157 0.0809  0.2138  236 TYR A N   
1582 C CA  . TYR A 218 ? 1.7079 1.2480 1.7324 -0.1236 0.0877  0.1907  236 TYR A CA  
1583 C C   . TYR A 218 ? 1.6156 1.1552 1.6655 -0.1241 0.0860  0.1522  236 TYR A C   
1584 O O   . TYR A 218 ? 1.5896 1.1569 1.6273 -0.1181 0.0801  0.1269  236 TYR A O   
1585 C CB  . TYR A 218 ? 1.4656 1.0178 1.4879 -0.1440 0.1075  0.2091  236 TYR A CB  
1586 C CG  . TYR A 218 ? 1.4066 1.0086 1.4089 -0.1484 0.1157  0.1926  236 TYR A CG  
1587 C CD1 . TYR A 218 ? 1.5125 1.1449 1.4747 -0.1331 0.1055  0.1880  236 TYR A CD1 
1588 C CD2 . TYR A 218 ? 1.4938 1.1132 1.5197 -0.1670 0.1321  0.1808  236 TYR A CD2 
1589 C CE1 . TYR A 218 ? 1.6395 1.3163 1.5824 -0.1340 0.1120  0.1706  236 TYR A CE1 
1590 C CE2 . TYR A 218 ? 1.4610 1.1293 1.4711 -0.1685 0.1400  0.1647  236 TYR A CE2 
1591 C CZ  . TYR A 218 ? 1.4464 1.1423 1.4132 -0.1509 0.1302  0.1593  236 TYR A CZ  
1592 O OH  . TYR A 218 ? 1.7176 1.4610 1.6679 -0.1492 0.1369  0.1405  236 TYR A OH  
1593 N N   . GLN A 219 ? 1.7233 1.2290 1.8065 -0.1298 0.0895  0.1469  237 GLN A N   
1594 C CA  . GLN A 219 ? 1.5192 1.0212 1.6219 -0.1272 0.0864  0.1104  237 GLN A CA  
1595 C C   . GLN A 219 ? 1.3492 0.8543 1.4422 -0.1067 0.0732  0.0960  237 GLN A C   
1596 O O   . GLN A 219 ? 1.3738 0.8973 1.4618 -0.1027 0.0694  0.0687  237 GLN A O   
1597 C CB  . GLN A 219 ? 1.5585 1.0187 1.6956 -0.1334 0.0891  0.1074  237 GLN A CB  
1598 C CG  . GLN A 219 ? 1.9111 1.3712 2.0705 -0.1578 0.1011  0.1094  237 GLN A CG  
1599 C CD  . GLN A 219 ? 2.0628 1.4768 2.2588 -0.1633 0.0990  0.1023  237 GLN A CD  
1600 O OE1 . GLN A 219 ? 1.8220 1.2062 2.0230 -0.1459 0.0894  0.0914  237 GLN A OE1 
1601 N NE2 . GLN A 219 ? 1.8340 1.2430 2.0573 -0.1872 0.1078  0.1079  237 GLN A NE2 
1602 N N   . ASN A 220 ? 1.4436 0.9318 1.5363 -0.0936 0.0661  0.1152  238 ASN A N   
1603 C CA  . ASN A 220 ? 1.3721 0.8687 1.4616 -0.0760 0.0550  0.1052  238 ASN A CA  
1604 C C   . ASN A 220 ? 1.3849 0.9186 1.4491 -0.0753 0.0477  0.0969  238 ASN A C   
1605 O O   . ASN A 220 ? 1.4107 0.9564 1.4739 -0.0701 0.0428  0.0740  238 ASN A O   
1606 C CB  . ASN A 220 ? 1.5397 1.0199 1.6355 -0.0626 0.0477  0.1302  238 ASN A CB  
1607 C CG  . ASN A 220 ? 1.9282 1.3689 2.0509 -0.0569 0.0515  0.1321  238 ASN A CG  
1608 O OD1 . ASN A 220 ? 1.6609 1.0875 1.7976 -0.0586 0.0570  0.1089  238 ASN A OD1 
1609 N ND2 . ASN A 220 ? 1.8069 1.2281 1.9357 -0.0479 0.0465  0.1583  238 ASN A ND2 
1610 N N   . ILE A 221 ? 1.3084 0.8587 1.3498 -0.0795 0.0463  0.1156  239 ILE A N   
1611 C CA  . ILE A 221 ? 1.2920 0.8749 1.3070 -0.0760 0.0362  0.1069  239 ILE A CA  
1612 C C   . ILE A 221 ? 1.2481 0.8482 1.2604 -0.0822 0.0403  0.0766  239 ILE A C   
1613 O O   . ILE A 221 ? 1.2640 0.8765 1.2699 -0.0755 0.0294  0.0574  239 ILE A O   
1614 C CB  . ILE A 221 ? 1.5104 1.1082 1.4958 -0.0780 0.0360  0.1303  239 ILE A CB  
1615 C CG1 . ILE A 221 ? 1.3114 0.8906 1.2967 -0.0696 0.0288  0.1614  239 ILE A CG1 
1616 C CG2 . ILE A 221 ? 1.5148 1.1443 1.4708 -0.0715 0.0228  0.1166  239 ILE A CG2 
1617 C CD1 . ILE A 221 ? 1.5234 1.1051 1.4826 -0.0750 0.0361  0.1906  239 ILE A CD1 
1618 N N   . ILE A 222 ? 1.2590 0.8598 1.2788 -0.0953 0.0549  0.0726  240 ILE A N   
1619 C CA  . ILE A 222 ? 1.1759 0.7970 1.1951 -0.1001 0.0576  0.0434  240 ILE A CA  
1620 C C   . ILE A 222 ? 1.0803 0.6868 1.1142 -0.0933 0.0515  0.0186  240 ILE A C   
1621 O O   . ILE A 222 ? 1.1987 0.8192 1.2218 -0.0872 0.0426  -0.0028 240 ILE A O   
1622 C CB  . ILE A 222 ? 1.4321 1.0594 1.4655 -0.1170 0.0747  0.0452  240 ILE A CB  
1623 C CG1 . ILE A 222 ? 1.4565 1.1049 1.4689 -0.1230 0.0836  0.0710  240 ILE A CG1 
1624 C CG2 . ILE A 222 ? 1.5168 1.1641 1.5574 -0.1198 0.0752  0.0116  240 ILE A CG2 
1625 C CD1 . ILE A 222 ? 1.7377 1.3997 1.7668 -0.1418 0.1031  0.0765  240 ILE A CD1 
1626 N N   . ILE A 223 ? 1.2170 0.7935 1.2735 -0.0927 0.0557  0.0214  241 ILE A N   
1627 C CA  . ILE A 223 ? 1.2306 0.7937 1.2971 -0.0850 0.0525  -0.0024 241 ILE A CA  
1628 C C   . ILE A 223 ? 1.2469 0.8172 1.3010 -0.0719 0.0413  -0.0059 241 ILE A C   
1629 O O   . ILE A 223 ? 1.1706 0.7473 1.2174 -0.0676 0.0362  -0.0274 241 ILE A O   
1630 C CB  . ILE A 223 ? 1.3624 0.8911 1.4519 -0.0827 0.0579  0.0020  241 ILE A CB  
1631 C CG1 . ILE A 223 ? 1.5433 1.0622 1.6508 -0.0988 0.0667  0.0013  241 ILE A CG1 
1632 C CG2 . ILE A 223 ? 1.3162 0.8326 1.4084 -0.0697 0.0549  -0.0204 241 ILE A CG2 
1633 C CD1 . ILE A 223 ? 1.3722 0.8521 1.5027 -0.0980 0.0697  0.0102  241 ILE A CD1 
1634 N N   . HIS A 224 ? 1.2370 0.8064 1.2906 -0.0659 0.0363  0.0161  242 HIS A N   
1635 C CA  . HIS A 224 ? 1.1681 0.7458 1.2180 -0.0562 0.0251  0.0144  242 HIS A CA  
1636 C C   . HIS A 224 ? 1.1306 0.7318 1.1587 -0.0583 0.0133  0.0056  242 HIS A C   
1637 O O   . HIS A 224 ? 1.1517 0.7571 1.1759 -0.0541 0.0045  -0.0073 242 HIS A O   
1638 C CB  . HIS A 224 ? 1.2071 0.7802 1.2693 -0.0488 0.0211  0.0389  242 HIS A CB  
1639 C CG  . HIS A 224 ? 1.2373 0.7877 1.3220 -0.0411 0.0304  0.0429  242 HIS A CG  
1640 N ND1 . HIS A 224 ? 1.2711 0.7992 1.3643 -0.0447 0.0399  0.0467  242 HIS A ND1 
1641 C CD2 . HIS A 224 ? 1.3110 0.8578 1.4122 -0.0290 0.0319  0.0427  242 HIS A CD2 
1642 C CE1 . HIS A 224 ? 1.3290 0.8380 1.4408 -0.0332 0.0447  0.0462  242 HIS A CE1 
1643 N NE2 . HIS A 224 ? 1.3079 0.8305 1.4240 -0.0227 0.0415  0.0439  242 HIS A NE2 
1644 N N   . LYS A 225 ? 1.2034 0.8189 1.2160 -0.0641 0.0131  0.0125  243 LYS A N   
1645 C CA  . LYS A 225 ? 1.2119 0.8498 1.2010 -0.0625 0.0002  0.0035  243 LYS A CA  
1646 C C   . LYS A 225 ? 1.2068 0.8536 1.1883 -0.0638 0.0002  -0.0249 243 LYS A C   
1647 O O   . LYS A 225 ? 1.3168 0.9693 1.2875 -0.0583 -0.0143 -0.0393 243 LYS A O   
1648 C CB  . LYS A 225 ? 1.2585 0.9112 1.2287 -0.0654 0.0026  0.0197  243 LYS A CB  
1649 C CG  . LYS A 225 ? 1.3304 1.0085 1.2713 -0.0615 -0.0083 0.0068  243 LYS A CG  
1650 C CD  . LYS A 225 ? 1.4358 1.1293 1.3530 -0.0619 -0.0039 0.0261  243 LYS A CD  
1651 C CE  . LYS A 225 ? 1.8614 1.5827 1.7456 -0.0549 -0.0131 0.0096  243 LYS A CE  
1652 N NZ  . LYS A 225 ? 1.7557 1.4938 1.6093 -0.0518 -0.0096 0.0296  243 LYS A NZ  
1653 N N   . THR A 226 ? 1.1558 0.9603 1.2763 -0.0885 -0.1611 -0.0201 244 THR A N   
1654 C CA  . THR A 226 ? 1.0206 0.8170 1.1184 -0.0986 -0.1239 -0.0360 244 THR A CA  
1655 C C   . THR A 226 ? 0.9664 0.7552 1.0950 -0.0829 -0.0931 -0.0291 244 THR A C   
1656 O O   . THR A 226 ? 0.9979 0.7909 1.1532 -0.0849 -0.0697 -0.0435 244 THR A O   
1657 C CB  . THR A 226 ? 1.1264 0.8988 1.1379 -0.1155 -0.1202 -0.0349 244 THR A CB  
1658 O OG1 . THR A 226 ? 1.2140 0.9838 1.1769 -0.1317 -0.1475 -0.0438 244 THR A OG1 
1659 C CG2 . THR A 226 ? 1.0852 0.8572 1.0910 -0.1233 -0.0812 -0.0534 244 THR A CG2 
1660 N N   . ALA A 227 ? 0.8943 0.6645 1.0146 -0.0669 -0.0968 -0.0079 245 ALA A N   
1661 C CA  . ALA A 227 ? 1.0157 0.7632 1.1385 -0.0547 -0.0718 -0.0027 245 ALA A CA  
1662 C C   . ALA A 227 ? 0.9111 0.6706 1.0865 -0.0451 -0.0499 -0.0114 245 ALA A C   
1663 O O   . ALA A 227 ? 0.8931 0.6353 1.0637 -0.0470 -0.0294 -0.0177 245 ALA A O   
1664 C CB  . ALA A 227 ? 1.0410 0.7613 1.1485 -0.0359 -0.0854 0.0187  245 ALA A CB  
1665 N N   . TYR A 228 ? 0.9806 0.7691 1.2089 -0.0364 -0.0551 -0.0101 246 TYR A N   
1666 C CA  . TYR A 228 ? 0.8977 0.6949 1.1720 -0.0281 -0.0285 -0.0118 246 TYR A CA  
1667 C C   . TYR A 228 ? 0.9780 0.7817 1.2668 -0.0482 -0.0181 -0.0272 246 TYR A C   
1668 O O   . TYR A 228 ? 0.9481 0.7258 1.2245 -0.0487 0.0023  -0.0293 246 TYR A O   
1669 C CB  . TYR A 228 ? 0.8844 0.7193 1.2251 -0.0145 -0.0327 -0.0050 246 TYR A CB  
1670 C CG  . TYR A 228 ? 0.9658 0.7856 1.3004 0.0141  -0.0332 0.0074  246 TYR A CG  
1671 C CD1 . TYR A 228 ? 1.0398 0.8372 1.3687 0.0340  -0.0004 0.0104  246 TYR A CD1 
1672 C CD2 . TYR A 228 ? 0.9910 0.8095 1.3165 0.0218  -0.0689 0.0154  246 TYR A CD2 
1673 C CE1 . TYR A 228 ? 0.9624 0.7390 1.2815 0.0633  -0.0014 0.0169  246 TYR A CE1 
1674 C CE2 . TYR A 228 ? 1.1034 0.9009 1.4253 0.0502  -0.0734 0.0251  246 TYR A CE2 
1675 C CZ  . TYR A 228 ? 1.0200 0.7976 1.3409 0.0721  -0.0387 0.0237  246 TYR A CZ  
1676 O OH  . TYR A 228 ? 1.0675 0.8180 1.3816 0.1035  -0.0436 0.0286  246 TYR A OH  
1677 N N   . TYR A 229 ? 1.0895 0.9205 1.4016 -0.0647 -0.0372 -0.0388 247 TYR A N   
1678 C CA  . TYR A 229 ? 0.9585 0.7902 1.2889 -0.0822 -0.0312 -0.0555 247 TYR A CA  
1679 C C   . TYR A 229 ? 0.7672 0.5690 1.0498 -0.0884 -0.0233 -0.0695 247 TYR A C   
1680 O O   . TYR A 229 ? 0.8001 0.5861 1.0954 -0.0936 -0.0114 -0.0784 247 TYR A O   
1681 C CB  . TYR A 229 ? 0.9368 0.7964 1.2965 -0.0981 -0.0596 -0.0681 247 TYR A CB  
1682 C CG  . TYR A 229 ? 1.0217 0.8694 1.3244 -0.1106 -0.0780 -0.0878 247 TYR A CG  
1683 C CD1 . TYR A 229 ? 1.1669 1.0110 1.4188 -0.1086 -0.0967 -0.0814 247 TYR A CD1 
1684 C CD2 . TYR A 229 ? 0.8938 0.7297 1.1895 -0.1241 -0.0756 -0.1133 247 TYR A CD2 
1685 C CE1 . TYR A 229 ? 1.1057 0.9365 1.2937 -0.1221 -0.1066 -0.0986 247 TYR A CE1 
1686 C CE2 . TYR A 229 ? 0.9783 0.8037 1.2174 -0.1334 -0.0849 -0.1354 247 TYR A CE2 
1687 C CZ  . TYR A 229 ? 1.0510 0.8748 1.2326 -0.1336 -0.0975 -0.1274 247 TYR A CZ  
1688 O OH  . TYR A 229 ? 1.2729 1.0838 1.3865 -0.1449 -0.1001 -0.1485 247 TYR A OH  
1689 N N   . SER A 230 ? 0.7663 0.5599 0.9991 -0.0886 -0.0299 -0.0703 248 SER A N   
1690 C CA  . SER A 230 ? 0.9098 0.6863 1.1126 -0.0952 -0.0186 -0.0850 248 SER A CA  
1691 C C   . SER A 230 ? 0.8700 0.6179 1.0700 -0.0845 -0.0031 -0.0744 248 SER A C   
1692 O O   . SER A 230 ? 0.7464 0.4804 0.9560 -0.0873 0.0051  -0.0874 248 SER A O   
1693 C CB  . SER A 230 ? 0.8679 0.6474 1.0184 -0.1035 -0.0254 -0.0864 248 SER A CB  
1694 O OG  . SER A 230 ? 0.9466 0.7415 1.0834 -0.1152 -0.0434 -0.1003 248 SER A OG  
1695 N N   . PHE A 231 ? 0.9605 0.6945 1.1471 -0.0708 -0.0034 -0.0526 249 PHE A N   
1696 C CA  . PHE A 231 ? 0.8309 0.5281 0.9999 -0.0613 0.0038  -0.0432 249 PHE A CA  
1697 C C   . PHE A 231 ? 0.8152 0.4898 0.9890 -0.0455 0.0128  -0.0308 249 PHE A C   
1698 O O   . PHE A 231 ? 0.8757 0.5187 1.0448 -0.0437 0.0193  -0.0315 249 PHE A O   
1699 C CB  . PHE A 231 ? 0.8207 0.5064 0.9535 -0.0600 -0.0051 -0.0302 249 PHE A CB  
1700 C CG  . PHE A 231 ? 1.0583 0.7629 1.1763 -0.0785 -0.0054 -0.0398 249 PHE A CG  
1701 C CD1 . PHE A 231 ? 0.9756 0.6751 1.0993 -0.0870 0.0044  -0.0490 249 PHE A CD1 
1702 C CD2 . PHE A 231 ? 0.9274 0.6544 1.0259 -0.0876 -0.0148 -0.0402 249 PHE A CD2 
1703 C CE1 . PHE A 231 ? 0.9287 0.6507 1.0405 -0.1039 0.0139  -0.0595 249 PHE A CE1 
1704 C CE2 . PHE A 231 ? 0.9732 0.7125 1.0426 -0.1059 -0.0092 -0.0495 249 PHE A CE2 
1705 C CZ  . PHE A 231 ? 0.9677 0.7074 1.0447 -0.1140 0.0099  -0.0598 249 PHE A CZ  
1706 N N   . PHE A 232 ? 0.8704 0.5584 1.0521 -0.0332 0.0135  -0.0198 250 PHE A N   
1707 C CA  . PHE A 232 ? 0.8823 0.5500 1.0634 -0.0161 0.0311  -0.0100 250 PHE A CA  
1708 C C   . PHE A 232 ? 0.8505 0.5229 1.0592 -0.0256 0.0484  -0.0133 250 PHE A C   
1709 O O   . PHE A 232 ? 0.8495 0.4819 1.0323 -0.0207 0.0628  -0.0075 250 PHE A O   
1710 C CB  . PHE A 232 ? 0.8041 0.4960 1.0059 0.0012  0.0311  -0.0015 250 PHE A CB  
1711 C CG  . PHE A 232 ? 0.8104 0.4813 1.0059 0.0233  0.0563  0.0055  250 PHE A CG  
1712 C CD1 . PHE A 232 ? 0.9764 0.5867 1.1116 0.0356  0.0608  0.0083  250 PHE A CD1 
1713 C CD2 . PHE A 232 ? 0.8548 0.5662 1.1048 0.0316  0.0760  0.0079  250 PHE A CD2 
1714 C CE1 . PHE A 232 ? 0.9999 0.5833 1.1134 0.0572  0.0869  0.0115  250 PHE A CE1 
1715 C CE2 . PHE A 232 ? 0.8937 0.5883 1.1346 0.0529  0.1083  0.0121  250 PHE A CE2 
1716 C CZ  . PHE A 232 ? 0.8857 0.5127 1.0502 0.0664  0.1149  0.0128  250 PHE A CZ  
1717 N N   . LEU A 233 ? 0.8933 0.6075 1.1488 -0.0410 0.0438  -0.0212 251 LEU A N   
1718 C CA  . LEU A 233 ? 0.9590 0.6767 1.2474 -0.0536 0.0576  -0.0212 251 LEU A CA  
1719 C C   . LEU A 233 ? 0.9329 0.6044 1.1945 -0.0620 0.0564  -0.0262 251 LEU A C   
1720 O O   . LEU A 233 ? 0.9139 0.5533 1.1625 -0.0627 0.0728  -0.0149 251 LEU A O   
1721 C CB  . LEU A 233 ? 0.8543 0.6196 1.1981 -0.0705 0.0431  -0.0313 251 LEU A CB  
1722 C CG  . LEU A 233 ? 0.7835 0.5533 1.1709 -0.0893 0.0510  -0.0311 251 LEU A CG  
1723 C CD1 . LEU A 233 ? 0.8006 0.5768 1.2110 -0.0847 0.0831  -0.0104 251 LEU A CD1 
1724 C CD2 . LEU A 233 ? 0.9791 0.7887 1.4163 -0.1064 0.0266  -0.0448 251 LEU A CD2 
1725 N N   . PRO A 234 ? 0.8964 0.5615 1.1502 -0.0685 0.0385  -0.0424 252 PRO A N   
1726 C CA  . PRO A 234 ? 0.8429 0.4645 1.0850 -0.0729 0.0329  -0.0480 252 PRO A CA  
1727 C C   . PRO A 234 ? 0.9578 0.5257 1.1512 -0.0601 0.0353  -0.0334 252 PRO A C   
1728 O O   . PRO A 234 ? 0.9809 0.5028 1.1576 -0.0629 0.0345  -0.0267 252 PRO A O   
1729 C CB  . PRO A 234 ? 0.8799 0.5177 1.1317 -0.0776 0.0184  -0.0707 252 PRO A CB  
1730 C CG  . PRO A 234 ? 0.8557 0.5284 1.0961 -0.0746 0.0179  -0.0693 252 PRO A CG  
1731 C CD  . PRO A 234 ? 0.8463 0.5429 1.1029 -0.0728 0.0237  -0.0569 252 PRO A CD  
1732 N N   . ILE A 235 ? 0.9369 0.5014 1.1009 -0.0468 0.0340  -0.0275 253 ILE A N   
1733 C CA  . ILE A 235 ? 0.9761 0.4817 1.0872 -0.0341 0.0305  -0.0162 253 ILE A CA  
