data_8ZR6
# 
_entry.id   8ZR6 
# 
_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   8ZR6         pdb_00008zr6 10.2210/pdb8zr6/pdb 
WWPDB D_1300048394 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZR6 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              stefan.arold@kaust.edu.sa 
_pdbx_contact_author.name_first         Stefan 
_pdbx_contact_author.name_last          Arold 
_pdbx_contact_author.name_mi            T. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5278-0668 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Arold, S.T.'    1 ? 
'Hameed, U.F.S.' 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                     'Arabidopsis Carboxyl esterase CXE15 E271Q mutant' 
_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 'Arold, S.T.'    1 ? 
primary 'Hameed, U.F.S.' 2 ? 
# 
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 'Strigolactones hydrolase CXE15' 35834.379 1  3.1.1.- E271Q ? ? 
2 non-polymer syn GLYCEROL                         92.094    1  ?       ?     ? ? 
3 water       nat water                            18.015    19 ?       ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carboxylesterase 15,AtCXE15' 
# 
_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       
;QVAEDCMGLLQLLSNGTVLRSESIDLITQQIPFKNNQTVLFKDSIYHKPNNLHLRLYKPISASNRTALPVVVFFHGGGFC
FGSRSWPHFHNFCLTLASSLNALVVSPDYRLAPEHRLPAAFEDAEAVLTWLWDQAVSDGVNHWFEDGTDVDFDRVFVVGD
SSGGNIAHQLAVRFGSGSIELTPVRVRGYVLMGPFFGGEERTNSENGPSEALLSLDLLDKFWRLSLPNGATRDHHMANPF
GPTSPTLESISLEPMLVIVGGSQLLRDRAKEYAYKLKKMGGKRVDYIEFENKEHGFYSNYPSSEAAEQVLRIIGDFMNNL
S
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QVAEDCMGLLQLLSNGTVLRSESIDLITQQIPFKNNQTVLFKDSIYHKPNNLHLRLYKPISASNRTALPVVVFFHGGGFC
FGSRSWPHFHNFCLTLASSLNALVVSPDYRLAPEHRLPAAFEDAEAVLTWLWDQAVSDGVNHWFEDGTDVDFDRVFVVGD
SSGGNIAHQLAVRFGSGSIELTPVRVRGYVLMGPFFGGEERTNSENGPSEALLSLDLLDKFWRLSLPNGATRDHHMANPF
GPTSPTLESISLEPMLVIVGGSQLLRDRAKEYAYKLKKMGGKRVDYIEFENKEHGFYSNYPSSEAAEQVLRIIGDFMNNL
S
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL GOL 
3 water    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   VAL n 
1 3   ALA n 
1 4   GLU n 
1 5   ASP n 
1 6   CYS n 
1 7   MET n 
1 8   GLY n 
1 9   LEU n 
1 10  LEU n 
1 11  GLN n 
1 12  LEU n 
1 13  LEU n 
1 14  SER n 
1 15  ASN n 
1 16  GLY n 
1 17  THR n 
1 18  VAL n 
1 19  LEU n 
1 20  ARG n 
1 21  SER n 
1 22  GLU n 
1 23  SER n 
1 24  ILE n 
1 25  ASP n 
1 26  LEU n 
1 27  ILE n 
1 28  THR n 
1 29  GLN n 
1 30  GLN n 
1 31  ILE n 
1 32  PRO n 
1 33  PHE n 
1 34  LYS n 
1 35  ASN n 
1 36  ASN n 
1 37  GLN n 
1 38  THR n 
1 39  VAL n 
1 40  LEU n 
1 41  PHE n 
1 42  LYS n 
1 43  ASP n 
1 44  SER n 
1 45  ILE n 
1 46  TYR n 
1 47  HIS n 
1 48  LYS n 
1 49  PRO n 
1 50  ASN n 
1 51  ASN n 
1 52  LEU n 
1 53  HIS n 
1 54  LEU n 
1 55  ARG n 
1 56  LEU n 
1 57  TYR n 
1 58  LYS n 
1 59  PRO n 
1 60  ILE n 
1 61  SER n 
1 62  ALA n 
1 63  SER n 
1 64  ASN n 
1 65  ARG n 
1 66  THR n 
1 67  ALA n 
1 68  LEU n 
1 69  PRO n 
1 70  VAL n 
1 71  VAL n 
1 72  VAL n 
1 73  PHE n 
1 74  PHE n 
1 75  HIS n 
1 76  GLY n 
1 77  GLY n 
1 78  GLY n 
1 79  PHE n 
1 80  CYS n 
1 81  PHE n 
1 82  GLY n 
1 83  SER n 
1 84  ARG n 
1 85  SER n 
1 86  TRP n 
1 87  PRO n 
1 88  HIS n 
1 89  PHE n 
1 90  HIS n 
1 91  ASN n 
1 92  PHE n 
1 93  CYS n 
1 94  LEU n 
1 95  THR n 
1 96  LEU n 
1 97  ALA n 
1 98  SER n 
1 99  SER n 
1 100 LEU n 
1 101 ASN n 
1 102 ALA n 
1 103 LEU n 
1 104 VAL n 
1 105 VAL n 
1 106 SER n 
1 107 PRO n 
1 108 ASP n 
1 109 TYR n 
1 110 ARG n 
1 111 LEU n 
1 112 ALA n 
1 113 PRO n 
1 114 GLU n 
1 115 HIS n 
1 116 ARG n 
1 117 LEU n 
1 118 PRO n 
1 119 ALA n 
1 120 ALA n 
1 121 PHE n 
1 122 GLU n 
1 123 ASP n 
1 124 ALA n 
1 125 GLU n 
1 126 ALA n 
1 127 VAL n 
1 128 LEU n 
1 129 THR n 
1 130 TRP n 
1 131 LEU n 
1 132 TRP n 
1 133 ASP n 
1 134 GLN n 
1 135 ALA n 
1 136 VAL n 
1 137 SER n 
1 138 ASP n 
1 139 GLY n 
1 140 VAL n 
1 141 ASN n 
1 142 HIS n 
1 143 TRP n 
1 144 PHE n 
1 145 GLU n 
1 146 ASP n 
1 147 GLY n 
1 148 THR n 
1 149 ASP n 
1 150 VAL n 
1 151 ASP n 
1 152 PHE n 
1 153 ASP n 
1 154 ARG n 
1 155 VAL n 
1 156 PHE n 
1 157 VAL n 
1 158 VAL n 
1 159 GLY n 
1 160 ASP n 
1 161 SER n 
1 162 SER n 
1 163 GLY n 
1 164 GLY n 
1 165 ASN n 
1 166 ILE n 
1 167 ALA n 
1 168 HIS n 
1 169 GLN n 
1 170 LEU n 
1 171 ALA n 
1 172 VAL n 
1 173 ARG n 
1 174 PHE n 
1 175 GLY n 
1 176 SER n 
1 177 GLY n 
1 178 SER n 
1 179 ILE n 
1 180 GLU n 
1 181 LEU n 
1 182 THR n 
1 183 PRO n 
1 184 VAL n 
1 185 ARG n 
1 186 VAL n 
1 187 ARG n 
1 188 GLY n 
1 189 TYR n 
1 190 VAL n 
1 191 LEU n 
1 192 MET n 
1 193 GLY n 
1 194 PRO n 
1 195 PHE n 
1 196 PHE n 
1 197 GLY n 
1 198 GLY n 
1 199 GLU n 
1 200 GLU n 
1 201 ARG n 
1 202 THR n 
1 203 ASN n 
1 204 SER n 
1 205 GLU n 
1 206 ASN n 
1 207 GLY n 
1 208 PRO n 
1 209 SER n 
1 210 GLU n 
1 211 ALA n 
1 212 LEU n 
1 213 LEU n 
1 214 SER n 
1 215 LEU n 
1 216 ASP n 
1 217 LEU n 
1 218 LEU n 
1 219 ASP n 
1 220 LYS n 
1 221 PHE n 
1 222 TRP n 
1 223 ARG n 
1 224 LEU n 
1 225 SER n 
1 226 LEU n 
1 227 PRO n 
1 228 ASN n 
1 229 GLY n 
1 230 ALA n 
1 231 THR n 
1 232 ARG n 
1 233 ASP n 
1 234 HIS n 
1 235 HIS n 
1 236 MET n 
1 237 ALA n 
1 238 ASN n 
1 239 PRO n 
1 240 PHE n 
1 241 GLY n 
1 242 PRO n 
1 243 THR n 
1 244 SER n 
1 245 PRO n 
1 246 THR n 
1 247 LEU n 
1 248 GLU n 
1 249 SER n 
1 250 ILE n 
1 251 SER n 
1 252 LEU n 
1 253 GLU n 
1 254 PRO n 
1 255 MET n 
1 256 LEU n 
1 257 VAL n 
1 258 ILE n 
1 259 VAL n 
1 260 GLY n 
1 261 GLY n 
1 262 SER n 
1 263 GLN n 
1 264 LEU n 
1 265 LEU n 
1 266 ARG n 
1 267 ASP n 
1 268 ARG n 
1 269 ALA n 
1 270 LYS n 
1 271 GLU n 
1 272 TYR n 
1 273 ALA n 
1 274 TYR n 
1 275 LYS n 
1 276 LEU n 
1 277 LYS n 
1 278 LYS n 
1 279 MET n 
1 280 GLY n 
1 281 GLY n 
1 282 LYS n 
1 283 ARG n 
1 284 VAL n 
1 285 ASP n 
1 286 TYR n 
1 287 ILE n 
1 288 GLU n 
1 289 PHE n 
1 290 GLU n 
1 291 ASN n 
1 292 LYS n 
1 293 GLU n 
1 294 HIS n 
1 295 GLY n 
1 296 PHE n 
1 297 TYR n 
1 298 SER n 
1 299 ASN n 
1 300 TYR n 
1 301 PRO n 
1 302 SER n 
1 303 SER n 
1 304 GLU n 
1 305 ALA n 
1 306 ALA n 
1 307 GLU n 
1 308 GLN n 
1 309 VAL n 
1 310 LEU n 
1 311 ARG n 
1 312 ILE n 
1 313 ILE n 
1 314 GLY n 
1 315 ASP n 
1 316 PHE n 
1 317 MET n 
1 318 ASN n 
1 319 ASN n 
1 320 LEU n 
1 321 SER 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                   321 
_entity_src_gen.gene_src_common_name               'thale cress' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CXE15, At5g06570, F15M7.10' 
_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      'Arabidopsis thaliana' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3702 
_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-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_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   GLN 1   9   9   GLN GLN A . n 
A 1 2   VAL 2   10  10  VAL VAL A . n 
A 1 3   ALA 3   11  11  ALA ALA A . n 
A 1 4   GLU 4   12  12  GLU GLU A . n 
A 1 5   ASP 5   13  13  ASP ASP A . n 
A 1 6   CYS 6   14  14  CYS CYS A . n 
A 1 7   MET 7   15  15  MET MET A . n 
A 1 8   GLY 8   16  16  GLY GLY A . n 
A 1 9   LEU 9   17  17  LEU LEU A . n 
A 1 10  LEU 10  18  18  LEU LEU A . n 
A 1 11  GLN 11  19  19  GLN GLN A . n 
A 1 12  LEU 12  20  20  LEU LEU A . n 
A 1 13  LEU 13  21  21  LEU LEU A . n 
A 1 14  SER 14  22  22  SER SER A . n 
A 1 15  ASN 15  23  23  ASN ASN A . n 
A 1 16  GLY 16  24  24  GLY GLY A . n 
A 1 17  THR 17  25  25  THR THR A . n 
A 1 18  VAL 18  26  26  VAL VAL A . n 
A 1 19  LEU 19  27  27  LEU LEU A . n 
A 1 20  ARG 20  28  28  ARG ARG A . n 
A 1 21  SER 21  29  29  SER SER A . n 
A 1 22  GLU 22  30  30  GLU GLU A . n 
A 1 23  SER 23  31  31  SER SER A . n 
A 1 24  ILE 24  32  32  ILE ILE A . n 
A 1 25  ASP 25  33  33  ASP ASP A . n 
A 1 26  LEU 26  34  34  LEU LEU A . n 
A 1 27  ILE 27  35  35  ILE ILE A . n 
A 1 28  THR 28  36  36  THR THR A . n 
A 1 29  GLN 29  37  37  GLN GLN A . n 
A 1 30  GLN 30  38  38  GLN GLN A . n 
A 1 31  ILE 31  39  39  ILE ILE A . n 
A 1 32  PRO 32  40  40  PRO PRO A . n 
A 1 33  PHE 33  41  41  PHE PHE A . n 
A 1 34  LYS 34  42  42  LYS LYS A . n 
A 1 35  ASN 35  43  43  ASN ASN A . n 
A 1 36  ASN 36  44  44  ASN ASN A . n 
A 1 37  GLN 37  45  45  GLN GLN A . n 
A 1 38  THR 38  46  46  THR THR A . n 
A 1 39  VAL 39  47  47  VAL VAL A . n 
A 1 40  LEU 40  48  48  LEU LEU A . n 
A 1 41  PHE 41  49  49  PHE PHE A . n 
A 1 42  LYS 42  50  50  LYS LYS A . n 
A 1 43  ASP 43  51  51  ASP ASP A . n 
A 1 44  SER 44  52  52  SER SER A . n 
A 1 45  ILE 45  53  53  ILE ILE A . n 
A 1 46  TYR 46  54  54  TYR TYR A . n 
A 1 47  HIS 47  55  55  HIS HIS A . n 
A 1 48  LYS 48  56  56  LYS LYS A . n 
A 1 49  PRO 49  57  57  PRO PRO A . n 
A 1 50  ASN 50  58  58  ASN ASN A . n 
A 1 51  ASN 51  59  59  ASN ASN A . n 
A 1 52  LEU 52  60  60  LEU LEU A . n 
A 1 53  HIS 53  61  61  HIS HIS A . n 
A 1 54  LEU 54  62  62  LEU LEU A . n 
A 1 55  ARG 55  63  63  ARG ARG A . n 
A 1 56  LEU 56  64  64  LEU LEU A . n 
A 1 57  TYR 57  65  65  TYR TYR A . n 
A 1 58  LYS 58  66  66  LYS LYS A . n 
A 1 59  PRO 59  67  67  PRO PRO A . n 
A 1 60  ILE 60  68  68  ILE ILE A . n 
A 1 61  SER 61  69  69  SER SER A . n 
A 1 62  ALA 62  70  70  ALA ALA A . n 
A 1 63  SER 63  71  71  SER SER A . n 
A 1 64  ASN 64  72  72  ASN ASN A . n 
A 1 65  ARG 65  73  73  ARG ARG A . n 
A 1 66  THR 66  74  74  THR THR A . n 
A 1 67  ALA 67  75  75  ALA ALA A . n 
A 1 68  LEU 68  76  76  LEU LEU A . n 
A 1 69  PRO 69  77  77  PRO PRO A . n 
A 1 70  VAL 70  78  78  VAL VAL A . n 
A 1 71  VAL 71  79  79  VAL VAL A . n 
A 1 72  VAL 72  80  80  VAL VAL A . n 
A 1 73  PHE 73  81  81  PHE PHE A . n 
A 1 74  PHE 74  82  82  PHE PHE A . n 
A 1 75  HIS 75  83  83  HIS HIS A . n 
A 1 76  GLY 76  84  84  GLY GLY A . n 
A 1 77  GLY 77  85  85  GLY GLY A . n 
A 1 78  GLY 78  86  86  GLY GLY A . n 
A 1 79  PHE 79  87  87  PHE PHE A . n 
A 1 80  CYS 80  88  88  CYS CYS A . n 
A 1 81  PHE 81  89  89  PHE PHE A . n 
A 1 82  GLY 82  90  90  GLY GLY A . n 
A 1 83  SER 83  91  91  SER SER A . n 
A 1 84  ARG 84  92  92  ARG ARG A . n 
A 1 85  SER 85  93  93  SER SER A . n 
A 1 86  TRP 86  94  94  TRP TRP A . n 
A 1 87  PRO 87  95  95  PRO PRO A . n 
A 1 88  HIS 88  96  96  HIS HIS A . n 
A 1 89  PHE 89  97  97  PHE PHE A . n 
A 1 90  HIS 90  98  98  HIS HIS A . n 
A 1 91  ASN 91  99  99  ASN ASN A . n 
A 1 92  PHE 92  100 100 PHE PHE A . n 
A 1 93  CYS 93  101 101 CYS CYS A . n 
A 1 94  LEU 94  102 102 LEU LEU A . n 
A 1 95  THR 95  103 103 THR THR A . n 
A 1 96  LEU 96  104 104 LEU LEU A . n 
A 1 97  ALA 97  105 105 ALA ALA A . n 
A 1 98  SER 98  106 106 SER SER A . n 
A 1 99  SER 99  107 107 SER SER A . n 
A 1 100 LEU 100 108 108 LEU LEU A . n 
A 1 101 ASN 101 109 109 ASN ASN A . n 
A 1 102 ALA 102 110 110 ALA ALA A . n 
A 1 103 LEU 103 111 111 LEU LEU A . n 
A 1 104 VAL 104 112 112 VAL VAL A . n 
A 1 105 VAL 105 113 113 VAL VAL A . n 
A 1 106 SER 106 114 114 SER SER A . n 
A 1 107 PRO 107 115 115 PRO PRO A . n 
A 1 108 ASP 108 116 116 ASP ASP A . n 
A 1 109 TYR 109 117 117 TYR TYR A . n 
A 1 110 ARG 110 118 118 ARG ARG A . n 
A 1 111 LEU 111 119 119 LEU LEU A . n 
A 1 112 ALA 112 120 120 ALA ALA A . n 
A 1 113 PRO 113 121 121 PRO PRO A . n 
A 1 114 GLU 114 122 122 GLU GLU A . n 
A 1 115 HIS 115 123 123 HIS HIS A . n 
A 1 116 ARG 116 124 124 ARG ARG A . n 
A 1 117 LEU 117 125 125 LEU LEU A . n 
A 1 118 PRO 118 126 126 PRO PRO A . n 
A 1 119 ALA 119 127 127 ALA ALA A . n 
A 1 120 ALA 120 128 128 ALA ALA A . n 
A 1 121 PHE 121 129 129 PHE PHE A . n 
A 1 122 GLU 122 130 130 GLU GLU A . n 
A 1 123 ASP 123 131 131 ASP ASP A . n 
A 1 124 ALA 124 132 132 ALA ALA A . n 
A 1 125 GLU 125 133 133 GLU GLU A . n 
A 1 126 ALA 126 134 134 ALA ALA A . n 
A 1 127 VAL 127 135 135 VAL VAL A . n 
A 1 128 LEU 128 136 136 LEU LEU A . n 
A 1 129 THR 129 137 137 THR THR A . n 
A 1 130 TRP 130 138 138 TRP TRP A . n 
A 1 131 LEU 131 139 139 LEU LEU A . n 
A 1 132 TRP 132 140 140 TRP TRP A . n 
A 1 133 ASP 133 141 141 ASP ASP A . n 
A 1 134 GLN 134 142 142 GLN GLN A . n 
A 1 135 ALA 135 143 143 ALA ALA A . n 
A 1 136 VAL 136 144 144 VAL VAL A . n 
A 1 137 SER 137 145 145 SER SER A . n 
A 1 138 ASP 138 146 146 ASP ASP A . n 
A 1 139 GLY 139 147 147 GLY GLY A . n 
A 1 140 VAL 140 148 148 VAL VAL A . n 
A 1 141 ASN 141 149 149 ASN ASN A . n 
A 1 142 HIS 142 150 150 HIS HIS A . n 
A 1 143 TRP 143 151 151 TRP TRP A . n 
A 1 144 PHE 144 152 152 PHE PHE A . n 
A 1 145 GLU 145 153 153 GLU GLU A . n 
A 1 146 ASP 146 154 154 ASP ASP A . n 
A 1 147 GLY 147 155 155 GLY GLY A . n 
A 1 148 THR 148 156 156 THR THR A . n 
A 1 149 ASP 149 157 157 ASP ASP A . n 
A 1 150 VAL 150 158 158 VAL VAL A . n 
A 1 151 ASP 151 159 159 ASP ASP A . n 
A 1 152 PHE 152 160 160 PHE PHE A . n 
A 1 153 ASP 153 161 161 ASP ASP A . n 
A 1 154 ARG 154 162 162 ARG ARG A . n 
A 1 155 VAL 155 163 163 VAL VAL A . n 
A 1 156 PHE 156 164 164 PHE PHE A . n 
A 1 157 VAL 157 165 165 VAL VAL A . n 
A 1 158 VAL 158 166 166 VAL VAL A . n 
A 1 159 GLY 159 167 167 GLY GLY A . n 
A 1 160 ASP 160 168 168 ASP ASP A . n 
A 1 161 SER 161 169 169 SER SER A . n 
A 1 162 SER 162 170 170 SER SER A . n 
A 1 163 GLY 163 171 171 GLY GLY A . n 
A 1 164 GLY 164 172 172 GLY GLY A . n 
A 1 165 ASN 165 173 173 ASN ASN A . n 
A 1 166 ILE 166 174 174 ILE ILE A . n 
A 1 167 ALA 167 175 175 ALA ALA A . n 
A 1 168 HIS 168 176 176 HIS HIS A . n 
A 1 169 GLN 169 177 177 GLN GLN A . n 
A 1 170 LEU 170 178 178 LEU LEU A . n 
A 1 171 ALA 171 179 179 ALA ALA A . n 
A 1 172 VAL 172 180 180 VAL VAL A . n 
A 1 173 ARG 173 181 181 ARG ARG A . n 
A 1 174 PHE 174 182 182 PHE PHE A . n 
A 1 175 GLY 175 183 183 GLY GLY A . n 
A 1 176 SER 176 184 184 SER SER A . n 
A 1 177 GLY 177 185 185 GLY GLY A . n 
A 1 178 SER 178 186 186 SER SER A . n 
A 1 179 ILE 179 187 187 ILE ILE A . n 
A 1 180 GLU 180 188 188 GLU GLU A . n 
A 1 181 LEU 181 189 189 LEU LEU A . n 
A 1 182 THR 182 190 190 THR THR A . n 
A 1 183 PRO 183 191 191 PRO PRO A . n 
A 1 184 VAL 184 192 192 VAL VAL A . n 
A 1 185 ARG 185 193 193 ARG ARG A . n 
A 1 186 VAL 186 194 194 VAL VAL A . n 
A 1 187 ARG 187 195 195 ARG ARG A . n 
A 1 188 GLY 188 196 196 GLY GLY A . n 
A 1 189 TYR 189 197 197 TYR TYR A . n 
A 1 190 VAL 190 198 198 VAL VAL A . n 
A 1 191 LEU 191 199 199 LEU LEU A . n 
A 1 192 MET 192 200 200 MET MET A . n 
A 1 193 GLY 193 201 201 GLY GLY A . n 
A 1 194 PRO 194 202 202 PRO PRO A . n 
A 1 195 PHE 195 203 203 PHE PHE A . n 
A 1 196 PHE 196 204 204 PHE PHE A . n 
A 1 197 GLY 197 205 205 GLY GLY A . n 
A 1 198 GLY 198 206 206 GLY GLY A . n 
A 1 199 GLU 199 207 207 GLU GLU A . n 
A 1 200 GLU 200 208 208 GLU GLU A . n 
A 1 201 ARG 201 209 209 ARG ARG A . n 
A 1 202 THR 202 210 210 THR THR A . n 
A 1 203 ASN 203 211 211 ASN ASN A . n 
A 1 204 SER 204 212 212 SER SER A . n 
A 1 205 GLU 205 213 213 GLU GLU A . n 
A 1 206 ASN 206 214 214 ASN ASN A . n 
A 1 207 GLY 207 215 215 GLY GLY A . n 
A 1 208 PRO 208 216 216 PRO PRO A . n 
A 1 209 SER 209 217 217 SER SER A . n 
A 1 210 GLU 210 218 218 GLU GLU A . n 
A 1 211 ALA 211 219 219 ALA ALA A . n 
A 1 212 LEU 212 220 220 LEU LEU A . n 
A 1 213 LEU 213 221 221 LEU LEU A . n 
A 1 214 SER 214 222 222 SER SER A . n 
A 1 215 LEU 215 223 223 LEU LEU A . n 
A 1 216 ASP 216 224 224 ASP ASP A . n 
A 1 217 LEU 217 225 225 LEU LEU A . n 
A 1 218 LEU 218 226 226 LEU LEU A . n 
A 1 219 ASP 219 227 227 ASP ASP A . n 
A 1 220 LYS 220 228 228 LYS LYS A . n 
A 1 221 PHE 221 229 229 PHE PHE A . n 
A 1 222 TRP 222 230 230 TRP TRP A . n 
A 1 223 ARG 223 231 231 ARG ARG A . n 
A 1 224 LEU 224 232 232 LEU LEU A . n 
A 1 225 SER 225 233 233 SER SER A . n 
A 1 226 LEU 226 234 234 LEU LEU A . n 
A 1 227 PRO 227 235 235 PRO PRO A . n 
A 1 228 ASN 228 236 236 ASN ASN A . n 
A 1 229 GLY 229 237 237 GLY GLY A . n 
A 1 230 ALA 230 238 238 ALA ALA A . n 
A 1 231 THR 231 239 239 THR THR A . n 
A 1 232 ARG 232 240 240 ARG ARG A . n 
A 1 233 ASP 233 241 241 ASP ASP A . n 
A 1 234 HIS 234 242 242 HIS HIS A . n 
A 1 235 HIS 235 243 243 HIS HIS A . n 
A 1 236 MET 236 244 244 MET MET A . n 
A 1 237 ALA 237 245 245 ALA ALA A . n 
A 1 238 ASN 238 246 246 ASN ASN A . n 
A 1 239 PRO 239 247 247 PRO PRO A . n 
A 1 240 PHE 240 248 248 PHE PHE A . n 
A 1 241 GLY 241 249 249 GLY GLY A . n 
A 1 242 PRO 242 250 250 PRO PRO A . n 
A 1 243 THR 243 251 251 THR THR A . n 
A 1 244 SER 244 252 252 SER SER A . n 
A 1 245 PRO 245 253 253 PRO PRO A . n 
A 1 246 THR 246 254 254 THR THR A . n 
A 1 247 LEU 247 255 255 LEU LEU A . n 
A 1 248 GLU 248 256 256 GLU GLU A . n 
A 1 249 SER 249 257 257 SER SER A . n 
A 1 250 ILE 250 258 258 ILE ILE A . n 
A 1 251 SER 251 259 259 SER SER A . n 
A 1 252 LEU 252 260 260 LEU LEU A . n 
A 1 253 GLU 253 261 261 GLU GLU A . n 
A 1 254 PRO 254 262 262 PRO PRO A . n 
A 1 255 MET 255 263 263 MET MET A . n 
A 1 256 LEU 256 264 264 LEU LEU A . n 
A 1 257 VAL 257 265 265 VAL VAL A . n 
A 1 258 ILE 258 266 266 ILE ILE A . n 
A 1 259 VAL 259 267 267 VAL VAL A . n 
A 1 260 GLY 260 268 268 GLY GLY A . n 
A 1 261 GLY 261 269 269 GLY GLY A . n 
A 1 262 SER 262 270 270 SER SER A . n 
A 1 263 GLN 263 271 271 GLN GLN A . n 
A 1 264 LEU 264 272 272 LEU LEU A . n 
A 1 265 LEU 265 273 273 LEU LEU A . n 
A 1 266 ARG 266 274 274 ARG ARG A . n 
A 1 267 ASP 267 275 275 ASP ASP A . n 
A 1 268 ARG 268 276 276 ARG ARG A . n 
A 1 269 ALA 269 277 277 ALA ALA A . n 
A 1 270 LYS 270 278 278 LYS LYS A . n 
A 1 271 GLU 271 279 279 GLU GLU A . n 
A 1 272 TYR 272 280 280 TYR TYR A . n 
A 1 273 ALA 273 281 281 ALA ALA A . n 
A 1 274 TYR 274 282 282 TYR TYR A . n 
A 1 275 LYS 275 283 283 LYS LYS A . n 
A 1 276 LEU 276 284 284 LEU LEU A . n 
A 1 277 LYS 277 285 285 LYS LYS A . n 
A 1 278 LYS 278 286 286 LYS LYS A . n 
A 1 279 MET 279 287 287 MET MET A . n 
A 1 280 GLY 280 288 288 GLY GLY A . n 
A 1 281 GLY 281 289 289 GLY GLY A . n 
A 1 282 LYS 282 290 290 LYS LYS A . n 
A 1 283 ARG 283 291 291 ARG ARG A . n 
A 1 284 VAL 284 292 292 VAL VAL A . n 
A 1 285 ASP 285 293 293 ASP ASP A . n 
A 1 286 TYR 286 294 294 TYR TYR A . n 
A 1 287 ILE 287 295 295 ILE ILE A . n 
A 1 288 GLU 288 296 296 GLU GLU A . n 
A 1 289 PHE 289 297 297 PHE PHE A . n 
A 1 290 GLU 290 298 298 GLU GLU A . n 
A 1 291 ASN 291 299 299 ASN ASN A . n 
A 1 292 LYS 292 300 300 LYS LYS A . n 
A 1 293 GLU 293 301 301 GLU GLU A . n 
A 1 294 HIS 294 302 302 HIS HIS A . n 
A 1 295 GLY 295 303 303 GLY GLY A . n 
A 1 296 PHE 296 304 304 PHE PHE A . n 
A 1 297 TYR 297 305 305 TYR TYR A . n 
A 1 298 SER 298 306 306 SER SER A . n 
A 1 299 ASN 299 307 307 ASN ASN A . n 
A 1 300 TYR 300 308 308 TYR TYR A . n 
A 1 301 PRO 301 309 309 PRO PRO A . n 
A 1 302 SER 302 310 310 SER SER A . n 
A 1 303 SER 303 311 311 SER SER A . n 
A 1 304 GLU 304 312 312 GLU GLU A . n 
A 1 305 ALA 305 313 313 ALA ALA A . n 
A 1 306 ALA 306 314 314 ALA ALA A . n 
A 1 307 GLU 307 315 315 GLU GLU A . n 
A 1 308 GLN 308 316 316 GLN GLN A . n 
A 1 309 VAL 309 317 317 VAL VAL A . n 
A 1 310 LEU 310 318 318 LEU LEU A . n 
A 1 311 ARG 311 319 319 ARG ARG A . n 
A 1 312 ILE 312 320 320 ILE ILE A . n 
A 1 313 ILE 313 321 321 ILE ILE A . n 
A 1 314 GLY 314 322 322 GLY GLY A . n 
A 1 315 ASP 315 323 323 ASP ASP A . n 
A 1 316 PHE 316 324 324 PHE PHE A . n 
A 1 317 MET 317 325 325 MET MET A . n 
A 1 318 ASN 318 326 326 ASN ASN A . n 
A 1 319 ASN 319 327 327 ASN ASN A . n 
A 1 320 LEU 320 328 328 LEU LEU A . n 
A 1 321 SER 321 329 329 SER SER A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        GOL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   GOL 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 GOL 1  401 401 GOL GOL A . 