1734 C C   . ILE A 235 ? 0.9073 0.3845 0.9877 -0.0276 0.0532  -0.0015 253 ILE A C   
1735 O O   . ILE A 235 ? 0.9198 0.3355 0.9533 -0.0261 0.0506  0.0063  253 ILE A O   
1736 C CB  . ILE A 235 ? 1.1078 0.6134 1.1963 -0.0225 0.0222  -0.0129 253 ILE A CB  
1737 C CG1 . ILE A 235 ? 1.0627 0.5980 1.1782 -0.0338 0.0071  -0.0243 253 ILE A CG1 
1738 C CG2 . ILE A 235 ? 1.2936 0.7299 1.3235 -0.0095 0.0126  -0.0038 253 ILE A CG2 
1739 C CD1 . ILE A 235 ? 1.0168 0.5546 1.1129 -0.0289 -0.0013 -0.0169 253 ILE A CD1 
1740 N N   . VAL A 236 ? 1.0029 0.5235 1.1090 -0.0239 0.0760  0.0028  254 VAL A N   
1741 C CA  . VAL A 236 ? 1.0338 0.5396 1.1205 -0.0181 0.1082  0.0160  254 VAL A CA  
1742 C C   . VAL A 236 ? 1.1341 0.6183 1.2239 -0.0384 0.1153  0.0228  254 VAL A C   
1743 O O   . VAL A 236 ? 1.0935 0.5243 1.1276 -0.0376 0.1327  0.0363  254 VAL A O   
1744 C CB  . VAL A 236 ? 1.0716 0.6430 1.2126 -0.0108 0.1294  0.0173  254 VAL A CB  
1745 C CG1 . VAL A 236 ? 1.1478 0.7266 1.3006 -0.0142 0.1702  0.0298  254 VAL A CG1 
1746 C CG2 . VAL A 236 ? 1.0552 0.6232 1.1733 0.0151  0.1255  0.0156  254 VAL A CG2 
1747 N N   . CYS A 237 ? 1.2174 0.7358 1.3651 -0.0575 0.1010  0.0139  255 CYS A N   
1748 C CA  . CYS A 237 ? 1.1534 0.6445 1.3077 -0.0781 0.1012  0.0206  255 CYS A CA  
1749 C C   . CYS A 237 ? 1.1993 0.6101 1.2917 -0.0764 0.0799  0.0243  255 CYS A C   
1750 O O   . CYS A 237 ? 1.2120 0.5678 1.2597 -0.0846 0.0891  0.0421  255 CYS A O   
1751 C CB  . CYS A 237 ? 0.9805 0.5141 1.2045 -0.0953 0.0818  0.0042  255 CYS A CB  
1752 S SG  . CYS A 237 ? 0.9974 0.6138 1.2982 -0.1044 0.0975  0.0040  255 CYS A SG  
1753 N N   . GLY A 238 ? 1.0420 0.4439 1.1318 -0.0673 0.0501  0.0094  256 GLY A N   
1754 C CA  . GLY A 238 ? 1.1024 0.4316 1.1476 -0.0644 0.0220  0.0119  256 GLY A CA  
1755 C C   . GLY A 238 ? 1.2746 0.5367 1.2296 -0.0537 0.0312  0.0305  256 GLY A C   
1756 O O   . GLY A 238 ? 1.2615 0.4512 1.1625 -0.0596 0.0203  0.0440  256 GLY A O   
1757 N N   . MET A 239 ? 1.2429 0.5216 1.1740 -0.0372 0.0495  0.0308  257 MET A N   
1758 C CA  . MET A 239 ? 1.2789 0.4894 1.1159 -0.0230 0.0595  0.0427  257 MET A CA  
1759 C C   . MET A 239 ? 1.4128 0.5983 1.2079 -0.0317 0.0981  0.0608  257 MET A C   
1760 O O   . MET A 239 ? 1.6822 0.7827 1.3869 -0.0326 0.0946  0.0740  257 MET A O   
1761 C CB  . MET A 239 ? 1.4626 0.6995 1.2929 -0.0015 0.0726  0.0362  257 MET A CB  
1762 C CG  . MET A 239 ? 1.3679 0.6137 1.2210 0.0040  0.0357  0.0244  257 MET A CG  
1763 S SD  . MET A 239 ? 1.1505 0.4321 1.0090 0.0251  0.0473  0.0196  257 MET A SD  
1764 C CE  . MET A 239 ? 1.5086 0.7087 1.2608 0.0486  0.0669  0.0254  257 MET A CE  
1765 N N   . GLN A 240 ? 1.3749 0.6320 1.2338 -0.0401 0.1346  0.0632  258 GLN A N   
1766 C CA  . GLN A 240 ? 1.4347 0.6801 1.2680 -0.0522 0.1790  0.0828  258 GLN A CA  
1767 C C   . GLN A 240 ? 1.5733 0.7564 1.3761 -0.0772 0.1608  0.0984  258 GLN A C   
1768 O O   . GLN A 240 ? 1.7027 0.8175 1.4188 -0.0842 0.1814  0.1188  258 GLN A O   
1769 C CB  . GLN A 240 ? 1.3285 0.6716 1.2616 -0.0600 0.2127  0.0820  258 GLN A CB  
1770 C CG  . GLN A 240 ? 1.4498 0.8477 1.4099 -0.0338 0.2344  0.0711  258 GLN A CG  
1771 C CD  . GLN A 240 ? 1.2254 0.7211 1.2972 -0.0420 0.2551  0.0698  258 GLN A CD  
1772 O OE1 . GLN A 240 ? 1.1455 0.6682 1.2744 -0.0692 0.2521  0.0759  258 GLN A OE1 
1773 N NE2 . GLN A 240 ? 1.3981 0.9431 1.5046 -0.0182 0.2705  0.0615  258 GLN A NE2 
1774 N N   . MET A 241 ? 1.5179 0.7180 1.3860 -0.0904 0.1220  0.0887  259 MET A N   
1775 C CA  . MET A 241 ? 1.4133 0.5472 1.2580 -0.1112 0.0960  0.1019  259 MET A CA  
1776 C C   . MET A 241 ? 1.4379 0.4700 1.1846 -0.1013 0.0598  0.1078  259 MET A C   
1777 O O   . MET A 241 ? 1.5674 0.5310 1.2576 -0.1150 0.0461  0.1276  259 MET A O   
1778 C CB  . MET A 241 ? 1.4097 0.5836 1.3502 -0.1215 0.0611  0.0833  259 MET A CB  
1779 C CG  . MET A 241 ? 1.2947 0.5320 1.3138 -0.1431 0.0847  0.0857  259 MET A CG  
1780 S SD  . MET A 241 ? 1.7305 0.9045 1.7160 -0.1770 0.0987  0.1208  259 MET A SD  
1781 C CE  . MET A 241 ? 1.3003 0.3931 1.2784 -0.1809 0.0308  0.1136  259 MET A CE  
1782 N N   . GLY A 242 ? 1.5046 0.5338 1.2353 -0.0781 0.0388  0.0919  260 GLY A N   
1783 C CA  . GLY A 242 ? 1.6979 0.6834 1.3686 -0.0655 -0.0021 0.0929  260 GLY A CA  
1784 C C   . GLY A 242 ? 1.8851 0.7856 1.4213 -0.0621 0.0219  0.1118  260 GLY A C   
1785 O O   . GLY A 242 ? 2.1920 1.0434 1.6630 -0.0578 -0.0138 0.1159  260 GLY A O   
1786 N N   . GLY A 243 ? 1.8887 0.7813 1.3879 -0.0625 0.0861  0.1212  261 GLY A N   
1787 C CA  . GLY A 243 ? 2.0418 0.8651 1.4142 -0.0566 0.1237  0.1359  261 GLY A CA  
1788 C C   . GLY A 243 ? 2.1195 0.9543 1.4568 -0.0259 0.1475  0.1193  261 GLY A C   
1789 O O   . GLY A 243 ? 2.1719 0.9364 1.3891 -0.0156 0.1753  0.1255  261 GLY A O   
1790 N N   . ILE A 244 ? 2.3573 1.2715 1.7882 -0.0109 0.1372  0.0983  262 ILE A N   
1791 C CA  . ILE A 244 ? 1.9493 0.8725 1.3548 0.0189  0.1555  0.0829  262 ILE A CA  
1792 C C   . ILE A 244 ? 2.1805 1.1642 1.6085 0.0254  0.2294  0.0852  262 ILE A C   
1793 O O   . ILE A 244 ? 2.3108 1.3854 1.8458 0.0113  0.2530  0.0886  262 ILE A O   
1794 C CB  . ILE A 244 ? 1.8258 0.8104 1.3228 0.0287  0.1191  0.0645  262 ILE A CB  
1795 C CG1 . ILE A 244 ? 1.8083 0.7533 1.3133 0.0182  0.0524  0.0624  262 ILE A CG1 
1796 C CG2 . ILE A 244 ? 1.8792 0.8518 1.3389 0.0591  0.1258  0.0505  262 ILE A CG2 
1797 C CD1 . ILE A 244 ? 2.0113 0.8905 1.4249 0.0246  0.0133  0.0628  262 ILE A CD1 
1798 N N   . SER A 245 ? 2.7543 1.6872 2.0846 0.0475  0.2655  0.0817  263 SER A N   
1799 C CA  . SER A 245 ? 2.6647 1.6581 2.0231 0.0585  0.3408  0.0808  263 SER A CA  
1800 C C   . SER A 245 ? 2.9066 2.0010 2.3865 0.0789  0.3424  0.0624  263 SER A C   
1801 O O   . SER A 245 ? 2.0696 1.1567 1.5601 0.0944  0.2952  0.0479  263 SER A O   
1802 C CB  . SER A 245 ? 2.3674 1.2751 1.5830 0.0820  0.3804  0.0759  263 SER A CB  
1803 O OG  . SER A 245 ? 2.5954 1.4417 1.7490 0.1111  0.3373  0.0550  263 SER A OG  
1804 N N   . LEU A 246 ? 2.2425 1.4298 1.8163 0.0768  0.3954  0.0654  264 LEU A N   
1805 C CA  . LEU A 246 ? 2.2888 1.5745 1.9878 0.0920  0.3896  0.0516  264 LEU A CA  
1806 C C   . LEU A 246 ? 2.3928 1.6550 2.0566 0.1343  0.3871  0.0303  264 LEU A C   
1807 O O   . LEU A 246 ? 2.3157 1.6054 2.0320 0.1456  0.3444  0.0198  264 LEU A O   
1808 C CB  . LEU A 246 ? 2.2080 1.5927 2.0161 0.0823  0.4451  0.0594  264 LEU A CB  
1809 C CG  . LEU A 246 ? 2.0705 1.4830 1.9281 0.0383  0.4472  0.0809  264 LEU A CG  
1810 C CD1 . LEU A 246 ? 1.9545 1.4681 1.9305 0.0293  0.5008  0.0883  264 LEU A CD1 
1811 C CD2 . LEU A 246 ? 1.7880 1.2159 1.6977 0.0201  0.3790  0.0776  264 LEU A CD2 
1812 N N   . ASP A 247 ? 2.6447 1.8507 2.2141 0.1579  0.4327  0.0236  265 ASP A N   
1813 C CA  . ASP A 247 ? 2.6324 1.8112 2.1686 0.2019  0.4337  -0.0003 265 ASP A CA  
1814 C C   . ASP A 247 ? 2.5350 1.6224 1.9876 0.2097  0.3639  -0.0088 265 ASP A C   
1815 O O   . ASP A 247 ? 2.5119 1.5600 1.9260 0.2447  0.3556  -0.0284 265 ASP A O   
1816 C CB  . ASP A 247 ? 2.8434 1.9803 2.2910 0.2261  0.5065  -0.0092 265 ASP A CB  
1817 C CG  . ASP A 247 ? 2.8931 2.1373 2.4508 0.2279  0.5819  -0.0060 265 ASP A CG  
1818 O OD1 . ASP A 247 ? 2.7957 2.1418 2.4971 0.2099  0.5698  0.0033  265 ASP A OD1 
1819 O OD2 . ASP A 247 ? 3.0137 2.2401 2.5148 0.2468  0.6536  -0.0136 265 ASP A OD2 
1820 N N   . ASN A 248 ? 2.3511 1.4042 1.7825 0.1789  0.3128  0.0046  266 ASN A N   
1821 C CA  . ASN A 248 ? 2.2804 1.2570 1.6528 0.1826  0.2454  -0.0018 266 ASN A CA  
1822 C C   . ASN A 248 ? 2.0647 1.0953 1.5265 0.1945  0.2112  -0.0108 266 ASN A C   
1823 O O   . ASN A 248 ? 1.8733 1.0007 1.4498 0.1835  0.2151  -0.0058 266 ASN A O   
1824 C CB  . ASN A 248 ? 2.2107 1.1572 1.5706 0.1473  0.2006  0.0140  266 ASN A CB  
1825 C CG  . ASN A 248 ? 2.1858 1.0415 1.4752 0.1496  0.1343  0.0090  266 ASN A CG  
1826 O OD1 . ASN A 248 ? 2.1527 1.0050 1.4585 0.1658  0.1048  -0.0024 266 ASN A OD1 
1827 N ND2 . ASN A 248 ? 2.2861 1.0646 1.4998 0.1319  0.1066  0.0192  266 ASN A ND2 
1828 N N   . LEU A 249 ? 2.1675 1.1276 1.5697 0.2152  0.1737  -0.0230 267 LEU A N   
1829 C CA  . LEU A 249 ? 2.0441 1.0404 1.5161 0.2259  0.1401  -0.0284 267 LEU A CA  
1830 C C   . LEU A 249 ? 1.7569 0.8063 1.3087 0.1921  0.0981  -0.0146 267 LEU A C   
1831 O O   . LEU A 249 ? 1.7315 0.8380 1.3592 0.1928  0.0827  -0.0134 267 LEU A O   
1832 C CB  . LEU A 249 ? 2.0500 0.9460 1.4349 0.2498  0.1027  -0.0421 267 LEU A CB  
1833 C CG  . LEU A 249 ? 2.0356 0.9522 1.4736 0.2713  0.0799  -0.0496 267 LEU A CG  
1834 C CD1 . LEU A 249 ? 2.2252 1.2011 1.7155 0.3037  0.1332  -0.0613 267 LEU A CD1 
1835 C CD2 . LEU A 249 ? 2.0550 0.9217 1.4339 0.2743  0.0331  -0.0582 267 LEU A CD2 
1836 N N   . LEU A 250 ? 1.7033 0.7325 1.2372 0.1636  0.0796  -0.0048 268 LEU A N   
1837 C CA  . LEU A 250 ? 1.8154 0.8974 1.4268 0.1340  0.0471  0.0038  268 LEU A CA  
1838 C C   . LEU A 250 ? 1.5562 0.7445 1.2700 0.1270  0.0711  0.0063  268 LEU A C   
1839 O O   . LEU A 250 ? 1.4808 0.7138 1.2528 0.1170  0.0467  0.0083  268 LEU A O   
1840 C CB  . LEU A 250 ? 1.7094 0.7632 1.2997 0.1092  0.0340  0.0112  268 LEU A CB  
1841 C CG  . LEU A 250 ? 2.1206 1.1227 1.6506 0.1039  -0.0092 0.0103  268 LEU A CG  
1842 C CD1 . LEU A 250 ? 1.5617 0.5514 1.0799 0.0829  -0.0189 0.0182  268 LEU A CD1 
1843 C CD2 . LEU A 250 ? 1.9600 1.0064 1.5495 0.0925  -0.0535 0.0093  268 LEU A CD2 
1844 N N   . TYR A 251 ? 1.5818 0.8086 1.3159 0.1308  0.1182  0.0071  269 TYR A N   
1845 C CA  . TYR A 251 ? 1.5388 0.8636 1.3740 0.1211  0.1352  0.0096  269 TYR A CA  
1846 C C   . TYR A 251 ? 1.3416 0.7064 1.2264 0.1388  0.1222  0.0053  269 TYR A C   
1847 O O   . TYR A 251 ? 1.3357 0.7758 1.3014 0.1291  0.1217  0.0077  269 TYR A O   
1848 C CB  . TYR A 251 ? 1.6334 0.9884 1.4852 0.1227  0.1895  0.0127  269 TYR A CB  
1849 C CG  . TYR A 251 ? 1.5015 0.8344 1.3282 0.0951  0.1975  0.0228  269 TYR A CG  
1850 C CD1 . TYR A 251 ? 1.5031 0.8917 1.4026 0.0665  0.1888  0.0280  269 TYR A CD1 
1851 C CD2 . TYR A 251 ? 1.7067 0.9543 1.4302 0.0979  0.2091  0.0268  269 TYR A CD2 
1852 C CE1 . TYR A 251 ? 1.4038 0.7653 1.2831 0.0423  0.1908  0.0373  269 TYR A CE1 
1853 C CE2 . TYR A 251 ? 1.7866 1.0051 1.4836 0.0720  0.2100  0.0391  269 TYR A CE2 
1854 C CZ  . TYR A 251 ? 1.6425 0.9190 1.4221 0.0447  0.2005  0.0446  269 TYR A CZ  
1855 O OH  . TYR A 251 ? 1.7776 1.0186 1.5333 0.0200  0.1966  0.0570  269 TYR A OH  
1856 N N   . LYS A 252 ? 1.4730 0.7827 1.3085 0.1639  0.1062  -0.0007 270 LYS A N   
1857 C CA  . LYS A 252 ? 1.4949 0.8277 1.3704 0.1772  0.0809  -0.0013 270 LYS A CA  
1858 C C   . LYS A 252 ? 1.3740 0.6795 1.2336 0.1575  0.0313  0.0062  270 LYS A C   
1859 O O   . LYS A 252 ? 1.2736 0.6266 1.1834 0.1433  0.0112  0.0135  270 LYS A O   
1860 C CB  . LYS A 252 ? 1.5573 0.8476 1.3996 0.2191  0.0926  -0.0133 270 LYS A CB  
1861 C CG  . LYS A 252 ? 1.5155 0.8374 1.4155 0.2376  0.0700  -0.0132 270 LYS A CG  
1862 C CD  . LYS A 252 ? 1.4675 0.8893 1.4710 0.2326  0.0868  -0.0093 270 LYS A CD  
1863 C CE  . LYS A 252 ? 1.5675 1.0125 1.6255 0.2534  0.0572  -0.0082 270 LYS A CE  
1864 N NZ  . LYS A 252 ? 2.0289 1.5676 2.1900 0.2474  0.0643  -0.0043 270 LYS A NZ  
1865 N N   . LYS A 253 ? 1.3124 0.5420 1.1027 0.1540  0.0111  0.0054  271 LYS A N   
1866 C CA  . LYS A 253 ? 1.2911 0.5034 1.0810 0.1306  -0.0316 0.0140  271 LYS A CA  
1867 C C   . LYS A 253 ? 1.3450 0.6290 1.1966 0.0984  -0.0302 0.0199  271 LYS A C   
1868 O O   . LYS A 253 ? 1.2675 0.5867 1.1535 0.0836  -0.0475 0.0274  271 LYS A O   
1869 C CB  . LYS A 253 ? 1.4674 0.6034 1.1926 0.1263  -0.0533 0.0119  271 LYS A CB  
1870 C CG  . LYS A 253 ? 1.7876 0.8720 1.4498 0.1527  -0.0540 0.0018  271 LYS A CG  
1871 C CD  . LYS A 253 ? 1.6231 0.6764 1.2382 0.1392  -0.0760 -0.0002 271 LYS A CD  
1872 C CE  . LYS A 253 ? 1.8634 0.8500 1.3952 0.1669  -0.0743 -0.0134 271 LYS A CE  
1873 N NZ  . LYS A 253 ? 2.0300 0.9739 1.5009 0.1553  -0.0986 -0.0152 271 LYS A NZ  
1874 N N   . VAL A 254 ? 1.3563 0.6590 1.2173 0.0880  -0.0081 0.0163  272 VAL A N   
1875 C CA  . VAL A 254 ? 1.1476 0.5126 1.0652 0.0610  -0.0056 0.0166  272 VAL A CA  
1876 C C   . VAL A 254 ? 1.1282 0.5607 1.0979 0.0592  -0.0011 0.0184  272 VAL A C   
1877 O O   . VAL A 254 ? 1.2175 0.6834 1.2127 0.0394  -0.0158 0.0206  272 VAL A O   
1878 C CB  . VAL A 254 ? 1.2957 0.6647 1.2158 0.0544  0.0181  0.0131  272 VAL A CB  
1879 C CG1 . VAL A 254 ? 1.2342 0.6725 1.2192 0.0327  0.0248  0.0096  272 VAL A CG1 
1880 C CG2 . VAL A 254 ? 1.3770 0.6787 1.2497 0.0488  -0.0003 0.0132  272 VAL A CG2 
1881 N N   . GLU A 255 ? 1.1120 0.5634 1.0969 0.0805  0.0184  0.0172  273 GLU A N   
1882 C CA  . GLU A 255 ? 1.0323 0.5440 1.0711 0.0806  0.0141  0.0195  273 GLU A CA  
1883 C C   . GLU A 255 ? 1.0441 0.5446 1.0697 0.0744  -0.0206 0.0281  273 GLU A C   
1884 O O   . GLU A 255 ? 1.0260 0.5638 1.0720 0.0524  -0.0333 0.0313  273 GLU A O   
1885 C CB  . GLU A 255 ? 1.0853 0.6120 1.1492 0.1106  0.0357  0.0167  273 GLU A CB  
1886 C CG  . GLU A 255 ? 1.0981 0.6870 1.2296 0.1137  0.0246  0.0193  273 GLU A CG  
1887 C CD  . GLU A 255 ? 1.1807 0.7951 1.3588 0.1449  0.0499  0.0144  273 GLU A CD  
1888 O OE1 . GLU A 255 ? 1.3639 0.9542 1.5182 0.1601  0.0865  0.0083  273 GLU A OE1 
1889 O OE2 . GLU A 255 ? 1.0294 0.6872 1.2679 0.1545  0.0333  0.0164  273 GLU A OE2 
1890 N N   . ASN A 256 ? 1.2194 0.6608 1.2020 0.0909  -0.0367 0.0323  274 ASN A N   
1891 C CA  . ASN A 256 ? 1.2001 0.6228 1.1671 0.0811  -0.0707 0.0452  274 ASN A CA  
1892 C C   . ASN A 256 ? 1.0972 0.5373 1.0646 0.0446  -0.0771 0.0497  274 ASN A C   
1893 O O   . ASN A 256 ? 1.0968 0.5686 1.0744 0.0256  -0.0878 0.0578  274 ASN A O   
1894 C CB  . ASN A 256 ? 1.3375 0.6821 1.2554 0.1001  -0.0898 0.0477  274 ASN A CB  
1895 C CG  . ASN A 256 ? 1.6534 0.9816 1.5743 0.1391  -0.0891 0.0425  274 ASN A CG  
1896 O OD1 . ASN A 256 ? 2.0482 1.3621 1.9717 0.1473  -0.1177 0.0521  274 ASN A OD1 
1897 N ND2 . ASN A 256 ? 1.6546 0.9836 1.5762 0.1635  -0.0552 0.0274  274 ASN A ND2 
1898 N N   . ILE A 257 ? 1.0442 0.4643 1.0010 0.0351  -0.0695 0.0433  275 ILE A N   
1899 C CA  . ILE A 257 ? 1.0783 0.5199 1.0495 0.0041  -0.0720 0.0439  275 ILE A CA  
1900 C C   . ILE A 257 ? 1.0805 0.5884 1.0853 -0.0109 -0.0571 0.0372  275 ILE A C   
1901 O O   . ILE A 257 ? 1.1150 0.6478 1.1207 -0.0321 -0.0619 0.0422  275 ILE A O   
1902 C CB  . ILE A 257 ? 1.1173 0.5305 1.0856 0.0010  -0.0695 0.0353  275 ILE A CB  
1903 C CG1 . ILE A 257 ? 1.2971 0.6356 1.2235 0.0124  -0.0937 0.0418  275 ILE A CG1 
1904 C CG2 . ILE A 257 ? 1.1141 0.5632 1.1181 -0.0269 -0.0668 0.0306  275 ILE A CG2 
1905 C CD1 . ILE A 257 ? 1.4374 0.7362 1.3556 0.0080  -0.1044 0.0360  275 ILE A CD1 
1906 N N   . ALA A 258 ? 1.0484 0.5819 1.0762 -0.0009 -0.0392 0.0264  276 ALA A N   
1907 C CA  . ALA A 258 ? 1.0389 0.6285 1.0984 -0.0150 -0.0311 0.0179  276 ALA A CA  
1908 C C   . ALA A 258 ? 1.0169 0.6245 1.0677 -0.0204 -0.0489 0.0279  276 ALA A C   
1909 O O   . ALA A 258 ? 1.0217 0.6509 1.0639 -0.0428 -0.0517 0.0262  276 ALA A O   
1910 C CB  . ALA A 258 ? 1.0139 0.6249 1.1049 -0.0033 -0.0139 0.0102  276 ALA A CB  
1911 N N   . ILE A 259 ? 1.0535 0.6451 1.1000 0.0008  -0.0621 0.0387  277 ILE A N   
1912 C CA  . ILE A 259 ? 1.1040 0.7014 1.1390 -0.0023 -0.0881 0.0518  277 ILE A CA  
1913 C C   . ILE A 259 ? 1.1417 0.7229 1.1344 -0.0296 -0.0976 0.0630  277 ILE A C   
1914 O O   . ILE A 259 ? 1.2000 0.8064 1.1783 -0.0519 -0.1002 0.0628  277 ILE A O   
1915 C CB  . ILE A 259 ? 0.9450 0.5120 0.9810 0.0285  -0.1048 0.0617  277 ILE A CB  
1916 C CG1 . ILE A 259 ? 0.9922 0.5938 1.0834 0.0529  -0.0902 0.0508  277 ILE A CG1 
1917 C CG2 . ILE A 259 ? 1.1216 0.6735 1.1328 0.0229  -0.1411 0.0807  277 ILE A CG2 
1918 C CD1 . ILE A 259 ? 1.0494 0.6229 1.1496 0.0901  -0.0933 0.0524  277 ILE A CD1 
1919 N N   . LEU A 260 ? 1.0373 0.5754 1.0087 -0.0302 -0.1005 0.0717  278 LEU A N   
1920 C CA  . LEU A 260 ? 1.0834 0.6093 1.0251 -0.0590 -0.1063 0.0859  278 LEU A CA  
1921 C C   . LEU A 260 ? 1.0955 0.6671 1.0468 -0.0848 -0.0815 0.0717  278 LEU A C   
1922 O O   . LEU A 260 ? 1.1624 0.7509 1.0857 -0.1070 -0.0812 0.0779  278 LEU A O   
1923 C CB  . LEU A 260 ? 1.2840 0.7620 1.2190 -0.0580 -0.1127 0.0932  278 LEU A CB  
1924 C CG  . LEU A 260 ? 1.3266 0.7467 1.2425 -0.0308 -0.1384 0.1032  278 LEU A CG  
1925 C CD1 . LEU A 260 ? 1.5234 0.8908 1.4291 -0.0320 -0.1486 0.1062  278 LEU A CD1 
1926 C CD2 . LEU A 260 ? 1.3723 0.7732 1.2606 -0.0352 -0.1668 0.1261  278 LEU A CD2 
1927 N N   . MET A 261 ? 1.1791 0.7675 1.1655 -0.0803 -0.0612 0.0510  279 MET A N   
1928 C CA  . MET A 261 ? 1.1305 0.7589 1.1332 -0.0999 -0.0383 0.0326  279 MET A CA  
1929 C C   . MET A 261 ? 1.1391 0.7993 1.1254 -0.1074 -0.0382 0.0251  279 MET A C   
1930 O O   . MET A 261 ? 1.2124 0.8892 1.1708 -0.1299 -0.0284 0.0230  279 MET A O   
1931 C CB  . MET A 261 ? 0.9999 0.6336 1.0443 -0.0894 -0.0252 0.0121  279 MET A CB  
1932 C CG  . MET A 261 ? 1.1180 0.7145 1.1729 -0.0846 -0.0315 0.0176  279 MET A CG  
1933 S SD  . MET A 261 ? 1.1319 0.7254 1.2267 -0.0757 -0.0232 -0.0037 279 MET A SD  
1934 C CE  . MET A 261 ? 1.2667 0.9119 1.4005 -0.0970 -0.0024 -0.0253 279 MET A CE  
1935 N N   . GLY A 262 ? 1.1027 0.7693 1.1037 -0.0894 -0.0498 0.0218  280 GLY A N   
1936 C CA  . GLY A 262 ? 1.1440 0.8356 1.1339 -0.0961 -0.0604 0.0156  280 GLY A CA  
1937 C C   . GLY A 262 ? 1.1083 0.7860 1.0376 -0.1144 -0.0751 0.0337  280 GLY A C   
1938 O O   . GLY A 262 ? 1.2306 0.9218 1.1241 -0.1366 -0.0640 0.0245  280 GLY A O   
1939 N N   . GLU A 263 ? 1.2444 0.8888 1.1563 -0.1054 -0.0985 0.0596  281 GLU A N   
1940 C CA  . GLU A 263 ? 1.4055 1.0246 1.2538 -0.1244 -0.1177 0.0840  281 GLU A CA  
1941 C C   . GLU A 263 ? 1.3939 1.0226 1.2070 -0.1564 -0.0871 0.0810  281 GLU A C   
1942 O O   . GLU A 263 ? 1.5165 1.1570 1.2814 -0.1766 -0.0816 0.0752  281 GLU A O   
1943 C CB  . GLU A 263 ? 1.3285 0.9010 1.1712 -0.1114 -0.1411 0.1105  281 GLU A CB  
1944 C CG  . GLU A 263 ? 1.5965 1.1333 1.3830 -0.1203 -0.1790 0.1397  281 GLU A CG  
1945 C CD  . GLU A 263 ? 1.7663 1.2507 1.5540 -0.1031 -0.2060 0.1623  281 GLU A CD  
1946 O OE1 . GLU A 263 ? 1.5331 1.0133 1.3687 -0.0736 -0.2010 0.1503  281 GLU A OE1 
1947 O OE2 . GLU A 263 ? 1.5683 1.0099 1.3028 -0.1195 -0.2326 0.1919  281 GLU A OE2 
1948 N N   . TYR A 264 ? 1.3283 0.9545 1.1705 -0.1597 -0.0653 0.0808  282 TYR A N   
1949 C CA  . TYR A 264 ? 1.4077 1.0519 1.2397 -0.1882 -0.0316 0.0773  282 TYR A CA  
1950 C C   . TYR A 264 ? 1.4590 1.1413 1.2761 -0.1983 -0.0069 0.0483  282 TYR A C   
1951 O O   . TYR A 264 ? 1.5189 1.2011 1.2696 -0.2216 0.0012  0.0536  282 TYR A O   
1952 C CB  . TYR A 264 ? 1.3373 0.9854 1.2334 -0.1817 -0.0163 0.0692  282 TYR A CB  
1953 C CG  . TYR A 264 ? 1.3421 1.0211 1.2607 -0.2060 0.0206  0.0603  282 TYR A CG  
1954 C CD1 . TYR A 264 ? 1.5495 1.2703 1.5047 -0.2036 0.0499  0.0254  282 TYR A CD1 
1955 C CD2 . TYR A 264 ? 1.5905 1.2576 1.5036 -0.2307 0.0259  0.0862  282 TYR A CD2 
1956 C CE1 . TYR A 264 ? 1.7896 1.5446 1.7795 -0.2216 0.0862  0.0136  282 TYR A CE1 
1957 C CE2 . TYR A 264 ? 1.4950 1.2002 1.4455 -0.2531 0.0639  0.0777  282 TYR A CE2 
1958 C CZ  . TYR A 264 ? 1.4970 1.2486 1.4884 -0.2464 0.0953  0.0399  282 TYR A CZ  
1959 O OH  . TYR A 264 ? 1.7356 1.5308 1.7771 -0.2647 0.1355  0.0280  282 TYR A OH  
1960 N N   . PHE A 265 ? 1.4273 1.1339 1.2961 -0.1804 0.0012  0.0179  283 PHE A N   
1961 C CA  . PHE A 265 ? 1.3682 1.1059 1.2306 -0.1885 0.0253  -0.0149 283 PHE A CA  
1962 C C   . PHE A 265 ? 1.4188 1.1487 1.2099 -0.1975 0.0061  -0.0148 283 PHE A C   
1963 O O   . PHE A 265 ? 1.5213 1.2593 1.2580 -0.2165 0.0272  -0.0293 283 PHE A O   
1964 C CB  . PHE A 265 ? 1.1766 0.9312 1.1081 -0.1681 0.0291  -0.0435 283 PHE A CB  
1965 C CG  . PHE A 265 ? 1.2965 1.0621 1.2873 -0.1654 0.0528  -0.0544 283 PHE A CG  
1966 C CD1 . PHE A 265 ? 1.4038 1.1983 1.4112 -0.1751 0.0859  -0.0820 283 PHE A CD1 
1967 C CD2 . PHE A 265 ? 1.2415 0.9856 1.2709 -0.1520 0.0397  -0.0387 283 PHE A CD2 
1968 C CE1 . PHE A 265 ? 1.2325 1.0394 1.3079 -0.1710 0.1018  -0.0921 283 PHE A CE1 
1969 C CE2 . PHE A 265 ? 1.1141 0.8628 1.1979 -0.1502 0.0521  -0.0476 283 PHE A CE2 
1970 C CZ  . PHE A 265 ? 1.2846 1.0672 1.3982 -0.1596 0.0813  -0.0735 283 PHE A CZ  
1971 N N   . GLN A 266 ? 1.4109 1.1224 1.1987 -0.1838 -0.0348 0.0011  284 GLN A N   
1972 C CA  . GLN A 266 ? 1.3214 1.0222 1.0469 -0.1920 -0.0634 0.0015  284 GLN A CA  
1973 C C   . GLN A 266 ? 1.4301 1.1046 1.0582 -0.2197 -0.0603 0.0236  284 GLN A C   
1974 O O   . GLN A 266 ? 1.7697 1.4395 1.3239 -0.2375 -0.0558 0.0104  284 GLN A O   
1975 C CB  . GLN A 266 ? 1.4891 1.1792 1.2448 -0.1712 -0.1102 0.0174  284 GLN A CB  
1976 C CG  . GLN A 266 ? 1.5516 1.2302 1.2564 -0.1781 -0.1513 0.0175  284 GLN A CG  
1977 C CD  . GLN A 266 ? 1.6725 1.3688 1.3625 -0.1878 -0.1413 -0.0195 284 GLN A CD  
1978 O OE1 . GLN A 266 ? 1.3379 1.0618 1.0986 -0.1765 -0.1269 -0.0446 284 GLN A OE1 
1979 N NE2 . GLN A 266 ? 1.9848 1.6580 1.5751 -0.2096 -0.1502 -0.0230 284 GLN A NE2 
1980 N N   . VAL A 267 ? 1.6081 1.2603 1.2287 -0.2259 -0.0612 0.0571  285 VAL A N   
1981 C CA  . VAL A 267 ? 1.6950 1.3202 1.2235 -0.2579 -0.0531 0.0830  285 VAL A CA  
1982 C C   . VAL A 267 ? 1.8064 1.4618 1.3094 -0.2801 0.0044  0.0577  285 VAL A C   
1983 O O   . VAL A 267 ? 1.8367 1.4796 1.2439 -0.3027 0.0146  0.0551  285 VAL A O   
1984 C CB  . VAL A 267 ? 1.6156 1.2124 1.1564 -0.2628 -0.0611 0.1216  285 VAL A CB  
1985 C CG1 . VAL A 267 ? 1.6962 1.2676 1.1468 -0.3025 -0.0446 0.1512  285 VAL A CG1 
1986 C CG2 . VAL A 267 ? 1.7677 1.3293 1.3240 -0.2378 -0.1182 0.1431  285 VAL A CG2 
1987 N N   . HIS A 268 ? 1.7538 1.4474 1.3419 -0.2714 0.0417  0.0357  286 HIS A N   
1988 C CA  . HIS A 268 ? 1.7023 1.4323 1.2890 -0.2855 0.0979  0.0049  286 HIS A CA  
1989 C C   . HIS A 268 ? 1.6689 1.4000 1.1965 -0.2844 0.0981  -0.0297 286 HIS A C   
1990 O O   . HIS A 268 ? 1.8405 1.5713 1.2867 -0.3064 0.1310  -0.0404 286 HIS A O   
1991 C CB  . HIS A 268 ? 1.7371 1.5045 1.4397 -0.2675 0.1215  -0.0184 286 HIS A CB  
1992 C CG  . HIS A 268 ? 1.7550 1.5646 1.4792 -0.2757 0.1778  -0.0539 286 HIS A CG  
1993 N ND1 . HIS A 268 ? 1.5406 1.3672 1.2343 -0.3046 0.2243  -0.0447 286 HIS A ND1 
1994 C CD2 . HIS A 268 ? 1.6539 1.4924 1.4329 -0.2579 0.1962  -0.0993 286 HIS A CD2 
1995 C CE1 . HIS A 268 ? 1.4704 1.3400 1.2041 -0.3013 0.2723  -0.0860 286 HIS A CE1 
1996 N NE2 . HIS A 268 ? 1.7431 1.6172 1.5278 -0.2720 0.2531  -0.1202 286 HIS A NE2 
1997 N N   . ASP A 269 ? 1.7128 1.4416 1.2758 -0.2604 0.0607  -0.0468 287 ASP A N   
1998 C CA  . ASP A 269 ? 1.8063 1.5305 1.3197 -0.2596 0.0511  -0.0805 287 ASP A CA  
1999 C C   . ASP A 269 ? 2.0021 1.6859 1.3809 -0.2838 0.0340  -0.0632 287 ASP A C   
2000 O O   . ASP A 269 ? 2.1261 1.8041 1.4227 -0.2986 0.0606  -0.0891 287 ASP A O   
2001 C CB  . ASP A 269 ? 1.6764 1.4012 1.2539 -0.2353 0.0051  -0.0895 287 ASP A CB  
2002 C CG  . ASP A 269 ? 1.8334 1.5609 1.3971 -0.2321 -0.0001 -0.1333 287 ASP A CG  
2003 O OD1 . ASP A 269 ? 2.0616 1.7686 1.5240 -0.2489 0.0044  -0.1479 287 ASP A OD1 
2004 O OD2 . ASP A 269 ? 1.6488 1.3932 1.2970 -0.2142 -0.0094 -0.1529 287 ASP A OD2 
2005 N N   . ASP A 270 ? 1.9700 1.6199 1.3187 -0.2876 -0.0107 -0.0194 288 ASP A N   
2006 C CA  . ASP A 270 ? 2.0562 1.6569 1.2701 -0.3118 -0.0358 0.0031  288 ASP A CA  
2007 C C   . ASP A 270 ? 2.1133 1.7102 1.2421 -0.3443 0.0232  0.0104  288 ASP A C   
2008 O O   . ASP A 270 ? 2.2097 1.7784 1.2144 -0.3654 0.0326  0.0014  288 ASP A O   
2009 C CB  . ASP A 270 ? 1.9942 1.5575 1.2055 -0.3074 -0.0958 0.0508  288 ASP A CB  
2010 C CG  . ASP A 270 ? 1.9966 1.5611 1.2695 -0.2796 -0.1566 0.0432  288 ASP A CG  
2011 O OD1 . ASP A 270 ? 1.9994 1.5957 1.3282 -0.2655 -0.1503 0.0044  288 ASP A OD1 
2012 O OD2 . ASP A 270 ? 2.0197 1.5537 1.2907 -0.2723 -0.2110 0.0763  288 ASP A OD2 
2013 N N   . TYR A 271 ? 2.0355 1.6604 1.2295 -0.3497 0.0649  0.0258  289 TYR A N   
2014 C CA  . TYR A 271 ? 2.0732 1.7075 1.2096 -0.3824 0.1291  0.0326  289 TYR A CA  
2015 C C   . TYR A 271 ? 2.0652 1.7289 1.1721 -0.3836 0.1832  -0.0210 289 TYR A C   
2016 O O   . TYR A 271 ? 2.1939 1.8461 1.1914 -0.4120 0.2264  -0.0221 289 TYR A O   
2017 C CB  . TYR A 271 ? 1.9423 1.6116 1.1857 -0.3847 0.1607  0.0510  289 TYR A CB  
2018 C CG  . TYR A 271 ? 1.9732 1.6734 1.1980 -0.4164 0.2365  0.0511  289 TYR A CG  
2019 C CD1 . TYR A 271 ? 2.0631 1.7294 1.1830 -0.4571 0.2510  0.0945  289 TYR A CD1 
2020 C CD2 . TYR A 271 ? 1.7958 1.5597 1.1134 -0.4062 0.2940  0.0091  289 TYR A CD2 
2021 C CE1 . TYR A 271 ? 1.9863 1.6877 1.0963 -0.4892 0.3277  0.0963  289 TYR A CE1 
2022 C CE2 . TYR A 271 ? 1.9472 1.7494 1.2651 -0.4337 0.3677  0.0074  289 TYR A CE2 
2023 C CZ  . TYR A 271 ? 2.0458 1.8198 1.2609 -0.4763 0.3878  0.0513  289 TYR A CZ  
2024 O OH  . TYR A 271 ? 2.0426 1.8612 1.2644 -0.5068 0.4683  0.0513  289 TYR A OH  
2025 N N   . ILE A 272 ? 2.0630 1.7604 1.2616 -0.3528 0.1825  -0.0664 290 ILE A N   
2026 C CA  . ILE A 272 ? 1.9597 1.6772 1.1333 -0.3487 0.2265  -0.1224 290 ILE A CA  
2027 C C   . ILE A 272 ? 2.4455 2.1094 1.4749 -0.3577 0.1948  -0.1354 290 ILE A C   
2028 O O   . ILE A 272 ? 2.2415 1.8966 1.1708 -0.3721 0.2390  -0.1639 290 ILE A O   
2029 C CB  . ILE A 272 ? 1.8707 1.6269 1.1794 -0.3143 0.2242  -0.1638 290 ILE A CB  
2030 C CG1 . ILE A 272 ? 1.8844 1.6866 1.3238 -0.3073 0.2540  -0.1523 290 ILE A CG1 
2031 C CG2 . ILE A 272 ? 2.4369 2.2038 1.7183 -0.3065 0.2608  -0.2253 290 ILE A CG2 
2032 C CD1 . ILE A 272 ? 2.1030 1.9320 1.6694 -0.2749 0.2432  -0.1841 290 ILE A CD1 
2033 N N   . ASP A 273 ? 2.1588 1.7852 1.1758 -0.3486 0.1172  -0.1165 291 ASP A N   
2034 C CA  . ASP A 273 ? 2.3070 1.8794 1.1984 -0.3557 0.0732  -0.1300 291 ASP A CA  
2035 C C   . ASP A 273 ? 2.3938 1.9164 1.1132 -0.3917 0.0891  -0.1036 291 ASP A C   
2036 O O   . ASP A 273 ? 2.5693 2.0606 1.1620 -0.4040 0.1064  -0.1343 291 ASP A O   
2037 C CB  . ASP A 273 ? 2.2736 1.8231 1.2066 -0.3400 -0.0151 -0.1081 291 ASP A CB  