C 3 HOH 1  501 11  HOH HOH A . 
C 3 HOH 2  502 7   HOH HOH A . 
C 3 HOH 3  503 2   HOH HOH A . 
C 3 HOH 4  504 19  HOH HOH A . 
C 3 HOH 5  505 10  HOH HOH A . 
C 3 HOH 6  506 1   HOH HOH A . 
C 3 HOH 7  507 4   HOH HOH A . 
C 3 HOH 8  508 3   HOH HOH A . 
C 3 HOH 9  509 6   HOH HOH A . 
C 3 HOH 10 510 9   HOH HOH A . 
C 3 HOH 11 511 18  HOH HOH A . 
C 3 HOH 12 512 12  HOH HOH A . 
C 3 HOH 13 513 5   HOH HOH A . 
C 3 HOH 14 514 15  HOH HOH A . 
C 3 HOH 15 515 16  HOH HOH A . 
C 3 HOH 16 516 20  HOH HOH A . 
C 3 HOH 17 517 8   HOH HOH A . 
C 3 HOH 18 518 17  HOH HOH A . 
C 3 HOH 19 519 14  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? v5.7 ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .    ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .    ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? BALBES ? ? ? .    ? 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                     8ZR6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.274 
_cell.length_a_esd                 ? 
_cell.length_b                     84.274 
_cell.length_b_esd                 ? 
_cell.length_c                     118.253 
_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                         8ZR6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 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                   8ZR6 
_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             2.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.01 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.26 M Sodium phosphate monobasic monohydrate, 0.14 M Potassium phosphate dibasic, pH 5.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-10-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.987 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZR6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.55 
_reflns.d_resolution_low                               48.45 
_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                                     14468 
_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                           99.89 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                20 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.03 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.55 
_reflns_shell.d_res_low                                     2.64 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.81 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1411 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.58 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.50 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.35 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.35 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.69 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               37.278 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 8ZR6 
_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                            2.55 
_refine.ls_d_res_low                             48.45 
_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                     14462 
_refine.ls_number_reflns_R_free                  1046 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 7.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20433 
_refine.ls_R_factor_R_free                       0.23598 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20181 
_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                    ? 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      AF-Q9FG13-F1 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.471 
_refine.pdbx_overall_ESU_R_Free                  0.269 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             20.336 
_refine.overall_SU_ML                            0.196 
_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                       2.55 
_refine_hist.d_res_low                        48.45 
_refine_hist.number_atoms_solvent             19 
_refine_hist.number_atoms_total               2554 
_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        2529 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         6 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          2.55 
_refine_ls_shell.d_res_low                           2.64 
_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                  99.50 
_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                     ? 
# 
_struct.entry_id                     8ZR6 
_struct.title                        'Arabidopsis Carboxyl esterase CXE15 E271Q mutant' 
_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        8ZR6 
_struct_keywords.text            'Strigolactone, catabolic enzyme, CXE15, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CXE15_ARATH 
_struct_ref.pdbx_db_accession          Q9FG13 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QVAEDCMGLLQLLSNGTVLRSESIDLITQQIPFKNNQTVLFKDSIYHKPNNLHLRLYKPISASNRTALPVVVFFHGGGFC
FGSRSWPHFHNFCLTLASSLNALVVSPDYRLAPEHRLPAAFEDAEAVLTWLWDQAVSDGVNHWFEDGTDVDFDRVFVVGD
SSGGNIAHQLAVRFGSGSIELTPVRVRGYVLMGPFFGGEERTNSENGPSEALLSLDLLDKFWRLSLPNGATRDHHMANPF
GPTSPTLESISLEPMLVIVGGSELLRDRAKEYAYKLKKMGGKRVDYIEFENKEHGFYSNYPSSEAAEQVLRIIGDFMNNL
S
;
_struct_ref.pdbx_align_begin           9 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8ZR6 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 321 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9FG13 
_struct_ref_seq.db_align_beg                  9 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  329 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       9 
_struct_ref_seq.pdbx_auth_seq_align_end       329 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             8ZR6 
_struct_ref_seq_dif.mon_id                       GLN 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      263 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q9FG13 
_struct_ref_seq_dif.db_mon_id                    GLU 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          271 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            271 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_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)' 6520  ? 
1 MORE         -44   ? 
1 'SSA (A^2)'  25140 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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' 7_556 y,x,-z+1 0.0000000000 1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 118.2530000000 
# 
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 GLN A 1   ? SER A 14  ? GLN A 9   SER A 22  1 ? 14 
HELX_P HELX_P2  AA2 ILE A 60  ? ASN A 64  ? ILE A 68  ASN A 72  1 ? 5  
HELX_P HELX_P3  AA3 TRP A 86  ? ASN A 101 ? TRP A 94  ASN A 109 1 ? 16 
HELX_P HELX_P4  AA4 PRO A 118 ? SER A 137 ? PRO A 126 SER A 145 1 ? 20 
HELX_P HELX_P5  AA5 ASP A 138 ? TRP A 143 ? ASP A 146 TRP A 151 5 ? 6  
HELX_P HELX_P6  AA6 SER A 161 ? SER A 176 ? SER A 169 SER A 184 1 ? 16 
HELX_P HELX_P7  AA7 THR A 202 ? GLY A 207 ? THR A 210 GLY A 215 1 ? 6  
HELX_P HELX_P8  AA8 SER A 214 ? LEU A 226 ? SER A 222 LEU A 234 1 ? 13 
HELX_P HELX_P9  AA9 LEU A 265 ? LYS A 278 ? LEU A 273 LYS A 286 1 ? 14 
HELX_P HELX_P10 AB1 GLY A 295 ? TYR A 300 ? GLY A 303 TYR A 308 1 ? 6  
HELX_P HELX_P11 AB2 SER A 303 ? SER A 321 ? SER A 311 SER A 329 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            6 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           A 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            6 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             14 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             14 
_struct_conn.ptnr2_symmetry                7_556 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.369 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       6 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      6 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        14 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       14 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          7_556 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 112 A . ? ALA 120 A PRO 113 A ? PRO 121 A 1 12.07 
2 LEU 117 A . ? LEU 125 A PRO 118 A ? PRO 126 A 1 28.10 
3 THR 182 A . ? THR 190 A PRO 183 A ? PRO 191 A 1 9.96  
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 39  ? HIS A 47  ? VAL A 47  HIS A 55  
AA1 2 LEU A 52  ? PRO A 59  ? LEU A 60  PRO A 67  
AA1 3 LEU A 103 ? PRO A 107 ? LEU A 111 PRO A 115 
AA1 4 LEU A 68  ? PHE A 74  ? LEU A 76  PHE A 82  
AA1 5 VAL A 150 ? ASP A 160 ? VAL A 158 ASP A 168 
AA1 6 VAL A 186 ? MET A 192 ? VAL A 194 MET A 200 
AA1 7 MET A 255 ? GLY A 260 ? MET A 263 GLY A 268 
AA1 8 VAL A 284 ? PHE A 289 ? VAL A 292 PHE A 297 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 40  ? N LEU A 48  O LYS A 58  ? O LYS A 66  
AA1 2 3 N ARG A 55  ? N ARG A 63  O SER A 106 ? O SER A 114 
AA1 3 4 O VAL A 105 ? O VAL A 113 N VAL A 71  ? N VAL A 79  
AA1 4 5 N VAL A 72  ? N VAL A 80  O PHE A 156 ? O PHE A 164 
AA1 5 6 N GLY A 159 ? N GLY A 167 O VAL A 190 ? O VAL A 198 
AA1 6 7 N LEU A 191 ? N LEU A 199 O LEU A 256 ? O LEU A 264 
AA1 7 8 N VAL A 257 ? N VAL A 265 O ASP A 285 ? O ASP A 293 
# 
_pdbx_entry_details.entry_id                   8ZR6 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLN A 37  ? ? -102.09 -168.19 
2 1 ARG A 162 ? ? -119.53 74.82   
3 1 SER A 169 ? ? 59.78   -120.76 
4 1 PRO A 253 ? ? -47.92  155.55  
5 1 LEU A 255 ? ? 78.77   -18.50  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 92  ? ? 0.166 'SIDE CHAIN' 
2 1 ARG A 118 ? ? 0.095 'SIDE CHAIN' 
3 1 ARG A 124 ? ? 0.245 'SIDE CHAIN' 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PHE N    N N N 264 
PHE CA   C N S 265 
PHE C    C N N 266 
PHE O    O N N 267 
PHE CB   C N N 268 
PHE CG   C Y N 269 
PHE CD1  C Y N 270 
PHE CD2  C Y N 271 
PHE CE1  C Y N 272 
PHE CE2  C Y N 273 
PHE CZ   C Y N 274 
PHE OXT  O N N 275 
PHE H    H N N 276 
PHE H2   H N N 277 
PHE HA   H N N 278 
PHE HB2  H N N 279 
PHE HB3  H N N 280 
PHE HD1  H N N 281 
PHE HD2  H N N 282 
PHE HE1  H N N 283 
PHE HE2  H N N 284 
PHE HZ   H N N 285 
PHE HXT  H N N 286 
PRO N    N N N 287 
PRO CA   C N S 288 
PRO C    C N N 289 
PRO O    O N N 290 
PRO CB   C N N 291 
PRO CG   C N N 292 
PRO CD   C N N 293 
PRO OXT  O N N 294 
PRO H    H N N 295 
PRO HA   H N N 296 
PRO HB2  H N N 297 
PRO HB3  H N N 298 
PRO HG2  H N N 299 
PRO HG3  H N N 300 
PRO HD2  H N N 301 
PRO HD3  H N N 302 
PRO HXT  H N N 303 
SER N    N N N 304 
SER CA   C N S 305 
SER C    C N N 306 
SER O    O N N 307 
SER CB   C N N 308 
SER OG   O N N 309 
SER OXT  O N N 310 
SER H    H N N 311 
SER H2   H N N 312 
SER HA   H N N 313 
SER HB2  H N N 314 
SER HB3  H N N 315 
SER HG   H N N 316 
SER HXT  H N N 317 
THR N    N N N 318 
THR CA   C N S 319 
THR C    C N N 320 
THR O    O N N 321 
THR CB   C N R 322 
THR OG1  O N N 323 
THR CG2  C N N 324 
THR OXT  O N N 325 
THR H    H N N 326 
THR H2   H N N 327 
THR HA   H N N 328 
THR HB   H N N 329 
THR HG1  H N N 330 
THR HG21 H N N 331 
THR HG22 H N N 332 
THR HG23 H N N 333 
THR HXT  H N N 334 
TRP N    N N N 335 
TRP CA   C N S 336 
TRP C    C N N 337 
TRP O    O N N 338 
TRP CB   C N N 339 
TRP CG   C Y N 340 
TRP CD1  C Y N 341 
TRP CD2  C Y N 342 
TRP NE1  N Y N 343 
TRP CE2  C Y N 344 
TRP CE3  C Y N 345 
TRP CZ2  C Y N 346 
TRP CZ3  C Y N 347 
TRP CH2  C Y N 348 
TRP OXT  O N N 349 
TRP H    H N N 350 
TRP H2   H N N 351 
TRP HA   H N N 352 
TRP HB2  H N N 353 
TRP HB3  H N N 354 
TRP HD1  H N N 355 
TRP HE1  H N N 356 
TRP HE3  H N N 357 
TRP HZ2  H N N 358 
TRP HZ3  H N N 359 
TRP HH2  H N N 360 
TRP HXT  H N N 361 
TYR N    N N N 362 
TYR CA   C N S 363 
TYR C    C N N 364 
TYR O    O N N 365 
TYR CB   C N N 366 
TYR CG   C Y N 367 
TYR CD1  C Y N 368 
TYR CD2  C Y N 369 
TYR CE1  C Y N 370 
TYR CE2  C Y N 371 
TYR CZ   C Y N 372 
TYR OH   O N N 373 
TYR OXT  O N N 374 
TYR H    H N N 375 
TYR H2   H N N 376 
TYR HA   H N N 377 
TYR HB2  H N N 378 
TYR HB3  H N N 379 
TYR HD1  H N N 380 
TYR HD2  H N N 381 
TYR HE1  H N N 382 
TYR HE2  H N N 383 
TYR HH   H N N 384 
TYR HXT  H N N 385 
VAL N    N N N 386 
VAL CA   C N S 387 
VAL C    C N N 388 
VAL O    O N N 389 
VAL CB   C N N 390 
VAL CG1  C N N 391 
VAL CG2  C N N 392 
VAL OXT  O N N 393 
VAL H    H N N 394 
VAL H2   H N N 395 
VAL HA   H N N 396 
VAL HB   H N N 397 
VAL HG11 H N N 398 
VAL HG12 H N N 399 
VAL HG13 H N N 400 
VAL HG21 H N N 401 
VAL HG22 H N N 402 
VAL HG23 H N N 403 
VAL HXT  H N N 404 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'Saudi Arabia' 
_pdbx_audit_support.grant_number           'King Abdullah University of Science and Technology' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-Q9FG13-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZR6 
_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]   0.011866 
_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]   0.011866 
_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]   0.008456 
_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 
H 
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   . GLN A 1 1   ? 50.073 47.458 65.101 1.00 60.58 ? 9   GLN A N   1 
ATOM   2    C CA  . GLN A 1 1   ? 50.061 46.129 65.720 1.00 66.11 ? 9   GLN A CA  1 
ATOM   3    C C   . GLN A 1 1   ? 48.677 45.480 65.684 1.00 69.97 ? 9   GLN A C   1 
ATOM   4    O O   . GLN A 1 1   ? 48.575 44.259 65.599 1.00 78.32 ? 9   GLN A O   1 
ATOM   5    C CB  . GLN A 1 1   ? 50.580 46.199 67.170 1.00 66.30 ? 9   GLN A CB  1 
ATOM   6    C CG  . GLN A 1 1   ? 49.645 46.900 68.153 1.00 71.62 ? 9   GLN A CG  1 
ATOM   7    C CD  . GLN A 1 1   ? 50.250 46.978 69.531 1.00 77.65 ? 9   GLN A CD  1 
ATOM   8    O OE1 . GLN A 1 1   ? 50.634 45.964 70.121 1.00 80.53 ? 9   GLN A OE1 1 
ATOM   9    N NE2 . GLN A 1 1   ? 50.356 48.182 70.078 1.00 74.68 ? 9   GLN A NE2 1 
ATOM   10   N N   . VAL A 1 2   ? 47.620 46.301 65.760 1.00 71.71 ? 10  VAL A N   1 
ATOM   11   C CA  . VAL A 1 2   ? 46.254 45.823 65.613 1.00 73.20 ? 10  VAL A CA  1 
ATOM   12   C C   . VAL A 1 2   ? 46.018 45.364 64.175 1.00 72.81 ? 10  VAL A C   1 
ATOM   13   O O   . VAL A 1 2   ? 45.329 44.372 63.944 1.00 73.21 ? 10  VAL A O   1 
ATOM   14   C CB  . VAL A 1 2   ? 45.222 46.899 66.032 1.00 65.65 ? 10  VAL A CB  1 
ATOM   15   C CG1 . VAL A 1 2   ? 43.791 46.429 65.773 1.00 59.91 ? 10  VAL A CG1 1 
ATOM   16   C CG2 . VAL A 1 2   ? 45.407 47.303 67.493 1.00 64.13 ? 10  VAL A CG2 1 
ATOM   17   N N   . ALA A 1 3   ? 46.594 46.106 63.221 1.00 75.42 ? 11  ALA A N   1 
ATOM   18   C CA  . ALA A 1 3   ? 46.535 45.760 61.810 1.00 68.39 ? 11  ALA A CA  1 
ATOM   19   C C   . ALA A 1 3   ? 47.347 44.506 61.492 1.00 64.57 ? 11  ALA A C   1 
ATOM   20   O O   . ALA A 1 3   ? 46.998 43.758 60.581 1.00 73.29 ? 11  ALA A O   1 
ATOM   21   C CB  . ALA A 1 3   ? 47.029 46.925 60.972 1.00 65.49 ? 11  ALA A CB  1 
ATOM   22   N N   . GLU A 1 4   ? 48.440 44.299 62.238 1.00 60.12 ? 12  GLU A N   1 
ATOM   23   C CA  . GLU A 1 4   ? 49.241 43.090 62.125 1.00 61.53 ? 12  GLU A CA  1 
ATOM   24   C C   . GLU A 1 4   ? 48.440 41.887 62.616 1.00 54.62 ? 12  GLU A C   1 
ATOM   25   O O   . GLU A 1 4   ? 48.393 40.859 61.944 1.00 51.24 ? 12  GLU A O   1 
ATOM   26   C CB  . GLU A 1 4   ? 50.555 43.230 62.921 1.00 72.13 ? 12  GLU A CB  1 
ATOM   27   C CG  . GLU A 1 4   ? 51.500 42.041 62.808 1.00 77.70 ? 12  GLU A CG  1 
ATOM   28   C CD  . GLU A 1 4   ? 52.820 42.179 63.546 1.00 81.75 ? 12  GLU A CD  1 
ATOM   29   O OE1 . GLU A 1 4   ? 53.022 43.219 64.213 1.00 81.36 ? 12  GLU A OE1 1 
ATOM   30   O OE2 . GLU A 1 4   ? 53.652 41.248 63.459 1.00 74.75 ? 12  GLU A OE2 1 
ATOM   31   N N   . ASP A 1 5   ? 47.818 42.033 63.794 1.00 56.71 ? 13  ASP A N   1 
ATOM   32   C CA  . ASP A 1 5   ? 47.003 40.981 64.383 1.00 60.51 ? 13  ASP A CA  1 
ATOM   33   C C   . ASP A 1 5   ? 45.765 40.662 63.546 1.00 62.76 ? 13  ASP A C   1 
ATOM   34   O O   . ASP A 1 5   ? 45.306 39.522 63.530 1.00 55.57 ? 13  ASP A O   1 
ATOM   35   C CB  . ASP A 1 5   ? 46.574 41.364 65.811 1.00 58.49 ? 13  ASP A CB  1 
ATOM   36   C CG  . ASP A 1 5   ? 47.692 41.341 66.833 1.00 52.99 ? 13  ASP A CG  1 
ATOM   37   O OD1 . ASP A 1 5   ? 48.400 40.316 66.915 1.00 49.10 ? 13  ASP A OD1 1 
ATOM   38   O OD2 . ASP A 1 5   ? 47.842 42.338 67.569 1.00 48.90 ? 13  ASP A OD2 1 
ATOM   39   N N   . CYS A 1 6   ? 45.233 41.684 62.863 1.00 73.41 ? 14  CYS A N   1 
ATOM   40   C CA  . CYS A 1 6   ? 44.107 41.520 61.957 1.00 76.80 ? 14  CYS A CA  1 
ATOM   41   C C   . CYS A 1 6   ? 44.465 40.609 60.784 1.00 67.86 ? 14  CYS A C   1 
ATOM   42   O O   . CYS A 1 6   ? 43.703 39.707 60.444 1.00 68.16 ? 14  CYS A O   1 
ATOM   43   C CB  . CYS A 1 6   ? 43.619 42.885 61.477 1.00 77.53 ? 14  CYS A CB  1 
ATOM   44   S SG  . CYS A 1 6   ? 42.287 42.813 60.251 1.00 70.23 ? 14  CYS A SG  1 
ATOM   45   N N   . MET A 1 7   ? 45.628 40.860 60.169 1.00 58.09 ? 15  MET A N   1 
ATOM   46   C CA  . MET A 1 7   ? 46.110 40.059 59.054 1.00 60.32 ? 15  MET A CA  1 