2038 C CG  . ASP A 273 ? 2.2991 1.7911 1.1144 -0.3477 -0.0740 -0.1196 291 ASP A CG  
2039 O OD1 . ASP A 273 ? 2.2696 1.7076 0.9336 -0.3741 -0.0814 -0.0983 291 ASP A OD1 
2040 O OD2 . ASP A 273 ? 2.3509 1.8479 1.2231 -0.3293 -0.1155 -0.1488 291 ASP A OD2 
2041 N N   . THR A 274 ? 2.5212 2.0292 1.2266 -0.4100 0.0828  -0.0464 292 THR A N   
2042 C CA  . THR A 274 ? 2.4863 1.9406 1.0262 -0.4490 0.0961  -0.0118 292 THR A CA  
2043 C C   . THR A 274 ? 2.5292 2.0193 1.0433 -0.4732 0.1976  -0.0201 292 THR A C   
2044 O O   . THR A 274 ? 2.5574 2.0053 0.9159 -0.5085 0.2261  -0.0020 292 THR A O   
2045 C CB  . THR A 274 ? 2.4512 1.8673 0.9883 -0.4599 0.0415  0.0557  292 THR A CB  
2046 O OG1 . THR A 274 ? 2.4145 1.8827 1.1038 -0.4478 0.0636  0.0718  292 THR A OG1 
2047 C CG2 . THR A 274 ? 2.3660 1.7406 0.9063 -0.4391 -0.0592 0.0649  292 THR A CG2 
2048 N N   . PHE A 275 ? 1.7496 2.1070 1.5675 -0.0866 0.3850  0.0068  293 PHE A N   
2049 C CA  . PHE A 275 ? 1.8435 2.3139 1.6503 -0.0831 0.4010  0.0198  293 PHE A CA  
2050 C C   . PHE A 275 ? 1.7586 2.2889 1.5851 -0.1363 0.3852  0.0721  293 PHE A C   
2051 O O   . PHE A 275 ? 1.6519 2.1351 1.5143 -0.1682 0.3673  0.0945  293 PHE A O   
2052 C CB  . PHE A 275 ? 1.7810 2.3156 1.5382 -0.0501 0.4169  -0.0019 293 PHE A CB  
2053 C CG  . PHE A 275 ? 1.8131 2.2925 1.5456 0.0034  0.4320  -0.0533 293 PHE A CG  
2054 C CD1 . PHE A 275 ? 1.8947 2.3909 1.6249 0.0401  0.4522  -0.0751 293 PHE A CD1 
2055 C CD2 . PHE A 275 ? 1.8849 2.2950 1.5952 0.0163  0.4247  -0.0792 293 PHE A CD2 
2056 C CE1 . PHE A 275 ? 1.9299 2.3689 1.6346 0.0888  0.4644  -0.1204 293 PHE A CE1 
2057 C CE2 . PHE A 275 ? 1.9665 2.3202 1.6530 0.0619  0.4361  -0.1247 293 PHE A CE2 
2058 C CZ  . PHE A 275 ? 1.9817 2.3469 1.6643 0.0983  0.4557  -0.1448 293 PHE A CZ  
2059 N N   . SER A 286 ? 1.8886 1.8068 1.6313 -0.0035 0.3518  -0.1661 304 SER A N   
2060 C CA  . SER A 286 ? 1.8782 1.7803 1.6122 -0.0232 0.3324  -0.1639 304 SER A CA  
2061 C C   . SER A 286 ? 1.8240 1.6739 1.6001 -0.0517 0.3136  -0.1431 304 SER A C   
2062 O O   . SER A 286 ? 1.7962 1.6016 1.5738 -0.0596 0.2994  -0.1525 304 SER A O   
2063 C CB  . SER A 286 ? 1.9766 1.8348 1.6786 0.0005  0.3334  -0.2054 304 SER A CB  
2064 O OG  . SER A 286 ? 2.0904 1.8710 1.8114 0.0130  0.3375  -0.2255 304 SER A OG  
2065 N N   . ASP A 287 ? 2.5370 2.3943 2.3462 -0.0658 0.3123  -0.1156 305 ASP A N   
2066 C CA  . ASP A 287 ? 1.7757 1.5860 1.6221 -0.0888 0.2927  -0.0957 305 ASP A CA  
2067 C C   . ASP A 287 ? 2.0577 1.8821 1.8968 -0.1164 0.2708  -0.0737 305 ASP A C   
2068 O O   . ASP A 287 ? 2.1551 1.9324 2.0096 -0.1266 0.2535  -0.0726 305 ASP A O   
2069 C CB  . ASP A 287 ? 1.8081 1.6275 1.6858 -0.0978 0.2932  -0.0711 305 ASP A CB  
2070 C CG  . ASP A 287 ? 2.1964 1.9938 2.0868 -0.0699 0.3126  -0.0921 305 ASP A CG  
2071 O OD1 . ASP A 287 ? 2.7726 2.5236 2.6582 -0.0483 0.3204  -0.1216 305 ASP A OD1 
2072 O OD2 . ASP A 287 ? 1.6484 1.4747 1.5533 -0.0706 0.3194  -0.0781 305 ASP A OD2 
2073 N N   . ILE A 288 ? 2.1833 2.0769 1.9987 -0.1280 0.2712  -0.0546 306 ILE A N   
2074 C CA  . ILE A 288 ? 1.7946 1.7066 1.6000 -0.1537 0.2509  -0.0308 306 ILE A CA  
2075 C C   . ILE A 288 ? 2.1487 2.0384 1.9315 -0.1441 0.2454  -0.0583 306 ILE A C   
2076 O O   . ILE A 288 ? 2.0459 1.9118 1.8345 -0.1606 0.2250  -0.0482 306 ILE A O   
2077 C CB  . ILE A 288 ? 1.8160 1.8152 1.5996 -0.1673 0.2550  -0.0030 306 ILE A CB  
2078 C CG1 . ILE A 288 ? 2.5038 2.5234 2.3132 -0.1821 0.2574  0.0259  306 ILE A CG1 
2079 C CG2 . ILE A 288 ? 1.8760 1.8953 1.6463 -0.1930 0.2343  0.0234  306 ILE A CG2 
2080 C CD1 . ILE A 288 ? 2.0728 2.1879 1.8634 -0.1937 0.2663  0.0514  306 ILE A CD1 
2081 N N   . GLN A 289 ? 1.9201 1.8162 1.6754 -0.1167 0.2618  -0.0941 307 GLN A N   
2082 C CA  . GLN A 289 ? 1.7436 1.6155 1.4756 -0.1082 0.2549  -0.1233 307 GLN A CA  
2083 C C   . GLN A 289 ? 1.7830 1.5792 1.5448 -0.1147 0.2418  -0.1325 307 GLN A C   
2084 O O   . GLN A 289 ? 1.7061 1.4891 1.4642 -0.1267 0.2244  -0.1338 307 GLN A O   
2085 C CB  . GLN A 289 ? 1.7593 1.6356 1.4573 -0.0748 0.2731  -0.1630 307 GLN A CB  
2086 C CG  . GLN A 289 ? 2.4900 2.4497 2.1543 -0.0618 0.2871  -0.1585 307 GLN A CG  
2087 C CD  . GLN A 289 ? 2.5194 2.4768 2.1451 -0.0231 0.3023  -0.2016 307 GLN A CD  
2088 O OE1 . GLN A 289 ? 2.6183 2.5051 2.2468 -0.0075 0.3045  -0.2320 307 GLN A OE1 
2089 N NE2 . GLN A 289 ? 2.4630 2.4980 2.0508 -0.0068 0.3118  -0.2037 307 GLN A NE2 
2090 N N   . ASN A 290 ? 2.0390 1.7905 1.8303 -0.1059 0.2499  -0.1384 308 ASN A N   
2091 C CA  . ASN A 290 ? 1.8857 1.5725 1.7068 -0.1092 0.2401  -0.1469 308 ASN A CA  
2092 C C   . ASN A 290 ? 1.8865 1.5616 1.7426 -0.1297 0.2226  -0.1142 308 ASN A C   
2093 O O   . ASN A 290 ? 1.9131 1.5421 1.7970 -0.1305 0.2143  -0.1179 308 ASN A O   
2094 C CB  . ASN A 290 ? 1.8542 1.4997 1.6876 -0.0868 0.2578  -0.1697 308 ASN A CB  
2095 C CG  . ASN A 290 ? 2.0058 1.6498 1.8013 -0.0633 0.2724  -0.2046 308 ASN A CG  
2096 O OD1 . ASN A 290 ? 1.9511 1.6103 1.7344 -0.0424 0.2912  -0.2129 308 ASN A OD1 
2097 N ND2 . ASN A 290 ? 1.7964 1.4215 1.5712 -0.0655 0.2623  -0.2261 308 ASN A ND2 
2098 N N   . ASN A 291 ? 2.5717 2.2875 2.4258 -0.1457 0.2159  -0.0818 309 ASN A N   
2099 C CA  . ASN A 291 ? 1.8631 1.5633 1.7436 -0.1651 0.1952  -0.0500 309 ASN A CA  
2100 C C   . ASN A 291 ? 1.6136 1.2716 1.5308 -0.1560 0.1981  -0.0501 309 ASN A C   
2101 O O   . ASN A 291 ? 1.7771 1.3941 1.7190 -0.1567 0.1838  -0.0485 309 ASN A O   
2102 C CB  . ASN A 291 ? 1.6710 1.3520 1.5510 -0.1757 0.1731  -0.0487 309 ASN A CB  
2103 C CG  . ASN A 291 ? 2.8974 2.5653 2.7955 -0.1934 0.1489  -0.0146 309 ASN A CG  
2104 O OD1 . ASN A 291 ? 1.8750 1.5574 1.7772 -0.2045 0.1458  0.0128  309 ASN A OD1 
2105 N ND2 . ASN A 291 ? 1.7586 1.3986 1.6664 -0.1959 0.1301  -0.0160 309 ASN A ND2 
2106 N N   . LYS A 292 ? 1.7749 1.4489 1.6946 -0.1454 0.2168  -0.0523 310 LYS A N   
2107 C CA  . LYS A 292 ? 1.7768 1.4188 1.7286 -0.1341 0.2219  -0.0535 310 LYS A CA  
2108 C C   . LYS A 292 ? 1.7212 1.3738 1.6887 -0.1514 0.2086  -0.0200 310 LYS A C   
2109 O O   . LYS A 292 ? 1.7685 1.4682 1.7200 -0.1668 0.2091  0.0001  310 LYS A O   
2110 C CB  . LYS A 292 ? 1.8804 1.5315 1.8255 -0.1100 0.2496  -0.0770 310 LYS A CB  
2111 C CG  . LYS A 292 ? 1.9131 1.5392 1.8430 -0.0914 0.2614  -0.1115 310 LYS A CG  
2112 C CD  . LYS A 292 ? 1.7717 1.3414 1.7303 -0.0862 0.2549  -0.1213 310 LYS A CD  
2113 C CE  . LYS A 292 ? 1.8189 1.3601 1.7633 -0.0706 0.2669  -0.1539 310 LYS A CE  
2114 N NZ  . LYS A 292 ? 1.8105 1.3045 1.7846 -0.0681 0.2615  -0.1605 310 LYS A NZ  
2115 N N   . LEU A 293 ? 1.8375 1.4472 1.8355 -0.1491 0.1954  -0.0138 311 LEU A N   
2116 C CA  . LEU A 293 ? 2.2530 1.8609 2.2666 -0.1632 0.1803  0.0141  311 LEU A CA  
2117 C C   . LEU A 293 ? 2.1571 1.7920 2.1761 -0.1548 0.2007  0.0110  311 LEU A C   
2118 O O   . LEU A 293 ? 1.9229 1.5391 1.9572 -0.1307 0.2161  -0.0104 311 LEU A O   
2119 C CB  . LEU A 293 ? 1.6818 1.2351 1.7235 -0.1564 0.1600  0.0165  311 LEU A CB  
2120 C CG  . LEU A 293 ? 1.4540 0.9910 1.5117 -0.1674 0.1399  0.0412  311 LEU A CG  
2121 C CD1 . LEU A 293 ? 1.5911 1.1475 1.6302 -0.1996 0.1203  0.0746  311 LEU A CD1 
2122 C CD2 . LEU A 293 ? 1.4031 0.8868 1.4844 -0.1530 0.1196  0.0379  311 LEU A CD2 
2123 N N   . THR A 294 ? 1.7426 1.4256 1.7490 -0.1748 0.2008  0.0336  312 THR A N   
2124 C CA  . THR A 294 ? 1.6415 1.3656 1.6495 -0.1685 0.2209  0.0317  312 THR A CA  
2125 C C   . THR A 294 ? 1.6843 1.4207 1.7058 -0.1952 0.2035  0.0649  312 THR A C   
2126 O O   . THR A 294 ? 2.1116 1.8361 2.1309 -0.2223 0.1778  0.0927  312 THR A O   
2127 C CB  . THR A 294 ? 1.7191 1.5078 1.6948 -0.1647 0.2428  0.0241  312 THR A CB  
2128 O OG1 . THR A 294 ? 1.5005 1.3272 1.4570 -0.1939 0.2290  0.0522  312 THR A OG1 
2129 C CG2 . THR A 294 ? 2.1644 1.9334 2.1240 -0.1383 0.2575  -0.0111 312 THR A CG2 
2130 N N   . TRP A 295 ? 1.5186 1.2771 1.5533 -0.1874 0.2168  0.0617  313 TRP A N   
2131 C CA  . TRP A 295 ? 1.4096 1.1830 1.4580 -0.2145 0.2006  0.0916  313 TRP A CA  
2132 C C   . TRP A 295 ? 1.8425 1.6719 1.8705 -0.2508 0.1927  0.1253  313 TRP A C   
2133 O O   . TRP A 295 ? 1.8288 1.6383 1.8624 -0.2826 0.1641  0.1572  313 TRP A O   
2134 C CB  . TRP A 295 ? 1.6875 1.4893 1.7503 -0.1973 0.2208  0.0787  313 TRP A CB  
2135 C CG  . TRP A 295 ? 1.8114 1.6187 1.8942 -0.2215 0.2032  0.1030  313 TRP A CG  
2136 C CD1 . TRP A 295 ? 1.7465 1.4963 1.8550 -0.2186 0.1832  0.1026  313 TRP A CD1 
2137 C CD2 . TRP A 295 ? 2.0417 1.9181 2.1202 -0.2524 0.2030  0.1309  313 TRP A CD2 
2138 N NE1 . TRP A 295 ? 1.8720 1.6442 1.9916 -0.2470 0.1687  0.1272  313 TRP A NE1 
2139 C CE2 . TRP A 295 ? 2.0220 1.8735 2.1250 -0.2703 0.1808  0.1465  313 TRP A CE2 
2140 C CE3 . TRP A 295 ? 1.7500 1.7106 1.8060 -0.2666 0.2186  0.1446  313 TRP A CE3 
2141 C CZ2 . TRP A 295 ? 1.3881 1.2941 1.4954 -0.3061 0.1732  0.1765  313 TRP A CZ2 
2142 C CZ3 . TRP A 295 ? 1.6638 1.6855 1.7246 -0.3003 0.2129  0.1757  313 TRP A CZ3 
2143 C CH2 . TRP A 295 ? 1.9961 1.9894 2.0833 -0.3219 0.1902  0.1921  313 TRP A CH2 
2144 N N   . PRO A 296 ? 1.7168 1.6155 1.7196 -0.2474 0.2150  0.1215  314 PRO A N   
2145 C CA  . PRO A 296 ? 1.6513 1.6095 1.6346 -0.2822 0.2068  0.1566  314 PRO A CA  
2146 C C   . PRO A 296 ? 1.6518 1.5693 1.6260 -0.3033 0.1798  0.1766  314 PRO A C   
2147 O O   . PRO A 296 ? 1.9238 1.8564 1.8948 -0.3404 0.1593  0.2160  314 PRO A O   
2148 C CB  . PRO A 296 ? 1.6034 1.6339 1.5577 -0.2612 0.2369  0.1377  314 PRO A CB  
2149 C CG  . PRO A 296 ? 1.5037 1.5234 1.4665 -0.2220 0.2608  0.1001  314 PRO A CG  
2150 C CD  . PRO A 296 ? 1.5260 1.4534 1.5147 -0.2108 0.2474  0.0859  314 PRO A CD  
2151 N N   . LEU A 297 ? 1.8740 1.7409 1.8436 -0.2812 0.1783  0.1517  315 LEU A N   
2152 C CA  . LEU A 297 ? 1.6049 1.4348 1.5655 -0.2977 0.1524  0.1687  315 LEU A CA  
2153 C C   . LEU A 297 ? 1.9219 1.6939 1.9025 -0.3190 0.1197  0.1951  315 LEU A C   
2154 O O   . LEU A 297 ? 1.9967 1.7674 1.9670 -0.3503 0.0960  0.2308  315 LEU A O   
2155 C CB  . LEU A 297 ? 1.4717 1.2584 1.4289 -0.2688 0.1567  0.1344  315 LEU A CB  
2156 C CG  . LEU A 297 ? 1.8876 1.6234 1.8430 -0.2780 0.1283  0.1456  315 LEU A CG  
2157 C CD1 . LEU A 297 ? 1.6285 1.4048 1.5569 -0.3061 0.1165  0.1773  315 LEU A CD1 
2158 C CD2 . LEU A 297 ? 1.7695 1.4720 1.7254 -0.2501 0.1351  0.1098  315 LEU A CD2 
2159 N N   . ILE A 298 ? 1.8183 1.5401 1.8254 -0.3010 0.1169  0.1778  316 ILE A N   
2160 C CA  . ILE A 298 ? 1.6698 1.3290 1.6937 -0.3147 0.0837  0.1970  316 ILE A CA  
2161 C C   . ILE A 298 ? 1.7026 1.3898 1.7263 -0.3540 0.0697  0.2358  316 ILE A C   
2162 O O   . ILE A 298 ? 1.9905 1.6415 2.0099 -0.3814 0.0371  0.2673  316 ILE A O   
2163 C CB  . ILE A 298 ? 1.9115 1.5221 1.9630 -0.2834 0.0864  0.1681  316 ILE A CB  
2164 C CG1 . ILE A 298 ? 1.7993 1.3818 1.8520 -0.2497 0.0970  0.1350  316 ILE A CG1 
2165 C CG2 . ILE A 298 ? 1.6969 1.2445 1.7630 -0.2946 0.0503  0.1859  316 ILE A CG2 
2166 C CD1 . ILE A 298 ? 1.5679 1.1121 1.6468 -0.2170 0.1034  0.1072  316 ILE A CD1 
2167 N N   . LYS A 299 ? 1.6113 1.3638 1.6389 -0.3580 0.0929  0.2351  317 LYS A N   
2168 C CA  . LYS A 299 ? 1.7424 1.5270 1.7739 -0.3983 0.0795  0.2727  317 LYS A CA  
2169 C C   . LYS A 299 ? 1.7117 1.5447 1.7180 -0.4348 0.0718  0.3114  317 LYS A C   
2170 O O   . LYS A 299 ? 1.7404 1.5632 1.7464 -0.4752 0.0445  0.3517  317 LYS A O   
2171 C CB  . LYS A 299 ? 1.5939 1.4429 1.6379 -0.3906 0.1068  0.2607  317 LYS A CB  
2172 C CG  . LYS A 299 ? 1.6606 1.4664 1.7286 -0.3528 0.1160  0.2233  317 LYS A CG  
2173 C CD  . LYS A 299 ? 1.8552 1.5710 1.9420 -0.3562 0.0809  0.2277  317 LYS A CD  
2174 C CE  . LYS A 299 ? 1.8833 1.5568 1.9906 -0.3123 0.0914  0.1883  317 LYS A CE  
2175 N NZ  . LYS A 299 ? 1.9266 1.5114 2.0462 -0.3065 0.0572  0.1878  317 LYS A NZ  
2176 N N   . ALA A 300 ? 2.1651 2.0486 2.1486 -0.4215 0.0940  0.3006  318 ALA A N   
2177 C CA  . ALA A 300 ? 2.3602 2.2882 2.3177 -0.4519 0.0859  0.3361  318 ALA A CA  
2178 C C   . ALA A 300 ? 2.0512 1.9022 2.0025 -0.4675 0.0495  0.3575  318 ALA A C   
2179 O O   . ALA A 300 ? 1.9629 1.8217 1.9033 -0.5071 0.0273  0.4022  318 ALA A O   
2180 C CB  . ALA A 300 ? 1.6375 1.6270 1.5701 -0.4274 0.1150  0.3133  318 ALA A CB  
2181 N N   . PHE A 301 ? 2.0339 1.8115 1.9914 -0.4365 0.0424  0.3274  319 PHE A N   
2182 C CA  . PHE A 301 ? 1.8056 1.5089 1.7567 -0.4450 0.0069  0.3445  319 PHE A CA  
2183 C C   . PHE A 301 ? 2.0280 1.6777 1.9912 -0.4737 -0.0269 0.3754  319 PHE A C   
2184 O O   . PHE A 301 ? 2.3854 2.0063 2.3336 -0.5030 -0.0573 0.4130  319 PHE A O   
2185 C CB  . PHE A 301 ? 1.7342 1.3774 1.6941 -0.4039 0.0072  0.3043  319 PHE A CB  
2186 C CG  . PHE A 301 ? 1.6926 1.3118 1.6324 -0.4005 -0.0086 0.3089  319 PHE A CG  
2187 C CD1 . PHE A 301 ? 1.6426 1.3121 1.5634 -0.3897 0.0124  0.2940  319 PHE A CD1 
2188 C CD2 . PHE A 301 ? 2.1047 1.6508 2.0428 -0.4061 -0.0458 0.3266  319 PHE A CD2 
2189 C CE1 . PHE A 301 ? 1.7139 1.3655 1.6166 -0.3865 -0.0026 0.2975  319 PHE A CE1 
2190 C CE2 . PHE A 301 ? 2.1149 1.6432 2.0339 -0.4009 -0.0604 0.3307  319 PHE A CE2 
2191 C CZ  . PHE A 301 ? 2.3649 1.9481 2.2674 -0.3921 -0.0383 0.3164  319 PHE A CZ  
2192 N N   . GLU A 302 ? 1.9785 1.6117 1.9670 -0.4654 -0.0236 0.3601  320 GLU A N   
2193 C CA  . GLU A 302 ? 1.8951 1.4748 1.8948 -0.4921 -0.0574 0.3858  320 GLU A CA  
2194 C C   . GLU A 302 ? 1.9628 1.5943 1.9519 -0.5432 -0.0665 0.4340  320 GLU A C   
2195 O O   . GLU A 302 ? 2.0363 1.6312 2.0189 -0.5543 -0.0991 0.4525  320 GLU A O   
2196 C CB  . GLU A 302 ? 1.9051 1.4725 1.9338 -0.4717 -0.0478 0.3573  320 GLU A CB  
2197 C CG  . GLU A 302 ? 2.1948 1.7171 2.2357 -0.4873 -0.0799 0.3708  320 GLU A CG  
2198 C CD  . GLU A 302 ? 2.1974 1.7268 2.2657 -0.4766 -0.0674 0.3496  320 GLU A CD  
2199 O OE1 . GLU A 302 ? 1.9513 1.5263 2.0283 -0.4504 -0.0310 0.3211  320 GLU A OE1 
2200 O OE2 . GLU A 302 ? 2.3211 1.8230 2.3991 -0.4792 -0.0898 0.3497  320 GLU A OE2 
2201 N N   . LEU A 303 ? 2.3658 2.0979 2.3528 -0.5547 -0.0342 0.4394  321 LEU A N   
2202 C CA  . LEU A 303 ? 2.8402 2.6378 2.8217 -0.5996 -0.0394 0.4822  321 LEU A CA  
2203 C C   . LEU A 303 ? 2.7434 2.5728 2.6955 -0.6196 -0.0468 0.5145  321 LEU A C   
2204 O O   . LEU A 303 ? 2.0067 1.8527 1.9531 -0.6469 -0.0676 0.5462  321 LEU A O   
2205 C CB  . LEU A 303 ? 2.5115 2.4135 2.5025 -0.6021 -0.0017 0.4761  321 LEU A CB  
2206 C CG  . LEU A 303 ? 1.6811 1.5781 1.7017 -0.6033 -0.0014 0.4648  321 LEU A CG  
2207 C CD1 . LEU A 303 ? 1.9232 1.7220 1.9611 -0.5640 -0.0114 0.4245  321 LEU A CD1 
2208 C CD2 . LEU A 303 ? 1.8253 1.8317 1.8511 -0.5886 0.0404  0.4475  321 LEU A CD2 
2209 N N   . CYS A 304 ? 2.0281 1.8683 1.9615 -0.6011 -0.0308 0.5022  322 CYS A N   
2210 C CA  . CYS A 304 ? 1.9541 1.8428 1.8579 -0.6215 -0.0321 0.5343  322 CYS A CA  
2211 C C   . CYS A 304 ? 2.2166 2.0212 2.1072 -0.6281 -0.0723 0.5538  322 CYS A C   
2212 O O   . CYS A 304 ? 1.9692 1.6785 1.8696 -0.6063 -0.0945 0.5333  322 CYS A O   
2213 C CB  . CYS A 304 ? 1.9382 1.8796 1.8263 -0.5822 0.0009  0.4976  322 CYS A CB  
2214 S SG  . CYS A 304 ? 1.8642 1.7129 1.7498 -0.5364 -0.0074 0.4542  322 CYS A SG  
2215 N N   . SER A 305 ? 2.1599 2.0078 2.0275 -0.6517 -0.0809 0.5897  323 SER A N   
2216 C CA  . SER A 305 ? 2.4283 2.2101 2.2790 -0.6559 -0.1170 0.6093  323 SER A CA  
2217 C C   . SER A 305 ? 2.1374 1.8822 1.9694 -0.6334 -0.1152 0.5949  323 SER A C   
2218 O O   . SER A 305 ? 2.0632 1.8480 1.8947 -0.6085 -0.0840 0.5629  323 SER A O   
2219 C CB  . SER A 305 ? 2.0135 1.8601 1.8462 -0.6899 -0.1255 0.6542  323 SER A CB  
2220 O OG  . SER A 305 ? 2.2556 2.2011 2.0687 -0.6939 -0.0945 0.6632  323 SER A OG  
2221 N N   . GLN A 306 ? 2.3888 2.0625 2.2071 -0.6291 -0.1489 0.6059  324 GLN A N   
2222 C CA  . GLN A 306 ? 2.3719 2.0053 2.1727 -0.6074 -0.1523 0.5932  324 GLN A CA  
2223 C C   . GLN A 306 ? 2.1777 1.9031 1.9570 -0.6015 -0.1241 0.5899  324 GLN A C   
2224 O O   . GLN A 306 ? 2.3023 2.0347 2.0838 -0.5618 -0.1050 0.5437  324 GLN A O   
2225 C CB  . GLN A 306 ? 2.2891 1.8427 2.0765 -0.6018 -0.1941 0.6073  324 GLN A CB  
2226 C CG  . GLN A 306 ? 2.2064 1.7115 1.9773 -0.5763 -0.2029 0.5934  324 GLN A CG  
2227 C CD  . GLN A 306 ? 2.0991 1.5680 1.8962 -0.5332 -0.1908 0.5379  324 GLN A CD  
2228 O OE1 . GLN A 306 ? 1.9961 1.4037 1.8137 -0.5233 -0.2052 0.5251  324 GLN A OE1 
2229 N NE2 . GLN A 306 ? 2.3225 1.8361 2.1203 -0.5023 -0.1634 0.4996  324 GLN A NE2 
2230 N N   . PRO A 307 ? 2.1279 1.9266 1.8860 -0.6356 -0.1209 0.6335  325 PRO A N   
2231 C CA  . PRO A 307 ? 2.1019 1.9960 1.8396 -0.6214 -0.0919 0.6215  325 PRO A CA  
2232 C C   . PRO A 307 ? 2.1012 2.0541 1.8538 -0.5911 -0.0520 0.5721  325 PRO A C   
2233 O O   . PRO A 307 ? 2.0880 2.0705 1.8296 -0.5584 -0.0327 0.5352  325 PRO A O   
2234 C CB  . PRO A 307 ? 2.1014 2.0704 1.8193 -0.6675 -0.0951 0.6818  325 PRO A CB  
2235 C CG  . PRO A 307 ? 2.2319 2.1232 1.9578 -0.6889 -0.1351 0.7113  325 PRO A CG  
2236 C CD  . PRO A 307 ? 2.2134 2.0186 1.9697 -0.6710 -0.1441 0.6781  325 PRO A CD  
2237 N N   . GLU A 308 ? 2.1923 2.1598 1.9686 -0.6007 -0.0405 0.5697  326 GLU A N   
2238 C CA  . GLU A 308 ? 1.9886 2.0046 1.7778 -0.5690 -0.0038 0.5223  326 GLU A CA  
2239 C C   . GLU A 308 ? 1.8797 1.8193 1.6860 -0.5267 -0.0015 0.4688  326 GLU A C   
2240 O O   . GLU A 308 ? 1.8143 1.7842 1.6199 -0.4931 0.0261  0.4251  326 GLU A O   
2241 C CB  . GLU A 308 ? 2.0143 2.0698 1.8242 -0.5903 0.0068  0.5359  326 GLU A CB  
2242 C CG  . GLU A 308 ? 2.0089 2.1918 1.8031 -0.6063 0.0315  0.5573  326 GLU A CG  
2243 C CD  . GLU A 308 ? 2.0629 2.2884 1.8767 -0.6394 0.0340  0.5855  326 GLU A CD  
2244 O OE1 . GLU A 308 ? 2.0326 2.1891 1.8637 -0.6688 0.0053  0.6114  326 GLU A OE1 
2245 O OE2 . GLU A 308 ? 2.1446 2.4736 1.9558 -0.6348 0.0635  0.5808  326 GLU A OE2 
2246 N N   . LYS A 309 ? 1.9892 1.8304 1.8093 -0.5269 -0.0310 0.4717  327 LYS A N   
2247 C CA  . LYS A 309 ? 1.9761 1.7518 1.8105 -0.4869 -0.0306 0.4249  327 LYS A CA  
2248 C C   . LYS A 309 ? 2.0574 1.8475 1.8708 -0.4648 -0.0253 0.4046  327 LYS A C   
2249 O O   . LYS A 309 ? 2.0388 1.8321 1.8586 -0.4317 -0.0049 0.3590  327 LYS A O   
2250 C CB  . LYS A 309 ? 1.8293 1.5033 1.6770 -0.4898 -0.0669 0.4355  327 LYS A CB  
2251 C CG  . LYS A 309 ? 1.9677 1.6154 1.8382 -0.5075 -0.0751 0.4480  327 LYS A CG  
2252 C CD  . LYS A 309 ? 2.1826 1.7263 2.0592 -0.5092 -0.1160 0.4598  327 LYS A CD  
2253 C CE  . LYS A 309 ? 2.3201 1.8370 2.2160 -0.5317 -0.1289 0.4755  327 LYS A CE  
2254 N NZ  . LYS A 309 ? 2.5296 1.9618 2.4304 -0.5127 -0.1661 0.4688  327 LYS A NZ  
2255 N N   . GLU A 310 ? 2.0954 1.8946 1.8829 -0.4838 -0.0443 0.4389  328 GLU A N   
2256 C CA  . GLU A 310 ? 1.9188 1.7393 1.6844 -0.4648 -0.0405 0.4215  328 GLU A CA  
2257 C C   . GLU A 310 ? 2.0486 1.9580 1.8020 -0.4516 -0.0051 0.3961  328 GLU A C   
2258 O O   . GLU A 310 ? 1.9819 1.8957 1.7304 -0.4226 0.0071  0.3557  328 GLU A O   
2259 C CB  . GLU A 310 ? 2.2988 2.1199 2.0367 -0.4892 -0.0671 0.4677  328 GLU A CB  
2260 C CG  . GLU A 310 ? 2.4445 2.1698 2.1871 -0.4965 -0.1060 0.4902  328 GLU A CG  
2261 C CD  . GLU A 310 ? 2.6353 2.3593 2.3469 -0.5194 -0.1325 0.5374  328 GLU A CD  
2262 O OE1 . GLU A 310 ? 2.3651 2.1688 2.0533 -0.5324 -0.1194 0.5555  328 GLU A OE1 
2263 O OE2 . GLU A 310 ? 2.4061 2.0495 2.1146 -0.5223 -0.1669 0.5563  328 GLU A OE2 
2264 N N   . ASP A 311 ? 1.9383 1.9205 1.6854 -0.4723 0.0102  0.4194  329 ASP A N   
2265 C CA  . ASP A 311 ? 1.9246 1.9938 1.6568 -0.4553 0.0432  0.3943  329 ASP A CA  
2266 C C   . ASP A 311 ? 1.8167 1.8638 1.5681 -0.4204 0.0657  0.3394  329 ASP A C   
2267 O O   . ASP A 311 ? 1.8481 1.9204 1.5856 -0.3926 0.0835  0.3009  329 ASP A O   
2268 C CB  . ASP A 311 ? 1.8721 2.0266 1.5975 -0.4832 0.0548  0.4312  329 ASP A CB  
2269 C CG  . ASP A 311 ? 1.9067 2.0929 1.6103 -0.5197 0.0347  0.4886  329 ASP A CG  
2270 O OD1 . ASP A 311 ? 1.9696 2.1128 1.6600 -0.5196 0.0128  0.4971  329 ASP A OD1 
2271 O OD2 . ASP A 311 ? 1.7732 2.0300 1.4726 -0.5487 0.0405  0.5267  329 ASP A OD2 
2272 N N   . ILE A 312 ? 2.4623 2.4601 2.2444 -0.4213 0.0638  0.3354  330 ILE A N   
2273 C CA  . ILE A 312 ? 2.1023 2.0743 1.9037 -0.3884 0.0839  0.2867  330 ILE A CA  
2274 C C   . ILE A 312 ? 2.0618 1.9780 1.8646 -0.3625 0.0777  0.2516  330 ILE A C   
2275 O O   . ILE A 312 ? 1.8309 1.7555 1.6299 -0.3349 0.0978  0.2098  330 ILE A O   
2276 C CB  . ILE A 312 ? 2.0836 2.0100 1.9178 -0.3949 0.0788  0.2923  330 ILE A CB  
2277 C CG1 . ILE A 312 ? 2.0119 2.0066 1.8468 -0.4180 0.0906  0.3195  330 ILE A CG1 
2278 C CG2 . ILE A 312 ? 1.9029 1.7884 1.7581 -0.3594 0.0951  0.2438  330 ILE A CG2 
2279 C CD1 . ILE A 312 ? 2.1007 2.0550 1.9667 -0.4286 0.0826  0.3281  330 ILE A CD1 
2280 N N   . ILE A 313 ? 2.2874 2.1459 2.0944 -0.3712 0.0486  0.2686  331 ILE A N   
2281 C CA  . ILE A 313 ? 2.3005 2.1137 2.1102 -0.3485 0.0409  0.2384  331 ILE A CA  
2282 C C   . ILE A 313 ? 2.2878 2.1526 2.0686 -0.3386 0.0522  0.2200  331 ILE A C   
2283 O O   . ILE A 313 ? 2.0456 1.8977 1.8284 -0.3148 0.0622  0.1793  331 ILE A O   
2284 C CB  . ILE A 313 ? 2.3309 2.0828 2.1452 -0.3584 0.0058  0.2638  331 ILE A CB  
2285 C CG1 . ILE A 313 ? 2.0470 1.7393 1.8894 -0.3617 -0.0069 0.2734  331 ILE A CG1 
2286 C CG2 . ILE A 313 ? 1.6890 1.4101 1.5041 -0.3358 -0.0022 0.2351  331 ILE A CG2 
2287 C CD1 . ILE A 313 ? 1.8112 1.4432 1.6521 -0.3732 -0.0447 0.3044  331 ILE A CD1 
2288 N N   . ARG A 314 ? 1.9054 1.8296 1.6579 -0.3573 0.0497  0.2502  332 ARG A N   
2289 C CA  . ARG A 314 ? 2.0329 2.0104 1.7545 -0.3470 0.0581  0.2338  332 ARG A CA  
2290 C C   . ARG A 314 ? 1.7735 1.7952 1.4863 -0.3246 0.0889  0.1950  332 ARG A C   
2291 O O   . ARG A 314 ? 1.6205 1.6708 1.3095 -0.3085 0.0956  0.1680  332 ARG A O   
2292 C CB  . ARG A 314 ? 1.9273 1.9641 1.6204 -0.3719 0.0487  0.2792  332 ARG A CB  
2293 C CG  . ARG A 314 ? 2.1379 2.1301 1.8299 -0.3908 0.0158  0.3163  332 ARG A CG  
2294 C CD  . ARG A 314 ? 2.2704 2.3192 1.9366 -0.4203 0.0071  0.3688  332 ARG A CD  
2295 N NE  . ARG A 314 ? 2.5703 2.5672 2.2334 -0.4381 -0.0263 0.4066  332 ARG A NE  
2296 C CZ  . ARG A 314 ? 2.8898 2.9160 2.5314 -0.4667 -0.0410 0.4585  332 ARG A CZ  
2297 N NH1 . ARG A 314 ? 2.4970 2.6125 2.1201 -0.4826 -0.0247 0.4813  332 ARG A NH1 
2298 N NH2 . ARG A 314 ? 2.6833 2.6491 2.3206 -0.4787 -0.0734 0.4893  332 ARG A NH2 
2299 N N   . ASN A 315 ? 2.4298 2.4561 2.1592 -0.3217 0.1061  0.1907  333 ASN A N   
2300 C CA  . ASN A 315 ? 1.6381 1.7053 1.3563 -0.2978 0.1347  0.1554  333 ASN A CA  
2301 C C   . ASN A 315 ? 2.0773 2.0836 1.8230 -0.2762 0.1454  0.1189  333 ASN A C   
2302 O O   . ASN A 315 ? 2.3328 2.3433 2.0685 -0.2502 0.1636  0.0787  333 ASN A O   
2303 C CB  . ASN A 315 ? 1.7113 1.8556 1.4201 -0.3100 0.1494  0.1822  333 ASN A CB  
2304 C CG  . ASN A 315 ? 2.0398 2.2579 1.7182 -0.3294 0.1425  0.2179  333 ASN A CG  
2305 O OD1 . ASN A 315 ? 1.6551 1.9337 1.3014 -0.3131 0.1543  0.2009  333 ASN A OD1 
2306 N ND2 . ASN A 315 ? 2.0058 2.2178 1.6924 -0.3636 0.1221  0.2678  333 ASN A ND2 
2307 N N   . LYS A 318 ? 1.9874 1.8666 1.7294 -0.1784 0.1889  -0.0553 336 LYS A N   
2308 C CA  . LYS A 318 ? 2.2757 2.1923 1.9794 -0.1744 0.1849  -0.0690 336 LYS A CA  
2309 C C   . LYS A 318 ? 2.6433 2.5922 2.3138 -0.1478 0.2059  -0.1005 336 LYS A C   
2310 O O   . LYS A 318 ? 2.5630 2.5466 2.2308 -0.1398 0.2229  -0.0930 336 LYS A O   
2311 C CB  . LYS A 318 ? 1.5883 1.5619 1.2777 -0.1962 0.1725  -0.0287 336 LYS A CB  
2312 N N   . ASP A 319 ? 2.0218 1.9593 1.6654 -0.1331 0.2031  -0.1368 337 ASP A N   
2313 C CA  . ASP A 319 ? 2.1142 2.0732 1.7198 -0.1032 0.2192  -0.1721 337 ASP A CA  
2314 C C   . ASP A 319 ? 2.2278 2.2709 1.7917 -0.0998 0.2182  -0.1640 337 ASP A C   
2315 O O   . ASP A 319 ? 2.3520 2.4043 1.8819 -0.0880 0.2109  -0.1908 337 ASP A O   
2316 C CB  . ASP A 319 ? 2.1456 2.0394 1.7428 -0.0890 0.2146  -0.2176 337 ASP A CB  
2317 C CG  . ASP A 319 ? 2.2308 2.0486 1.8689 -0.0922 0.2167  -0.2234 337 ASP A CG  
2318 O OD1 . ASP A 319 ? 2.1542 1.9706 1.8168 -0.0914 0.2292  -0.2056 337 ASP A OD1 
2319 O OD2 . ASP A 319 ? 2.3311 2.0945 1.9772 -0.0961 0.2055  -0.2453 337 ASP A OD2 
2320 N N   . ASN A 320 ? 2.0810 2.1887 1.6480 -0.1111 0.2251  -0.1252 338 ASN A N   
2321 C CA  . ASN A 320 ? 2.2567 2.4568 1.7871 -0.1097 0.2264  -0.1096 338 ASN A CA  
2322 C C   . ASN A 320 ? 2.2334 2.5002 1.7660 -0.1094 0.2445  -0.0828 338 ASN A C   
2323 O O   . ASN A 320 ? 2.3107 2.5644 1.8799 -0.1321 0.2443  -0.0500 338 ASN A O   
2324 C CB  . ASN A 320 ? 2.0048 2.2229 1.5394 -0.1398 0.2052  -0.0742 338 ASN A CB  
2325 C CG  . ASN A 320 ? 2.0436 2.3516 1.5344 -0.1342 0.2043  -0.0667 338 ASN A CG  
2326 O OD1 . ASN A 320 ? 1.9939 2.3418 1.4473 -0.1035 0.2161  -0.0980 338 ASN A OD1 
2327 N ND2 . ASN A 320 ? 2.2805 2.6207 1.7735 -0.1616 0.1893  -0.0251 338 ASN A ND2 
2328 N N   . VAL A 321 ? 2.0769 2.4176 1.5695 -0.0828 0.2589  -0.0975 339 VAL A N   
2329 C CA  . VAL A 321 ? 1.9852 2.3978 1.4782 -0.0782 0.2782  -0.0769 339 VAL A CA  
2330 C C   . VAL A 321 ? 2.0634 2.5353 1.5750 -0.1184 0.2714  -0.0161 339 VAL A C   
2331 O O   . VAL A 321 ? 2.0653 2.5539 1.6042 -0.1345 0.2790  0.0124  339 VAL A O   
2332 C CB  . VAL A 321 ? 2.0170 2.5054 1.4586 -0.0376 0.2933  -0.1060 339 VAL A CB  
2333 C CG1 . VAL A 321 ? 1.9738 2.5472 1.4167 -0.0321 0.3137  -0.0838 339 VAL A CG1 
2334 C CG2 . VAL A 321 ? 2.0548 2.4714 1.4751 0.0016  0.2967  -0.1665 339 VAL A CG2 
2335 N N   . THR A 322 ? 2.5899 3.0938 2.0859 -0.1360 0.2561  0.0052  340 THR A N   
2336 C CA  . THR A 322 ? 2.0000 2.5618 1.5078 -0.1748 0.2484  0.0656  340 THR A CA  
2337 C C   . THR A 322 ? 1.9827 2.4721 1.5393 -0.2088 0.2361  0.0957  340 THR A C   
2338 O O   . THR A 322 ? 1.8894 2.4142 1.4651 -0.2348 0.2378  0.1374  340 THR A O   
2339 C CB  . THR A 322 ? 2.2502 2.8458 1.7317 -0.1854 0.2321  0.0808  340 THR A CB  
2340 O OG1 . THR A 322 ? 2.4148 2.9196 1.9046 -0.1852 0.2142  0.0568  340 THR A OG1 
2341 C CG2 . THR A 322 ? 2.6701 3.3559 2.1009 -0.1520 0.2441  0.0570  340 THR A CG2 