ATOM   47   C C   . MET A 1 7   ? 46.384 38.617 59.480 1.00 52.18 ? 15  MET A C   1 
ATOM   48   O O   . MET A 1 7   ? 46.127 37.685 58.720 1.00 57.63 ? 15  MET A O   1 
ATOM   49   C CB  . MET A 1 7   ? 47.393 40.682 58.477 1.00 64.07 ? 15  MET A CB  1 
ATOM   50   C CG  . MET A 1 7   ? 47.148 41.939 57.650 1.00 72.11 ? 15  MET A CG  1 
ATOM   51   S SD  . MET A 1 7   ? 46.159 41.691 56.148 1.00 86.57 ? 15  MET A SD  1 
ATOM   52   C CE  . MET A 1 7   ? 46.839 40.164 55.542 1.00 86.18 ? 15  MET A CE  1 
ATOM   53   N N   . GLY A 1 8   ? 46.912 38.450 60.698 1.00 40.49 ? 16  GLY A N   1 
ATOM   54   C CA  . GLY A 1 8   ? 47.186 37.138 61.259 1.00 37.61 ? 16  GLY A CA  1 
ATOM   55   C C   . GLY A 1 8   ? 45.925 36.363 61.631 1.00 38.12 ? 16  GLY A C   1 
ATOM   56   O O   . GLY A 1 8   ? 45.924 35.134 61.616 1.00 34.79 ? 16  GLY A O   1 
ATOM   57   N N   . LEU A 1 9   ? 44.861 37.099 61.978 1.00 45.41 ? 17  LEU A N   1 
ATOM   58   C CA  . LEU A 1 9   ? 43.575 36.502 62.297 1.00 41.74 ? 17  LEU A CA  1 
ATOM   59   C C   . LEU A 1 9   ? 42.987 35.842 61.051 1.00 36.48 ? 17  LEU A C   1 
ATOM   60   O O   . LEU A 1 9   ? 42.582 34.683 61.098 1.00 30.50 ? 17  LEU A O   1 
ATOM   61   C CB  . LEU A 1 9   ? 42.626 37.572 62.862 1.00 44.00 ? 17  LEU A CB  1 
ATOM   62   C CG  . LEU A 1 9   ? 41.243 37.098 63.303 1.00 51.13 ? 17  LEU A CG  1 
ATOM   63   C CD1 . LEU A 1 9   ? 41.335 36.056 64.401 1.00 54.82 ? 17  LEU A CD1 1 
ATOM   64   C CD2 . LEU A 1 9   ? 40.402 38.265 63.769 1.00 47.30 ? 17  LEU A CD2 1 
ATOM   65   N N   . LEU A 1 10  ? 42.966 36.592 59.942 1.00 34.64 ? 18  LEU A N   1 
ATOM   66   C CA  . LEU A 1 10  ? 42.529 36.078 58.653 1.00 37.40 ? 18  LEU A CA  1 
ATOM   67   C C   . LEU A 1 10  ? 43.244 34.785 58.266 1.00 37.92 ? 18  LEU A C   1 
ATOM   68   O O   . LEU A 1 10  ? 42.599 33.824 57.851 1.00 33.32 ? 18  LEU A O   1 
ATOM   69   C CB  . LEU A 1 10  ? 42.751 37.131 57.554 1.00 41.81 ? 18  LEU A CB  1 
ATOM   70   C CG  . LEU A 1 10  ? 41.543 37.995 57.209 1.00 48.07 ? 18  LEU A CG  1 
ATOM   71   C CD1 . LEU A 1 10  ? 41.027 38.748 58.415 1.00 44.80 ? 18  LEU A CD1 1 
ATOM   72   C CD2 . LEU A 1 10  ? 41.884 38.966 56.094 1.00 55.13 ? 18  LEU A CD2 1 
ATOM   73   N N   . GLN A 1 11  ? 44.576 34.778 58.402 1.00 35.49 ? 19  GLN A N   1 
ATOM   74   C CA  . GLN A 1 11  ? 45.376 33.610 58.071 1.00 34.18 ? 19  GLN A CA  1 
ATOM   75   C C   . GLN A 1 11  ? 45.008 32.424 58.957 1.00 31.71 ? 19  GLN A C   1 
ATOM   76   O O   . GLN A 1 11  ? 44.707 31.345 58.453 1.00 35.99 ? 19  GLN A O   1 
ATOM   77   C CB  . GLN A 1 11  ? 46.872 33.929 58.192 1.00 37.15 ? 19  GLN A CB  1 
ATOM   78   C CG  . GLN A 1 11  ? 47.355 34.889 57.115 1.00 47.47 ? 19  GLN A CG  1 
ATOM   79   C CD  . GLN A 1 11  ? 48.828 35.201 57.221 1.00 55.04 ? 19  GLN A CD  1 
ATOM   80   O OE1 . GLN A 1 11  ? 49.538 34.708 58.106 1.00 64.74 ? 19  GLN A OE1 1 
ATOM   81   N NE2 . GLN A 1 11  ? 49.320 36.031 56.312 1.00 55.32 ? 19  GLN A NE2 1 
ATOM   82   N N   . LEU A 1 12  ? 45.020 32.647 60.276 1.00 32.08 ? 20  LEU A N   1 
ATOM   83   C CA  . LEU A 1 12  ? 44.692 31.618 61.251 1.00 35.04 ? 20  LEU A CA  1 
ATOM   84   C C   . LEU A 1 12  ? 43.274 31.069 61.097 1.00 32.82 ? 20  LEU A C   1 
ATOM   85   O O   . LEU A 1 12  ? 43.055 29.868 61.245 1.00 30.34 ? 20  LEU A O   1 
ATOM   86   C CB  . LEU A 1 12  ? 44.859 32.191 62.670 1.00 35.82 ? 20  LEU A CB  1 
ATOM   87   C CG  . LEU A 1 12  ? 46.289 32.281 63.181 1.00 33.32 ? 20  LEU A CG  1 
ATOM   88   C CD1 . LEU A 1 12  ? 46.371 33.152 64.417 1.00 31.00 ? 20  LEU A CD1 1 
ATOM   89   C CD2 . LEU A 1 12  ? 46.848 30.901 63.484 1.00 31.39 ? 20  LEU A CD2 1 
ATOM   90   N N   . LEU A 1 13  ? 42.321 31.962 60.808 1.00 34.61 ? 21  LEU A N   1 
ATOM   91   C CA  . LEU A 1 13  ? 40.913 31.606 60.740 1.00 34.63 ? 21  LEU A CA  1 
ATOM   92   C C   . LEU A 1 13  ? 40.621 30.587 59.639 1.00 31.25 ? 21  LEU A C   1 
ATOM   93   O O   . LEU A 1 13  ? 39.900 29.618 59.868 1.00 30.22 ? 21  LEU A O   1 
ATOM   94   C CB  . LEU A 1 13  ? 40.083 32.880 60.513 1.00 34.92 ? 21  LEU A CB  1 
ATOM   95   C CG  . LEU A 1 13  ? 38.577 32.704 60.440 1.00 41.49 ? 21  LEU A CG  1 
ATOM   96   C CD1 . LEU A 1 13  ? 38.002 32.330 61.792 1.00 47.00 ? 21  LEU A CD1 1 
ATOM   97   C CD2 . LEU A 1 13  ? 37.916 33.964 59.921 1.00 45.84 ? 21  LEU A CD2 1 
ATOM   98   N N   . SER A 1 14  ? 41.198 30.811 58.453 1.00 29.59 ? 22  SER A N   1 
ATOM   99   C CA  . SER A 1 14  ? 40.920 29.986 57.287 1.00 29.44 ? 22  SER A CA  1 
ATOM   100  C C   . SER A 1 14  ? 41.983 28.920 57.026 1.00 29.21 ? 22  SER A C   1 
ATOM   101  O O   . SER A 1 14  ? 42.043 28.361 55.933 1.00 24.34 ? 22  SER A O   1 
ATOM   102  C CB  . SER A 1 14  ? 40.770 30.872 56.056 1.00 24.90 ? 22  SER A CB  1 
ATOM   103  O OG  . SER A 1 14  ? 39.689 31.769 56.231 1.00 23.50 ? 22  SER A OG  1 
ATOM   104  N N   . ASN A 1 15  ? 42.799 28.625 58.045 1.00 33.66 ? 23  ASN A N   1 
ATOM   105  C CA  . ASN A 1 15  ? 43.929 27.725 57.890 1.00 40.68 ? 23  ASN A CA  1 
ATOM   106  C C   . ASN A 1 15  ? 43.508 26.257 57.936 1.00 37.72 ? 23  ASN A C   1 
ATOM   107  O O   . ASN A 1 15  ? 44.038 25.439 57.188 1.00 38.40 ? 23  ASN A O   1 
ATOM   108  C CB  . ASN A 1 15  ? 44.981 28.019 58.959 1.00 42.17 ? 23  ASN A CB  1 
ATOM   109  C CG  . ASN A 1 15  ? 46.331 27.455 58.618 1.00 45.45 ? 23  ASN A CG  1 
ATOM   110  O OD1 . ASN A 1 15  ? 47.209 28.162 58.113 1.00 41.14 ? 23  ASN A OD1 1 
ATOM   111  N ND2 . ASN A 1 15  ? 46.519 26.164 58.854 1.00 47.29 ? 23  ASN A ND2 1 
ATOM   112  N N   . GLY A 1 16  ? 42.561 25.933 58.825 1.00 35.89 ? 24  GLY A N   1 
ATOM   113  C CA  . GLY A 1 16  ? 42.041 24.580 58.943 1.00 34.99 ? 24  GLY A CA  1 
ATOM   114  C C   . GLY A 1 16  ? 43.037 23.608 59.573 1.00 36.21 ? 24  GLY A C   1 
ATOM   115  O O   . GLY A 1 16  ? 44.093 24.020 60.051 1.00 42.62 ? 24  GLY A O   1 
ATOM   116  N N   . THR A 1 17  ? 42.681 22.318 59.560 1.00 31.39 ? 25  THR A N   1 
ATOM   117  C CA  . THR A 1 17  ? 43.485 21.266 60.163 1.00 29.46 ? 25  THR A CA  1 
ATOM   118  C C   . THR A 1 17  ? 43.604 20.100 59.189 1.00 25.04 ? 25  THR A C   1 
ATOM   119  O O   . THR A 1 17  ? 42.803 19.980 58.267 1.00 24.61 ? 25  THR A O   1 
ATOM   120  C CB  . THR A 1 17  ? 42.869 20.810 61.493 1.00 31.27 ? 25  THR A CB  1 
ATOM   121  O OG1 . THR A 1 17  ? 42.506 21.961 62.245 1.00 46.51 ? 25  THR A OG1 1 
ATOM   122  C CG2 . THR A 1 17  ? 43.810 19.946 62.317 1.00 30.36 ? 25  THR A CG2 1 
ATOM   123  N N   . VAL A 1 18  ? 44.617 19.255 59.408 1.00 23.94 ? 26  VAL A N   1 
ATOM   124  C CA  . VAL A 1 18  ? 44.858 18.085 58.583 1.00 24.86 ? 26  VAL A CA  1 
ATOM   125  C C   . VAL A 1 18  ? 44.652 16.822 59.415 1.00 30.22 ? 26  VAL A C   1 
ATOM   126  O O   . VAL A 1 18  ? 45.319 16.634 60.429 1.00 34.87 ? 26  VAL A O   1 
ATOM   127  C CB  . VAL A 1 18  ? 46.279 18.136 57.987 1.00 21.67 ? 26  VAL A CB  1 
ATOM   128  C CG1 . VAL A 1 18  ? 46.603 16.862 57.212 1.00 20.22 ? 26  VAL A CG1 1 
ATOM   129  C CG2 . VAL A 1 18  ? 46.466 19.377 57.117 1.00 20.70 ? 26  VAL A CG2 1 
ATOM   130  N N   . LEU A 1 19  ? 43.722 15.967 58.972 1.00 34.10 ? 27  LEU A N   1 
ATOM   131  C CA  . LEU A 1 19  ? 43.487 14.683 59.610 1.00 30.20 ? 27  LEU A CA  1 
ATOM   132  C C   . LEU A 1 19  ? 44.672 13.753 59.380 1.00 31.27 ? 27  LEU A C   1 
ATOM   133  O O   . LEU A 1 19  ? 45.034 13.478 58.238 1.00 33.78 ? 27  LEU A O   1 
ATOM   134  C CB  . LEU A 1 19  ? 42.221 14.021 59.061 1.00 29.43 ? 27  LEU A CB  1 
ATOM   135  C CG  . LEU A 1 19  ? 40.896 14.688 59.415 1.00 31.88 ? 27  LEU A CG  1 
ATOM   136  C CD1 . LEU A 1 19  ? 39.736 13.792 59.037 1.00 34.99 ? 27  LEU A CD1 1 
ATOM   137  C CD2 . LEU A 1 19  ? 40.830 15.057 60.897 1.00 29.77 ? 27  LEU A CD2 1 
ATOM   138  N N   . ARG A 1 20  ? 45.260 13.276 60.483 1.00 35.66 ? 28  ARG A N   1 
ATOM   139  C CA  . ARG A 1 20  ? 46.360 12.328 60.431 1.00 46.98 ? 28  ARG A CA  1 
ATOM   140  C C   . ARG A 1 20  ? 45.911 10.974 59.885 1.00 43.82 ? 28  ARG A C   1 
ATOM   141  O O   . ARG A 1 20  ? 46.670 10.311 59.180 1.00 46.80 ? 28  ARG A O   1 
ATOM   142  C CB  . ARG A 1 20  ? 46.971 12.151 61.833 1.00 58.75 ? 28  ARG A CB  1 
ATOM   143  C CG  . ARG A 1 20  ? 47.679 13.391 62.373 1.00 68.94 ? 28  ARG A CG  1 
ATOM   144  C CD  . ARG A 1 20  ? 48.985 13.672 61.650 1.00 80.29 ? 28  ARG A CD  1 
ATOM   145  N NE  . ARG A 1 20  ? 49.735 14.752 62.285 1.00 89.38 ? 28  ARG A NE  1 
ATOM   146  C CZ  . ARG A 1 20  ? 50.025 15.915 61.713 1.00 90.10 ? 28  ARG A CZ  1 
ATOM   147  N NH1 . ARG A 1 20  ? 49.595 16.217 60.499 1.00 86.64 ? 28  ARG A NH1 1 
ATOM   148  N NH2 . ARG A 1 20  ? 50.761 16.801 62.380 1.00 86.96 ? 28  ARG A NH2 1 
ATOM   149  N N   . SER A 1 21  ? 44.673 10.582 60.213 1.00 37.44 ? 29  SER A N   1 
ATOM   150  C CA  . SER A 1 21  ? 44.143 9.275  59.854 1.00 33.63 ? 29  SER A CA  1 
ATOM   151  C C   . SER A 1 21  ? 42.758 9.375  59.219 1.00 27.23 ? 29  SER A C   1 
ATOM   152  O O   . SER A 1 21  ? 42.130 10.430 59.259 1.00 26.15 ? 29  SER A O   1 
ATOM   153  C CB  . SER A 1 21  ? 44.088 8.387  61.095 1.00 34.57 ? 29  SER A CB  1 
ATOM   154  O OG  . SER A 1 21  ? 43.627 7.080  60.794 1.00 38.26 ? 29  SER A OG  1 
ATOM   155  N N   . GLU A 1 22  ? 42.297 8.262  58.631 1.00 25.19 ? 30  GLU A N   1 
ATOM   156  C CA  . GLU A 1 22  ? 40.928 8.138  58.156 1.00 24.01 ? 30  GLU A CA  1 
ATOM   157  C C   . GLU A 1 22  ? 39.923 8.405  59.270 1.00 28.86 ? 30  GLU A C   1 
ATOM   158  O O   . GLU A 1 22  ? 40.189 8.108  60.433 1.00 32.84 ? 30  GLU A O   1 
ATOM   159  C CB  . GLU A 1 22  ? 40.633 6.733  57.640 1.00 22.98 ? 30  GLU A CB  1 
ATOM   160  C CG  . GLU A 1 22  ? 41.330 6.367  56.356 1.00 25.69 ? 30  GLU A CG  1 
ATOM   161  C CD  . GLU A 1 22  ? 40.972 4.985  55.855 1.00 24.08 ? 30  GLU A CD  1 
ATOM   162  O OE1 . GLU A 1 22  ? 40.076 4.338  56.443 1.00 23.04 ? 30  GLU A OE1 1 
ATOM   163  O OE2 . GLU A 1 22  ? 41.604 4.540  54.874 1.00 26.07 ? 30  GLU A OE2 1 
ATOM   164  N N   . SER A 1 23  ? 38.757 8.935  58.884 1.00 28.89 ? 31  SER A N   1 
ATOM   165  C CA  . SER A 1 23  ? 37.650 9.135  59.801 1.00 27.66 ? 31  SER A CA  1 
ATOM   166  C C   . SER A 1 23  ? 36.335 8.764  59.126 1.00 26.99 ? 31  SER A C   1 
ATOM   167  O O   . SER A 1 23  ? 36.228 8.817  57.904 1.00 26.03 ? 31  SER A O   1 
ATOM   168  C CB  . SER A 1 23  ? 37.608 10.578 60.280 1.00 30.63 ? 31  SER A CB  1 
ATOM   169  O OG  . SER A 1 23  ? 38.860 10.961 60.821 1.00 37.57 ? 31  SER A OG  1 
ATOM   170  N N   . ILE A 1 24  ? 35.350 8.371  59.941 1.00 27.84 ? 32  ILE A N   1 
ATOM   171  C CA  . ILE A 1 24  ? 34.000 8.115  59.473 1.00 25.47 ? 32  ILE A CA  1 
ATOM   172  C C   . ILE A 1 24  ? 33.068 9.093  60.181 1.00 24.78 ? 32  ILE A C   1 
ATOM   173  O O   . ILE A 1 24  ? 33.226 9.348  61.372 1.00 31.62 ? 32  ILE A O   1 
ATOM   174  C CB  . ILE A 1 24  ? 33.575 6.641  59.709 1.00 25.14 ? 32  ILE A CB  1 
ATOM   175  C CG1 . ILE A 1 24  ? 34.555 5.674  59.053 1.00 27.30 ? 32  ILE A CG1 1 
ATOM   176  C CG2 . ILE A 1 24  ? 32.150 6.373  59.222 1.00 27.24 ? 32  ILE A CG2 1 
ATOM   177  C CD1 . ILE A 1 24  ? 34.112 4.207  59.073 1.00 30.40 ? 32  ILE A CD1 1 
ATOM   178  N N   . ASP A 1 25  ? 32.118 9.652  59.425 1.00 24.92 ? 33  ASP A N   1 
ATOM   179  C CA  . ASP A 1 25  ? 30.996 10.377 59.998 1.00 24.15 ? 33  ASP A CA  1 
ATOM   180  C C   . ASP A 1 25  ? 29.683 9.709  59.605 1.00 22.98 ? 33  ASP A C   1 
ATOM   181  O O   . ASP A 1 25  ? 29.629 8.940  58.647 1.00 17.71 ? 33  ASP A O   1 
ATOM   182  C CB  . ASP A 1 25  ? 30.988 11.852 59.570 1.00 26.69 ? 33  ASP A CB  1 
ATOM   183  C CG  . ASP A 1 25  ? 31.507 12.801 60.627 1.00 33.46 ? 33  ASP A CG  1 
ATOM   184  O OD1 . ASP A 1 25  ? 31.020 12.728 61.778 1.00 41.12 ? 33  ASP A OD1 1 
ATOM   185  O OD2 . ASP A 1 25  ? 32.379 13.637 60.301 1.00 34.58 ? 33  ASP A OD2 1 
ATOM   186  N N   . LEU A 1 26  ? 28.633 10.019 60.371 1.00 23.74 ? 34  LEU A N   1 
ATOM   187  C CA  . LEU A 1 26  ? 27.309 9.470  60.140 1.00 24.03 ? 34  LEU A CA  1 
ATOM   188  C C   . LEU A 1 26  ? 26.398 10.621 59.725 1.00 23.01 ? 34  LEU A C   1 
ATOM   189  O O   . LEU A 1 26  ? 26.269 11.596 60.458 1.00 24.84 ? 34  LEU A O   1 
ATOM   190  C CB  . LEU A 1 26  ? 26.824 8.774  61.417 1.00 24.26 ? 34  LEU A CB  1 
ATOM   191  C CG  . LEU A 1 26  ? 25.639 7.837  61.272 1.00 25.57 ? 34  LEU A CG  1 
ATOM   192  C CD1 . LEU A 1 26  ? 25.989 6.610  60.456 1.00 24.37 ? 34  LEU A CD1 1 
ATOM   193  C CD2 . LEU A 1 26  ? 25.134 7.413  62.627 1.00 26.85 ? 34  LEU A CD2 1 
ATOM   194  N N   . ILE A 1 27  ? 25.834 10.509 58.525 1.00 26.54 ? 35  ILE A N   1 
ATOM   195  C CA  . ILE A 1 27  ? 25.008 11.607 57.954 1.00 32.75 ? 35  ILE A CA  1 
ATOM   196  C C   . ILE A 1 27  ? 23.554 11.137 57.786 1.00 38.08 ? 35  ILE A C   1 
ATOM   197  O O   . ILE A 1 27  ? 23.351 9.994  57.349 1.00 39.30 ? 35  ILE A O   1 
ATOM   198  C CB  . ILE A 1 27  ? 25.639 12.059 56.623 1.00 34.13 ? 35  ILE A CB  1 
ATOM   199  C CG1 . ILE A 1 27  ? 25.664 10.938 55.588 1.00 40.77 ? 35  ILE A CG1 1 
ATOM   200  C CG2 . ILE A 1 27  ? 27.029 12.655 56.845 1.00 34.30 ? 35  ILE A CG2 1 
ATOM   201  C CD1 . ILE A 1 27  ? 24.550 11.026 54.562 1.00 39.41 ? 35  ILE A CD1 1 
ATOM   202  N N   . THR A 1 28  ? 22.587 11.989 58.136 1.00 51.04 ? 36  THR A N   1 
ATOM   203  C CA  . THR A 1 28  ? 21.149 11.655 58.006 1.00 59.95 ? 36  THR A CA  1 
ATOM   204  C C   . THR A 1 28  ? 20.711 11.873 56.579 1.00 55.09 ? 36  THR A C   1 
ATOM   205  O O   . THR A 1 28  ? 21.150 12.862 55.973 1.00 56.81 ? 36  THR A O   1 
ATOM   206  C CB  . THR A 1 28  ? 20.345 12.508 58.983 1.00 67.08 ? 36  THR A CB  1 
ATOM   207  O OG1 . THR A 1 28  ? 20.798 12.096 60.268 1.00 68.93 ? 36  THR A OG1 1 
ATOM   208  C CG2 . THR A 1 28  ? 18.848 12.293 58.863 1.00 70.33 ? 36  THR A CG2 1 
ATOM   209  N N   . GLN A 1 29  ? 19.855 11.001 56.059 1.00 57.40 ? 37  GLN A N   1 
ATOM   210  C CA  . GLN A 1 29  ? 19.480 11.091 54.628 1.00 64.94 ? 37  GLN A CA  1 
ATOM   211  C C   . GLN A 1 29  ? 18.103 11.728 54.427 1.00 68.28 ? 37  GLN A C   1 
ATOM   212  O O   . GLN A 1 29  ? 17.547 12.276 55.395 1.00 65.70 ? 37  GLN A O   1 
ATOM   213  C CB  . GLN A 1 29  ? 19.483 9.697  54.009 1.00 76.00 ? 37  GLN A CB  1 
ATOM   214  C CG  . GLN A 1 29  ? 20.751 9.383  53.223 1.00 87.05 ? 37  GLN A CG  1 
ATOM   215  C CD  . GLN A 1 29  ? 21.157 10.497 52.283 1.00 95.98 ? 37  GLN A CD  1 
ATOM   216  O OE1 . GLN A 1 29  ? 22.119 11.232 52.530 1.00 85.63 ? 37  GLN A OE1 1 
ATOM   217  N NE2 . GLN A 1 29  ? 20.421 10.631 51.189 1.00 98.38 ? 37  GLN A NE2 1 
ATOM   218  N N   . GLN A 1 30  ? 17.575 11.633 53.208 1.00 73.88 ? 38  GLN A N   1 
ATOM   219  C CA  . GLN A 1 30  ? 16.282 12.270 52.854 1.00 79.26 ? 38  GLN A CA  1 
ATOM   220  C C   . GLN A 1 30  ? 15.137 11.875 53.793 1.00 88.21 ? 38  GLN A C   1 
ATOM   221  O O   . GLN A 1 30  ? 15.005 10.672 54.095 1.00 90.91 ? 38  GLN A O   1 
ATOM   222  C CB  . GLN A 1 30  ? 15.917 11.817 51.445 1.00 74.15 ? 38  GLN A CB  1 
ATOM   223  C CG  . GLN A 1 30  ? 16.855 12.345 50.365 1.00 69.86 ? 38  GLN A CG  1 
ATOM   224  C CD  . GLN A 1 30  ? 16.527 11.831 48.980 1.00 64.31 ? 38  GLN A CD  1 
ATOM   225  O OE1 . GLN A 1 30  ? 15.927 10.764 48.816 1.00 64.34 ? 38  GLN A OE1 1 
ATOM   226  N NE2 . GLN A 1 30  ? 16.914 12.591 47.966 1.00 57.20 ? 38  GLN A NE2 1 
ATOM   227  N N   . ILE A 1 31  ? 14.334 12.855 54.216 1.00 92.80 ? 39  ILE A N   1 
ATOM   228  C CA  . ILE A 1 31  ? 13.131 12.573 55.057 1.00 87.09 ? 39  ILE A CA  1 
ATOM   229  C C   . ILE A 1 31  ? 11.905 12.945 54.213 1.00 73.14 ? 39  ILE A C   1 
ATOM   230  O O   . ILE A 1 31  ? 11.602 14.146 54.116 1.00 59.27 ? 39  ILE A O   1 
ATOM   231  C CB  . ILE A 1 31  ? 13.175 13.363 56.376 1.00 91.59 ? 39  ILE A CB  1 
ATOM   232  C CG1 . ILE A 1 31  ? 14.439 13.065 57.175 1.00 91.75 ? 39  ILE A CG1 1 
ATOM   233  C CG2 . ILE A 1 31  ? 11.912 13.110 57.198 1.00 87.36 ? 39  ILE A CG2 1 
ATOM   234  C CD1 . ILE A 1 31  ? 14.605 11.601 57.540 1.00 91.57 ? 39  ILE A CD1 1 
ATOM   235  N N   . PRO A 1 32  ? 11.206 11.977 53.588 1.00 72.92 ? 40  PRO A N   1 
ATOM   236  C CA  . PRO A 1 32  ? 10.071 12.264 52.659 1.00 70.06 ? 40  PRO A CA  1 
ATOM   237  C C   . PRO A 1 32  ? 9.010  13.141 53.310 1.00 70.13 ? 40  PRO A C   1 
ATOM   238  O O   . PRO A 1 32  ? 8.698  14.218 52.759 1.00 76.01 ? 40  PRO A O   1 
ATOM   239  C CB  . PRO A 1 32  ? 9.541  10.884 52.300 1.00 63.20 ? 40  PRO A CB  1 
ATOM   240  C CG  . PRO A 1 32  ? 10.753 9.990  52.466 1.00 66.67 ? 40  PRO A CG  1 
ATOM   241  C CD  . PRO A 1 32  ? 11.439 10.504 53.686 1.00 71.23 ? 40  PRO A CD  1 
ATOM   242  N N   . PHE A 1 33  ? 8.448  12.697 54.431 1.00 60.91 ? 41  PHE A N   1 
ATOM   243  C CA  . PHE A 1 33  ? 7.329  13.462 55.045 1.00 56.42 ? 41  PHE A CA  1 
ATOM   244  C C   . PHE A 1 33  ? 7.863  14.176 56.275 1.00 55.94 ? 41  PHE A C   1 
ATOM   245  O O   . PHE A 1 33  ? 7.955  13.566 57.359 1.00 54.41 ? 41  PHE A O   1 
ATOM   246  C CB  . PHE A 1 33  ? 6.150  12.516 55.302 1.00 49.38 ? 41  PHE A CB  1 