2342 N N   . CYS A 323 ? 2.1313 2.5210 1.7080 -0.2087 0.2226  0.0749  341 CYS A N   
2343 C CA  . CYS A 323 ? 1.8989 2.2174 1.5196 -0.2345 0.2098  0.0986  341 CYS A CA  
2344 C C   . CYS A 323 ? 1.9236 2.2328 1.5691 -0.2282 0.2264  0.0942  341 CYS A C   
2345 O O   . CYS A 323 ? 1.9745 2.2762 1.6484 -0.2548 0.2200  0.1299  341 CYS A O   
2346 C CB  . CYS A 323 ? 2.1852 2.4093 1.8204 -0.2291 0.1945  0.0721  341 CYS A CB  
2347 S SG  . CYS A 323 ? 1.9810 2.2132 1.5889 -0.2349 0.1736  0.0734  341 CYS A SG  
2348 N N   . ILE A 324 ? 2.0910 2.3978 1.7245 -0.1923 0.2461  0.0501  342 ILE A N   
2349 C CA  . ILE A 324 ? 2.1695 2.4689 1.8241 -0.1814 0.2630  0.0427  342 ILE A CA  
2350 C C   . ILE A 324 ? 2.1504 2.5440 1.8034 -0.1973 0.2726  0.0802  342 ILE A C   
2351 O O   . ILE A 324 ? 2.2167 2.6031 1.9010 -0.2147 0.2732  0.1026  342 ILE A O   
2352 C CB  . ILE A 324 ? 2.1617 2.4432 1.7959 -0.1370 0.2815  -0.0116 342 ILE A CB  
2353 C CG1 . ILE A 324 ? 2.1473 2.3353 1.7861 -0.1274 0.2703  -0.0454 342 ILE A CG1 
2354 C CG2 . ILE A 324 ? 2.1325 2.4092 1.7866 -0.1232 0.2995  -0.0187 342 ILE A CG2 
2355 C CD1 . ILE A 324 ? 2.1804 2.3531 1.7866 -0.0876 0.2824  -0.0973 342 ILE A CD1 
2356 N N   . LYS A 325 ? 2.0007 2.4881 1.6174 -0.1918 0.2796  0.0878  343 LYS A N   
2357 C CA  . LYS A 325 ? 1.9992 2.5892 1.6141 -0.2090 0.2890  0.1266  343 LYS A CA  
2358 C C   . LYS A 325 ? 1.9339 2.5241 1.5736 -0.2611 0.2683  0.1851  343 LYS A C   
2359 O O   . LYS A 325 ? 1.9007 2.5356 1.5592 -0.2855 0.2712  0.2195  343 LYS A O   
2360 C CB  . LYS A 325 ? 2.1871 2.8836 1.7552 -0.1880 0.3010  0.1208  343 LYS A CB  
2361 C CG  . LYS A 325 ? 2.1840 2.8778 1.7199 -0.1332 0.3185  0.0611  343 LYS A CG  
2362 C CD  . LYS A 325 ? 2.1759 2.8625 1.7266 -0.1107 0.3377  0.0413  343 LYS A CD  
2363 C CE  . LYS A 325 ? 2.2862 2.9460 1.8037 -0.0559 0.3511  -0.0195 343 LYS A CE  
2364 N NZ  . LYS A 325 ? 2.4698 3.2235 1.9349 -0.0256 0.3594  -0.0342 343 LYS A NZ  
2365 N N   . PHE A 326 ? 2.0359 2.5750 1.6752 -0.2790 0.2458  0.1970  344 PHE A N   
2366 C CA  . PHE A 326 ? 2.2120 2.7322 1.8730 -0.3260 0.2226  0.2505  344 PHE A CA  
2367 C C   . PHE A 326 ? 1.8263 2.2718 1.5299 -0.3395 0.2157  0.2558  344 PHE A C   
2368 O O   . PHE A 326 ? 1.7769 2.2413 1.4993 -0.3741 0.2076  0.2982  344 PHE A O   
2369 C CB  . PHE A 326 ? 1.8687 2.3378 1.5197 -0.3342 0.1996  0.2547  344 PHE A CB  
2370 C CG  . PHE A 326 ? 2.2905 2.7742 1.9436 -0.3787 0.1771  0.3144  344 PHE A CG  
2371 C CD1 . PHE A 326 ? 2.0557 2.4654 1.7404 -0.4083 0.1554  0.3428  344 PHE A CD1 
2372 C CD2 . PHE A 326 ? 2.3774 2.9471 1.9985 -0.3895 0.1763  0.3424  344 PHE A CD2 
2373 C CE1 . PHE A 326 ? 1.9923 2.4066 1.6755 -0.4492 0.1322  0.3984  344 PHE A CE1 
2374 C CE2 . PHE A 326 ? 2.1361 2.7163 1.7574 -0.4316 0.1548  0.4003  344 PHE A CE2 
2375 C CZ  . PHE A 326 ? 2.0858 2.5845 1.7375 -0.4621 0.1321  0.4285  344 PHE A CZ  
2376 N N   . ILE A 327 ? 2.2833 2.6450 2.0018 -0.3126 0.2183  0.2130  345 ILE A N   
2377 C CA  . ILE A 327 ? 2.6504 2.9421 2.4081 -0.3202 0.2121  0.2143  345 ILE A CA  
2378 C C   . ILE A 327 ? 2.5316 2.8788 2.3000 -0.3166 0.2323  0.2163  345 ILE A C   
2379 O O   . ILE A 327 ? 1.9147 2.2439 1.7121 -0.3400 0.2237  0.2405  345 ILE A O   
2380 C CB  . ILE A 327 ? 1.9195 2.1173 1.6897 -0.2912 0.2113  0.1693  345 ILE A CB  
2381 C CG1 . ILE A 327 ? 2.2253 2.3724 1.9896 -0.2998 0.1879  0.1733  345 ILE A CG1 
2382 C CG2 . ILE A 327 ? 1.6535 1.7891 1.4624 -0.2923 0.2084  0.1669  345 ILE A CG2 
2383 C CD1 . ILE A 327 ? 2.8048 2.8586 2.5896 -0.2815 0.1809  0.1409  345 ILE A CD1 
2384 N N   . ASN A 328 ? 2.1152 2.5302 1.8591 -0.2856 0.2581  0.1895  346 ASN A N   
2385 C CA  . ASN A 328 ? 2.0575 2.5382 1.8084 -0.2797 0.2781  0.1921  346 ASN A CA  
2386 C C   . ASN A 328 ? 1.9860 2.5495 1.7416 -0.3231 0.2712  0.2482  346 ASN A C   
2387 O O   . ASN A 328 ? 2.0374 2.6195 1.8182 -0.3405 0.2729  0.2669  346 ASN A O   
2388 C CB  . ASN A 328 ? 1.8971 2.4378 1.6139 -0.2341 0.3050  0.1526  346 ASN A CB  
2389 C CG  . ASN A 328 ? 1.9711 2.4267 1.6836 -0.1934 0.3117  0.0981  346 ASN A CG  
2390 O OD1 . ASN A 328 ? 2.0259 2.4852 1.7049 -0.1657 0.3172  0.0672  346 ASN A OD1 
2391 N ND2 . ASN A 328 ? 2.0220 2.4007 1.7677 -0.1903 0.3101  0.0865  346 ASN A ND2 
2392 N N   . ASP A 329 ? 1.9480 2.5640 1.6792 -0.3423 0.2628  0.2766  347 ASP A N   
2393 C CA  . ASP A 329 ? 2.0617 2.7538 1.7970 -0.3889 0.2539  0.3356  347 ASP A CA  
2394 C C   . ASP A 329 ? 2.1446 2.7570 1.9143 -0.4323 0.2253  0.3709  347 ASP A C   
2395 O O   . ASP A 329 ? 2.1571 2.8077 1.9454 -0.4682 0.2199  0.4096  347 ASP A O   
2396 C CB  . ASP A 329 ? 2.1303 2.8876 1.8308 -0.3983 0.2495  0.3584  347 ASP A CB  
2397 C CG  . ASP A 329 ? 1.9883 2.8388 1.6512 -0.3558 0.2761  0.3269  347 ASP A CG  
2398 O OD1 . ASP A 329 ? 2.0101 2.8701 1.6727 -0.3189 0.2974  0.2877  347 ASP A OD1 
2399 O OD2 . ASP A 329 ? 1.8492 2.7628 1.4806 -0.3571 0.2749  0.3409  347 ASP A OD2 
2400 N N   . ILE A 330 ? 1.9846 2.4870 1.7620 -0.4293 0.2054  0.3580  348 ILE A N   
2401 C CA  . ILE A 330 ? 2.1466 2.5641 1.9536 -0.4628 0.1765  0.3855  348 ILE A CA  
2402 C C   . ILE A 330 ? 2.2619 2.6555 2.1012 -0.4586 0.1828  0.3726  348 ILE A C   
2403 O O   . ILE A 330 ? 2.2828 2.6676 2.1438 -0.4955 0.1660  0.4078  348 ILE A O   
2404 C CB  . ILE A 330 ? 2.3838 2.6939 2.1913 -0.4512 0.1562  0.3676  348 ILE A CB  
2405 C CG1 . ILE A 330 ? 1.7676 2.1025 1.5447 -0.4632 0.1447  0.3897  348 ILE A CG1 
2406 C CG2 . ILE A 330 ? 2.0706 2.2863 1.9081 -0.4744 0.1274  0.3859  348 ILE A CG2 
2407 C CD1 . ILE A 330 ? 1.8437 2.0889 1.6176 -0.4473 0.1274  0.3685  348 ILE A CD1 
2408 N N   . TYR A 331 ? 2.4237 2.8045 2.2658 -0.4137 0.2059  0.3220  349 TYR A N   
2409 C CA  . TYR A 331 ? 1.9548 2.3209 1.8254 -0.4049 0.2147  0.3075  349 TYR A CA  
2410 C C   . TYR A 331 ? 2.1362 2.6075 2.0106 -0.4282 0.2255  0.3375  349 TYR A C   
2411 O O   . TYR A 331 ? 2.1087 2.5687 2.0111 -0.4526 0.2152  0.3564  349 TYR A O   
2412 C CB  . TYR A 331 ? 1.9599 2.3053 1.8264 -0.3510 0.2401  0.2502  349 TYR A CB  
2413 C CG  . TYR A 331 ? 2.0397 2.2777 1.9123 -0.3285 0.2303  0.2184  349 TYR A CG  
2414 C CD1 . TYR A 331 ? 1.8202 1.9755 1.7116 -0.3506 0.2005  0.2362  349 TYR A CD1 
2415 C CD2 . TYR A 331 ? 2.2957 2.5161 2.1542 -0.2846 0.2501  0.1708  349 TYR A CD2 
2416 C CE1 . TYR A 331 ? 1.5722 1.6406 1.4700 -0.3289 0.1924  0.2080  349 TYR A CE1 
2417 C CE2 . TYR A 331 ? 2.2113 2.3415 2.0774 -0.2674 0.2414  0.1442  349 TYR A CE2 
2418 C CZ  . TYR A 331 ? 1.7655 1.8248 1.6522 -0.2892 0.2134  0.1632  349 TYR A CZ  
2419 O OH  . TYR A 331 ? 1.9843 1.9640 1.8794 -0.2712 0.2053  0.1376  349 TYR A OH  
2420 N N   . GLU A 332 ? 2.1072 2.6854 1.9532 -0.4204 0.2455  0.3416  350 GLU A N   
2421 C CA  . GLU A 332 ? 1.9325 2.6270 1.7807 -0.4376 0.2594  0.3674  350 GLU A CA  
2422 C C   . GLU A 332 ? 2.0278 2.7556 1.8859 -0.5007 0.2356  0.4317  350 GLU A C   
2423 O O   . GLU A 332 ? 2.0343 2.8417 1.9059 -0.5263 0.2403  0.4593  350 GLU A O   
2424 C CB  . GLU A 332 ? 2.1040 2.9063 1.9152 -0.4043 0.2878  0.3499  350 GLU A CB  
2425 C CG  . GLU A 332 ? 1.9865 2.7632 1.7850 -0.3421 0.3119  0.2873  350 GLU A CG  
2426 C CD  . GLU A 332 ? 2.3868 3.2443 2.1410 -0.3057 0.3327  0.2653  350 GLU A CD  
2427 O OE1 . GLU A 332 ? 2.2371 3.1825 1.9718 -0.3274 0.3306  0.2994  350 GLU A OE1 
2428 O OE2 . GLU A 332 ? 2.2729 3.1047 2.0103 -0.2546 0.3499  0.2141  350 GLU A OE2 
2429 N N   . HIS A 333 ? 2.3552 3.0248 2.2064 -0.5269 0.2094  0.4572  351 HIS A N   
2430 C CA  . HIS A 333 ? 2.4406 3.1294 2.2986 -0.5884 0.1837  0.5208  351 HIS A CA  
2431 C C   . HIS A 333 ? 2.3755 2.9953 2.2704 -0.6178 0.1609  0.5351  351 HIS A C   
2432 O O   . HIS A 333 ? 2.3657 3.0301 2.2776 -0.6390 0.1500  0.5561  351 HIS A O   
2433 C CB  . HIS A 333 ? 2.5305 3.1639 2.3689 -0.6030 0.1602  0.5409  351 HIS A CB  
2434 C CG  . HIS A 333 ? 2.5789 3.3013 2.3802 -0.5892 0.1764  0.5437  351 HIS A CG  
2435 N ND1 . HIS A 333 ? 2.5122 3.3656 2.3003 -0.5772 0.2013  0.5444  351 HIS A ND1 
2436 C CD2 . HIS A 333 ? 2.6630 3.3606 2.4380 -0.5793 0.1684  0.5410  351 HIS A CD2 
2437 C CE1 . HIS A 333 ? 2.5232 3.4310 2.2764 -0.5630 0.2092  0.5445  351 HIS A CE1 
2438 N NE2 . HIS A 333 ? 2.6533 3.4697 2.3976 -0.5660 0.1902  0.5437  351 HIS A NE2 
2439 N N   . TYR A 334 ? 1.9999 2.4956 1.9096 -0.6004 0.1463  0.5069  352 TYR A N   
2440 C CA  . TYR A 334 ? 2.3967 2.8199 2.3389 -0.6213 0.1240  0.5140  352 TYR A CA  
2441 C C   . TYR A 334 ? 1.9696 2.4217 1.9330 -0.5936 0.1476  0.4796  352 TYR A C   
2442 O O   . TYR A 334 ? 1.7981 2.1915 1.7891 -0.6036 0.1315  0.4778  352 TYR A O   
2443 C CB  . TYR A 334 ? 2.0254 2.3084 1.9733 -0.6090 0.0972  0.4970  352 TYR A CB  
2444 C CG  . TYR A 334 ? 1.9998 2.2425 1.9294 -0.6405 0.0673  0.5358  352 TYR A CG  
2445 C CD1 . TYR A 334 ? 1.9299 2.1821 1.8313 -0.6204 0.0749  0.5266  352 TYR A CD1 
2446 C CD2 . TYR A 334 ? 2.0276 2.2165 1.9673 -0.6719 0.0283  0.5662  352 TYR A CD2 
2447 C CE1 . TYR A 334 ? 2.5389 2.7570 2.4222 -0.6470 0.0479  0.5624  352 TYR A CE1 
2448 C CE2 . TYR A 334 ? 2.2950 2.4431 2.2165 -0.6871 -0.0004 0.5923  352 TYR A CE2 
2449 C CZ  . TYR A 334 ? 2.2781 2.4433 2.1718 -0.6781 0.0103  0.5943  352 TYR A CZ  
2450 O OH  . TYR A 334 ? 2.3916 2.5187 2.2665 -0.6922 -0.0180 0.6209  352 TYR A OH  
2451 N N   . ASN A 335 ? 2.1291 2.6681 2.0782 -0.5568 0.1839  0.4516  353 ASN A N   
2452 C CA  . ASN A 335 ? 2.2475 2.8306 2.2119 -0.5295 0.2086  0.4225  353 ASN A CA  
2453 C C   . ASN A 335 ? 1.9968 2.4685 1.9850 -0.5014 0.2020  0.3844  353 ASN A C   
2454 O O   . ASN A 335 ? 1.5410 1.9967 1.5569 -0.5139 0.1935  0.3877  353 ASN A O   
2455 C CB  . ASN A 335 ? 1.8349 2.5088 1.8163 -0.5741 0.2055  0.4637  353 ASN A CB  
2456 C CG  . ASN A 335 ? 1.7620 2.5451 1.7214 -0.5844 0.2094  0.4895  353 ASN A CG  
2457 O OD1 . ASN A 335 ? 2.0775 2.9589 2.0221 -0.5526 0.2381  0.4710  353 ASN A OD1 
2458 N ND2 . ASN A 335 ? 2.7826 3.5437 2.7387 -0.6228 0.1776  0.5286  353 ASN A ND2 
2459 N N   . ILE A 336 ? 1.7387 2.1364 1.7155 -0.4630 0.2058  0.3480  354 ILE A N   
2460 C CA  . ILE A 336 ? 1.6853 1.9869 1.6824 -0.4311 0.2035  0.3101  354 ILE A CA  
2461 C C   . ILE A 336 ? 1.6676 2.0136 1.6719 -0.3928 0.2345  0.2753  354 ILE A C   
2462 O O   . ILE A 336 ? 1.7366 2.0227 1.7632 -0.3721 0.2335  0.2510  354 ILE A O   
2463 C CB  . ILE A 336 ? 1.7034 1.9248 1.6868 -0.4013 0.2009  0.2815  354 ILE A CB  
2464 C CG1 . ILE A 336 ? 1.8242 2.0297 1.7900 -0.4325 0.1774  0.3142  354 ILE A CG1 
2465 C CG2 . ILE A 336 ? 1.7622 1.8775 1.7706 -0.3827 0.1874  0.2575  354 ILE A CG2 
2466 C CD1 . ILE A 336 ? 1.8097 1.9636 1.7913 -0.4786 0.1397  0.3556  354 ILE A CD1 
2467 N N   . ARG A 337 ? 1.7925 2.2451 1.7764 -0.3801 0.2618  0.2726  355 ARG A N   
2468 C CA  . ARG A 337 ? 1.5041 2.0026 1.4891 -0.3391 0.2919  0.2390  355 ARG A CA  
2469 C C   . ARG A 337 ? 1.5620 2.0830 1.5789 -0.3572 0.2872  0.2517  355 ARG A C   
2470 O O   . ARG A 337 ? 1.4692 1.9922 1.4950 -0.3209 0.3058  0.2200  355 ARG A O   
2471 C CB  . ARG A 337 ? 1.5843 2.1984 1.5366 -0.3217 0.3189  0.2362  355 ARG A CB  
2472 C CG  . ARG A 337 ? 1.7576 2.3507 1.6754 -0.2955 0.3257  0.2147  355 ARG A CG  
2473 C CD  . ARG A 337 ? 1.7529 2.4616 1.6349 -0.2737 0.3507  0.2093  355 ARG A CD  
2474 N NE  . ARG A 337 ? 2.1213 2.8077 1.9691 -0.2508 0.3536  0.1887  355 ARG A NE  
2475 C CZ  . ARG A 337 ? 2.1223 2.8937 1.9324 -0.2274 0.3713  0.1793  355 ARG A CZ  
2476 N NH1 . ARG A 337 ? 2.0311 2.9224 1.8318 -0.2215 0.3894  0.1892  355 ARG A NH1 
2477 N NH2 . ARG A 337 ? 2.0475 2.7863 1.8278 -0.2083 0.3698  0.1587  355 ARG A NH2 
2478 N N   . ASP A 338 ? 1.3849 1.9214 1.4182 -0.4129 0.2616  0.2973  356 ASP A N   
2479 C CA  . ASP A 338 ? 1.7340 2.2798 1.7993 -0.4355 0.2509  0.3100  356 ASP A CA  
2480 C C   . ASP A 338 ? 1.5096 1.9287 1.5993 -0.4395 0.2223  0.3019  356 ASP A C   
2481 O O   . ASP A 338 ? 1.5494 1.9526 1.6640 -0.4325 0.2200  0.2894  356 ASP A O   
2482 C CB  . ASP A 338 ? 1.8607 2.4890 1.9312 -0.4972 0.2356  0.3649  356 ASP A CB  
2483 C CG  . ASP A 338 ? 1.5498 2.3038 1.5923 -0.4968 0.2594  0.3795  356 ASP A CG  
2484 O OD1 . ASP A 338 ? 1.5708 2.3126 1.5858 -0.4857 0.2626  0.3768  356 ASP A OD1 
2485 O OD2 . ASP A 338 ? 1.5676 2.4321 1.6149 -0.5037 0.2730  0.3911  356 ASP A OD2 
2486 N N   . HIS A 339 ? 1.0642 1.5815 1.9760 -0.0644 0.3814  0.1420  357 HIS A N   
2487 C CA  . HIS A 339 ? 1.3479 1.8503 2.2836 -0.1008 0.3504  0.1304  357 HIS A CA  
2488 C C   . HIS A 339 ? 1.2471 1.6949 2.1309 -0.1056 0.3207  0.0946  357 HIS A C   
2489 O O   . HIS A 339 ? 1.2344 1.6726 2.1546 -0.1271 0.2996  0.0826  357 HIS A O   
2490 C CB  . HIS A 339 ? 0.9595 1.4553 1.8639 -0.1192 0.3468  0.1430  357 HIS A CB  
2491 C CG  . HIS A 339 ? 1.2348 1.7837 2.1943 -0.1172 0.3746  0.1815  357 HIS A CG  
2492 N ND1 . HIS A 339 ? 1.6104 2.1769 2.5361 -0.0890 0.4048  0.2020  357 HIS A ND1 
2493 C CD2 . HIS A 339 ? 0.9689 1.5452 1.9961 -0.1367 0.3729  0.2008  357 HIS A CD2 