ATOM   247  C CG  . PHE A 1 33  ? 5.383  12.126 54.048 1.00 41.36 ? 41  PHE A CG  1 
ATOM   248  C CD1 . PHE A 1 33  ? 5.866  11.143 53.195 1.00 38.20 ? 41  PHE A CD1 1 
ATOM   249  C CD2 . PHE A 1 33  ? 4.187  12.752 53.725 1.00 39.31 ? 41  PHE A CD2 1 
ATOM   250  C CE1 . PHE A 1 33  ? 5.170  10.798 52.050 1.00 38.86 ? 41  PHE A CE1 1 
ATOM   251  C CE2 . PHE A 1 33  ? 3.493  12.400 52.581 1.00 38.61 ? 41  PHE A CE2 1 
ATOM   252  C CZ  . PHE A 1 33  ? 3.986  11.426 51.748 1.00 41.38 ? 41  PHE A CZ  1 
ATOM   253  N N   . LYS A 1 34  ? 8.182  15.458 56.122 1.00 58.26 ? 42  LYS A N   1 
ATOM   254  C CA  . LYS A 1 34  ? 8.823  16.176 57.248 1.00 64.14 ? 42  LYS A CA  1 
ATOM   255  C C   . LYS A 1 34  ? 7.798  16.929 58.093 1.00 56.88 ? 42  LYS A C   1 
ATOM   256  O O   . LYS A 1 34  ? 6.801  17.408 57.529 1.00 66.15 ? 42  LYS A O   1 
ATOM   257  C CB  . LYS A 1 34  ? 9.907  17.109 56.699 1.00 80.62 ? 42  LYS A CB  1 
ATOM   258  C CG  . LYS A 1 34  ? 11.320 16.583 56.894 1.00 89.69 ? 42  LYS A CG  1 
ATOM   259  C CD  . LYS A 1 34  ? 12.407 17.477 56.312 1.00 94.09 ? 42  LYS A CD  1 
ATOM   260  C CE  . LYS A 1 34  ? 12.609 17.256 54.849 1.00 92.50 ? 42  LYS A CE  1 
ATOM   261  N NZ  . LYS A 1 34  ? 12.244 18.443 54.072 1.00 94.72 ? 42  LYS A NZ  1 
ATOM   262  N N   . ASN A 1 35  ? 8.060  17.036 59.390 1.00 54.01 ? 43  ASN A N   1 
ATOM   263  C CA  . ASN A 1 35  ? 7.209  17.752 60.327 1.00 49.50 ? 43  ASN A CA  1 
ATOM   264  C C   . ASN A 1 35  ? 7.631  19.219 60.345 1.00 44.98 ? 43  ASN A C   1 
ATOM   265  O O   . ASN A 1 35  ? 8.822  19.515 60.303 1.00 42.06 ? 43  ASN A O   1 
ATOM   266  C CB  . ASN A 1 35  ? 7.289  17.135 61.724 1.00 47.03 ? 43  ASN A CB  1 
ATOM   267  C CG  . ASN A 1 35  ? 6.410  15.919 61.887 1.00 43.83 ? 43  ASN A CG  1 
ATOM   268  O OD1 . ASN A 1 35  ? 6.310  15.067 60.997 1.00 40.42 ? 43  ASN A OD1 1 
ATOM   269  N ND2 . ASN A 1 35  ? 5.731  15.826 63.020 1.00 42.45 ? 43  ASN A ND2 1 
ATOM   270  N N   . ASN A 1 36  ? 6.647  20.126 60.409 1.00 51.26 ? 44  ASN A N   1 
ATOM   271  C CA  . ASN A 1 36  ? 6.884  21.549 60.215 1.00 50.73 ? 44  ASN A CA  1 
ATOM   272  C C   . ASN A 1 36  ? 6.366  22.432 61.346 1.00 49.90 ? 44  ASN A C   1 
ATOM   273  O O   . ASN A 1 36  ? 5.475  22.044 62.098 1.00 53.48 ? 44  ASN A O   1 
ATOM   274  C CB  . ASN A 1 36  ? 6.240  22.018 58.904 1.00 53.62 ? 44  ASN A CB  1 
ATOM   275  C CG  . ASN A 1 36  ? 6.981  21.591 57.666 1.00 62.50 ? 44  ASN A CG  1 
ATOM   276  O OD1 . ASN A 1 36  ? 8.104  21.079 57.717 1.00 79.25 ? 44  ASN A OD1 1 
ATOM   277  N ND2 . ASN A 1 36  ? 6.366  21.810 56.516 1.00 65.47 ? 44  ASN A ND2 1 
ATOM   278  N N   . GLN A 1 37  ? 6.953  23.631 61.428 1.00 42.86 ? 45  GLN A N   1 
ATOM   279  C CA  . GLN A 1 37  ? 6.516  24.696 62.315 1.00 37.01 ? 45  GLN A CA  1 
ATOM   280  C C   . GLN A 1 37  ? 6.916  26.028 61.688 1.00 32.63 ? 45  GLN A C   1 
ATOM   281  O O   . GLN A 1 37  ? 7.977  26.124 61.072 1.00 30.80 ? 45  GLN A O   1 
ATOM   282  C CB  . GLN A 1 37  ? 7.164  24.591 63.709 1.00 40.42 ? 45  GLN A CB  1 
ATOM   283  C CG  . GLN A 1 37  ? 6.400  23.746 64.712 1.00 44.71 ? 45  GLN A CG  1 
ATOM   284  C CD  . GLN A 1 37  ? 6.914  23.962 66.119 1.00 55.34 ? 45  GLN A CD  1 
ATOM   285  O OE1 . GLN A 1 37  ? 7.051  25.097 66.593 1.00 57.45 ? 45  GLN A OE1 1 
ATOM   286  N NE2 . GLN A 1 37  ? 7.217  22.884 66.826 1.00 64.38 ? 45  GLN A NE2 1 
ATOM   287  N N   . THR A 1 38  ? 6.070  27.050 61.868 1.00 24.87 ? 46  THR A N   1 
ATOM   288  C CA  . THR A 1 38  ? 6.414  28.409 61.486 1.00 23.06 ? 46  THR A CA  1 
ATOM   289  C C   . THR A 1 38  ? 6.942  29.189 62.688 1.00 22.01 ? 46  THR A C   1 
ATOM   290  O O   . THR A 1 38  ? 6.495  28.983 63.814 1.00 19.98 ? 46  THR A O   1 
ATOM   291  C CB  . THR A 1 38  ? 5.223  29.114 60.848 1.00 24.21 ? 46  THR A CB  1 
ATOM   292  O OG1 . THR A 1 38  ? 4.096  29.011 61.719 1.00 27.94 ? 46  THR A OG1 1 
ATOM   293  C CG2 . THR A 1 38  ? 4.883  28.540 59.484 1.00 23.88 ? 46  THR A CG2 1 
ATOM   294  N N   . VAL A 1 39  ? 7.915  30.069 62.430 1.00 23.90 ? 47  VAL A N   1 
ATOM   295  C CA  . VAL A 1 39  ? 8.460  30.950 63.448 1.00 22.94 ? 47  VAL A CA  1 
ATOM   296  C C   . VAL A 1 39  ? 8.442  32.369 62.893 1.00 25.14 ? 47  VAL A C   1 
ATOM   297  O O   . VAL A 1 39  ? 9.037  32.636 61.851 1.00 23.61 ? 47  VAL A O   1 
ATOM   298  C CB  . VAL A 1 39  ? 9.888  30.566 63.892 1.00 21.49 ? 47  VAL A CB  1 
ATOM   299  C CG1 . VAL A 1 39  ? 10.394 31.512 64.980 1.00 20.61 ? 47  VAL A CG1 1 
ATOM   300  C CG2 . VAL A 1 39  ? 9.959  29.115 64.355 1.00 20.60 ? 47  VAL A CG2 1 
ATOM   301  N N   . LEU A 1 40  ? 7.755  33.262 63.611 1.00 27.26 ? 48  LEU A N   1 
ATOM   302  C CA  . LEU A 1 40  ? 7.690  34.673 63.270 1.00 26.39 ? 48  LEU A CA  1 
ATOM   303  C C   . LEU A 1 40  ? 8.881  35.375 63.918 1.00 23.29 ? 48  LEU A C   1 
ATOM   304  O O   . LEU A 1 40  ? 9.275  35.012 65.023 1.00 23.86 ? 48  LEU A O   1 
ATOM   305  C CB  . LEU A 1 40  ? 6.341  35.212 63.777 1.00 29.18 ? 48  LEU A CB  1 
ATOM   306  C CG  . LEU A 1 40  ? 5.959  36.637 63.426 1.00 30.86 ? 48  LEU A CG  1 
ATOM   307  C CD1 . LEU A 1 40  ? 5.758  36.815 61.941 1.00 29.94 ? 48  LEU A CD1 1 
ATOM   308  C CD2 . LEU A 1 40  ? 4.692  37.035 64.154 1.00 35.97 ? 48  LEU A CD2 1 
ATOM   309  N N   . PHE A 1 41  ? 9.470  36.356 63.220 1.00 24.75 ? 49  PHE A N   1 
ATOM   310  C CA  . PHE A 1 41  ? 10.582 37.116 63.772 1.00 26.07 ? 49  PHE A CA  1 
ATOM   311  C C   . PHE A 1 41  ? 10.727 38.526 63.202 1.00 25.97 ? 49  PHE A C   1 
ATOM   312  O O   . PHE A 1 41  ? 10.249 38.810 62.106 1.00 25.75 ? 49  PHE A O   1 
ATOM   313  C CB  . PHE A 1 41  ? 11.907 36.354 63.593 1.00 25.45 ? 49  PHE A CB  1 
ATOM   314  C CG  . PHE A 1 41  ? 12.286 36.022 62.171 1.00 26.15 ? 49  PHE A CG  1 
ATOM   315  C CD1 . PHE A 1 41  ? 11.730 34.931 61.524 1.00 28.80 ? 49  PHE A CD1 1 
ATOM   316  C CD2 . PHE A 1 41  ? 13.200 36.799 61.480 1.00 25.52 ? 49  PHE A CD2 1 
ATOM   317  C CE1 . PHE A 1 41  ? 12.087 34.623 60.215 1.00 27.79 ? 49  PHE A CE1 1 
ATOM   318  C CE2 . PHE A 1 41  ? 13.549 36.488 60.169 1.00 24.82 ? 49  PHE A CE2 1 
ATOM   319  C CZ  . PHE A 1 41  ? 12.994 35.403 59.546 1.00 24.02 ? 49  PHE A CZ  1 
ATOM   320  N N   . LYS A 1 42  ? 11.403 39.390 63.974 1.00 29.37 ? 50  LYS A N   1 
ATOM   321  C CA  . LYS A 1 42  ? 11.573 40.800 63.653 1.00 32.56 ? 50  LYS A CA  1 
ATOM   322  C C   . LYS A 1 42  ? 12.810 41.371 64.345 1.00 32.10 ? 50  LYS A C   1 
ATOM   323  O O   . LYS A 1 42  ? 13.213 40.881 65.399 1.00 29.98 ? 50  LYS A O   1 
ATOM   324  C CB  . LYS A 1 42  ? 10.329 41.606 64.084 1.00 39.79 ? 50  LYS A CB  1 
ATOM   325  C CG  . LYS A 1 42  ? 10.423 43.104 63.767 1.00 59.17 ? 50  LYS A CG  1 
ATOM   326  C CD  . LYS A 1 42  ? 9.181  43.906 64.136 1.00 60.55 ? 50  LYS A CD  1 
ATOM   327  C CE  . LYS A 1 42  ? 9.146  44.311 65.590 1.00 58.69 ? 50  LYS A CE  1 
ATOM   328  N NZ  . LYS A 1 42  ? 10.155 45.346 65.916 1.00 66.30 ? 50  LYS A NZ  1 
ATOM   329  N N   . ASP A 1 43  ? 13.393 42.421 63.750 1.00 29.75 ? 51  ASP A N   1 
ATOM   330  C CA  . ASP A 1 43  ? 14.496 43.152 64.355 1.00 28.81 ? 51  ASP A CA  1 
ATOM   331  C C   . ASP A 1 43  ? 14.040 44.443 65.032 1.00 27.02 ? 51  ASP A C   1 
ATOM   332  O O   . ASP A 1 43  ? 13.165 45.139 64.523 1.00 26.23 ? 51  ASP A O   1 
ATOM   333  C CB  . ASP A 1 43  ? 15.567 43.483 63.302 1.00 28.12 ? 51  ASP A CB  1 
ATOM   334  C CG  . ASP A 1 43  ? 16.321 42.278 62.779 1.00 27.35 ? 51  ASP A CG  1 
ATOM   335  O OD1 . ASP A 1 43  ? 16.734 41.429 63.603 1.00 24.15 ? 51  ASP A OD1 1 
ATOM   336  O OD2 . ASP A 1 43  ? 16.528 42.196 61.550 1.00 25.89 ? 51  ASP A OD2 1 
ATOM   337  N N   . SER A 1 44  ? 14.656 44.750 66.182 1.00 29.85 ? 52  SER A N   1 
ATOM   338  C CA  . SER A 1 44  ? 14.423 45.991 66.905 1.00 27.81 ? 52  SER A CA  1 
ATOM   339  C C   . SER A 1 44  ? 15.736 46.570 67.422 1.00 26.85 ? 52  SER A C   1 
ATOM   340  O O   . SER A 1 44  ? 16.623 45.822 67.830 1.00 26.44 ? 52  SER A O   1 
ATOM   341  C CB  . SER A 1 44  ? 13.489 45.775 68.092 1.00 32.04 ? 52  SER A CB  1 
ATOM   342  O OG  . SER A 1 44  ? 12.172 45.456 67.681 1.00 43.22 ? 52  SER A OG  1 
ATOM   343  N N   . ILE A 1 45  ? 15.837 47.904 67.406 1.00 29.30 ? 53  ILE A N   1 
ATOM   344  C CA  . ILE A 1 45  ? 16.937 48.613 68.038 1.00 32.54 ? 53  ILE A CA  1 
ATOM   345  C C   . ILE A 1 45  ? 16.733 48.503 69.546 1.00 28.37 ? 53  ILE A C   1 
ATOM   346  O O   . ILE A 1 45  ? 15.624 48.712 70.033 1.00 29.78 ? 53  ILE A O   1 
ATOM   347  C CB  . ILE A 1 45  ? 17.014 50.100 67.580 1.00 39.10 ? 53  ILE A CB  1 
ATOM   348  C CG1 . ILE A 1 45  ? 17.123 50.227 66.051 1.00 51.71 ? 53  ILE A CG1 1 
ATOM   349  C CG2 . ILE A 1 45  ? 18.173 50.830 68.262 1.00 38.84 ? 53  ILE A CG2 1 
ATOM   350  C CD1 . ILE A 1 45  ? 16.892 51.636 65.516 1.00 54.56 ? 53  ILE A CD1 1 
ATOM   351  N N   . TYR A 1 46  ? 17.799 48.155 70.276 1.00 28.63 ? 54  TYR A N   1 
ATOM   352  C CA  . TYR A 1 46  ? 17.748 48.149 71.730 1.00 31.25 ? 54  TYR A CA  1 
ATOM   353  C C   . TYR A 1 46  ? 18.693 49.181 72.346 1.00 27.51 ? 54  TYR A C   1 
ATOM   354  O O   . TYR A 1 46  ? 18.508 49.570 73.495 1.00 26.24 ? 54  TYR A O   1 
ATOM   355  C CB  . TYR A 1 46  ? 18.006 46.727 72.274 1.00 29.18 ? 54  TYR A CB  1 
ATOM   356  C CG  . TYR A 1 46  ? 19.439 46.246 72.248 1.00 25.85 ? 54  TYR A CG  1 
ATOM   357  C CD1 . TYR A 1 46  ? 20.324 46.582 73.262 1.00 25.38 ? 54  TYR A CD1 1 
ATOM   358  C CD2 . TYR A 1 46  ? 19.900 45.426 71.228 1.00 26.48 ? 54  TYR A CD2 1 
ATOM   359  C CE1 . TYR A 1 46  ? 21.639 46.129 73.254 1.00 26.82 ? 54  TYR A CE1 1 
ATOM   360  C CE2 . TYR A 1 46  ? 21.213 44.967 71.208 1.00 26.15 ? 54  TYR A CE2 1 
ATOM   361  C CZ  . TYR A 1 46  ? 22.082 45.321 72.225 1.00 26.02 ? 54  TYR A CZ  1 
ATOM   362  O OH  . TYR A 1 46  ? 23.384 44.874 72.219 1.00 23.63 ? 54  TYR A OH  1 
ATOM   363  N N   . HIS A 1 47  ? 19.695 49.618 71.575 1.00 29.34 ? 55  HIS A N   1 
ATOM   364  C CA  . HIS A 1 47  ? 20.558 50.721 71.965 1.00 28.31 ? 55  HIS A CA  1 
ATOM   365  C C   . HIS A 1 47  ? 20.726 51.644 70.760 1.00 28.09 ? 55  HIS A C   1 
ATOM   366  O O   . HIS A 1 47  ? 21.452 51.319 69.823 1.00 26.62 ? 55  HIS A O   1 
ATOM   367  C CB  . HIS A 1 47  ? 21.918 50.204 72.473 1.00 28.30 ? 55  HIS A CB  1 
ATOM   368  C CG  . HIS A 1 47  ? 22.692 51.205 73.278 1.00 29.68 ? 55  HIS A CG  1 
ATOM   369  N ND1 . HIS A 1 47  ? 23.709 51.951 72.718 1.00 31.91 ? 55  HIS A ND1 1 
ATOM   370  C CD2 . HIS A 1 47  ? 22.546 51.571 74.570 1.00 30.37 ? 55  HIS A CD2 1 
ATOM   371  C CE1 . HIS A 1 47  ? 24.162 52.737 73.686 1.00 29.54 ? 55  HIS A CE1 1 
ATOM   372  N NE2 . HIS A 1 47  ? 23.488 52.535 74.821 1.00 29.91 ? 55  HIS A NE2 1 
ATOM   373  N N   . LYS A 1 48  ? 20.034 52.789 70.790 1.00 31.87 ? 56  LYS A N   1 
ATOM   374  C CA  . LYS A 1 48  ? 20.002 53.709 69.662 1.00 33.67 ? 56  LYS A CA  1 
ATOM   375  C C   . LYS A 1 48  ? 21.359 54.361 69.392 1.00 31.83 ? 56  LYS A C   1 
ATOM   376  O O   . LYS A 1 48  ? 21.775 54.440 68.239 1.00 31.29 ? 56  LYS A O   1 
ATOM   377  C CB  . LYS A 1 48  ? 18.923 54.784 69.881 1.00 36.00 ? 56  LYS A CB  1 
ATOM   378  C CG  . LYS A 1 48  ? 17.512 54.215 70.008 1.00 44.69 ? 56  LYS A CG  1 
ATOM   379  C CD  . LYS A 1 48  ? 16.542 55.164 70.704 1.00 52.80 ? 56  LYS A CD  1 
ATOM   380  C CE  . LYS A 1 48  ? 15.280 54.461 71.149 1.00 60.78 ? 56  LYS A CE  1 
ATOM   381  N NZ  . LYS A 1 48  ? 14.498 53.935 69.997 1.00 61.79 ? 56  LYS A NZ  1 
ATOM   382  N N   . PRO A 1 49  ? 22.101 54.835 70.424 1.00 30.91 ? 57  PRO A N   1 
ATOM   383  C CA  . PRO A 1 49  ? 23.389 55.487 70.200 1.00 29.31 ? 57  PRO A CA  1 
ATOM   384  C C   . PRO A 1 49  ? 24.415 54.627 69.462 1.00 31.38 ? 57  PRO A C   1 
ATOM   385  O O   . PRO A 1 49  ? 25.102 55.123 68.573 1.00 28.95 ? 57  PRO A O   1 
ATOM   386  C CB  . PRO A 1 49  ? 23.866 55.832 71.613 1.00 28.94 ? 57  PRO A CB  1 
ATOM   387  C CG  . PRO A 1 49  ? 22.636 55.814 72.459 1.00 29.81 ? 57  PRO A CG  1 
ATOM   388  C CD  . PRO A 1 49  ? 21.728 54.793 71.848 1.00 30.34 ? 57  PRO A CD  1 
ATOM   389  N N   . ASN A 1 50  ? 24.518 53.345 69.840 1.00 33.38 ? 58  ASN A N   1 
ATOM   390  C CA  . ASN A 1 50  ? 25.434 52.420 69.187 1.00 32.94 ? 58  ASN A CA  1 
ATOM   391  C C   . ASN A 1 50  ? 24.803 51.652 68.026 1.00 32.15 ? 58  ASN A C   1 
ATOM   392  O O   . ASN A 1 50  ? 25.461 50.806 67.425 1.00 36.65 ? 58  ASN A O   1 
ATOM   393  C CB  . ASN A 1 50  ? 26.006 51.417 70.198 1.00 34.32 ? 58  ASN A CB  1 
ATOM   394  C CG  . ASN A 1 50  ? 26.939 52.023 71.219 1.00 32.63 ? 58  ASN A CG  1 
ATOM   395  O OD1 . ASN A 1 50  ? 26.769 51.838 72.422 1.00 39.92 ? 58  ASN A OD1 1 
ATOM   396  N ND2 . ASN A 1 50  ? 27.968 52.726 70.772 1.00 31.87 ? 58  ASN A ND2 1 
ATOM   397  N N   . ASN A 1 51  ? 23.531 51.946 67.725 1.00 33.51 ? 59  ASN A N   1 
ATOM   398  C CA  . ASN A 1 51  ? 22.811 51.329 66.621 1.00 32.46 ? 59  ASN A CA  1 
ATOM   399  C C   . ASN A 1 51  ? 22.828 49.803 66.720 1.00 32.03 ? 59  ASN A C   1 
ATOM   400  O O   . ASN A 1 51  ? 23.010 49.105 65.723 1.00 33.50 ? 59  ASN A O   1 
ATOM   401  C CB  . ASN A 1 51  ? 23.386 51.818 65.283 1.00 32.28 ? 59  ASN A CB  1 
ATOM   402  C CG  . ASN A 1 51  ? 22.455 51.622 64.109 1.00 34.32 ? 59  ASN A CG  1 
ATOM   403  O OD1 . ASN A 1 51  ? 21.264 51.944 64.170 1.00 38.33 ? 59  ASN A OD1 1 
ATOM   404  N ND2 . ASN A 1 51  ? 22.971 51.089 63.011 1.00 34.00 ? 59  ASN A ND2 1 
ATOM   405  N N   . LEU A 1 52  ? 22.626 49.300 67.944 1.00 32.94 ? 60  LEU A N   1 
ATOM   406  C CA  . LEU A 1 52  ? 22.627 47.872 68.217 1.00 37.72 ? 60  LEU A CA  1 
ATOM   407  C C   . LEU A 1 52  ? 21.211 47.310 68.118 1.00 39.41 ? 60  LEU A C   1 
ATOM   408  O O   . LEU A 1 52  ? 20.296 47.810 68.772 1.00 35.85 ? 60  LEU A O   1 
ATOM   409  C CB  . LEU A 1 52  ? 23.201 47.615 69.615 1.00 36.07 ? 60  LEU A CB  1 
ATOM   410  C CG  . LEU A 1 52  ? 24.676 47.942 69.782 1.00 36.39 ? 60  LEU A CG  1 
ATOM   411  C CD1 . LEU A 1 52  ? 25.090 47.869 71.236 1.00 33.03 ? 60  LEU A CD1 1 
ATOM   412  C CD2 . LEU A 1 52  ? 25.535 47.008 68.945 1.00 36.10 ? 60  LEU A CD2 1 
ATOM   413  N N   . HIS A 1 53  ? 21.052 46.267 67.293 1.00 31.58 ? 61  HIS A N   1 
ATOM   414  C CA  . HIS A 1 53  ? 19.765 45.625 67.087 1.00 29.82 ? 61  HIS A CA  1 
ATOM   415  C C   . HIS A 1 53  ? 19.718 44.238 67.719 1.00 31.28 ? 61  HIS A C   1 
ATOM   416  O O   . HIS A 1 53  ? 20.750 43.597 67.905 1.00 28.35 ? 61  HIS A O   1 
ATOM   417  C CB  . HIS A 1 53  ? 19.455 45.501 65.592 1.00 29.17 ? 61  HIS A CB  1 
ATOM   418  C CG  . HIS A 1 53  ? 19.393 46.812 64.871 1.00 30.87 ? 61  HIS A CG  1 
ATOM   419  N ND1 . HIS A 1 53  ? 20.529 47.563 64.646 1.00 35.81 ? 61  HIS A ND1 1 
ATOM   420  C CD2 . HIS A 1 53  ? 18.332 47.456 64.341 1.00 31.33 ? 61  HIS A CD2 1 
ATOM   421  C CE1 . HIS A 1 53  ? 20.129 48.641 63.990 1.00 35.87 ? 61  HIS A CE1 1 
ATOM   422  N NE2 . HIS A 1 53  ? 18.808 48.615 63.785 1.00 34.41 ? 61  HIS A NE2 1 
ATOM   423  N N   . LEU A 1 54  ? 18.501 43.792 68.049 1.00 30.56 ? 62  LEU A N   1 
ATOM   424  C CA  . LEU A 1 54  ? 18.264 42.408 68.416 1.00 28.30 ? 62  LEU A CA  1 
ATOM   425  C C   . LEU A 1 54  ? 17.160 41.852 67.525 1.00 30.61 ? 62  LEU A C   1 
ATOM   426  O O   . LEU A 1 54  ? 16.444 42.607 66.867 1.00 26.55 ? 62  LEU A O   1 
ATOM   427  C CB  . LEU A 1 54  ? 17.905 42.249 69.910 1.00 29.04 ? 62  LEU A CB  1 
ATOM   428  C CG  . LEU A 1 54  ? 16.783 43.121 70.487 1.00 29.35 ? 62  LEU A CG  1 
ATOM   429  C CD1 . LEU A 1 54  ? 15.405 42.593 70.123 1.00 29.49 ? 62  LEU A CD1 1 
ATOM   430  C CD2 . LEU A 1 54  ? 16.905 43.218 72.000 1.00 29.27 ? 62  LEU A CD2 1 
ATOM   431  N N   . ARG A 1 55  ? 17.060 40.520 67.501 1.00 30.32 ? 63  ARG A N   1 
ATOM   432  C CA  . ARG A 1 55  ? 16.009 39.833 66.774 1.00 28.00 ? 63  ARG A CA  1 
ATOM   433  C C   . ARG A 1 55  ? 15.131 39.072 67.761 1.00 26.65 ? 63  ARG A C   1 
ATOM   434  O O   . ARG A 1 55  ? 15.641 38.382 68.643 1.00 28.63 ? 63  ARG A O   1 
ATOM   435  C CB  . ARG A 1 55  ? 16.605 38.888 65.734 1.00 27.29 ? 63  ARG A CB  1 
ATOM   436  C CG  . ARG A 1 55  ? 15.556 38.269 64.825 1.00 29.80 ? 63  ARG A CG  1 
ATOM   437  C CD  . ARG A 1 55  ? 16.179 37.681 63.589 1.00 28.41 ? 63  ARG A CD  1 
ATOM   438  N NE  . ARG A 1 55  ? 16.659 38.720 62.687 1.00 27.52 ? 63  ARG A NE  1 
ATOM   439  C CZ  . ARG A 1 55  ? 17.261 38.490 61.530 1.00 24.42 ? 63  ARG A CZ  1 
ATOM   440  N NH1 . ARG A 1 55  ? 17.582 37.264 61.149 1.00 25.15 ? 63  ARG A NH1 1 
ATOM   441  N NH2 . ARG A 1 55  ? 17.551 39.515 60.734 1.00 25.77 ? 63  ARG A NH2 1 
ATOM   442  N N   . LEU A 1 56  ? 13.811 39.225 67.598 1.00 24.50 ? 64  LEU A N   1 
ATOM   443  C CA  . LEU A 1 56  ? 12.824 38.543 68.418 1.00 25.77 ? 64  LEU A CA  1 
ATOM   444  C C   . LEU A 1 56  ? 12.199 37.415 67.603 1.00 26.90 ? 64  LEU A C   1 
ATOM   445  O O   . LEU A 1 56  ? 11.776 37.641 66.471 1.00 22.10 ? 64  LEU A O   1 
ATOM   446  C CB  . LEU A 1 56  ? 11.740 39.533 68.855 1.00 25.55 ? 64  LEU A CB  1 
ATOM   447  C CG  . LEU A 1 56  ? 12.232 40.745 69.630 1.00 27.01 ? 64  LEU A CG  1 
ATOM   448  C CD1 . LEU A 1 56  ? 11.149 41.799 69.738 1.00 26.75 ? 64  LEU A CD1 1 
ATOM   449  C CD2 . LEU A 1 56  ? 12.717 40.346 71.005 1.00 28.24 ? 64  LEU A CD2 1 
ATOM   450  N N   . TYR A 1 57  ? 12.151 36.208 68.183 1.00 27.57 ? 65  TYR A N   1 
ATOM   451  C CA  . TYR A 1 57  ? 11.530 35.060 67.538 1.00 28.40 ? 65  TYR A CA  1 
ATOM   452  C C   . TYR A 1 57  ? 10.303 34.592 68.313 1.00 27.06 ? 65  TYR A C   1 
ATOM   453  O O   . TYR A 1 57  ? 10.322 34.543 69.539 1.00 27.47 ? 65  TYR A O   1 
ATOM   454  C CB  . TYR A 1 57  ? 12.492 33.877 67.428 1.00 26.66 ? 65  TYR A CB  1 
ATOM   455  C CG  . TYR A 1 57  ? 13.750 34.143 66.635 1.00 27.05 ? 65  TYR A CG  1 
ATOM   456  C CD1 . TYR A 1 57  ? 14.782 34.907 67.162 1.00 27.69 ? 65  TYR A CD1 1 
ATOM   457  C CD2 . TYR A 1 57  ? 13.915 33.615 65.361 1.00 25.60 ? 65  TYR A CD2 1 
ATOM   458  C CE1 . TYR A 1 57  ? 15.949 35.140 66.442 1.00 30.02 ? 65  TYR A CE1 1 
ATOM   459  C CE2 . TYR A 1 57  ? 15.073 33.844 64.630 1.00 26.30 ? 65  TYR A CE2 1 
ATOM   460  C CZ  . TYR A 1 57  ? 16.090 34.607 65.174 1.00 27.33 ? 65  TYR A CZ  1 
ATOM   461  O OH  . TYR A 1 57  ? 17.238 34.823 64.456 1.00 27.98 ? 65  TYR A OH  1 
ATOM   462  N N   . LYS A 1 58  ? 9.251  34.219 67.580 1.00 26.88 ? 66  LYS A N   1 
ATOM   463  C CA  . LYS A 1 58  ? 8.035  33.715 68.190 1.00 26.73 ? 66  LYS A CA  1 
ATOM   464  C C   . LYS A 1 58  ? 7.549  32.480 67.438 1.00 28.15 ? 66  LYS A C   1 
ATOM   465  O O   . LYS A 1 58  ? 7.266  32.559 66.244 1.00 25.92 ? 66  LYS A O   1 
ATOM   466  C CB  . LYS A 1 58  ? 6.952  34.797 68.192 1.00 28.59 ? 66  LYS A CB  1 
ATOM   467  C CG  . LYS A 1 58  ? 5.737  34.423 69.017 1.00 31.70 ? 66  LYS A CG  1 
ATOM   468  C CD  . LYS A 1 58  ? 4.766  35.567 69.205 1.00 33.28 ? 66  LYS A CD  1 
ATOM   469  C CE  . LYS A 1 58  ? 4.044  35.931 67.941 1.00 36.53 ? 66  LYS A CE  1 
ATOM   470  N NZ  . LYS A 1 58  ? 2.941  36.894 68.208 1.00 40.75 ? 66  LYS A NZ  1 
ATOM   471  N N   . PRO A 1 59  ? 7.450  31.302 68.100 1.00 31.13 ? 67  PRO A N   1 
ATOM   472  C CA  . PRO A 1 59  ? 6.770  30.158 67.508 1.00 30.25 ? 67  PRO A CA  1 
ATOM   473  C C   . PRO A 1 59  ? 5.262  30.368 67.476 1.00 27.74 ? 67  PRO A C   1 
ATOM   474  O O   . PRO A 1 59  ? 4.649  30.561 68.521 1.00 30.33 ? 67  PRO A O   1 
ATOM   475  C CB  . PRO A 1 59  ? 7.174  29.004 68.425 1.00 34.35 ? 67  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 59  ? 7.402  29.657 69.758 1.00 35.90 ? 67  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 59  ? 7.967  31.024 69.450 1.00 32.87 ? 67  PRO A CD  1 
ATOM   478  N N   . ILE A 1 60  ? 4.681  30.345 66.272 1.00 36.45 ? 68  ILE A N   1 
ATOM   479  C CA  . ILE A 1 60  ? 3.320  30.813 66.064 1.00 42.02 ? 68  ILE A CA  1 
ATOM   480  C C   . ILE A 1 60  ? 2.274  29.930 66.743 1.00 48.98 ? 68  ILE A C   1 
ATOM   481  O O   . ILE A 1 60  ? 1.439  30.433 67.493 1.00 56.11 ? 68  ILE A O   1 
ATOM   482  C CB  . ILE A 1 60  ? 3.051  30.980 64.549 1.00 38.64 ? 68  ILE A CB  1 
ATOM   483  C CG1 . ILE A 1 60  ? 3.923  32.122 63.982 1.00 39.38 ? 68  ILE A CG1 1 
ATOM   484  C CG2 . ILE A 1 60  ? 1.566  31.208 64.257 1.00 38.43 ? 68  ILE A CG2 1 
ATOM   485  C CD1 . ILE A 1 60  ? 3.731  32.406 62.508 1.00 41.04 ? 68  ILE A CD1 1 
ATOM   486  N N   . SER A 1 61  ? 2.322  28.619 66.480 1.00 52.36 ? 69  SER A N   1 
ATOM   487  C CA  . SER A 1 61  ? 1.328  27.701 67.015 1.00 60.16 ? 69  SER A CA  1 
ATOM   488  C C   . SER A 1 61  ? 1.340  27.643 68.543 1.00 63.44 ? 69  SER A C   1 
ATOM   489  O O   . SER A 1 61  ? 0.286  27.507 69.158 1.00 66.27 ? 69  SER A O   1 
ATOM   490  C CB  . SER A 1 61  ? 1.515  26.301 66.434 1.00 59.36 ? 69  SER A CB  1 
ATOM   491  O OG  . SER A 1 61  ? 2.779  25.757 66.773 1.00 73.84 ? 69  SER A OG  1 
ATOM   492  N N   . ALA A 1 62  ? 2.534  27.760 69.141 1.00 65.29 ? 70  ALA A N   1 
ATOM   493  C CA  . ALA A 1 62  ? 2.699  27.687 70.586 1.00 63.88 ? 70  ALA A CA  1 
ATOM   494  C C   . ALA A 1 62  ? 2.335  28.988 71.300 1.00 74.23 ? 70  ALA A C   1 
ATOM   495  O O   . ALA A 1 62  ? 1.902  28.957 72.451 1.00 81.41 ? 70  ALA A O   1 
ATOM   496  C CB  . ALA A 1 62  ? 4.130  27.300 70.926 1.00 58.18 ? 70  ALA A CB  1 
ATOM   497  N N   . SER A 1 63  ? 2.530  30.123 70.615 1.00 75.72 ? 71  SER A N   1 
ATOM   498  C CA  . SER A 1 63  ? 2.236  31.435 71.173 1.00 73.81 ? 71  SER A CA  1 
ATOM   499  C C   . SER A 1 63  ? 0.741  31.663 71.386 1.00 74.76 ? 71  SER A C   1 
ATOM   500  O O   . SER A 1 63  ? 0.348  32.356 72.322 1.00 73.88 ? 71  SER A O   1 
ATOM   501  C CB  . SER A 1 63  ? 2.802  32.534 70.277 1.00 70.47 ? 71  SER A CB  1 
ATOM   502  O OG  . SER A 1 63  ? 2.232  32.497 68.980 1.00 68.32 ? 71  SER A OG  1 
ATOM   503  N N   . ASN A 1 64  ? -0.081 31.070 70.509 1.00 76.21 ? 72  ASN A N   1 
ATOM   504  C CA  . ASN A 1 64  ? -1.530 31.162 70.603 1.00 79.86 ? 72  ASN A CA  1 
ATOM   505  C C   . ASN A 1 64  ? -2.129 30.262 71.684 1.00 88.43 ? 72  ASN A C   1 
ATOM   506  O O   . ASN A 1 64  ? -3.317 30.369 71.982 1.00 80.33 ? 72  ASN A O   1 
ATOM   507  C CB  . ASN A 1 64  ? -2.165 30.811 69.249 1.00 79.71 ? 72  ASN A CB  1 
ATOM   508  C CG  . ASN A 1 64  ? -1.780 31.744 68.126 1.00 82.21 ? 72  ASN A CG  1 
ATOM   509  O OD1 . ASN A 1 64  ? -1.169 32.798 68.334 1.00 81.00 ? 72  ASN A OD1 1 
ATOM   510  N ND2 . ASN A 1 64  ? -2.139 31.378 66.903 1.00 83.26 ? 72  ASN A ND2 1 
ATOM   511  N N   . ARG A 1 65  ? -1.302 29.377 72.261 1.00 92.31 ? 73  ARG A N   1 
ATOM   512  C CA  . ARG A 1 65  ? -1.757 28.400 73.238 1.00 83.64 ? 73  ARG A CA  1 
ATOM   513  C C   . ARG A 1 65  ? -1.458 28.796 74.684 1.00 78.61 ? 73  ARG A C   1 
ATOM   514  O O   . ARG A 1 65  ? -2.265 28.526 75.571 1.00 81.79 ? 73  ARG A O   1 
ATOM   515  C CB  . ARG A 1 65  ? -1.118 27.032 72.933 1.00 86.57 ? 73  ARG A CB  1 
ATOM   516  C CG  . ARG A 1 65  ? -1.489 26.457 71.562 1.00 93.11 ? 73  ARG A CG  1 
ATOM   517  C CD  . ARG A 1 65  ? -2.969 26.131 71.438 1.00 92.76 ? 73  ARG A CD  1 
ATOM   518  N NE  . ARG A 1 65  ? -3.258 25.289 70.281 1.00 93.52 ? 73  ARG A NE  1 
ATOM   519  C CZ  . ARG A 1 65  ? -3.195 25.687 69.015 1.00 91.07 ? 73  ARG A CZ  1 
ATOM   520  N NH1 . ARG A 1 65  ? -2.965 26.950 68.696 1.00 93.01 ? 73  ARG A NH1 1 
ATOM   521  N NH2 . ARG A 1 65  ? -3.384 24.796 68.046 1.00 80.96 ? 73  ARG A NH2 1 
ATOM   522  N N   . THR A 1 66  ? -0.299 29.428 74.920 1.00 80.40 ? 74  THR A N   1 
ATOM   523  C CA  . THR A 1 66  ? 0.118  29.791 76.266 1.00 67.42 ? 74  THR A CA  1 
ATOM   524  C C   . THR A 1 66  ? 1.073  30.983 76.291 1.00 61.28 ? 74  THR A C   1 
ATOM   525  O O   . THR A 1 66  ? 1.471  31.490 75.244 1.00 65.46 ? 74  THR A O   1 
ATOM   526  C CB  . THR A 1 66  ? 0.775  28.581 76.947 1.00 66.64 ? 74  THR A CB  1 
ATOM   527  O OG1 . THR A 1 66  ? 0.913  28.854 78.341 1.00 64.22 ? 74  THR A OG1 1 
ATOM   528  C CG2 . THR A 1 66  ? 2.138  28.237 76.346 1.00 66.63 ? 74  THR A CG2 1 
ATOM   529  N N   . ALA A 1 67  ? 1.431  31.414 77.509 1.00 48.10 ? 75  ALA A N   1 
ATOM   530  C CA  . ALA A 1 67  ? 2.446  32.436 77.712 1.00 40.70 ? 75  ALA A CA  1 
ATOM   531  C C   . ALA A 1 67  ? 3.838  31.824 77.571 1.00 36.48 ? 75  ALA A C   1 
ATOM   532  O O   . ALA A 1 67  ? 4.143  30.819 78.208 1.00 44.69 ? 75  ALA A O   1 
ATOM   533  C CB  . ALA A 1 67  ? 2.287  33.077 79.080 1.00 39.98 ? 75  ALA A CB  1 
ATOM   534  N N   . LEU A 1 68  ? 4.678  32.450 76.739 1.00 31.68 ? 76  LEU A N   1 
ATOM   535  C CA  . LEU A 1 68  ? 5.977  31.903 76.385 1.00 26.61 ? 76  LEU A CA  1 
ATOM   536  C C   . LEU A 1 68  ? 7.064  32.305 77.379 1.00 27.03 ? 76  LEU A C   1 
ATOM   537  O O   . LEU A 1 68  ? 7.106  33.453 77.817 1.00 24.82 ? 76  LEU A O   1 
ATOM   538  C CB  . LEU A 1 68  ? 6.381  32.411 74.999 1.00 25.81 ? 76  LEU A CB  1 
ATOM   539  C CG  . LEU A 1 68  ? 5.418  32.108 73.864 1.00 27.15 ? 76  LEU A CG  1 
ATOM   540  C CD1 . LEU A 1 68  ? 5.899  32.728 72.582 1.00 28.74 ? 76  LEU A CD1 1 
ATOM   541  C CD2 . LEU A 1 68  ? 5.237  30.616 73.677 1.00 27.72 ? 76  LEU A CD2 1 
ATOM   542  N N   . PRO A 1 69  ? 7.987  31.387 77.753 1.00 25.53 ? 77  PRO A N   1 
ATOM   543  C CA  . PRO A 1 69  ? 9.212  31.788 78.430 1.00 24.69 ? 77  PRO A CA  1 
ATOM   544  C C   . PRO A 1 69  ? 10.173 32.492 77.479 1.00 26.95 ? 77  PRO A C   1 
ATOM   545  O O   . PRO A 1 69  ? 10.018 32.405 76.263 1.00 26.25 ? 77  PRO A O   1 
ATOM   546  C CB  . PRO A 1 69  ? 9.778  30.463 78.942 1.00 25.18 ? 77  PRO A CB  1 
ATOM   547  C CG  . PRO A 1 69  ? 9.254  29.436 77.984 1.00 23.58 ? 77  PRO A CG  1 
ATOM   548  C CD  . PRO A 1 69  ? 7.903  29.933 77.534 1.00 24.55 ? 77  PRO A CD  1 
ATOM   549  N N   . VAL A 1 70  ? 11.161 33.189 78.042 1.00 28.11 ? 78  VAL A N   1 
ATOM   550  C CA  . VAL A 1 70  ? 12.115 33.927 77.236 1.00 26.47 ? 78  VAL A CA  1 
ATOM   551  C C   . VAL A 1 70  ? 13.467 33.222 77.270 1.00 27.01 ? 78  VAL A C   1 
ATOM   552  O O   . VAL A 1 70  ? 13.937 32.818 78.331 1.00 26.59 ? 78  VAL A O   1 
ATOM   553  C CB  . VAL A 1 70  ? 12.219 35.392 77.699 1.00 28.12 ? 78  VAL A CB  1 
ATOM   554  C CG1 . VAL A 1 70  ? 13.191 36.179 76.823 1.00 29.31 ? 78  VAL A CG1 1 
ATOM   555  C CG2 . VAL A 1 70  ? 10.841 36.052 77.722 1.00 27.08 ? 78  VAL A CG2 1 
ATOM   556  N N   . VAL A 1 71  ? 14.059 33.056 76.083 1.00 26.78 ? 79  VAL A N   1 
ATOM   557  C CA  . VAL A 1 71  ? 15.436 32.618 75.950 1.00 24.98 ? 79  VAL A CA  1 
ATOM   558  C C   . VAL A 1 71  ? 16.201 33.773 75.310 1.00 27.32 ? 79  VAL A C   1 
ATOM   559  O O   . VAL A 1 71  ? 15.875 34.195 74.204 1.00 30.17 ? 79  VAL A O   1 
ATOM   560  C CB  . VAL A 1 71  ? 15.563 31.314 75.127 1.00 23.31 ? 79  VAL A CB  1 
ATOM   561  C CG1 . VAL A 1 71  ? 17.024 30.977 74.841 1.00 26.16 ? 79  VAL A CG1 1 
ATOM   562  C CG2 . VAL A 1 71  ? 14.864 30.152 75.822 1.00 23.55 ? 79  VAL A CG2 1 
ATOM   563  N N   . VAL A 1 72  ? 17.203 34.293 76.028 1.00 27.79 ? 80  VAL A N   1 
ATOM   564  C CA  . VAL A 1 72  ? 18.116 35.271 75.463 1.00 29.30 ? 80  VAL A CA  1 
ATOM   565  C C   . VAL A 1 72  ? 19.347 34.513 74.976 1.00 27.49 ? 80  VAL A C   1 
ATOM   566  O O   . VAL A 1 72  ? 20.075 33.933 75.780 1.00 26.95 ? 80  VAL A O   1 
ATOM   567  C CB  . VAL A 1 72  ? 18.488 36.389 76.463 1.00 28.19 ? 80  VAL A CB  1 
ATOM   568  C CG1 . VAL A 1 72  ? 19.264 37.502 75.766 1.00 28.59 ? 80  VAL A CG1 1 
ATOM   569  C CG2 . VAL A 1 72  ? 17.251 36.943 77.159 1.00 25.71 ? 80  VAL A CG2 1 
ATOM   570  N N   . PHE A 1 73  ? 19.551 34.513 73.652 1.00 28.33 ? 81  PHE A N   1 
ATOM   571  C CA  . PHE A 1 73  ? 20.668 33.820 73.029 1.00 28.30 ? 81  PHE A CA  1 
ATOM   572  C C   . PHE A 1 73  ? 21.784 34.793 72.664 1.00 29.55 ? 81  PHE A C   1 
ATOM   573  O O   . PHE A 1 73  ? 21.555 35.733 71.907 1.00 29.23 ? 81  PHE A O   1 
ATOM   574  C CB  . PHE A 1 73  ? 20.219 33.093 71.756 1.00 31.06 ? 81  PHE A CB  1 
ATOM   575  C CG  . PHE A 1 73  ? 21.362 32.457 71.001 1.00 31.09 ? 81  PHE A CG  1 
ATOM   576  C CD1 . PHE A 1 73  ? 21.982 31.314 71.481 1.00 30.94 ? 81  PHE A CD1 1 
ATOM   577  C CD2 . PHE A 1 73  ? 21.842 33.023 69.832 1.00 27.75 ? 81  PHE A CD2 1 
ATOM   578  C CE1 . PHE A 1 73  ? 23.042 30.737 70.792 1.00 30.53 ? 81  PHE A CE1 1 
ATOM   579  C CE2 . PHE A 1 73  ? 22.903 32.444 69.147 1.00 32.06 ? 81  PHE A CE2 1 
ATOM   580  C CZ  . PHE A 1 73  ? 23.495 31.304 69.629 1.00 32.15 ? 81  PHE A CZ  1 
ATOM   581  N N   . PHE A 1 74  ? 22.991 34.540 73.186 1.00 28.77 ? 82  PHE A N   1 
ATOM   582  C CA  . PHE A 1 74  ? 24.164 35.330 72.845 1.00 27.44 ? 82  PHE A CA  1 
ATOM   583  C C   . PHE A 1 74  ? 25.076 34.520 71.929 1.00 27.45 ? 82  PHE A C   1 
ATOM   584  O O   . PHE A 1 74  ? 25.590 33.478 72.328 1.00 29.70 ? 82  PHE A O   1 
ATOM   585  C CB  . PHE A 1 74  ? 24.905 35.773 74.113 1.00 26.88 ? 82  PHE A CB  1 
ATOM   586  C CG  . PHE A 1 74  ? 24.174 36.832 74.902 1.00 25.70 ? 82  PHE A CG  1 
ATOM   587  C CD1 . PHE A 1 74  ? 24.211 38.158 74.511 1.00 27.62 ? 82  PHE A CD1 1 
ATOM   588  C CD2 . PHE A 1 74  ? 23.428 36.496 76.020 1.00 27.36 ? 82  PHE A CD2 1 
ATOM   589  C CE1 . PHE A 1 74  ? 23.531 39.133 75.237 1.00 31.11 ? 82  PHE A CE1 1 
ATOM   590  C CE2 . PHE A 1 74  ? 22.748 37.470 76.741 1.00 30.35 ? 82  PHE A CE2 1 
ATOM   591  C CZ  . PHE A 1 74  ? 22.802 38.783 76.346 1.00 29.29 ? 82  PHE A CZ  1 
ATOM   592  N N   . HIS A 1 75  ? 25.269 35.049 70.725 1.00 32.59 ? 83  HIS A N   1 
ATOM   593  C CA  . HIS A 1 75  ? 26.058 34.355 69.682 1.00 31.73 ? 83  HIS A CA  1 
ATOM   594  C C   . HIS A 1 75  ? 27.538 34.293 70.019 1.00 32.31 ? 83  HIS A C   1 
ATOM   595  O O   . HIS A 1 75  ? 28.034 34.993 70.909 1.00 31.66 ? 83  HIS A O   1 
ATOM   596  C CB  . HIS A 1 75  ? 25.869 35.034 68.323 1.00 31.49 ? 83  HIS A CB  1 
ATOM   597  C CG  . HIS A 1 75  ? 26.483 36.377 68.114 1.00 32.06 ? 83  HIS A CG  1 
ATOM   598  N ND1 . HIS A 1 75  ? 27.817 36.575 67.839 1.00 36.24 ? 83  HIS A ND1 1 
ATOM   599  C CD2 . HIS A 1 75  ? 25.919 37.585 68.075 1.00 34.12 ? 83  HIS A CD2 1 
ATOM   600  C CE1 . HIS A 1 75  ? 28.041 37.867 67.678 1.00 35.39 ? 83  HIS A CE1 1 
ATOM   601  N NE2 . HIS A 1 75  ? 26.901 38.498 67.814 1.00 34.82 ? 83  HIS A NE2 1 
ATOM   602  N N   . GLY A 1 76  ? 28.232 33.469 69.256 1.00 33.58 ? 84  GLY A N   1 
ATOM   603  C CA  . GLY A 1 76  ? 29.657 33.282 69.496 1.00 32.04 ? 84  GLY A CA  1 
ATOM   604  C C   . GLY A 1 76  ? 30.514 34.137 68.615 1.00 31.45 ? 84  GLY A C   1 
ATOM   605  O O   . GLY A 1 76  ? 30.046 35.196 68.187 1.00 33.82 ? 84  GLY A O   1 
ATOM   606  N N   . GLY A 1 77  ? 31.683 33.636 68.260 1.00 36.42 ? 85  GLY A N   1 
ATOM   607  C CA  . GLY A 1 77  ? 32.698 34.444 67.576 1.00 29.84 ? 85  GLY A CA  1 
ATOM   608  C C   . GLY A 1 77  ? 33.809 34.458 68.588 1.00 28.16 ? 85  GLY A C   1 
ATOM   609  O O   . GLY A 1 77  ? 33.841 33.539 69.429 1.00 26.36 ? 85  GLY A O   1 
ATOM   610  N N   . GLY A 1 78  ? 34.678 35.441 68.573 1.00 29.23 ? 86  GLY A N   1 
ATOM   611  C CA  . GLY A 1 78  ? 35.658 35.486 69.670 1.00 27.08 ? 86  GLY A CA  1 
ATOM   612  C C   . GLY A 1 78  ? 35.609 36.865 70.252 1.00 30.31 ? 86  GLY A C   1 
ATOM   613  O O   . GLY A 1 78  ? 36.693 37.398 70.532 1.00 30.47 ? 86  GLY A O   1 
ATOM   614  N N   . PHE A 1 79  ? 34.395 37.402 70.435 1.00 27.95 ? 87  PHE A N   1 
ATOM   615  C CA  . PHE A 1 79  ? 34.234 38.821 70.852 1.00 25.19 ? 87  PHE A CA  1 
ATOM   616  C C   . PHE A 1 79  ? 34.729 39.646 69.665 1.00 26.04 ? 87  PHE A C   1 
ATOM   617  O O   . PHE A 1 79  ? 34.948 40.860 69.829 1.00 26.94 ? 87  PHE A O   1 
ATOM   618  C CB  . PHE A 1 79  ? 34.936 39.199 72.162 1.00 25.13 ? 87  PHE A CB  1 
ATOM   619  C CG  . PHE A 1 79  ? 34.425 38.487 73.407 1.00 27.37 ? 87  PHE A CG  1 
ATOM   620  C CD1 . PHE A 1 79  ? 33.152 38.745 73.903 1.00 29.60 ? 87  PHE A CD1 1 
ATOM   621  C CD2 . PHE A 1 79  ? 35.221 37.567 74.080 1.00 30.14 ? 87  PHE A CD2 1 
ATOM   622  C CE1 . PHE A 1 79  ? 32.692 38.100 75.040 1.00 32.74 ? 87  PHE A CE1 1 
ATOM   623  C CE2 . PHE A 1 79  ? 34.754 36.924 75.216 1.00 32.39 ? 87  PHE A CE2 1 
ATOM   624  C CZ  . PHE A 1 79  ? 33.493 37.193 75.693 1.00 29.65 ? 87  PHE A CZ  1 
ATOM   625  N N   . CYS A 1 80  ? 34.878 39.007 68.500 1.00 32.55 ? 88  CYS A N   1 
ATOM   626  C CA  . CYS A 1 80  ? 35.432 39.714 67.317 1.00 32.80 ? 88  CYS A CA  1 
ATOM   627  C C   . CYS A 1 80  ? 34.559 39.476 66.074 1.00 35.37 ? 88  CYS A C   1 
ATOM   628  O O   . CYS A 1 80  ? 34.762 40.202 65.077 1.00 40.37 ? 88  CYS A O   1 
ATOM   629  C CB  . CYS A 1 80  ? 36.847 39.234 67.017 1.00 34.45 ? 88  CYS A CB  1 
ATOM   630  S SG  . CYS A 1 80  ? 38.005 39.470 68.391 1.00 30.65 ? 88  CYS A SG  1 
ATOM   631  N N   . PHE A 1 81  ? 33.637 38.508 66.119 1.00 37.56 ? 89  PHE A N   1 
ATOM   632  C CA  . PHE A 1 81  ? 32.848 38.177 64.901 1.00 36.31 ? 89  PHE A CA  1 
ATOM   633  C C   . PHE A 1 81  ? 31.430 37.774 65.249 1.00 34.06 ? 89  PHE A C   1 
ATOM   634  O O   . PHE A 1 81  ? 31.164 37.441 66.424 1.00 32.76 ? 89  PHE A O   1 
ATOM   635  C CB  . PHE A 1 81  ? 33.402 36.934 64.203 1.00 34.94 ? 89  PHE A CB  1 
ATOM   636  C CG  . PHE A 1 81  ? 34.816 37.029 63.653 1.00 35.38 ? 89  PHE A CG  1 
ATOM   637  C CD1 . PHE A 1 81  ? 35.082 37.750 62.495 1.00 38.06 ? 89  PHE A CD1 1 
ATOM   638  C CD2 . PHE A 1 81  ? 35.869 36.375 64.281 1.00 37.60 ? 89  PHE A CD2 1 
ATOM   639  C CE1 . PHE A 1 81  ? 36.368 37.824 61.990 1.00 37.29 ? 89  PHE A CE1 1 
ATOM   640  C CE2 . PHE A 1 81  ? 37.153 36.453 63.770 1.00 39.14 ? 89  PHE A CE2 1 
ATOM   641  C CZ  . PHE A 1 81  ? 37.398 37.173 62.625 1.00 37.73 ? 89  PHE A CZ  1 
ATOM   642  N N   . GLY A 1 82  ? 30.532 37.801 64.258 1.00 29.04 ? 90  GLY A N   1 
ATOM   643  C CA  . GLY A 1 82  ? 29.173 37.278 64.493 1.00 30.41 ? 90  GLY A CA  1 
ATOM   644  C C   . GLY A 1 82  ? 28.063 38.305 64.477 1.00 31.47 ? 90  GLY A C   1 
ATOM   645  O O   . GLY A 1 82  ? 28.262 39.399 65.045 1.00 31.63 ? 90  GLY A O   1 