2494 C CE1 . HIS A 339 ? 1.3175 1.9319 2.3073 -0.0934 0.4263  0.2381  357 HIS A CE1 
2495 N NE2 . HIS A 339 ? 1.5307 2.1386 2.5606 -0.1205 0.3969  0.2315  357 HIS A NE2 
2496 N N   . TYR A 340 ? 1.2627 1.6695 2.0576 -0.0853 0.3201  0.0773  358 TYR A N   
2497 C CA  . TYR A 340 ? 1.2189 1.5748 1.9706 -0.0869 0.2949  0.0461  358 TYR A CA  
2498 C C   . TYR A 340 ? 1.1367 1.5104 1.9485 -0.0771 0.2922  0.0420  358 TYR A C   
2499 O O   . TYR A 340 ? 1.1915 1.5376 2.0033 -0.0905 0.2666  0.0234  358 TYR A O   
2500 C CB  . TYR A 340 ? 1.1749 1.4805 1.8237 -0.0652 0.2962  0.0281  358 TYR A CB  
2501 C CG  . TYR A 340 ? 1.3327 1.5938 1.9542 -0.0599 0.2768  0.0006  358 TYR A CG  
2502 C CD1 . TYR A 340 ? 1.2698 1.4938 1.8772 -0.0861 0.2471  -0.0160 358 TYR A CD1 
2503 C CD2 . TYR A 340 ? 1.1958 1.4538 1.8128 -0.0274 0.2910  -0.0050 358 TYR A CD2 
2504 C CE1 . TYR A 340 ? 1.1979 1.3810 1.7804 -0.0807 0.2307  -0.0378 358 TYR A CE1 
2505 C CE2 . TYR A 340 ? 1.3429 1.5614 1.9389 -0.0220 0.2728  -0.0268 358 TYR A CE2 
2506 C CZ  . TYR A 340 ? 1.3061 1.4869 1.8825 -0.0491 0.2420  -0.0432 358 TYR A CZ  
2507 O OH  . TYR A 340 ? 1.3808 1.5212 1.9345 -0.0430 0.2252  -0.0619 358 TYR A OH  
2508 N N   . VAL A 341 ? 1.1685 1.5871 2.0312 -0.0527 0.3178  0.0611  359 VAL A N   
2509 C CA  . VAL A 341 ? 1.1269 1.5691 2.0600 -0.0449 0.3108  0.0621  359 VAL A CA  
2510 C C   . VAL A 341 ? 1.1000 1.5619 2.1071 -0.0779 0.2876  0.0647  359 VAL A C   
2511 O O   . VAL A 341 ? 1.1441 1.5892 2.1654 -0.0871 0.2598  0.0496  359 VAL A O   
2512 C CB  . VAL A 341 ? 1.1639 1.6567 2.1522 -0.0127 0.3466  0.0890  359 VAL A CB  
2513 C CG1 . VAL A 341 ? 0.9113 1.4346 1.9873 -0.0070 0.3342  0.0949  359 VAL A CG1 
2514 C CG2 . VAL A 341 ? 1.0524 1.5134 1.9533 0.0227  0.3735  0.0831  359 VAL A CG2 
2515 N N   . GLU A 342 ? 0.9830 1.4766 2.0340 -0.0954 0.2990  0.0840  360 GLU A N   
2516 C CA  . GLU A 342 ? 1.0025 1.5060 2.1176 -0.1271 0.2800  0.0844  360 GLU A CA  
2517 C C   . GLU A 342 ? 1.0458 1.4902 2.1022 -0.1495 0.2521  0.0565  360 GLU A C   
2518 O O   . GLU A 342 ? 1.1267 1.5553 2.2050 -0.1656 0.2282  0.0433  360 GLU A O   
2519 C CB  . GLU A 342 ? 1.1603 1.6978 2.3175 -0.1394 0.2990  0.1101  360 GLU A CB  
2520 C CG  . GLU A 342 ? 1.1371 1.7193 2.3253 -0.1144 0.3240  0.1392  360 GLU A CG  
2521 C CD  . GLU A 342 ? 1.2064 1.7937 2.3732 -0.1192 0.3320  0.1593  360 GLU A CD  
2522 O OE1 . GLU A 342 ? 1.2495 1.8076 2.3816 -0.1406 0.3161  0.1514  360 GLU A OE1 
2523 O OE2 . GLU A 342 ? 1.3523 1.9716 2.5382 -0.0999 0.3553  0.1844  360 GLU A OE2 
2524 N N   . TYR A 343 ? 1.3831 1.7921 2.3633 -0.1507 0.2545  0.0484  361 TYR A N   
2525 C CA  . TYR A 343 ? 1.1564 1.5098 2.0849 -0.1696 0.2329  0.0262  361 TYR A CA  
2526 C C   . TYR A 343 ? 0.9508 1.2683 1.8444 -0.1596 0.2123  0.0034  361 TYR A C   
2527 O O   . TYR A 343 ? 0.9248 1.2076 1.8077 -0.1761 0.1931  -0.0115 361 TYR A O   
2528 C CB  . TYR A 343 ? 1.0497 1.3762 1.9114 -0.1714 0.2367  0.0255  361 TYR A CB  
2529 C CG  . TYR A 343 ? 1.0500 1.3192 1.8619 -0.1874 0.2170  0.0057  361 TYR A CG  
2530 C CD1 . TYR A 343 ? 0.8602 1.1180 1.6943 -0.2139 0.2148  0.0099  361 TYR A CD1 
2531 C CD2 . TYR A 343 ? 0.9769 1.2020 1.7241 -0.1747 0.2042  -0.0149 361 TYR A CD2 
2532 C CE1 . TYR A 343 ? 1.3707 1.5768 2.1653 -0.2267 0.2023  -0.0041 361 TYR A CE1 
2533 C CE2 . TYR A 343 ? 0.8542 1.0276 1.5619 -0.1889 0.1889  -0.0293 361 TYR A CE2 
2534 C CZ  . TYR A 343 ? 1.0134 1.1786 1.7458 -0.2146 0.1889  -0.0230 361 TYR A CZ  
2535 O OH  . TYR A 343 ? 1.1163 1.2308 1.8150 -0.2269 0.1790  -0.0334 361 TYR A OH  
2536 N N   . GLU A 344 ? 0.9023 1.2238 1.7739 -0.1308 0.2183  0.0018  362 GLU A N   
2537 C CA  . GLU A 344 ? 0.9435 1.2345 1.7887 -0.1182 0.1998  -0.0156 362 GLU A CA  
2538 C C   . GLU A 344 ? 0.8398 1.1492 1.7480 -0.1282 0.1802  -0.0143 362 GLU A C   
2539 O O   . GLU A 344 ? 0.8531 1.1231 1.7344 -0.1382 0.1554  -0.0307 362 GLU A O   
2540 C CB  . GLU A 344 ? 0.9991 1.2984 1.8255 -0.0824 0.2166  -0.0124 362 GLU A CB  
2541 C CG  . GLU A 344 ? 1.3220 1.5804 2.1066 -0.0655 0.2010  -0.0301 362 GLU A CG  
2542 C CD  . GLU A 344 ? 1.0987 1.3781 1.9440 -0.0640 0.1807  -0.0261 362 GLU A CD  
2543 O OE1 . GLU A 344 ? 0.9098 1.2437 1.8375 -0.0668 0.1845  -0.0071 362 GLU A OE1 
2544 O OE2 . GLU A 344 ? 1.1831 1.4237 1.9950 -0.0607 0.1588  -0.0403 362 GLU A OE2 
2545 N N   . LYS A 345 ? 0.9133 1.2802 1.9047 -0.1268 0.1898  0.0064  363 LYS A N   
2546 C CA  . LYS A 345 ? 0.8308 1.2155 1.8877 -0.1399 0.1655  0.0083  363 LYS A CA  
2547 C C   . LYS A 345 ? 0.7966 1.1423 1.8347 -0.1727 0.1464  -0.0072 363 LYS A C   
2548 O O   . LYS A 345 ? 0.8781 1.1900 1.8965 -0.1816 0.1170  -0.0228 363 LYS A O   
2549 C CB  . LYS A 345 ? 0.9500 1.4036 2.1082 -0.1370 0.1813  0.0362  363 LYS A CB  
2550 C CG  . LYS A 345 ? 1.1474 1.6410 2.3351 -0.1014 0.2043  0.0552  363 LYS A CG  
2551 C CD  . LYS A 345 ? 1.1784 1.7416 2.4758 -0.0997 0.2228  0.0872  363 LYS A CD  
2552 C CE  . LYS A 345 ? 1.3710 1.9732 2.7009 -0.0608 0.2533  0.1097  363 LYS A CE  
2553 N NZ  . LYS A 345 ? 1.3811 2.0537 2.8267 -0.0580 0.2754  0.1458  363 LYS A NZ  
2554 N N   . LYS A 346 ? 0.8918 1.2386 1.9325 -0.1896 0.1644  -0.0017 364 LYS A N   
2555 C CA  . LYS A 346 ? 0.7653 1.0757 1.7971 -0.2187 0.1541  -0.0134 364 LYS A CA  
2556 C C   . LYS A 346 ? 0.9290 1.1716 1.8737 -0.2219 0.1414  -0.0361 364 LYS A C   
2557 O O   . LYS A 346 ? 0.9201 1.1224 1.8442 -0.2366 0.1224  -0.0513 364 LYS A O   
2558 C CB  . LYS A 346 ? 0.9048 1.2330 1.9635 -0.2324 0.1799  0.0019  364 LYS A CB  
2559 C CG  . LYS A 346 ? 1.1224 1.5040 2.2411 -0.2250 0.1895  0.0265  364 LYS A CG  
2560 C CD  . LYS A 346 ? 1.5752 1.9546 2.6609 -0.2241 0.2049  0.0426  364 LYS A CD  
2561 C CE  . LYS A 346 ? 1.5017 1.9239 2.6261 -0.2126 0.2130  0.0668  364 LYS A CE  
2562 N NZ  . LYS A 346 ? 1.5712 1.9930 2.6672 -0.2117 0.2260  0.0831  364 LYS A NZ  
2563 N N   . GLN A 347 ? 0.9406 1.1660 1.8306 -0.2087 0.1519  -0.0382 365 GLN A N   
2564 C CA  . GLN A 347 ? 0.8186 0.9814 1.6336 -0.2117 0.1427  -0.0558 365 GLN A CA  
2565 C C   . GLN A 347 ? 0.9080 1.0451 1.6950 -0.2007 0.1174  -0.0694 365 GLN A C   
2566 O O   . GLN A 347 ? 0.8303 0.9151 1.5711 -0.2102 0.1048  -0.0831 365 GLN A O   
2567 C CB  . GLN A 347 ? 0.8339 0.9859 1.6044 -0.2010 0.1553  -0.0541 365 GLN A CB  
2568 C CG  . GLN A 347 ? 0.9358 1.0279 1.6466 -0.2110 0.1515  -0.0654 365 GLN A CG  
2569 C CD  . GLN A 347 ? 0.8610 0.9413 1.5896 -0.2358 0.1630  -0.0590 365 GLN A CD  
2570 O OE1 . GLN A 347 ? 0.9317 1.0458 1.7147 -0.2462 0.1725  -0.0479 365 GLN A OE1 
2571 N NE2 . GLN A 347 ? 0.8668 0.8986 1.5553 -0.2446 0.1645  -0.0636 365 GLN A NE2 
2572 N N   . LYS A 348 ? 0.8618 1.0341 1.6765 -0.1791 0.1115  -0.0632 366 LYS A N   
2573 C CA  . LYS A 348 ? 0.8140 0.9686 1.6141 -0.1683 0.0845  -0.0712 366 LYS A CA  
2574 C C   . LYS A 348 ? 0.7968 0.9443 1.6206 -0.1887 0.0588  -0.0759 366 LYS A C   
2575 O O   . LYS A 348 ? 0.8251 0.9274 1.6022 -0.1917 0.0340  -0.0884 366 LYS A O   
2576 C CB  . LYS A 348 ? 0.7623 0.9627 1.6038 -0.1399 0.0875  -0.0584 366 LYS A CB  
2577 C CG  . LYS A 348 ? 1.1865 1.3680 2.0107 -0.1232 0.0619  -0.0630 366 LYS A CG  
2578 C CD  . LYS A 348 ? 1.0067 1.2304 1.8723 -0.0907 0.0742  -0.0480 366 LYS A CD  
2579 C CE  . LYS A 348 ? 1.0964 1.3000 1.9469 -0.0717 0.0504  -0.0497 366 LYS A CE  
2580 N NZ  . LYS A 348 ? 1.1690 1.4126 2.0665 -0.0371 0.0678  -0.0328 366 LYS A NZ  
2581 N N   . MET A 349 ? 0.8416 1.0293 1.7340 -0.2034 0.0633  -0.0658 367 MET A N   
2582 C CA  . MET A 349 ? 0.8718 1.0445 1.7824 -0.2264 0.0375  -0.0734 367 MET A CA  
2583 C C   . MET A 349 ? 0.8449 0.9450 1.6787 -0.2443 0.0379  -0.0925 367 MET A C   
2584 O O   . MET A 349 ? 0.9187 0.9729 1.7094 -0.2525 0.0103  -0.1069 367 MET A O   
2585 C CB  . MET A 349 ? 0.9882 1.2121 1.9875 -0.2404 0.0480  -0.0587 367 MET A CB  
2586 C CG  . MET A 349 ? 1.0202 1.3112 2.1093 -0.2281 0.0379  -0.0388 367 MET A CG  
2587 S SD  . MET A 349 ? 1.6771 1.9578 2.7861 -0.2370 -0.0189 -0.0457 367 MET A SD  
2588 C CE  . MET A 349 ? 1.4971 1.7423 2.6116 -0.2765 -0.0333 -0.0607 367 MET A CE  
2589 N N   . LYS A 350 ? 0.8699 0.9577 1.6856 -0.2498 0.0698  -0.0907 368 LYS A N   
2590 C CA  . LYS A 350 ? 1.0038 1.0251 1.7571 -0.2648 0.0780  -0.1041 368 LYS A CA  
2591 C C   . LYS A 350 ? 0.9364 0.9030 1.6075 -0.2535 0.0660  -0.1159 368 LYS A C   
2592 O O   . LYS A 350 ? 1.0465 0.9528 1.6602 -0.2626 0.0576  -0.1293 368 LYS A O   
2593 C CB  . LYS A 350 ? 1.0713 1.0993 1.8369 -0.2713 0.1137  -0.0935 368 LYS A CB  
2594 C CG  . LYS A 350 ? 1.2786 1.2490 2.0097 -0.2889 0.1300  -0.1010 368 LYS A CG  
2595 C CD  . LYS A 350 ? 1.3100 1.3054 2.0910 -0.2998 0.1612  -0.0845 368 LYS A CD  
2596 C CE  . LYS A 350 ? 1.4883 1.5103 2.2714 -0.2895 0.1746  -0.0696 368 LYS A CE  
2597 N NZ  . LYS A 350 ? 1.6097 1.6558 2.4160 -0.2907 0.1943  -0.0485 368 LYS A NZ  
2598 N N   . ILE A 351 ? 0.8523 0.8347 1.5131 -0.2326 0.0669  -0.1107 369 ILE A N   
2599 C CA  . ILE A 351 ? 0.9532 0.8854 1.5427 -0.2205 0.0565  -0.1193 369 ILE A CA  
2600 C C   . ILE A 351 ? 0.9406 0.8538 1.5095 -0.2179 0.0205  -0.1268 369 ILE A C   
2601 O O   . ILE A 351 ? 0.9479 0.7999 1.4469 -0.2201 0.0109  -0.1365 369 ILE A O   
2602 C CB  . ILE A 351 ? 0.8717 0.8244 1.4600 -0.1980 0.0640  -0.1132 369 ILE A CB  
2603 C CG1 . ILE A 351 ? 0.9346 0.8883 1.5219 -0.2040 0.0925  -0.1077 369 ILE A CG1 
2604 C CG2 . ILE A 351 ? 0.9846 0.8907 1.5114 -0.1830 0.0488  -0.1202 369 ILE A CG2 
2605 C CD1 . ILE A 351 ? 0.9759 0.9509 1.5623 -0.1846 0.0997  -0.1035 369 ILE A CD1 
2606 N N   . LEU A 352 ? 0.9662 0.9315 1.5969 -0.2131 -0.0004 -0.1198 370 LEU A N   
2607 C CA  . LEU A 352 ? 0.9285 0.8812 1.5492 -0.2127 -0.0420 -0.1237 370 LEU A CA  
2608 C C   . LEU A 352 ? 0.9724 0.8770 1.5572 -0.2381 -0.0569 -0.1381 370 LEU A C   
2609 O O   . LEU A 352 ? 1.0623 0.9162 1.5837 -0.2400 -0.0860 -0.1476 370 LEU A O   
2610 C CB  . LEU A 352 ? 0.9013 0.9268 1.6138 -0.2036 -0.0597 -0.1084 370 LEU A CB  
2611 C CG  . LEU A 352 ? 0.8784 0.9415 1.6159 -0.1731 -0.0461 -0.0950 370 LEU A CG  
2612 C CD1 . LEU A 352 ? 0.8491 0.9880 1.6890 -0.1636 -0.0525 -0.0755 370 LEU A CD1 
2613 C CD2 . LEU A 352 ? 1.0032 1.0248 1.6797 -0.1555 -0.0657 -0.0986 370 LEU A CD2 
2614 N N   . GLU A 353 ? 0.9458 0.8609 1.5657 -0.2571 -0.0369 -0.1396 371 GLU A N   
2615 C CA  . GLU A 353 ? 0.9961 0.8547 1.5744 -0.2802 -0.0441 -0.1559 371 GLU A CA  
2616 C C   . GLU A 353 ? 1.0485 0.8255 1.5226 -0.2788 -0.0275 -0.1674 371 GLU A C   
2617 O O   . GLU A 353 ? 1.1250 0.8380 1.5264 -0.2865 -0.0480 -0.1820 371 GLU A O   
2618 C CB  . GLU A 353 ? 1.1218 1.0050 1.7605 -0.2978 -0.0170 -0.1528 371 GLU A CB  
2619 C CG  . GLU A 353 ? 1.3781 1.3316 2.1191 -0.3040 -0.0348 -0.1414 371 GLU A CG  
2620 C CD  . GLU A 353 ? 1.4567 1.4339 2.2587 -0.3198 -0.0045 -0.1351 371 GLU A CD  
2621 O OE1 . GLU A 353 ? 1.7674 1.7059 2.5326 -0.3260 0.0289  -0.1397 371 GLU A OE1 
2622 O OE2 . GLU A 353 ? 1.1593 1.1950 2.0518 -0.3255 -0.0129 -0.1226 371 GLU A OE2 
2623 N N   . ALA A 354 ? 1.1220 0.8981 1.5866 -0.2692 0.0093  -0.1597 372 ALA A N   
2624 C CA  . ALA A 354 ? 1.1072 0.8106 1.4853 -0.2664 0.0285  -0.1652 372 ALA A CA  
2625 C C   . ALA A 354 ? 1.1190 0.7868 1.4304 -0.2517 -0.0012 -0.1688 372 ALA A C   
2626 O O   . ALA A 354 ? 1.2102 0.8054 1.4363 -0.2538 -0.0028 -0.1778 372 ALA A O   
2627 C CB  . ALA A 354 ? 1.0429 0.7607 1.4395 -0.2603 0.0666  -0.1528 372 ALA A CB  
2628 N N   . ILE A 355 ? 1.0920 0.8078 1.4398 -0.2349 -0.0224 -0.1599 373 ILE A N   
2629 C CA  . ILE A 355 ? 1.1431 0.8303 1.4373 -0.2185 -0.0501 -0.1591 373 ILE A CA  
2630 C C   . ILE A 355 ? 1.2159 0.8688 1.4678 -0.2282 -0.0922 -0.1687 373 ILE A C   
2631 O O   . ILE A 355 ? 1.2904 0.8793 1.4545 -0.2237 -0.1051 -0.1729 373 ILE A O   
2632 C CB  . ILE A 355 ? 1.0999 0.8488 1.4534 -0.1971 -0.0612 -0.1464 373 ILE A CB  
2633 C CG1 . ILE A 355 ? 1.0542 0.8141 1.4187 -0.1868 -0.0236 -0.1406 373 ILE A CG1 
2634 C CG2 . ILE A 355 ? 1.1545 0.8812 1.4680 -0.1805 -0.0960 -0.1426 373 ILE A CG2 
2635 C CD1 . ILE A 355 ? 1.0116 0.8322 1.4369 -0.1668 -0.0243 -0.1307 373 ILE A CD1 
2636 N N   . ASN A 356 ? 1.2019 0.8944 1.5138 -0.2425 -0.1159 -0.1713 374 ASN A N   
2637 C CA  . ASN A 356 ? 1.2794 0.9353 1.5506 -0.2563 -0.1621 -0.1823 374 ASN A CA  
2638 C C   . ASN A 356 ? 1.3556 0.9201 1.5249 -0.2708 -0.1465 -0.2010 374 ASN A C   
2639 O O   . ASN A 356 ? 1.4488 0.9548 1.5395 -0.2773 -0.1823 -0.2122 374 ASN A O   
2640 C CB  . ASN A 356 ? 1.2474 0.9637 1.6146 -0.2722 -0.1882 -0.1806 374 ASN A CB  
2641 C CG  . ASN A 356 ? 1.2049 0.9996 1.6609 -0.2563 -0.2156 -0.1604 374 ASN A CG  
2642 O OD1 . ASN A 356 ? 1.1788 0.9929 1.6384 -0.2317 -0.2024 -0.1481 374 ASN A OD1 
2643 N ND2 . ASN A 356 ? 1.3570 1.1951 1.8886 -0.2698 -0.2528 -0.1558 374 ASN A ND2 
2644 N N   . GLN A 357 ? 1.3452 0.8939 1.5124 -0.2752 -0.0935 -0.2032 375 GLN A N   
2645 C CA  . GLN A 357 ? 1.3980 0.8582 1.4725 -0.2846 -0.0670 -0.2175 375 GLN A CA  