ATOM   646  N N   . SER A 1 83  ? 26.941 37.982 63.830 1.00 38.19 ? 91  SER A N   1 
ATOM   647  C CA  . SER A 1 83  ? 25.754 38.818 63.869 1.00 37.88 ? 91  SER A CA  1 
ATOM   648  C C   . SER A 1 83  ? 24.536 37.922 64.059 1.00 38.67 ? 91  SER A C   1 
ATOM   649  O O   . SER A 1 83  ? 24.539 36.773 63.621 1.00 37.25 ? 91  SER A O   1 
ATOM   650  C CB  . SER A 1 83  ? 25.615 39.642 62.593 1.00 37.50 ? 91  SER A CB  1 
ATOM   651  O OG  . SER A 1 83  ? 24.486 40.500 62.648 1.00 34.11 ? 91  SER A OG  1 
ATOM   652  N N   . ARG A 1 84  ? 23.501 38.465 64.710 1.00 31.67 ? 92  ARG A N   1 
ATOM   653  C CA  . ARG A 1 84  ? 22.236 37.769 64.876 1.00 30.50 ? 92  ARG A CA  1 
ATOM   654  C C   . ARG A 1 84  ? 21.644 37.352 63.529 1.00 30.18 ? 92  ARG A C   1 
ATOM   655  O O   . ARG A 1 84  ? 20.965 36.332 63.442 1.00 31.13 ? 92  ARG A O   1 
ATOM   656  C CB  . ARG A 1 84  ? 21.242 38.668 65.624 1.00 31.06 ? 92  ARG A CB  1 
ATOM   657  C CG  . ARG A 1 84  ? 20.789 39.830 64.777 1.00 36.28 ? 92  ARG A CG  1 
ATOM   658  C CD  . ARG A 1 84  ? 20.219 40.978 65.563 1.00 37.06 ? 92  ARG A CD  1 
ATOM   659  N NE  . ARG A 1 84  ? 19.740 42.043 64.688 1.00 43.23 ? 92  ARG A NE  1 
ATOM   660  C CZ  . ARG A 1 84  ? 20.186 42.282 63.460 1.00 37.84 ? 92  ARG A CZ  1 
ATOM   661  N NH1 . ARG A 1 84  ? 21.466 42.167 63.151 1.00 40.06 ? 92  ARG A NH1 1 
ATOM   662  N NH2 . ARG A 1 84  ? 19.333 42.709 62.534 1.00 43.45 ? 92  ARG A NH2 1 
ATOM   663  N N   . SER A 1 85  ? 21.905 38.151 62.485 1.00 30.82 ? 93  SER A N   1 
ATOM   664  C CA  . SER A 1 85  ? 21.338 37.906 61.168 1.00 31.33 ? 93  SER A CA  1 
ATOM   665  C C   . SER A 1 85  ? 22.058 36.812 60.380 1.00 27.07 ? 93  SER A C   1 
ATOM   666  O O   . SER A 1 85  ? 21.492 36.283 59.429 1.00 28.56 ? 93  SER A O   1 
ATOM   667  C CB  . SER A 1 85  ? 21.305 39.192 60.346 1.00 28.34 ? 93  SER A CB  1 
ATOM   668  O OG  . SER A 1 85  ? 22.607 39.651 60.030 1.00 33.28 ? 93  SER A OG  1 
ATOM   669  N N   . TRP A 1 86  ? 23.296 36.481 60.772 1.00 29.84 ? 94  TRP A N   1 
ATOM   670  C CA  . TRP A 1 86  ? 24.045 35.414 60.121 1.00 34.34 ? 94  TRP A CA  1 
ATOM   671  C C   . TRP A 1 86  ? 23.205 34.142 60.028 1.00 33.46 ? 94  TRP A C   1 
ATOM   672  O O   . TRP A 1 86  ? 22.606 33.728 61.019 1.00 34.02 ? 94  TRP A O   1 
ATOM   673  C CB  . TRP A 1 86  ? 25.364 35.088 60.858 1.00 32.41 ? 94  TRP A CB  1 
ATOM   674  C CG  . TRP A 1 86  ? 26.517 36.003 60.565 1.00 29.74 ? 94  TRP A CG  1 
ATOM   675  C CD1 . TRP A 1 86  ? 26.476 37.210 59.934 1.00 30.21 ? 94  TRP A CD1 1 
ATOM   676  C CD2 . TRP A 1 86  ? 27.894 35.758 60.877 1.00 28.19 ? 94  TRP A CD2 1 
ATOM   677  N NE1 . TRP A 1 86  ? 27.742 37.742 59.849 1.00 28.88 ? 94  TRP A NE1 1 
ATOM   678  C CE2 . TRP A 1 86  ? 28.633 36.869 60.419 1.00 27.79 ? 94  TRP A CE2 1 
ATOM   679  C CE3 . TRP A 1 86  ? 28.577 34.709 61.509 1.00 29.94 ? 94  TRP A CE3 1 
ATOM   680  C CZ2 . TRP A 1 86  ? 30.020 36.957 60.568 1.00 28.40 ? 94  TRP A CZ2 1 
ATOM   681  C CZ3 . TRP A 1 86  ? 29.950 34.798 61.656 1.00 30.85 ? 94  TRP A CZ3 1 
ATOM   682  C CH2 . TRP A 1 86  ? 30.657 35.911 61.189 1.00 29.83 ? 94  TRP A CH2 1 
ATOM   683  N N   . PRO A 1 87  ? 23.133 33.485 58.846 1.00 34.35 ? 95  PRO A N   1 
ATOM   684  C CA  . PRO A 1 87  ? 22.353 32.260 58.697 1.00 33.37 ? 95  PRO A CA  1 
ATOM   685  C C   . PRO A 1 87  ? 22.622 31.229 59.789 1.00 30.32 ? 95  PRO A C   1 
ATOM   686  O O   . PRO A 1 87  ? 21.692 30.636 60.328 1.00 28.46 ? 95  PRO A O   1 
ATOM   687  C CB  . PRO A 1 87  ? 22.774 31.751 57.316 1.00 32.57 ? 95  PRO A CB  1 
ATOM   688  C CG  . PRO A 1 87  ? 23.178 32.984 56.570 1.00 31.88 ? 95  PRO A CG  1 
ATOM   689  C CD  . PRO A 1 87  ? 23.791 33.898 57.595 1.00 35.85 ? 95  PRO A CD  1 
ATOM   690  N N   . HIS A 1 88  ? 23.905 31.037 60.111 1.00 33.62 ? 96  HIS A N   1 
ATOM   691  C CA  . HIS A 1 88  ? 24.327 30.110 61.148 1.00 35.36 ? 96  HIS A CA  1 
ATOM   692  C C   . HIS A 1 88  ? 23.568 30.314 62.460 1.00 35.80 ? 96  HIS A C   1 
ATOM   693  O O   . HIS A 1 88  ? 23.012 29.368 63.014 1.00 36.16 ? 96  HIS A O   1 
ATOM   694  C CB  . HIS A 1 88  ? 25.843 30.266 61.367 1.00 40.25 ? 96  HIS A CB  1 
ATOM   695  C CG  . HIS A 1 88  ? 26.407 29.427 62.472 1.00 46.39 ? 96  HIS A CG  1 
ATOM   696  N ND1 . HIS A 1 88  ? 26.411 28.049 62.400 1.00 56.44 ? 96  HIS A ND1 1 
ATOM   697  C CD2 . HIS A 1 88  ? 26.974 29.805 63.637 1.00 51.40 ? 96  HIS A CD2 1 
ATOM   698  C CE1 . HIS A 1 88  ? 26.973 27.627 63.523 1.00 58.63 ? 96  HIS A CE1 1 
ATOM   699  N NE2 . HIS A 1 88  ? 27.327 28.657 64.299 1.00 56.16 ? 96  HIS A NE2 1 
ATOM   700  N N   . PHE A 1 89  ? 23.549 31.561 62.944 1.00 36.01 ? 97  PHE A N   1 
ATOM   701  C CA  . PHE A 1 89  ? 22.941 31.883 64.225 1.00 35.11 ? 97  PHE A CA  1 
ATOM   702  C C   . PHE A 1 89  ? 21.422 32.017 64.130 1.00 37.11 ? 97  PHE A C   1 
ATOM   703  O O   . PHE A 1 89  ? 20.705 31.613 65.044 1.00 38.33 ? 97  PHE A O   1 
ATOM   704  C CB  . PHE A 1 89  ? 23.560 33.167 64.792 1.00 30.19 ? 97  PHE A CB  1 
ATOM   705  C CG  . PHE A 1 89  ? 25.015 33.023 65.168 1.00 29.83 ? 97  PHE A CG  1 
ATOM   706  C CD1 . PHE A 1 89  ? 25.429 32.025 66.035 1.00 33.27 ? 97  PHE A CD1 1 
ATOM   707  C CD2 . PHE A 1 89  ? 25.967 33.892 64.664 1.00 33.16 ? 97  PHE A CD2 1 
ATOM   708  C CE1 . PHE A 1 89  ? 26.771 31.893 66.380 1.00 33.11 ? 97  PHE A CE1 1 
ATOM   709  C CE2 . PHE A 1 89  ? 27.307 33.755 65.009 1.00 36.03 ? 97  PHE A CE2 1 
ATOM   710  C CZ  . PHE A 1 89  ? 27.701 32.756 65.864 1.00 33.27 ? 97  PHE A CZ  1 
ATOM   711  N N   . HIS A 1 90  ? 20.944 32.590 63.019 1.00 32.08 ? 98  HIS A N   1 
ATOM   712  C CA  . HIS A 1 90  ? 19.518 32.700 62.759 1.00 30.96 ? 98  HIS A CA  1 
ATOM   713  C C   . HIS A 1 90  ? 18.851 31.326 62.767 1.00 30.21 ? 98  HIS A C   1 
ATOM   714  O O   . HIS A 1 90  ? 17.804 31.143 63.385 1.00 25.48 ? 98  HIS A O   1 
ATOM   715  C CB  . HIS A 1 90  ? 19.267 33.408 61.416 1.00 27.22 ? 98  HIS A CB  1 
ATOM   716  C CG  . HIS A 1 90  ? 17.821 33.494 61.032 1.00 25.97 ? 98  HIS A CG  1 
ATOM   717  N ND1 . HIS A 1 90  ? 16.920 34.239 61.769 1.00 24.03 ? 98  HIS A ND1 1 
ATOM   718  C CD2 . HIS A 1 90  ? 17.167 32.921 59.999 1.00 23.94 ? 98  HIS A CD2 1 
ATOM   719  C CE1 . HIS A 1 90  ? 15.751 34.099 61.166 1.00 24.91 ? 98  HIS A CE1 1 
ATOM   720  N NE2 . HIS A 1 90  ? 15.856 33.308 60.094 1.00 24.30 ? 98  HIS A NE2 1 
ATOM   721  N N   . ASN A 1 91  ? 19.477 30.369 62.070 1.00 33.77 ? 99  ASN A N   1 
ATOM   722  C CA  . ASN A 1 91  ? 18.999 28.996 62.018 1.00 35.39 ? 99  ASN A CA  1 
ATOM   723  C C   . ASN A 1 91  ? 18.868 28.413 63.423 1.00 28.94 ? 99  ASN A C   1 
ATOM   724  O O   . ASN A 1 91  ? 17.865 27.782 63.747 1.00 26.86 ? 99  ASN A O   1 
ATOM   725  C CB  . ASN A 1 91  ? 19.943 28.133 61.162 1.00 39.16 ? 99  ASN A CB  1 
ATOM   726  C CG  . ASN A 1 91  ? 19.435 26.737 60.856 1.00 50.36 ? 99  ASN A CG  1 
ATOM   727  O OD1 . ASN A 1 91  ? 18.304 26.353 61.189 1.00 52.00 ? 99  ASN A OD1 1 
ATOM   728  N ND2 . ASN A 1 91  ? 20.270 25.942 60.194 1.00 53.46 ? 99  ASN A ND2 1 
ATOM   729  N N   . PHE A 1 92  ? 19.887 28.641 64.257 1.00 29.73 ? 100 PHE A N   1 
ATOM   730  C CA  . PHE A 1 92  ? 19.896 28.100 65.605 1.00 28.48 ? 100 PHE A CA  1 
ATOM   731  C C   . PHE A 1 92  ? 18.750 28.664 66.445 1.00 30.12 ? 100 PHE A C   1 
ATOM   732  O O   . PHE A 1 92  ? 18.153 27.940 67.238 1.00 29.93 ? 100 PHE A O   1 
ATOM   733  C CB  . PHE A 1 92  ? 21.244 28.367 66.285 1.00 27.72 ? 100 PHE A CB  1 
ATOM   734  C CG  . PHE A 1 92  ? 21.391 27.622 67.588 1.00 27.74 ? 100 PHE A CG  1 
ATOM   735  C CD1 . PHE A 1 92  ? 21.483 26.238 67.607 1.00 25.68 ? 100 PHE A CD1 1 
ATOM   736  C CD2 . PHE A 1 92  ? 21.403 28.300 68.796 1.00 26.70 ? 100 PHE A CD2 1 
ATOM   737  C CE1 . PHE A 1 92  ? 21.602 25.551 68.809 1.00 28.20 ? 100 PHE A CE1 1 
ATOM   738  C CE2 . PHE A 1 92  ? 21.521 27.609 69.996 1.00 29.27 ? 100 PHE A CE2 1 
ATOM   739  C CZ  . PHE A 1 92  ? 21.619 26.239 69.996 1.00 30.65 ? 100 PHE A CZ  1 
ATOM   740  N N   . CYS A 1 93  ? 18.447 29.955 66.257 1.00 28.84 ? 101 CYS A N   1 
ATOM   741  C CA  . CYS A 1 93  ? 17.370 30.612 66.983 1.00 27.80 ? 101 CYS A CA  1 
ATOM   742  C C   . CYS A 1 93  ? 15.987 30.156 66.516 1.00 28.10 ? 101 CYS A C   1 
ATOM   743  O O   . CYS A 1 93  ? 15.070 30.050 67.328 1.00 29.20 ? 101 CYS A O   1 
ATOM   744  C CB  . CYS A 1 93  ? 17.515 32.128 66.897 1.00 29.60 ? 101 CYS A CB  1 
ATOM   745  S SG  . CYS A 1 93  ? 18.910 32.790 67.848 1.00 27.70 ? 101 CYS A SG  1 
ATOM   746  N N   . LEU A 1 94  ? 15.841 29.893 65.211 1.00 29.29 ? 102 LEU A N   1 
ATOM   747  C CA  . LEU A 1 94  ? 14.643 29.253 64.690 1.00 29.20 ? 102 LEU A CA  1 
ATOM   748  C C   . LEU A 1 94  ? 14.388 27.944 65.433 1.00 28.08 ? 102 LEU A C   1 
ATOM   749  O O   . LEU A 1 94  ? 13.264 27.667 65.847 1.00 29.28 ? 102 LEU A O   1 
ATOM   750  C CB  . LEU A 1 94  ? 14.769 28.958 63.185 1.00 27.72 ? 102 LEU A CB  1 
ATOM   751  C CG  . LEU A 1 94  ? 14.741 30.159 62.248 1.00 29.53 ? 102 LEU A CG  1 
ATOM   752  C CD1 . LEU A 1 94  ? 14.882 29.718 60.807 1.00 26.50 ? 102 LEU A CD1 1 
ATOM   753  C CD2 . LEU A 1 94  ? 13.470 30.967 62.424 1.00 28.71 ? 102 LEU A CD2 1 
ATOM   754  N N   . THR A 1 95  ? 15.454 27.154 65.596 1.00 30.20 ? 103 THR A N   1 
ATOM   755  C CA  . THR A 1 95  ? 15.382 25.871 66.273 1.00 29.67 ? 103 THR A CA  1 
ATOM   756  C C   . THR A 1 95  ? 15.016 26.045 67.746 1.00 28.21 ? 103 THR A C   1 
ATOM   757  O O   . THR A 1 95  ? 14.083 25.405 68.229 1.00 22.57 ? 103 THR A O   1 
ATOM   758  C CB  . THR A 1 95  ? 16.709 25.129 66.080 1.00 29.80 ? 103 THR A CB  1 
ATOM   759  O OG1 . THR A 1 95  ? 16.979 25.024 64.683 1.00 30.72 ? 103 THR A OG1 1 
ATOM   760  C CG2 . THR A 1 95  ? 16.693 23.761 66.687 1.00 32.42 ? 103 THR A CG2 1 
ATOM   761  N N   . LEU A 1 96  ? 15.750 26.927 68.441 1.00 26.57 ? 104 LEU A N   1 
ATOM   762  C CA  . LEU A 1 96  ? 15.481 27.243 69.836 1.00 30.82 ? 104 LEU A CA  1 
ATOM   763  C C   . LEU A 1 96  ? 14.015 27.605 70.063 1.00 30.37 ? 104 LEU A C   1 
ATOM   764  O O   . LEU A 1 96  ? 13.370 27.069 70.962 1.00 28.88 ? 104 LEU A O   1 
ATOM   765  C CB  . LEU A 1 96  ? 16.353 28.422 70.302 1.00 33.19 ? 104 LEU A CB  1 
ATOM   766  C CG  . LEU A 1 96  ? 17.826 28.135 70.583 1.00 36.51 ? 104 LEU A CG  1 
ATOM   767  C CD1 . LEU A 1 96  ? 18.555 29.412 70.951 1.00 41.55 ? 104 LEU A CD1 1 
ATOM   768  C CD2 . LEU A 1 96  ? 17.998 27.116 71.694 1.00 35.39 ? 104 LEU A CD2 1 
ATOM   769  N N   . ALA A 1 97  ? 13.505 28.520 69.234 1.00 26.87 ? 105 ALA A N   1 
ATOM   770  C CA  . ALA A 1 97  ? 12.148 29.018 69.375 1.00 26.51 ? 105 ALA A CA  1 
ATOM   771  C C   . ALA A 1 97  ? 11.122 27.892 69.280 1.00 26.07 ? 105 ALA A C   1 
ATOM   772  O O   . ALA A 1 97  ? 10.282 27.741 70.163 1.00 28.16 ? 105 ALA A O   1 
ATOM   773  C CB  . ALA A 1 97  ? 11.870 30.082 68.321 1.00 25.72 ? 105 ALA A CB  1 
ATOM   774  N N   . SER A 1 98  ? 11.205 27.101 68.207 1.00 27.52 ? 106 SER A N   1 
ATOM   775  C CA  . SER A 1 98  ? 10.226 26.060 67.940 1.00 33.22 ? 106 SER A CA  1 
ATOM   776  C C   . SER A 1 98  ? 10.373 24.870 68.885 1.00 32.95 ? 106 SER A C   1 
ATOM   777  O O   . SER A 1 98  ? 9.379  24.351 69.390 1.00 35.21 ? 106 SER A O   1 
ATOM   778  C CB  . SER A 1 98  ? 10.326 25.595 66.489 1.00 32.20 ? 106 SER A CB  1 
ATOM   779  O OG  . SER A 1 98  ? 11.653 25.226 66.154 1.00 36.07 ? 106 SER A OG  1 
ATOM   780  N N   . SER A 1 99  ? 11.622 24.451 69.114 1.00 35.81 ? 107 SER A N   1 
ATOM   781  C CA  . SER A 1 99  ? 11.918 23.300 69.952 1.00 36.07 ? 107 SER A CA  1 
ATOM   782  C C   . SER A 1 99  ? 11.537 23.532 71.413 1.00 34.91 ? 107 SER A C   1 
ATOM   783  O O   . SER A 1 99  ? 10.894 22.687 72.029 1.00 31.05 ? 107 SER A O   1 
ATOM   784  C CB  . SER A 1 99  ? 13.397 22.945 69.849 1.00 38.58 ? 107 SER A CB  1 
ATOM   785  O OG  . SER A 1 99  ? 13.691 21.755 70.557 1.00 51.88 ? 107 SER A OG  1 
ATOM   786  N N   . LEU A 1 100 ? 11.928 24.694 71.952 1.00 37.98 ? 108 LEU A N   1 
ATOM   787  C CA  . LEU A 1 100 ? 11.675 25.029 73.345 1.00 32.24 ? 108 LEU A CA  1 
ATOM   788  C C   . LEU A 1 100 ? 10.319 25.701 73.557 1.00 30.59 ? 108 LEU A C   1 
ATOM   789  O O   . LEU A 1 100 ? 9.939  25.963 74.695 1.00 28.23 ? 108 LEU A O   1 
ATOM   790  C CB  . LEU A 1 100 ? 12.786 25.961 73.852 1.00 30.20 ? 108 LEU A CB  1 
ATOM   791  C CG  . LEU A 1 100 ? 14.214 25.459 73.642 1.00 31.02 ? 108 LEU A CG  1 
ATOM   792  C CD1 . LEU A 1 100 ? 15.224 26.497 74.060 1.00 33.71 ? 108 LEU A CD1 1 
ATOM   793  C CD2 . LEU A 1 100 ? 14.459 24.172 74.400 1.00 33.49 ? 108 LEU A CD2 1 
ATOM   794  N N   . ASN A 1 101 ? 9.598  25.964 72.457 1.00 31.01 ? 109 ASN A N   1 
ATOM   795  C CA  . ASN A 1 101 ? 8.359  26.727 72.484 1.00 36.25 ? 109 ASN A CA  1 
ATOM   796  C C   . ASN A 1 101 ? 8.526  27.991 73.326 1.00 35.33 ? 109 ASN A C   1 
ATOM   797  O O   . ASN A 1 101 ? 7.802  28.206 74.298 1.00 32.73 ? 109 ASN A O   1 
ATOM   798  C CB  . ASN A 1 101 ? 7.192  25.872 72.981 1.00 41.58 ? 109 ASN A CB  1 
ATOM   799  C CG  . ASN A 1 101 ? 6.896  24.696 72.083 1.00 53.87 ? 109 ASN A CG  1 
ATOM   800  O OD1 . ASN A 1 101 ? 6.926  23.540 72.514 1.00 65.62 ? 109 ASN A OD1 1 
ATOM   801  N ND2 . ASN A 1 101 ? 6.602  24.958 70.810 1.00 55.60 ? 109 ASN A ND2 1 
ATOM   802  N N   . ALA A 1 102 ? 9.497  28.819 72.924 1.00 28.10 ? 110 ALA A N   1 
ATOM   803  C CA  . ALA A 1 102 ? 9.868  30.008 73.670 1.00 28.88 ? 110 ALA A CA  1 
ATOM   804  C C   . ALA A 1 102 ? 10.052 31.201 72.739 1.00 29.29 ? 110 ALA A C   1 
ATOM   805  O O   . ALA A 1 102 ? 10.326 31.032 71.553 1.00 27.00 ? 110 ALA A O   1 
ATOM   806  C CB  . ALA A 1 102 ? 11.153 29.757 74.441 1.00 29.52 ? 110 ALA A CB  1 
ATOM   807  N N   . LEU A 1 103 ? 9.898  32.406 73.299 1.00 30.82 ? 111 LEU A N   1 
ATOM   808  C CA  . LEU A 1 103 ? 10.297 33.621 72.616 1.00 30.38 ? 111 LEU A CA  1 
ATOM   809  C C   . LEU A 1 103 ? 11.808 33.790 72.762 1.00 29.99 ? 111 LEU A C   1 
ATOM   810  O O   . LEU A 1 103 ? 12.317 33.850 73.879 1.00 27.94 ? 111 LEU A O   1 
ATOM   811  C CB  . LEU A 1 103 ? 9.597  34.846 73.195 1.00 32.99 ? 111 LEU A CB  1 
ATOM   812  C CG  . LEU A 1 103 ? 9.836  36.123 72.384 1.00 39.27 ? 111 LEU A CG  1 
ATOM   813  C CD1 . LEU A 1 103 ? 8.615  37.037 72.434 1.00 37.79 ? 111 LEU A CD1 1 
ATOM   814  C CD2 . LEU A 1 103 ? 11.112 36.802 72.823 1.00 40.55 ? 111 LEU A CD2 1 
ATOM   815  N N   . VAL A 1 104 ? 12.517 33.872 71.629 1.00 25.79 ? 112 VAL A N   1 
ATOM   816  C CA  . VAL A 1 104 ? 13.966 33.989 71.646 1.00 26.32 ? 112 VAL A CA  1 
ATOM   817  C C   . VAL A 1 104 ? 14.386 35.427 71.353 1.00 26.87 ? 112 VAL A C   1 
ATOM   818  O O   . VAL A 1 104 ? 13.849 36.065 70.448 1.00 22.20 ? 112 VAL A O   1 
ATOM   819  C CB  . VAL A 1 104 ? 14.624 32.997 70.660 1.00 29.82 ? 112 VAL A CB  1 
ATOM   820  C CG1 . VAL A 1 104 ? 16.148 33.137 70.665 1.00 26.87 ? 112 VAL A CG1 1 
ATOM   821  C CG2 . VAL A 1 104 ? 14.200 31.560 70.964 1.00 28.79 ? 112 VAL A CG2 1 
ATOM   822  N N   . VAL A 1 105 ? 15.350 35.923 72.139 1.00 25.62 ? 113 VAL A N   1 
ATOM   823  C CA  . VAL A 1 105 ? 15.940 37.232 71.923 1.00 28.86 ? 113 VAL A CA  1 
ATOM   824  C C   . VAL A 1 105 ? 17.402 37.037 71.531 1.00 28.60 ? 113 VAL A C   1 
ATOM   825  O O   . VAL A 1 105 ? 18.182 36.505 72.314 1.00 32.54 ? 113 VAL A O   1 
ATOM   826  C CB  . VAL A 1 105 ? 15.800 38.123 73.174 1.00 29.92 ? 113 VAL A CB  1 
ATOM   827  C CG1 . VAL A 1 105 ? 16.354 39.525 72.921 1.00 28.06 ? 113 VAL A CG1 1 
ATOM   828  C CG2 . VAL A 1 105 ? 14.349 38.181 73.643 1.00 31.69 ? 113 VAL A CG2 1 
ATOM   829  N N   . SER A 1 106 ? 17.756 37.463 70.312 1.00 29.43 ? 114 SER A N   1 
ATOM   830  C CA  . SER A 1 106 ? 19.103 37.288 69.792 1.00 32.52 ? 114 SER A CA  1 
ATOM   831  C C   . SER A 1 106 ? 19.730 38.643 69.474 1.00 28.38 ? 114 SER A C   1 
ATOM   832  O O   . SER A 1 106 ? 19.544 39.171 68.382 1.00 30.14 ? 114 SER A O   1 
ATOM   833  C CB  . SER A 1 106 ? 19.085 36.393 68.555 1.00 32.31 ? 114 SER A CB  1 
ATOM   834  O OG  . SER A 1 106 ? 20.398 36.058 68.132 1.00 31.43 ? 114 SER A OG  1 
ATOM   835  N N   . PRO A 1 107 ? 20.470 39.262 70.424 1.00 29.09 ? 115 PRO A N   1 
ATOM   836  C CA  . PRO A 1 107 ? 21.083 40.563 70.190 1.00 29.11 ? 115 PRO A CA  1 
ATOM   837  C C   . PRO A 1 107 ? 22.444 40.504 69.506 1.00 30.15 ? 115 PRO A C   1 
ATOM   838  O O   . PRO A 1 107 ? 23.222 39.576 69.725 1.00 29.26 ? 115 PRO A O   1 
ATOM   839  C CB  . PRO A 1 107 ? 21.227 41.119 71.603 1.00 27.57 ? 115 PRO A CB  1 
ATOM   840  C CG  . PRO A 1 107 ? 21.483 39.892 72.444 1.00 28.48 ? 115 PRO A CG  1 
ATOM   841  C CD  . PRO A 1 107 ? 20.709 38.762 71.789 1.00 28.51 ? 115 PRO A CD  1 
ATOM   842  N N   . ASP A 1 108 ? 22.712 41.520 68.679 1.00 29.11 ? 116 ASP A N   1 
ATOM   843  C CA  . ASP A 1 108 ? 24.069 41.886 68.319 1.00 27.92 ? 116 ASP A CA  1 
ATOM   844  C C   . ASP A 1 108 ? 24.718 42.519 69.544 1.00 30.36 ? 116 ASP A C   1 
ATOM   845  O O   . ASP A 1 108 ? 24.031 43.063 70.406 1.00 36.20 ? 116 ASP A O   1 
ATOM   846  C CB  . ASP A 1 108 ? 24.092 42.870 67.139 1.00 30.21 ? 116 ASP A CB  1 
ATOM   847  C CG  . ASP A 1 108 ? 23.830 42.254 65.776 1.00 34.54 ? 116 ASP A CG  1 
ATOM   848  O OD1 . ASP A 1 108 ? 24.048 41.036 65.622 1.00 33.70 ? 116 ASP A OD1 1 
ATOM   849  O OD2 . ASP A 1 108 ? 23.393 42.988 64.872 1.00 36.79 ? 116 ASP A OD2 1 
ATOM   850  N N   . TYR A 1 109 ? 26.047 42.417 69.616 1.00 26.04 ? 117 TYR A N   1 
ATOM   851  C CA  . TYR A 1 109 ? 26.825 43.171 70.580 1.00 26.12 ? 117 TYR A CA  1 
ATOM   852  C C   . TYR A 1 109 ? 28.074 43.692 69.878 1.00 27.58 ? 117 TYR A C   1 
ATOM   853  O O   . TYR A 1 109 ? 28.494 43.139 68.864 1.00 30.40 ? 117 TYR A O   1 
ATOM   854  C CB  . TYR A 1 109 ? 27.164 42.326 71.821 1.00 28.18 ? 117 TYR A CB  1 
ATOM   855  C CG  . TYR A 1 109 ? 27.777 40.970 71.542 1.00 28.25 ? 117 TYR A CG  1 
ATOM   856  C CD1 . TYR A 1 109 ? 26.981 39.864 71.274 1.00 27.46 ? 117 TYR A CD1 1 
ATOM   857  C CD2 . TYR A 1 109 ? 29.154 40.791 71.559 1.00 30.60 ? 117 TYR A CD2 1 
ATOM   858  C CE1 . TYR A 1 109 ? 27.540 38.612 71.030 1.00 25.75 ? 117 TYR A CE1 1 
ATOM   859  C CE2 . TYR A 1 109 ? 29.725 39.546 71.314 1.00 31.46 ? 117 TYR A CE2 1 
ATOM   860  C CZ  . TYR A 1 109 ? 28.915 38.457 71.051 1.00 31.15 ? 117 TYR A CZ  1 
ATOM   861  O OH  . TYR A 1 109 ? 29.489 37.230 70.811 1.00 28.47 ? 117 TYR A OH  1 
ATOM   862  N N   . ARG A 1 110 ? 28.632 44.788 70.403 1.00 29.30 ? 118 ARG A N   1 
ATOM   863  C CA  . ARG A 1 110 ? 29.828 45.405 69.771 1.00 31.22 ? 118 ARG A CA  1 
ATOM   864  C C   . ARG A 1 110 ? 30.988 44.401 69.814 1.00 29.66 ? 118 ARG A C   1 
ATOM   865  O O   . ARG A 1 110 ? 31.170 43.747 70.866 1.00 24.12 ? 118 ARG A O   1 
ATOM   866  C CB  . ARG A 1 110 ? 30.187 46.724 70.464 1.00 30.36 ? 118 ARG A CB  1 
ATOM   867  C CG  . ARG A 1 110 ? 29.468 47.914 69.846 1.00 31.57 ? 118 ARG A CG  1 
ATOM   868  C CD  . ARG A 1 110 ? 29.289 49.065 70.821 1.00 31.28 ? 118 ARG A CD  1 
ATOM   869  N NE  . ARG A 1 110 ? 29.205 48.615 72.214 1.00 31.29 ? 118 ARG A NE  1 
ATOM   870  C CZ  . ARG A 1 110 ? 29.902 49.143 73.212 1.00 29.13 ? 118 ARG A CZ  1 
ATOM   871  N NH1 . ARG A 1 110 ? 30.988 49.849 72.954 1.00 31.16 ? 118 ARG A NH1 1 
ATOM   872  N NH2 . ARG A 1 110 ? 29.512 48.961 74.461 1.00 29.56 ? 118 ARG A NH2 1 
ATOM   873  N N   . LEU A 1 111 ? 31.738 44.288 68.716 1.00 30.16 ? 119 LEU A N   1 
ATOM   874  C CA  . LEU A 1 111 ? 32.828 43.280 68.651 1.00 29.12 ? 119 LEU A CA  1 
ATOM   875  C C   . LEU A 1 111 ? 34.197 43.974 68.675 1.00 27.47 ? 119 LEU A C   1 
ATOM   876  O O   . LEU A 1 111 ? 34.263 45.182 68.358 1.00 31.63 ? 119 LEU A O   1 
ATOM   877  C CB  . LEU A 1 111 ? 32.655 42.427 67.396 1.00 27.67 ? 119 LEU A CB  1 
ATOM   878  C CG  . LEU A 1 111 ? 31.269 41.805 67.201 1.00 29.61 ? 119 LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 111 ? 31.030 41.453 65.745 1.00 30.42 ? 119 LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 111 ? 31.096 40.585 68.084 1.00 28.11 ? 119 LEU A CD2 1 
ATOM   881  N N   . ALA A 1 112 ? 35.244 43.229 69.036 1.00 27.69 ? 120 ALA A N   1 
ATOM   882  C CA  . ALA A 1 112 ? 36.619 43.778 69.063 1.00 33.07 ? 120 ALA A CA  1 
ATOM   883  C C   . ALA A 1 112 ? 37.275 43.523 67.702 1.00 33.17 ? 120 ALA A C   1 
ATOM   884  O O   . ALA A 1 112 ? 36.745 42.682 66.947 1.00 34.12 ? 120 ALA A O   1 
ATOM   885  C CB  . ALA A 1 112 ? 37.373 43.125 70.199 1.00 34.63 ? 120 ALA A CB  1 
ATOM   886  N N   . PRO A 1 113 ? 38.383 44.200 67.322 1.00 38.94 ? 121 PRO A N   1 
ATOM   887  C CA  . PRO A 1 113 ? 39.214 45.038 68.240 1.00 42.72 ? 121 PRO A CA  1 
ATOM   888  C C   . PRO A 1 113 ? 38.625 46.435 68.411 1.00 38.51 ? 121 PRO A C   1 
ATOM   889  O O   . PRO A 1 113 ? 38.981 47.097 69.411 1.00 36.24 ? 121 PRO A O   1 
ATOM   890  C CB  . PRO A 1 113 ? 40.592 45.038 67.585 1.00 42.27 ? 121 PRO A CB  1 
ATOM   891  C CG  . PRO A 1 113 ? 40.260 44.979 66.105 1.00 40.80 ? 121 PRO A CG  1 
ATOM   892  C CD  . PRO A 1 113 ? 38.999 44.183 65.957 1.00 40.32 ? 121 PRO A CD  1 
ATOM   893  N N   . GLU A 1 114 ? 37.759 46.879 67.492 1.00 33.89 ? 122 GLU A N   1 
ATOM   894  C CA  . GLU A 1 114 ? 37.263 48.273 67.605 1.00 35.63 ? 122 GLU A CA  1 
ATOM   895  C C   . GLU A 1 114 ? 36.716 48.511 69.010 1.00 34.71 ? 122 GLU A C   1 
ATOM   896  O O   . GLU A 1 114 ? 37.083 49.523 69.631 1.00 29.85 ? 122 GLU A O   1 
ATOM   897  C CB  . GLU A 1 114 ? 36.176 48.533 66.567 1.00 42.75 ? 122 GLU A CB  1 
ATOM   898  C CG  . GLU A 1 114 ? 35.675 49.973 66.545 1.00 49.01 ? 122 GLU A CG  1 
ATOM   899  C CD  . GLU A 1 114 ? 34.598 50.200 65.501 1.00 59.83 ? 122 GLU A CD  1 
ATOM   900  O OE1 . GLU A 1 114 ? 34.028 49.201 65.019 1.00 60.88 ? 122 GLU A OE1 1 
ATOM   901  O OE2 . GLU A 1 114 ? 34.328 51.372 65.168 1.00 62.37 ? 122 GLU A OE2 1 
ATOM   902  N N   . HIS A 1 115 ? 35.876 47.589 69.493 1.00 34.64 ? 123 HIS A N   1 
ATOM   903  C CA  . HIS A 1 115 ? 35.299 47.711 70.859 1.00 31.52 ? 123 HIS A CA  1 
ATOM   904  C C   . HIS A 1 115 ? 35.855 46.587 71.737 1.00 28.67 ? 123 HIS A C   1 
ATOM   905  O O   . HIS A 1 115 ? 35.269 45.483 71.758 1.00 33.97 ? 123 HIS A O   1 
ATOM   906  C CB  . HIS A 1 115 ? 33.769 47.666 70.807 1.00 31.21 ? 123 HIS A CB  1 
ATOM   907  C CG  . HIS A 1 115 ? 33.196 48.209 69.544 1.00 31.48 ? 123 HIS A CG  1 
ATOM   908  N ND1 . HIS A 1 115 ? 32.888 47.414 68.462 1.00 32.23 ? 123 HIS A ND1 1 
ATOM   909  C CD2 . HIS A 1 115 ? 32.874 49.458 69.192 1.00 29.72 ? 123 HIS A CD2 1 
ATOM   910  C CE1 . HIS A 1 115 ? 32.395 48.170 67.494 1.00 31.51 ? 123 HIS A CE1 1 
ATOM   911  N NE2 . HIS A 1 115 ? 32.378 49.415 67.915 1.00 33.01 ? 123 HIS A NE2 1 
ATOM   912  N N   . ARG A 1 116 ? 36.949 46.866 72.449 1.00 27.11 ? 124 ARG A N   1 
ATOM   913  C CA  . ARG A 1 116 ? 37.589 45.835 73.306 1.00 26.76 ? 124 ARG A CA  1 
ATOM   914  C C   . ARG A 1 116 ? 36.698 45.532 74.521 1.00 27.38 ? 124 ARG A C   1 
ATOM   915  O O   . ARG A 1 116 ? 35.953 46.438 74.956 1.00 24.18 ? 124 ARG A O   1 
ATOM   916  C CB  . ARG A 1 116 ? 38.970 46.317 73.762 1.00 26.11 ? 124 ARG A CB  1 
ATOM   917  C CG  . ARG A 1 116 ? 40.082 46.018 72.768 1.00 28.32 ? 124 ARG A CG  1 
ATOM   918  C CD  . ARG A 1 116 ? 41.391 46.654 73.204 1.00 29.36 ? 124 ARG A CD  1 
ATOM   919  N NE  . ARG A 1 116 ? 42.462 46.461 72.221 1.00 32.26 ? 124 ARG A NE  1 
ATOM   920  C CZ  . ARG A 1 116 ? 42.828 45.284 71.734 1.00 29.80 ? 124 ARG A CZ  1 
ATOM   921  N NH1 . ARG A 1 116 ? 43.207 44.320 72.553 1.00 28.60 ? 124 ARG A NH1 1 
ATOM   922  N NH2 . ARG A 1 116 ? 42.813 45.074 70.429 1.00 30.56 ? 124 ARG A NH2 1 
ATOM   923  N N   . LEU A 1 117 ? 36.783 44.309 75.052 1.00 30.32 ? 125 LEU A N   1 
ATOM   924  C CA  . LEU A 1 117 ? 36.000 43.932 76.258 1.00 31.39 ? 125 LEU A CA  1 
ATOM   925  C C   . LEU A 1 117 ? 36.256 44.961 77.370 1.00 31.58 ? 125 LEU A C   1 
ATOM   926  O O   . LEU A 1 117 ? 37.437 45.317 77.582 1.00 34.97 ? 125 LEU A O   1 
ATOM   927  C CB  . LEU A 1 117 ? 36.420 42.531 76.691 1.00 32.13 ? 125 LEU A CB  1 
ATOM   928  C CG  . LEU A 1 117 ? 35.689 41.371 76.010 1.00 33.69 ? 125 LEU A CG  1 
ATOM   929  C CD1 . LEU A 1 117 ? 36.023 40.074 76.724 1.00 31.91 ? 125 LEU A CD1 1 
ATOM   930  C CD2 . LEU A 1 117 ? 34.192 41.622 76.016 1.00 32.83 ? 125 LEU A CD2 1 
ATOM   931  N N   . PRO A 1 118 ? 35.226 45.435 78.108 1.00 30.14 ? 126 PRO A N   1 
ATOM   932  C CA  . PRO A 1 118 ? 33.973 44.681 78.383 1.00 31.96 ? 126 PRO A CA  1 
ATOM   933  C C   . PRO A 1 118 ? 32.799 45.230 77.582 1.00 31.26 ? 126 PRO A C   1 
ATOM   934  O O   . PRO A 1 118 ? 31.646 45.125 78.058 1.00 38.49 ? 126 PRO A O   1 
ATOM   935  C CB  . PRO A 1 118 ? 33.764 44.948 79.864 1.00 29.61 ? 126 PRO A CB  1 
ATOM   936  C CG  . PRO A 1 118 ? 34.228 46.396 79.995 1.00 26.68 ? 126 PRO A CG  1 
ATOM   937  C CD  . PRO A 1 118 ? 35.196 46.711 78.885 1.00 25.11 ? 126 PRO A CD  1 
ATOM   938  N N   . ALA A 1 119 ? 33.068 45.802 76.405 1.00 28.08 ? 127 ALA A N   1 
ATOM   939  C CA  . ALA A 1 119 ? 31.994 46.398 75.574 1.00 28.70 ? 127 ALA A CA  1 
ATOM   940  C C   . ALA A 1 119 ? 30.815 45.428 75.480 1.00 29.11 ? 127 ALA A C   1 
ATOM   941  O O   . ALA A 1 119 ? 29.668 45.837 75.763 1.00 28.96 ? 127 ALA A O   1 
ATOM   942  C CB  . ALA A 1 119 ? 32.536 46.734 74.204 1.00 27.29 ? 127 ALA A CB  1 
ATOM   943  N N   . ALA A 1 120 ? 31.091 44.181 75.092 1.00 30.27 ? 128 ALA A N   1 
ATOM   944  C CA  . ALA A 1 120 ? 30.020 43.169 74.936 1.00 27.06 ? 128 ALA A CA  1 
ATOM   945  C C   . ALA A 1 120 ? 29.223 43.028 76.234 1.00 30.04 ? 128 ALA A C   1 
ATOM   946  O O   . ALA A 1 120 ? 27.983 42.909 76.158 1.00 27.75 ? 128 ALA A O   1 
ATOM   947  C CB  . ALA A 1 120 ? 30.633 41.848 74.533 1.00 25.48 ? 128 ALA A CB  1 
ATOM   948  N N   . PHE A 1 121 ? 29.901 43.040 77.385 1.00 31.41 ? 129 PHE A N   1 
ATOM   949  C CA  . PHE A 1 121 ? 29.199 42.803 78.636 1.00 30.03 ? 129 PHE A CA  1 
ATOM   950  C C   . PHE A 1 121 ? 28.249 43.955 78.955 1.00 31.95 ? 129 PHE A C   1 
ATOM   951  O O   . PHE A 1 121 ? 27.132 43.730 79.417 1.00 33.61 ? 129 PHE A O   1 
ATOM   952  C CB  . PHE A 1 121 ? 30.199 42.578 79.781 1.00 27.29 ? 129 PHE A CB  1 
ATOM   953  C CG  . PHE A 1 121 ? 31.202 41.482 79.506 1.00 27.26 ? 129 PHE A CG  1 
ATOM   954  C CD1 . PHE A 1 121 ? 30.809 40.292 78.915 1.00 26.85 ? 129 PHE A CD1 1 
ATOM   955  C CD2 . PHE A 1 121 ? 32.536 41.638 79.844 1.00 26.58 ? 129 PHE A CD2 1 
ATOM   956  C CE1 . PHE A 1 121 ? 31.734 39.286 78.660 1.00 28.51 ? 129 PHE A CE1 1 
ATOM   957  C CE2 . PHE A 1 121 ? 33.454 40.626 79.591 1.00 26.21 ? 129 PHE A CE2 1 
ATOM   958  C CZ  . PHE A 1 121 ? 33.049 39.459 79.003 1.00 26.98 ? 129 PHE A CZ  1 
ATOM   959  N N   . GLU A 1 122 ? 28.705 45.185 78.695 1.00 32.84 ? 130 GLU A N   1 
ATOM   960  C CA  . GLU A 1 122 ? 27.868 46.365 78.828 1.00 39.06 ? 130 GLU A CA  1 
ATOM   961  C C   . GLU A 1 122 ? 26.631 46.254 77.936 1.00 37.43 ? 130 GLU A C   1 
ATOM   962  O O   . GLU A 1 122 ? 25.519 46.543 78.370 1.00 33.51 ? 130 GLU A O   1 
ATOM   963  C CB  . GLU A 1 122 ? 28.689 47.615 78.479 1.00 45.74 ? 130 GLU A CB  1 
ATOM   964  C CG  . GLU A 1 122 ? 27.920 48.920 78.547 1.00 59.61 ? 130 GLU A CG  1 
ATOM   965  C CD  . GLU A 1 122 ? 28.702 50.121 78.054 1.00 62.06 ? 130 GLU A CD  1 
ATOM   966  O OE1 . GLU A 1 122 ? 29.920 49.978 77.795 1.00 54.49 ? 130 GLU A OE1 1 
ATOM   967  O OE2 . GLU A 1 122 ? 28.089 51.203 77.911 1.00 65.45 ? 130 GLU A OE2 1 
ATOM   968  N N   . ASP A 1 123 ? 26.842 45.817 76.689 1.00 34.71 ? 131 ASP A N   1 
ATOM   969  C CA  . ASP A 1 123 ? 25.764 45.659 75.729 1.00 31.62 ? 131 ASP A CA  1 
ATOM   970  C C   . ASP A 1 123 ? 24.775 44.577 76.157 1.00 32.73 ? 131 ASP A C   1 
ATOM   971  O O   . ASP A 1 123 ? 23.569 44.738 75.983 1.00 32.50 ? 131 ASP A O   1 
ATOM   972  C CB  . ASP A 1 123 ? 26.337 45.339 74.341 1.00 32.21 ? 131 ASP A CB  1 
ATOM   973  C CG  . ASP A 1 123 ? 27.158 46.458 73.730 1.00 31.15 ? 131 ASP A CG  1 
ATOM   974  O OD1 . ASP A 1 123 ? 27.183 47.564 74.310 1.00 34.98 ? 131 ASP A OD1 1 
ATOM   975  O OD2 . ASP A 1 123 ? 27.787 46.226 72.678 1.00 32.53 ? 131 ASP A OD2 1 
ATOM   976  N N   . ALA A 1 124 ? 25.293 43.480 76.722 1.00 30.88 ? 132 ALA A N   1 
ATOM   977  C CA  . ALA A 1 124 ? 24.447 42.396 77.196 1.00 29.71 ? 132 ALA A CA  1 
ATOM   978  C C   . ALA A 1 124 ? 23.503 42.874 78.297 1.00 32.29 ? 132 ALA A C   1 
ATOM   979  O O   . ALA A 1 124 ? 22.346 42.463 78.341 1.00 29.22 ? 132 ALA A O   1 
ATOM   980  C CB  . ALA A 1 124 ? 25.293 41.236 77.689 1.00 28.15 ? 132 ALA A CB  1 
ATOM   981  N N   . GLU A 1 125 ? 24.003 43.744 79.184 1.00 33.47 ? 133 GLU A N   1 
ATOM   982  C CA  . GLU A 1 125 ? 23.171 44.339 80.218 1.00 30.65 ? 133 GLU A CA  1 
ATOM   983  C C   . GLU A 1 125 ? 22.118 45.272 79.624 1.00 26.25 ? 133 GLU A C   1 
ATOM   984  O O   . GLU A 1 125 ? 21.010 45.364 80.146 1.00 27.84 ? 133 GLU A O   1 
ATOM   985  C CB  . GLU A 1 125 ? 24.013 45.106 81.243 1.00 27.92 ? 133 GLU A CB  1 
ATOM   986  C CG  . GLU A 1 125 ? 24.829 44.207 82.148 1.00 31.55 ? 133 GLU A CG  1 
ATOM   987  C CD  . GLU A 1 125 ? 25.484 44.908 83.322 1.00 35.24 ? 133 GLU A CD  1 
ATOM   988  O OE1 . GLU A 1 125 ? 25.088 46.053 83.640 1.00 38.00 ? 133 GLU A OE1 1 
ATOM   989  O OE2 . GLU A 1 125 ? 26.405 44.310 83.923 1.00 35.07 ? 133 GLU A OE2 1 
ATOM   990  N N   . ALA A 1 126 ? 22.477 45.969 78.540 1.00 22.65 ? 134 ALA A N   1 
ATOM   991  C CA  . ALA A 1 126 ? 21.541 46.847 77.856 1.00 23.11 ? 134 ALA A CA  1 
ATOM   992  C C   . ALA A 1 126 ? 20.369 46.061 77.267 1.00 26.34 ? 134 ALA A C   1 
ATOM   993  O O   . ALA A 1 126 ? 19.240 46.549 77.261 1.00 26.26 ? 134 ALA A O   1 
ATOM   994  C CB  . ALA A 1 126 ? 22.253 47.644 76.774 1.00 20.22 ? 134 ALA A CB  1 
ATOM   995  N N   . VAL A 1 127 ? 20.650 44.842 76.782 1.00 28.00 ? 135 VAL A N   1 
ATOM   996  C CA  . VAL A 1 127 ? 19.623 43.940 76.281 1.00 25.88 ? 135 VAL A CA  1 
ATOM   997  C C   . VAL A 1 127 ? 18.633 43.591 77.389 1.00 24.95 ? 135 VAL A C   1 
ATOM   998  O O   . VAL A 1 127 ? 17.427 43.711 77.201 1.00 22.99 ? 135 VAL A O   1 
ATOM   999  C CB  . VAL A 1 127 ? 20.244 42.653 75.671 1.00 26.39 ? 135 VAL A CB  1 
ATOM   1000 C CG1 . VAL A 1 127 ? 19.183 41.588 75.389 1.00 26.71 ? 135 VAL A CG1 1 
ATOM   1001 C CG2 . VAL A 1 127 ? 21.040 42.970 74.409 1.00 26.21 ? 135 VAL A CG2 1 
ATOM   1002 N N   . LEU A 1 128 ? 19.161 43.150 78.537 1.00 28.43 ? 136 LEU A N   1 
ATOM   1003 C CA  . LEU A 1 128 ? 18.337 42.810 79.687 1.00 29.03 ? 136 LEU A CA  1 
ATOM   1004 C C   . LEU A 1 128 ? 17.550 44.016 80.194 1.00 29.02 ? 136 LEU A C   1 
ATOM   1005 O O   . LEU A 1 128 ? 16.382 43.882 80.551 1.00 32.77 ? 136 LEU A O   1 
ATOM   1006 C CB  . LEU A 1 128 ? 19.206 42.226 80.816 1.00 27.65 ? 136 LEU A CB  1 
ATOM   1007 C CG  . LEU A 1 128 ? 19.392 40.708 80.791 1.00 28.76 ? 136 LEU A CG  1 
ATOM   1008 C CD1 . LEU A 1 128 ? 18.081 39.988 81.034 1.00 32.34 ? 136 LEU A CD1 1 
ATOM   1009 C CD2 . LEU A 1 128 ? 19.985 40.241 79.484 1.00 31.54 ? 136 LEU A CD2 1 
ATOM   1010 N N   . THR A 1 129 ? 18.196 45.186 80.218 1.00 28.59 ? 137 THR A N   1 
ATOM   1011 C CA  . THR A 1 129 ? 17.528 46.427 80.577 1.00 28.21 ? 137 THR A CA  1 
ATOM   1012 C C   . THR A 1 129 ? 16.427 46.772 79.577 1.00 25.43 ? 137 THR A C   1 
ATOM   1013 O O   . THR A 1 129 ? 15.365 47.249 79.969 1.00 26.30 ? 137 THR A O   1 
ATOM   1014 C CB  . THR A 1 129 ? 18.543 47.558 80.701 1.00 29.25 ? 137 THR A CB  1 
ATOM   1015 O OG1 . THR A 1 129 ? 19.394 47.268 81.808 1.00 31.56 ? 137 THR A OG1 1 
ATOM   1016 C CG2 . THR A 1 129 ? 17.889 48.913 80.904 1.00 29.89 ? 137 THR A CG2 1 
ATOM   1017 N N   . TRP A 1 130 ? 16.692 46.531 78.289 1.00 26.06 ? 138 TRP A N   1 
ATOM   1018 C CA  . TRP A 1 130 ? 15.699 46.748 77.250 1.00 24.34 ? 138 TRP A CA  1 
ATOM   1019 C C   . TRP A 1 130 ? 14.479 45.857 77.475 1.00 24.83 ? 138 TRP A C   1 
ATOM   1020 O O   . TRP A 1 130 ? 13.349 46.323 77.351 1.00 25.80 ? 138 TRP A O   1 
ATOM   1021 C CB  . TRP A 1 130 ? 16.293 46.496 75.859 1.00 27.26 ? 138 TRP A CB  1 
ATOM   1022 C CG  . TRP A 1 130 ? 15.327 46.717 74.735 1.00 27.57 ? 138 TRP A CG  1 
ATOM   1023 C CD1 . TRP A 1 130 ? 15.044 47.896 74.114 1.00 27.83 ? 138 TRP A CD1 1 
ATOM   1024 C CD2 . TRP A 1 130 ? 14.491 45.729 74.122 1.00 25.64 ? 138 TRP A CD2 1 
ATOM   1025 N NE1 . TRP A 1 130 ? 14.098 47.700 73.137 1.00 26.76 ? 138 TRP A NE1 1 
ATOM   1026 C CE2 . TRP A 1 130 ? 13.738 46.378 73.123 1.00 25.34 ? 138 TRP A CE2 1 
ATOM   1027 C CE3 . TRP A 1 130 ? 14.308 44.355 74.319 1.00 27.06 ? 138 TRP A CE3 1 
ATOM   1028 C CZ2 . TRP A 1 130 ? 12.822 45.700 72.321 1.00 25.06 ? 138 TRP A CZ2 1 
ATOM   1029 C CZ3 . TRP A 1 130 ? 13.400 43.685 73.523 1.00 27.92 ? 138 TRP A CZ3 1 
ATOM   1030 C CH2 . TRP A 1 130 ? 12.670 44.356 72.538 1.00 26.34 ? 138 TRP A CH2 1 
ATOM   1031 N N   . LEU A 1 131 ? 14.722 44.580 77.803 1.00 25.61 ? 139 LEU A N   1 
ATOM   1032 C CA  . LEU A 1 131 ? 13.656 43.639 78.116 1.00 29.82 ? 139 LEU A CA  1 
ATOM   1033 C C   . LEU A 1 131 ? 12.806 44.117 79.289 1.00 25.80 ? 139 LEU A C   1 
ATOM   1034 O O   . LEU A 1 131 ? 11.580 44.036 79.240 1.00 25.18 ? 139 LEU A O   1 
ATOM   1035 C CB  . LEU A 1 131 ? 14.217 42.247 78.451 1.00 33.47 ? 139 LEU A CB  1 
ATOM   1036 C CG  . LEU A 1 131 ? 14.531 41.345 77.272 1.00 44.49 ? 139 LEU A CG  1 
ATOM   1037 C CD1 . LEU A 1 131 ? 15.097 40.024 77.747 1.00 49.77 ? 139 LEU A CD1 1 
ATOM   1038 C CD2 . LEU A 1 131 ? 13.296 41.103 76.412 1.00 45.61 ? 139 LEU A CD2 1 
ATOM   1039 N N   . TRP A 1 132 ? 13.474 44.598 80.344 1.00 25.64 ? 140 TRP A N   1 
ATOM   1040 C CA  . TRP A 1 132 ? 12.783 45.178 81.484 1.00 27.97 ? 140 TRP A CA  1 
ATOM   1041 C C   . TRP A 1 132 ? 11.860 46.310 81.036 1.00 28.99 ? 140 TRP A C   1 
ATOM   1042 O O   . TRP A 1 132 ? 10.690 46.349 81.413 1.00 25.62 ? 140 TRP A O   1 
ATOM   1043 C CB  . TRP A 1 132 ? 13.775 45.697 82.530 1.00 25.47 ? 140 TRP A CB  1 
ATOM   1044 C CG  . TRP A 1 132 ? 13.102 46.398 83.664 1.00 24.32 ? 140 TRP A CG  1 