2646 C C   . GLN A 357 ? 1.4460 0.8455 1.4302 -0.2676 -0.0458 -0.2124 375 GLN A C   
2647 O O   . GLN A 357 ? 1.5192 0.8386 1.4173 -0.2712 -0.0202 -0.2213 375 GLN A O   
2648 C CB  . GLN A 357 ? 1.6397 1.1123 1.7644 -0.2961 -0.0174 -0.2171 375 GLN A CB  
2649 C CG  . GLN A 357 ? 1.3205 0.8303 1.5175 -0.3162 -0.0325 -0.2242 375 GLN A CG  
2650 C CD  . GLN A 357 ? 1.3175 0.8342 1.5608 -0.3263 0.0180  -0.2212 375 GLN A CD  
2651 O OE1 . GLN A 357 ? 1.5839 1.0935 1.8229 -0.3179 0.0622  -0.2102 375 GLN A OE1 
2652 N NE2 . GLN A 357 ? 1.4963 1.0272 1.7898 -0.3451 0.0103  -0.2289 375 GLN A NE2 
2653 N N   . LEU A 358 ? 1.4118 0.8441 1.4141 -0.2483 -0.0526 -0.1974 376 LEU A N   
2654 C CA  . LEU A 358 ? 1.4595 0.8343 1.3823 -0.2325 -0.0342 -0.1901 376 LEU A CA  
2655 C C   . LEU A 358 ? 1.5781 0.8766 1.3883 -0.2308 -0.0653 -0.1985 376 LEU A C   
2656 O O   . LEU A 358 ? 1.6497 0.8706 1.3676 -0.2258 -0.0374 -0.1986 376 LEU A O   
2657 C CB  . LEU A 358 ? 1.4244 0.8479 1.3925 -0.2126 -0.0400 -0.1740 376 LEU A CB  
2658 C CG  . LEU A 358 ? 1.4268 0.8713 1.4381 -0.2073 0.0051  -0.1631 376 LEU A CG  
2659 C CD1 . LEU A 358 ? 1.3040 0.7853 1.3470 -0.1873 -0.0078 -0.1519 376 LEU A CD1 
2660 C CD2 . LEU A 358 ? 1.6090 0.9802 1.5521 -0.2077 0.0462  -0.1596 376 LEU A CD2 
2661 N N   . HIS A 359 ? 1.6056 0.9242 1.4220 -0.2347 -0.1234 -0.2032 377 HIS A N   
2662 C CA  . HIS A 359 ? 1.7252 0.9750 1.4337 -0.2341 -0.1649 -0.2097 377 HIS A CA  
2663 C C   . HIS A 359 ? 1.7630 0.9804 1.4104 -0.2102 -0.1614 -0.1930 377 HIS A C   
2664 O O   . HIS A 359 ? 1.8608 0.9923 1.3926 -0.2051 -0.1491 -0.1947 377 HIS A O   
2665 C CB  . HIS A 359 ? 1.8203 0.9805 1.4300 -0.2497 -0.1479 -0.2307 377 HIS A CB  
2666 C CG  . HIS A 359 ? 1.8038 0.9853 1.4647 -0.2743 -0.1614 -0.2486 377 HIS A CG  
2667 N ND1 . HIS A 359 ? 1.8278 0.9610 1.4610 -0.2876 -0.1188 -0.2642 377 HIS A ND1 
2668 C CD2 . HIS A 359 ? 1.7674 1.0131 1.5122 -0.2876 -0.2111 -0.2510 377 HIS A CD2 
2669 C CE1 . HIS A 359 ? 1.8075 0.9720 1.5022 -0.3088 -0.1429 -0.2772 377 HIS A CE1 
2670 N NE2 . HIS A 359 ? 1.7701 1.0040 1.5347 -0.3099 -0.1994 -0.2689 377 HIS A NE2 
2671 N N   . HIS A 360 ? 1.6893 0.9735 1.4148 -0.1943 -0.1694 -0.1759 378 HIS A N   
2672 C CA  . HIS A 360 ? 1.7203 0.9830 1.4052 -0.1709 -0.1733 -0.1583 378 HIS A CA  
2673 C C   . HIS A 360 ? 1.6586 1.0020 1.4379 -0.1576 -0.2077 -0.1446 378 HIS A C   
2674 O O   . HIS A 360 ? 1.5619 0.9717 1.4378 -0.1551 -0.1867 -0.1418 378 HIS A O   
2675 C CB  . HIS A 360 ? 1.6933 0.9306 1.3672 -0.1610 -0.1124 -0.1500 378 HIS A CB  
2676 C CG  . HIS A 360 ? 1.9603 1.1572 1.5773 -0.1391 -0.1123 -0.1323 378 HIS A CG  
2677 N ND1 . HIS A 360 ? 1.9234 1.1654 1.5951 -0.1204 -0.1302 -0.1176 378 HIS A ND1 
2678 C CD2 . HIS A 360 ? 1.8365 0.9494 1.3469 -0.1314 -0.0935 -0.1253 378 HIS A CD2 
2679 C CE1 . HIS A 360 ? 1.7675 0.9561 1.3724 -0.1035 -0.1248 -0.1025 378 HIS A CE1 
2680 N NE2 . HIS A 360 ? 1.8474 0.9585 1.3540 -0.1097 -0.1026 -0.1057 378 HIS A NE2 
2681 N N   . GLU A 361 ? 1.7209 1.0562 1.4703 -0.1480 -0.2592 -0.1345 379 GLU A N   
2682 C CA  . GLU A 361 ? 1.6726 1.0865 1.5199 -0.1367 -0.2970 -0.1200 379 GLU A CA  
2683 C C   . GLU A 361 ? 1.5974 1.0516 1.5090 -0.1136 -0.2622 -0.1067 379 GLU A C   
2684 O O   . GLU A 361 ? 1.5138 1.0409 1.5276 -0.1104 -0.2538 -0.1044 379 GLU A O   
2685 C CB  . GLU A 361 ? 1.7639 1.1540 1.5614 -0.1291 -0.3584 -0.1069 379 GLU A CB  
2686 C CG  . GLU A 361 ? 1.8620 1.1978 1.5751 -0.1525 -0.4002 -0.1221 379 GLU A CG  
2687 C CD  . GLU A 361 ? 2.0900 1.3780 1.7170 -0.1435 -0.4548 -0.1082 379 GLU A CD  
2688 O OE1 . GLU A 361 ? 2.1053 1.4073 1.7477 -0.1181 -0.4587 -0.0844 379 GLU A OE1 
2689 O OE2 . GLU A 361 ? 2.5087 1.7412 2.0487 -0.1617 -0.4946 -0.1210 379 GLU A OE2 
2690 N N   . GLY A 362 ? 1.6334 1.0361 1.4826 -0.0971 -0.2403 -0.0977 380 GLY A N   
2691 C CA  . GLY A 362 ? 1.5805 1.0112 1.4827 -0.0746 -0.2153 -0.0859 380 GLY A CA  
2692 C C   . GLY A 362 ? 1.4936 0.9561 1.4532 -0.0815 -0.1678 -0.0965 380 GLY A C   
2693 O O   . GLY A 362 ? 1.4308 0.9497 1.4697 -0.0697 -0.1600 -0.0929 380 GLY A O   
2694 N N   . ILE A 363 ? 1.4955 0.9198 1.4138 -0.0994 -0.1346 -0.1081 381 ILE A N   
2695 C CA  . ILE A 363 ? 1.4183 0.8715 1.3900 -0.1078 -0.0931 -0.1152 381 ILE A CA  
2696 C C   . ILE A 363 ? 1.3521 0.8801 1.4093 -0.1171 -0.1036 -0.1216 381 ILE A C   
2697 O O   . ILE A 363 ? 1.2851 0.8606 1.4078 -0.1126 -0.0837 -0.1213 381 ILE A O   
2698 C CB  . ILE A 363 ? 1.4387 0.8369 1.3564 -0.1247 -0.0561 -0.1215 381 ILE A CB  
2699 C CG1 . ILE A 363 ? 1.5095 0.8334 1.3460 -0.1135 -0.0421 -0.1106 381 ILE A CG1 
2700 C CG2 . ILE A 363 ? 1.3608 0.7915 1.3394 -0.1341 -0.0179 -0.1248 381 ILE A CG2 
2701 C CD1 . ILE A 363 ? 1.5382 0.8047 1.3242 -0.1264 0.0001  -0.1116 381 ILE A CD1 
2702 N N   . GLU A 364 ? 1.3767 0.9128 1.4321 -0.1305 -0.1356 -0.1270 382 GLU A N   
2703 C CA  . GLU A 364 ? 1.3180 0.9261 1.4624 -0.1396 -0.1473 -0.1295 382 GLU A CA  
2704 C C   . GLU A 364 ? 1.2793 0.9507 1.5009 -0.1172 -0.1606 -0.1155 382 GLU A C   
2705 O O   . GLU A 364 ? 1.2119 0.9412 1.5090 -0.1146 -0.1412 -0.1138 382 GLU A O   
2706 C CB  . GLU A 364 ? 1.3654 0.9639 1.4930 -0.1585 -0.1872 -0.1369 382 GLU A CB  
2707 C CG  . GLU A 364 ? 1.3880 0.9391 1.4656 -0.1826 -0.1656 -0.1539 382 GLU A CG  
2708 C CD  . GLU A 364 ? 1.4391 0.9789 1.5034 -0.2031 -0.2072 -0.1648 382 GLU A CD  
2709 O OE1 . GLU A 364 ? 1.4253 1.0197 1.5570 -0.2035 -0.2491 -0.1576 382 GLU A OE1 
2710 O OE2 . GLU A 364 ? 1.4986 0.9722 1.4860 -0.2187 -0.1977 -0.1801 382 GLU A OE2 
2711 N N   . TYR A 365 ? 1.3270 0.9860 1.5291 -0.0989 -0.1911 -0.1033 383 TYR A N   
2712 C CA  . TYR A 365 ? 1.2971 1.0121 1.5746 -0.0739 -0.1987 -0.0876 383 TYR A CA  
2713 C C   . TYR A 365 ? 1.2542 0.9735 1.5461 -0.0577 -0.1534 -0.0891 383 TYR A C   
2714 O O   . TYR A 365 ? 1.2053 0.9804 1.5704 -0.0454 -0.1393 -0.0844 383 TYR A O   
2715 C CB  . TYR A 365 ? 1.3616 1.0562 1.6130 -0.0558 -0.2376 -0.0713 383 TYR A CB  
2716 C CG  . TYR A 365 ? 1.4789 1.2130 1.7945 -0.0238 -0.2313 -0.0543 383 TYR A CG  
2717 C CD1 . TYR A 365 ? 1.5403 1.3499 1.9589 -0.0142 -0.2447 -0.0408 383 TYR A CD1 
2718 C CD2 . TYR A 365 ? 1.5544 1.2477 1.8306 -0.0024 -0.2086 -0.0509 383 TYR A CD2 
2719 C CE1 . TYR A 365 ? 1.7340 1.5753 2.2103 0.0184  -0.2322 -0.0245 383 TYR A CE1 
2720 C CE2 . TYR A 365 ? 1.5617 1.2831 1.8923 0.0283  -0.1993 -0.0374 383 TYR A CE2 
2721 C CZ  . TYR A 365 ? 1.8128 1.6072 2.2411 0.0399  -0.2093 -0.0244 383 TYR A CZ  
2722 O OH  . TYR A 365 ? 1.6489 1.4668 2.1299 0.0737  -0.1939 -0.0101 383 TYR A OH  
2723 N N   . VAL A 366 ? 1.2791 0.9366 1.5003 -0.0576 -0.1303 -0.0948 384 VAL A N   
2724 C CA  . VAL A 366 ? 1.2506 0.9034 1.4800 -0.0450 -0.0940 -0.0974 384 VAL A CA  
2725 C C   . VAL A 366 ? 1.1853 0.8791 1.4608 -0.0583 -0.0665 -0.1070 384 VAL A C   
2726 O O   . VAL A 366 ? 1.1533 0.8795 1.4707 -0.0441 -0.0490 -0.1067 384 VAL A O   
2727 C CB  . VAL A 366 ? 1.2919 0.8702 1.4443 -0.0470 -0.0769 -0.0993 384 VAL A CB  
2728 C CG1 . VAL A 366 ? 1.2636 0.8343 1.4264 -0.0419 -0.0430 -0.1049 384 VAL A CG1 
2729 C CG2 . VAL A 366 ? 1.3588 0.8985 1.4686 -0.0283 -0.1010 -0.0858 384 VAL A CG2 
2730 N N   . LEU A 367 ? 1.1716 0.8609 1.4364 -0.0846 -0.0613 -0.1149 385 LEU A N   
2731 C CA  . LEU A 367 ? 1.1122 0.8390 1.4205 -0.0980 -0.0355 -0.1207 385 LEU A CA  
2732 C C   . LEU A 367 ? 1.0721 0.8726 1.4606 -0.0921 -0.0442 -0.1148 385 LEU A C   
2733 O O   . LEU A 367 ? 1.0294 0.8672 1.4585 -0.0880 -0.0209 -0.1144 385 LEU A O   
2734 C CB  . LEU A 367 ? 1.2050 0.9061 1.4864 -0.1256 -0.0257 -0.1280 385 LEU A CB  
2735 C CG  . LEU A 367 ? 1.1501 0.7806 1.3614 -0.1313 -0.0076 -0.1297 385 LEU A CG  
2736 C CD1 . LEU A 367 ? 1.2450 0.8522 1.4374 -0.1556 0.0081  -0.1350 385 LEU A CD1 
2737 C CD2 . LEU A 367 ? 1.1292 0.7528 1.3458 -0.1244 0.0171  -0.1282 385 LEU A CD2 
2738 N N   . LYS A 368 ? 1.0902 0.9118 1.5031 -0.0918 -0.0781 -0.1083 386 LYS A N   
2739 C CA  . LYS A 368 ? 1.0776 0.9722 1.5795 -0.0845 -0.0861 -0.0975 386 LYS A CA  
2740 C C   . LYS A 368 ? 1.0684 0.9886 1.6030 -0.0522 -0.0712 -0.0876 386 LYS A C   
2741 O O   . LYS A 368 ? 1.1690 1.1407 1.7634 -0.0432 -0.0502 -0.0816 386 LYS A O   
2742 C CB  . LYS A 368 ? 1.0857 0.9941 1.6105 -0.0917 -0.1323 -0.0902 386 LYS A CB  
2743 C CG  . LYS A 368 ? 1.1161 1.0067 1.6218 -0.1242 -0.1458 -0.1018 386 LYS A CG  
2744 C CD  . LYS A 368 ? 1.1400 1.0337 1.6565 -0.1329 -0.1995 -0.0968 386 LYS A CD  
2745 C CE  . LYS A 368 ? 1.1643 1.0273 1.6495 -0.1654 -0.2129 -0.1126 386 LYS A CE  
2746 N NZ  . LYS A 368 ? 1.4080 1.2652 1.8933 -0.1770 -0.2723 -0.1104 386 LYS A NZ  
2747 N N   . TYR A 369 ? 1.0898 0.9704 1.5827 -0.0329 -0.0790 -0.0850 387 TYR A N   
2748 C CA  . TYR A 369 ? 1.2190 1.1107 1.7333 -0.0006 -0.0602 -0.0783 387 TYR A CA  
2749 C C   . TYR A 369 ? 1.1373 1.0195 1.6329 0.0001  -0.0199 -0.0908 387 TYR A C   
2750 O O   . TYR A 369 ? 1.2500 1.1670 1.7850 0.0189  0.0028  -0.0869 387 TYR A O   
2751 C CB  . TYR A 369 ? 1.2091 1.0494 1.6749 0.0170  -0.0751 -0.0740 387 TYR A CB  
2752 C CG  . TYR A 369 ? 1.3623 1.2029 1.8456 0.0523  -0.0557 -0.0678 387 TYR A CG  
2753 C CD1 . TYR A 369 ? 1.4969 1.3869 2.0535 0.0780  -0.0635 -0.0480 387 TYR A CD1 
2754 C CD2 . TYR A 369 ? 1.3766 1.1646 1.8056 0.0600  -0.0295 -0.0807 387 TYR A CD2 
2755 C CE1 . TYR A 369 ? 1.6800 1.5644 2.2508 0.1133  -0.0403 -0.0423 387 TYR A CE1 
2756 C CE2 . TYR A 369 ? 1.5490 1.3274 1.9868 0.0926  -0.0107 -0.0781 387 TYR A CE2 
2757 C CZ  . TYR A 369 ? 1.6833 1.5084 2.1894 0.1206  -0.0137 -0.0594 387 TYR A CZ  
2758 O OH  . TYR A 369 ? 1.8315 1.6416 2.3448 0.1560  0.0105  -0.0568 387 TYR A OH  
2759 N N   . VAL A 370 ? 1.1296 0.9638 1.5650 -0.0205 -0.0108 -0.1042 388 VAL A N   
2760 C CA  . VAL A 370 ? 1.0900 0.9125 1.5068 -0.0240 0.0197  -0.1148 388 VAL A CA  
2761 C C   . VAL A 370 ? 1.2772 1.1592 1.7472 -0.0306 0.0354  -0.1121 388 VAL A C   
2762 O O   . VAL A 370 ? 1.2755 1.1709 1.7517 -0.0172 0.0586  -0.1141 388 VAL A O   
2763 C CB  . VAL A 370 ? 1.0638 0.8320 1.4237 -0.0484 0.0237  -0.1240 388 VAL A CB  
2764 C CG1 . VAL A 370 ? 1.2584 1.0220 1.6098 -0.0571 0.0481  -0.1320 388 VAL A CG1 
2765 C CG2 . VAL A 370 ? 1.3069 1.0137 1.6141 -0.0389 0.0141  -0.1238 388 VAL A CG2 
2766 N N   . MET A 371 ? 1.1507 1.0645 1.6549 -0.0513 0.0236  -0.1076 389 MET A N   
2767 C CA  . MET A 371 ? 1.1823 1.1540 1.7438 -0.0581 0.0388  -0.1016 389 MET A CA  
2768 C C   . MET A 371 ? 1.2380 1.2626 1.8611 -0.0303 0.0454  -0.0875 389 MET A C   
2769 O O   . MET A 371 ? 1.2780 1.3371 1.9285 -0.0222 0.0719  -0.0826 389 MET A O   
2770 C CB  . MET A 371 ? 1.1671 1.1553 1.7548 -0.0861 0.0231  -0.1000 389 MET A CB  
2771 C CG  . MET A 371 ? 1.1493 1.0941 1.6889 -0.1126 0.0307  -0.1107 389 MET A CG  
2772 S SD  . MET A 371 ? 1.0246 0.9748 1.5586 -0.1188 0.0647  -0.1121 389 MET A SD  
2773 C CE  . MET A 371 ? 1.1142 1.1441 1.7308 -0.1167 0.0768  -0.0983 389 MET A CE  
2774 N N   . ASP A 372 ? 1.4935 1.5249 2.1404 -0.0142 0.0229  -0.0781 390 ASP A N   
2775 C CA  . ASP A 372 ? 1.4664 1.5476 2.1806 0.0157  0.0323  -0.0604 390 ASP A CA  
2776 C C   . ASP A 372 ? 1.4994 1.5590 2.1813 0.0457  0.0661  -0.0653 390 ASP A C   
2777 O O   . ASP A 372 ? 1.5616 1.6614 2.2922 0.0710  0.0905  -0.0521 390 ASP A O   
2778 C CB  . ASP A 372 ? 1.4932 1.5828 2.2409 0.0263  -0.0032 -0.0466 390 ASP A CB  
2779 C CG  . ASP A 372 ? 1.5092 1.6323 2.3067 0.0002  -0.0385 -0.0387 390 ASP A CG  
2780 O OD1 . ASP A 372 ? 1.5699 1.7116 2.3824 -0.0239 -0.0306 -0.0435 390 ASP A OD1 
2781 O OD2 . ASP A 372 ? 1.5362 1.6644 2.3573 0.0034  -0.0762 -0.0273 390 ASP A OD2 
2782 N N   . ILE A 373 ? 1.4705 1.4643 2.0712 0.0437  0.0693  -0.0833 391 ILE A N   
2783 C CA  . ILE A 373 ? 1.4604 1.4235 2.0209 0.0685  0.0989  -0.0924 391 ILE A CA  
2784 C C   . ILE A 373 ? 1.4095 1.3986 1.9730 0.0661  0.1290  -0.0944 391 ILE A C   
2785 O O   . ILE A 373 ? 1.2594 1.2581 1.8276 0.0948  0.1582  -0.0912 391 ILE A O   
2786 C CB  . ILE A 373 ? 1.4053 1.2911 1.8835 0.0606  0.0922  -0.1110 391 ILE A CB  
2787 C CG1 . ILE A 373 ? 1.4337 1.2919 1.9062 0.0709  0.0674  -0.1050 391 ILE A CG1 
2788 C CG2 . ILE A 373 ? 1.5005 1.3476 1.9302 0.0799  0.1195  -0.1248 391 ILE A CG2 
2789 C CD1 . ILE A 373 ? 1.3911 1.1745 1.7907 0.0617  0.0607  -0.1186 391 ILE A CD1 
2790 N N   . LEU A 374 ? 1.5091 1.5074 2.0676 0.0336  0.1243  -0.0983 392 LEU A N   
2791 C CA  . LEU A 374 ? 1.4389 1.4574 1.9928 0.0282  0.1493  -0.0986 392 LEU A CA  
2792 C C   . LEU A 374 ? 1.4377 1.4033 1.9162 0.0424  0.1670  -0.1149 392 LEU A C   
2793 O O   . LEU A 374 ? 1.2312 1.1816 1.6710 0.0255  0.1725  -0.1228 392 LEU A O   
2794 C CB  . LEU A 374 ? 1.5212 1.6094 2.1500 0.0455  0.1697  -0.0775 392 LEU A CB  
2795 C CG  . LEU A 374 ? 1.5947 1.7402 2.3029 0.0238  0.1540  -0.0614 392 LEU A CG  
2796 C CD1 . LEU A 374 ? 1.4867 1.6550 2.2531 0.0346  0.1309  -0.0490 392 LEU A CD1 
2797 C CD2 . LEU A 374 ? 1.3291 1.5324 2.0889 0.0271  0.1822  -0.0440 392 LEU A CD2 
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