ATOM   1045 C CD1 . TRP A 1 132 ? 12.536 45.828 84.765 1.00 26.86 ? 140 TRP A CD1 1 
ATOM   1046 C CD2 . TRP A 1 132 ? 12.871 47.805 83.775 1.00 22.92 ? 140 TRP A CD2 1 
ATOM   1047 N NE1 . TRP A 1 132 ? 11.990 46.797 85.572 1.00 26.59 ? 140 TRP A NE1 1 
ATOM   1048 C CE2 . TRP A 1 132 ? 12.180 48.022 84.986 1.00 25.25 ? 140 TRP A CE2 1 
ATOM   1049 C CE3 . TRP A 1 132 ? 13.192 48.907 82.973 1.00 22.20 ? 140 TRP A CE3 1 
ATOM   1050 C CZ2 . TRP A 1 132 ? 11.807 49.297 85.411 1.00 21.68 ? 140 TRP A CZ2 1 
ATOM   1051 C CZ3 . TRP A 1 132 ? 12.823 50.169 83.396 1.00 22.65 ? 140 TRP A CZ3 1 
ATOM   1052 C CH2 . TRP A 1 132 ? 12.138 50.355 84.601 1.00 23.11 ? 140 TRP A CH2 1 
ATOM   1053 N N   . ASP A 1 133 ? 12.407 47.221 80.224 1.00 29.09 ? 141 ASP A N   1 
ATOM   1054 C CA  . ASP A 1 133 ? 11.660 48.366 79.730 1.00 30.34 ? 141 ASP A CA  1 
ATOM   1055 C C   . ASP A 1 133 ? 10.394 47.910 79.006 1.00 28.39 ? 141 ASP A C   1 
ATOM   1056 O O   . ASP A 1 133 ? 9.315  48.456 79.232 1.00 24.09 ? 141 ASP A O   1 
ATOM   1057 C CB  . ASP A 1 133 ? 12.546 49.218 78.803 1.00 34.21 ? 141 ASP A CB  1 
ATOM   1058 C CG  . ASP A 1 133 ? 12.189 50.687 78.793 1.00 42.89 ? 141 ASP A CG  1 
ATOM   1059 O OD1 . ASP A 1 133 ? 11.043 51.016 78.427 1.00 56.06 ? 141 ASP A OD1 1 
ATOM   1060 O OD2 . ASP A 1 133 ? 13.053 51.508 79.163 1.00 49.49 ? 141 ASP A OD2 1 
ATOM   1061 N N   . GLN A 1 134 ? 10.538 46.888 78.153 1.00 26.13 ? 142 GLN A N   1 
ATOM   1062 C CA  . GLN A 1 134 ? 9.425  46.333 77.400 1.00 26.25 ? 142 GLN A CA  1 
ATOM   1063 C C   . GLN A 1 134 ? 8.391  45.655 78.297 1.00 26.24 ? 142 GLN A C   1 
ATOM   1064 O O   . GLN A 1 134 ? 7.189  45.776 78.065 1.00 26.38 ? 142 GLN A O   1 
ATOM   1065 C CB  . GLN A 1 134 ? 9.938  45.319 76.367 1.00 28.64 ? 142 GLN A CB  1 
ATOM   1066 C CG  . GLN A 1 134 ? 10.863 45.908 75.310 1.00 27.77 ? 142 GLN A CG  1 
ATOM   1067 C CD  . GLN A 1 134 ? 10.175 46.940 74.467 1.00 27.48 ? 142 GLN A CD  1 
ATOM   1068 O OE1 . GLN A 1 134 ? 9.121  46.691 73.880 1.00 29.94 ? 142 GLN A OE1 1 
ATOM   1069 N NE2 . GLN A 1 134 ? 10.750 48.124 74.393 1.00 30.37 ? 142 GLN A NE2 1 
ATOM   1070 N N   . ALA A 1 135 ? 8.870  44.934 79.317 1.00 23.56 ? 143 ALA A N   1 
ATOM   1071 C CA  . ALA A 1 135 ? 7.999  44.215 80.232 1.00 25.25 ? 143 ALA A CA  1 
ATOM   1072 C C   . ALA A 1 135 ? 7.090  45.141 81.040 1.00 25.39 ? 143 ALA A C   1 
ATOM   1073 O O   . ALA A 1 135 ? 5.900  44.873 81.178 1.00 28.40 ? 143 ALA A O   1 
ATOM   1074 C CB  . ALA A 1 135 ? 8.835  43.359 81.170 1.00 27.88 ? 143 ALA A CB  1 
ATOM   1075 N N   . VAL A 1 136 ? 7.658  46.232 81.566 1.00 26.00 ? 144 VAL A N   1 
ATOM   1076 C CA  . VAL A 1 136 ? 6.936  47.130 82.456 1.00 24.61 ? 144 VAL A CA  1 
ATOM   1077 C C   . VAL A 1 136 ? 6.052  48.143 81.731 1.00 24.51 ? 144 VAL A C   1 
ATOM   1078 O O   . VAL A 1 136 ? 5.183  48.752 82.349 1.00 23.32 ? 144 VAL A O   1 
ATOM   1079 C CB  . VAL A 1 136 ? 7.913  47.866 83.406 1.00 25.56 ? 144 VAL A CB  1 
ATOM   1080 C CG1 . VAL A 1 136 ? 8.741  46.873 84.214 1.00 26.24 ? 144 VAL A CG1 1 
ATOM   1081 C CG2 . VAL A 1 136 ? 8.810  48.847 82.654 1.00 27.20 ? 144 VAL A CG2 1 
ATOM   1082 N N   . SER A 1 137 ? 6.275  48.326 80.424 1.00 30.01 ? 145 SER A N   1 
ATOM   1083 C CA  . SER A 1 137 ? 5.515  49.288 79.641 1.00 31.45 ? 145 SER A CA  1 
ATOM   1084 C C   . SER A 1 137 ? 4.535  48.650 78.657 1.00 35.57 ? 145 SER A C   1 
ATOM   1085 O O   . SER A 1 137 ? 3.911  49.356 77.868 1.00 36.36 ? 145 SER A O   1 
ATOM   1086 C CB  . SER A 1 137 ? 6.467  50.192 78.873 1.00 30.41 ? 145 SER A CB  1 
ATOM   1087 O OG  . SER A 1 137 ? 7.155  49.469 77.866 1.00 36.81 ? 145 SER A OG  1 
ATOM   1088 N N   . ASP A 1 138 ? 4.407  47.317 78.715 1.00 44.27 ? 146 ASP A N   1 
ATOM   1089 C CA  . ASP A 1 138 ? 3.597  46.558 77.773 1.00 52.54 ? 146 ASP A CA  1 
ATOM   1090 C C   . ASP A 1 138 ? 3.959  46.881 76.323 1.00 50.22 ? 146 ASP A C   1 
ATOM   1091 O O   . ASP A 1 138 ? 3.083  47.023 75.471 1.00 44.37 ? 146 ASP A O   1 
ATOM   1092 C CB  . ASP A 1 138 ? 2.093  46.793 78.036 1.00 60.62 ? 146 ASP A CB  1 
ATOM   1093 C CG  . ASP A 1 138 ? 1.611  46.341 79.405 1.00 68.52 ? 146 ASP A CG  1 
ATOM   1094 O OD1 . ASP A 1 138 ? 2.425  45.762 80.164 1.00 62.24 ? 146 ASP A OD1 1 
ATOM   1095 O OD2 . ASP A 1 138 ? 0.422  46.566 79.720 1.00 63.87 ? 146 ASP A OD2 1 
ATOM   1096 N N   . GLY A 1 139 ? 5.267  46.981 76.055 1.00 49.87 ? 147 GLY A N   1 
ATOM   1097 C CA  . GLY A 1 139 ? 5.777  47.108 74.700 1.00 45.53 ? 147 GLY A CA  1 
ATOM   1098 C C   . GLY A 1 139 ? 5.750  45.783 73.941 1.00 43.29 ? 147 GLY A C   1 
ATOM   1099 O O   . GLY A 1 139 ? 5.913  45.763 72.723 1.00 42.57 ? 147 GLY A O   1 
ATOM   1100 N N   . VAL A 1 140 ? 5.546  44.685 74.681 1.00 41.44 ? 148 VAL A N   1 
ATOM   1101 C CA  . VAL A 1 140 ? 5.431  43.350 74.115 1.00 40.91 ? 148 VAL A CA  1 
ATOM   1102 C C   . VAL A 1 140 ? 4.306  43.235 73.088 1.00 43.23 ? 148 VAL A C   1 
ATOM   1103 O O   . VAL A 1 140 ? 4.450  42.532 72.090 1.00 44.51 ? 148 VAL A O   1 
ATOM   1104 C CB  . VAL A 1 140 ? 5.256  42.324 75.262 1.00 41.54 ? 148 VAL A CB  1 
ATOM   1105 C CG1 . VAL A 1 140 ? 4.782  40.971 74.748 1.00 47.02 ? 148 VAL A CG1 1 
ATOM   1106 C CG2 . VAL A 1 140 ? 6.543  42.176 76.060 1.00 40.35 ? 148 VAL A CG2 1 
ATOM   1107 N N   . ASN A 1 141 ? 3.189  43.930 73.337 1.00 48.31 ? 149 ASN A N   1 
ATOM   1108 C CA  . ASN A 1 141 ? 2.055  43.913 72.425 1.00 54.25 ? 149 ASN A CA  1 
ATOM   1109 C C   . ASN A 1 141 ? 2.338  44.590 71.083 1.00 48.37 ? 149 ASN A C   1 
ATOM   1110 O O   . ASN A 1 141 ? 1.590  44.392 70.128 1.00 48.13 ? 149 ASN A O   1 
ATOM   1111 C CB  . ASN A 1 141 ? 0.831  44.559 73.086 1.00 55.96 ? 149 ASN A CB  1 
ATOM   1112 C CG  . ASN A 1 141 ? 0.257  43.726 74.202 1.00 64.09 ? 149 ASN A CG  1 
ATOM   1113 O OD1 . ASN A 1 141 ? 0.219  44.144 75.362 1.00 69.70 ? 149 ASN A OD1 1 
ATOM   1114 N ND2 . ASN A 1 141 ? -0.198 42.521 73.875 1.00 63.16 ? 149 ASN A ND2 1 
ATOM   1115 N N   . HIS A 1 142 ? 3.413  45.388 71.022 1.00 39.54 ? 150 HIS A N   1 
ATOM   1116 C CA  . HIS A 1 142 ? 3.823  46.048 69.793 1.00 39.44 ? 150 HIS A CA  1 
ATOM   1117 C C   . HIS A 1 142 ? 5.084  45.434 69.184 1.00 39.25 ? 150 HIS A C   1 
ATOM   1118 O O   . HIS A 1 142 ? 5.654  45.993 68.249 1.00 39.29 ? 150 HIS A O   1 
ATOM   1119 C CB  . HIS A 1 142 ? 4.028  47.549 70.054 1.00 45.81 ? 150 HIS A CB  1 
ATOM   1120 C CG  . HIS A 1 142 ? 2.839  48.229 70.665 1.00 56.04 ? 150 HIS A CG  1 
ATOM   1121 N ND1 . HIS A 1 142 ? 2.424  47.939 71.953 1.00 67.77 ? 150 HIS A ND1 1 
ATOM   1122 C CD2 . HIS A 1 142 ? 2.017  49.168 70.148 1.00 57.28 ? 150 HIS A CD2 1 
ATOM   1123 C CE1 . HIS A 1 142 ? 1.365  48.703 72.179 1.00 61.77 ? 150 HIS A CE1 1 
ATOM   1124 N NE2 . HIS A 1 142 ? 1.085  49.460 71.114 1.00 62.09 ? 150 HIS A NE2 1 
ATOM   1125 N N   . TRP A 1 143 ? 5.513  44.280 69.713 1.00 39.54 ? 151 TRP A N   1 
ATOM   1126 C CA  . TRP A 1 143 ? 6.609  43.524 69.128 1.00 39.99 ? 151 TRP A CA  1 
ATOM   1127 C C   . TRP A 1 143 ? 6.212  42.970 67.764 1.00 39.53 ? 151 TRP A C   1 
ATOM   1128 O O   . TRP A 1 143 ? 6.915  43.169 66.781 1.00 39.20 ? 151 TRP A O   1 
ATOM   1129 C CB  . TRP A 1 143 ? 7.055  42.370 70.040 1.00 39.40 ? 151 TRP A CB  1 
ATOM   1130 C CG  . TRP A 1 143 ? 7.856  42.796 71.232 1.00 35.59 ? 151 TRP A CG  1 
ATOM   1131 C CD1 . TRP A 1 143 ? 8.204  44.067 71.582 1.00 32.41 ? 151 TRP A CD1 1 
ATOM   1132 C CD2 . TRP A 1 143 ? 8.420  41.938 72.224 1.00 32.20 ? 151 TRP A CD2 1 
ATOM   1133 N NE1 . TRP A 1 143 ? 8.945  44.052 72.737 1.00 32.81 ? 151 TRP A NE1 1 
ATOM   1134 C CE2 . TRP A 1 143 ? 9.094  42.756 73.153 1.00 31.31 ? 151 TRP A CE2 1 
ATOM   1135 C CE3 . TRP A 1 143 ? 8.421  40.553 72.421 1.00 34.84 ? 151 TRP A CE3 1 
ATOM   1136 C CZ2 . TRP A 1 143 ? 9.765  42.233 74.257 1.00 30.54 ? 151 TRP A CZ2 1 
ATOM   1137 C CZ3 . TRP A 1 143 ? 9.081  40.039 73.518 1.00 31.72 ? 151 TRP A CZ3 1 
ATOM   1138 C CH2 . TRP A 1 143 ? 9.744  40.874 74.421 1.00 30.27 ? 151 TRP A CH2 1 
ATOM   1139 N N   . PHE A 1 144 ? 5.080  42.263 67.724 1.00 40.44 ? 152 PHE A N   1 
ATOM   1140 C CA  . PHE A 1 144 ? 4.536  41.766 66.472 1.00 37.45 ? 152 PHE A CA  1 
ATOM   1141 C C   . PHE A 1 144 ? 3.187  42.439 66.232 1.00 35.61 ? 152 PHE A C   1 
ATOM   1142 O O   . PHE A 1 144 ? 2.631  43.056 67.139 1.00 41.32 ? 152 PHE A O   1 
ATOM   1143 C CB  . PHE A 1 144 ? 4.456  40.230 66.506 1.00 36.03 ? 152 PHE A CB  1 
ATOM   1144 C CG  . PHE A 1 144 ? 5.796  39.579 66.786 1.00 33.23 ? 152 PHE A CG  1 
ATOM   1145 C CD1 . PHE A 1 144 ? 6.795  39.566 65.824 1.00 34.13 ? 152 PHE A CD1 1 
ATOM   1146 C CD2 . PHE A 1 144 ? 6.068  39.016 68.022 1.00 33.28 ? 152 PHE A CD2 1 
ATOM   1147 C CE1 . PHE A 1 144 ? 8.032  38.978 66.089 1.00 33.95 ? 152 PHE A CE1 1 
ATOM   1148 C CE2 . PHE A 1 144 ? 7.306  38.435 68.285 1.00 34.97 ? 152 PHE A CE2 1 
ATOM   1149 C CZ  . PHE A 1 144 ? 8.280  38.418 67.317 1.00 32.72 ? 152 PHE A CZ  1 
ATOM   1150 N N   . GLU A 1 145 ? 2.685  42.340 64.997 1.00 34.06 ? 153 GLU A N   1 
ATOM   1151 C CA  . GLU A 1 145 ? 1.439  42.985 64.614 1.00 40.86 ? 153 GLU A CA  1 
ATOM   1152 C C   . GLU A 1 145 ? 0.269  42.457 65.440 1.00 38.68 ? 153 GLU A C   1 
ATOM   1153 O O   . GLU A 1 145 ? -0.559 43.235 65.909 1.00 40.18 ? 153 GLU A O   1 
ATOM   1154 C CB  . GLU A 1 145 ? 1.174  42.794 63.114 1.00 46.76 ? 153 GLU A CB  1 
ATOM   1155 C CG  . GLU A 1 145 ? 2.100  43.618 62.234 1.00 53.77 ? 153 GLU A CG  1 
ATOM   1156 C CD  . GLU A 1 145 ? 1.946  43.383 60.746 1.00 58.27 ? 153 GLU A CD  1 
ATOM   1157 O OE1 . GLU A 1 145 ? 1.042  42.611 60.353 1.00 63.72 ? 153 GLU A OE1 1 
ATOM   1158 O OE2 . GLU A 1 145 ? 2.734  43.968 59.969 1.00 64.05 ? 153 GLU A OE2 1 
ATOM   1159 N N   . ASP A 1 146 ? 0.222  41.132 65.617 1.00 39.16 ? 154 ASP A N   1 
ATOM   1160 C CA  . ASP A 1 146 ? -0.739 40.495 66.502 1.00 40.78 ? 154 ASP A CA  1 
ATOM   1161 C C   . ASP A 1 146 ? -0.230 40.546 67.942 1.00 41.46 ? 154 ASP A C   1 
ATOM   1162 O O   . ASP A 1 146 ? 0.837  41.094 68.210 1.00 39.22 ? 154 ASP A O   1 
ATOM   1163 C CB  . ASP A 1 146 ? -0.997 39.041 66.061 1.00 45.06 ? 154 ASP A CB  1 
ATOM   1164 C CG  . ASP A 1 146 ? 0.120  38.069 66.393 1.00 52.11 ? 154 ASP A CG  1 
ATOM   1165 O OD1 . ASP A 1 146 ? 1.278  38.333 65.993 1.00 51.26 ? 154 ASP A OD1 1 
ATOM   1166 O OD2 . ASP A 1 146 ? -0.163 37.043 67.051 1.00 56.20 ? 154 ASP A OD2 1 
ATOM   1167 N N   . GLY A 1 147 ? -1.005 39.968 68.865 1.00 39.74 ? 155 GLY A N   1 
ATOM   1168 C CA  . GLY A 1 147 ? -0.631 39.932 70.269 1.00 38.83 ? 155 GLY A CA  1 
ATOM   1169 C C   . GLY A 1 147 ? 0.456  38.906 70.577 1.00 37.05 ? 155 GLY A C   1 
ATOM   1170 O O   . GLY A 1 147 ? 0.669  37.968 69.811 1.00 39.86 ? 155 GLY A O   1 
ATOM   1171 N N   . THR A 1 148 ? 1.139  39.108 71.710 1.00 36.69 ? 156 THR A N   1 
ATOM   1172 C CA  . THR A 1 148 ? 2.152  38.186 72.194 1.00 34.76 ? 156 THR A CA  1 
ATOM   1173 C C   . THR A 1 148 ? 2.123  38.168 73.720 1.00 34.40 ? 156 THR A C   1 
ATOM   1174 O O   . THR A 1 148 ? 2.225  39.216 74.352 1.00 35.13 ? 156 THR A O   1 
ATOM   1175 C CB  . THR A 1 148 ? 3.532  38.577 71.655 1.00 35.69 ? 156 THR A CB  1 
ATOM   1176 O OG1 . THR A 1 148 ? 3.459  38.676 70.233 1.00 34.65 ? 156 THR A OG1 1 
ATOM   1177 C CG2 . THR A 1 148 ? 4.616  37.579 72.046 1.00 35.03 ? 156 THR A CG2 1 
ATOM   1178 N N   . ASP A 1 149 ? 1.968  36.971 74.297 1.00 35.97 ? 157 ASP A N   1 
ATOM   1179 C CA  . ASP A 1 149 ? 1.948  36.798 75.740 1.00 38.96 ? 157 ASP A CA  1 
ATOM   1180 C C   . ASP A 1 149 ? 3.289  36.223 76.191 1.00 33.29 ? 157 ASP A C   1 
ATOM   1181 O O   . ASP A 1 149 ? 3.658  35.120 75.791 1.00 29.32 ? 157 ASP A O   1 
ATOM   1182 C CB  . ASP A 1 149 ? 0.776  35.885 76.149 1.00 43.82 ? 157 ASP A CB  1 
ATOM   1183 C CG  . ASP A 1 149 ? 0.429  35.895 77.626 1.00 57.18 ? 157 ASP A CG  1 
ATOM   1184 O OD1 . ASP A 1 149 ? 1.151  36.559 78.406 1.00 68.45 ? 157 ASP A OD1 1 
ATOM   1185 O OD2 . ASP A 1 149 ? -0.573 35.249 78.003 1.00 64.16 ? 157 ASP A OD2 1 
ATOM   1186 N N   . VAL A 1 150 ? 4.013  36.989 77.017 1.00 30.92 ? 158 VAL A N   1 
ATOM   1187 C CA  . VAL A 1 150 ? 5.345  36.616 77.464 1.00 32.72 ? 158 VAL A CA  1 
ATOM   1188 C C   . VAL A 1 150 ? 5.390  36.526 78.987 1.00 31.24 ? 158 VAL A C   1 
ATOM   1189 O O   . VAL A 1 150 ? 4.854  37.391 79.680 1.00 28.25 ? 158 VAL A O   1 
ATOM   1190 C CB  . VAL A 1 150 ? 6.401  37.622 76.950 1.00 36.90 ? 158 VAL A CB  1 
ATOM   1191 C CG1 . VAL A 1 150 ? 7.809  37.201 77.357 1.00 38.87 ? 158 VAL A CG1 1 
ATOM   1192 C CG2 . VAL A 1 150 ? 6.304  37.804 75.440 1.00 43.45 ? 158 VAL A CG2 1 
ATOM   1193 N N   . ASP A 1 151 ? 6.049  35.476 79.492 1.00 26.87 ? 159 ASP A N   1 
ATOM   1194 C CA  . ASP A 1 151 ? 6.269  35.309 80.918 1.00 25.22 ? 159 ASP A CA  1 
ATOM   1195 C C   . ASP A 1 151 ? 7.684  35.753 81.280 1.00 25.21 ? 159 ASP A C   1 
ATOM   1196 O O   . ASP A 1 151 ? 8.632  34.979 81.155 1.00 24.77 ? 159 ASP A O   1 
ATOM   1197 C CB  . ASP A 1 151 ? 6.042  33.851 81.333 1.00 24.30 ? 159 ASP A CB  1 
ATOM   1198 C CG  . ASP A 1 151 ? 6.052  33.624 82.828 1.00 26.55 ? 159 ASP A CG  1 
ATOM   1199 O OD1 . ASP A 1 151 ? 6.279  34.599 83.579 1.00 27.39 ? 159 ASP A OD1 1 
ATOM   1200 O OD2 . ASP A 1 151 ? 5.817  32.474 83.252 1.00 32.86 ? 159 ASP A OD2 1 
ATOM   1201 N N   . PHE A 1 152 ? 7.804  37.002 81.747 1.00 24.54 ? 160 PHE A N   1 
ATOM   1202 C CA  . PHE A 1 152 ? 9.085  37.572 82.134 1.00 26.31 ? 160 PHE A CA  1 
ATOM   1203 C C   . PHE A 1 152 ? 9.613  37.023 83.458 1.00 26.47 ? 160 PHE A C   1 
ATOM   1204 O O   . PHE A 1 152 ? 10.742 37.320 83.838 1.00 28.37 ? 160 PHE A O   1 
ATOM   1205 C CB  . PHE A 1 152 ? 8.982  39.104 82.208 1.00 27.90 ? 160 PHE A CB  1 
ATOM   1206 C CG  . PHE A 1 152 ? 8.910  39.752 80.851 1.00 26.89 ? 160 PHE A CG  1 
ATOM   1207 C CD1 . PHE A 1 152 ? 10.018 39.784 80.022 1.00 27.27 ? 160 PHE A CD1 1 
ATOM   1208 C CD2 . PHE A 1 152 ? 7.728  40.307 80.391 1.00 27.66 ? 160 PHE A CD2 1 
ATOM   1209 C CE1 . PHE A 1 152 ? 9.949  40.375 78.766 1.00 29.18 ? 160 PHE A CE1 1 
ATOM   1210 C CE2 . PHE A 1 152 ? 7.660  40.894 79.135 1.00 28.06 ? 160 PHE A CE2 1 
ATOM   1211 C CZ  . PHE A 1 152 ? 8.771  40.925 78.329 1.00 30.05 ? 160 PHE A CZ  1 
ATOM   1212 N N   . ASP A 1 153 ? 8.795  36.226 84.155 1.00 26.15 ? 161 ASP A N   1 
ATOM   1213 C CA  . ASP A 1 153 ? 9.253  35.506 85.330 1.00 27.70 ? 161 ASP A CA  1 
ATOM   1214 C C   . ASP A 1 153 ? 10.049 34.252 84.966 1.00 30.27 ? 161 ASP A C   1 
ATOM   1215 O O   . ASP A 1 153 ? 10.735 33.694 85.820 1.00 30.60 ? 161 ASP A O   1 
ATOM   1216 C CB  . ASP A 1 153 ? 8.064  35.132 86.218 1.00 26.45 ? 161 ASP A CB  1 
ATOM   1217 C CG  . ASP A 1 153 ? 8.465  34.811 87.637 1.00 28.99 ? 161 ASP A CG  1 
ATOM   1218 O OD1 . ASP A 1 153 ? 9.031  35.701 88.310 1.00 31.71 ? 161 ASP A OD1 1 
ATOM   1219 O OD2 . ASP A 1 153 ? 8.222  33.674 88.075 1.00 32.47 ? 161 ASP A OD2 1 
ATOM   1220 N N   . ARG A 1 154 ? 9.948  33.820 83.700 1.00 33.37 ? 162 ARG A N   1 
ATOM   1221 C CA  . ARG A 1 154 ? 10.657 32.648 83.206 1.00 33.15 ? 162 ARG A CA  1 
ATOM   1222 C C   . ARG A 1 154 ? 11.599 33.023 82.064 1.00 30.98 ? 162 ARG A C   1 
ATOM   1223 O O   . ARG A 1 154 ? 11.317 32.743 80.900 1.00 33.02 ? 162 ARG A O   1 
ATOM   1224 C CB  . ARG A 1 154 ? 9.654  31.568 82.748 1.00 35.44 ? 162 ARG A CB  1 
ATOM   1225 C CG  . ARG A 1 154 ? 8.853  30.949 83.888 1.00 40.46 ? 162 ARG A CG  1 
ATOM   1226 C CD  . ARG A 1 154 ? 7.967  29.800 83.431 1.00 47.08 ? 162 ARG A CD  1 
ATOM   1227 N NE  . ARG A 1 154 ? 6.776  30.259 82.721 1.00 63.12 ? 162 ARG A NE  1 
ATOM   1228 C CZ  . ARG A 1 154 ? 6.372  29.817 81.534 1.00 61.07 ? 162 ARG A CZ  1 
ATOM   1229 N NH1 . ARG A 1 154 ? 7.015  28.852 80.896 1.00 60.95 ? 162 ARG A NH1 1 
ATOM   1230 N NH2 . ARG A 1 154 ? 5.285  30.349 80.980 1.00 51.91 ? 162 ARG A NH2 1 
ATOM   1231 N N   . VAL A 1 155 ? 12.721 33.660 82.419 1.00 28.34 ? 163 VAL A N   1 
ATOM   1232 C CA  . VAL A 1 155 ? 13.752 34.026 81.462 1.00 26.82 ? 163 VAL A CA  1 
ATOM   1233 C C   . VAL A 1 155 ? 14.965 33.118 81.641 1.00 26.81 ? 163 VAL A C   1 
ATOM   1234 O O   . VAL A 1 155 ? 15.336 32.785 82.765 1.00 25.68 ? 163 VAL A O   1 
ATOM   1235 C CB  . VAL A 1 155 ? 14.164 35.512 81.594 1.00 28.00 ? 163 VAL A CB  1 
ATOM   1236 C CG1 . VAL A 1 155 ? 15.261 35.872 80.591 1.00 31.24 ? 163 VAL A CG1 1 
ATOM   1237 C CG2 . VAL A 1 155 ? 12.958 36.431 81.445 1.00 27.08 ? 163 VAL A CG2 1 
ATOM   1238 N N   . PHE A 1 156 ? 15.577 32.733 80.516 1.00 28.84 ? 164 PHE A N   1 
ATOM   1239 C CA  . PHE A 1 156 ? 16.793 31.937 80.521 1.00 27.19 ? 164 PHE A CA  1 
ATOM   1240 C C   . PHE A 1 156 ? 17.799 32.552 79.555 1.00 27.02 ? 164 PHE A C   1 
ATOM   1241 O O   . PHE A 1 156 ? 17.410 33.089 78.520 1.00 29.69 ? 164 PHE A O   1 
ATOM   1242 C CB  . PHE A 1 156 ? 16.503 30.483 80.137 1.00 27.52 ? 164 PHE A CB  1 
ATOM   1243 C CG  . PHE A 1 156 ? 15.515 29.797 81.046 1.00 27.30 ? 164 PHE A CG  1 
ATOM   1244 C CD1 . PHE A 1 156 ? 14.153 29.920 80.834 1.00 26.62 ? 164 PHE A CD1 1 
ATOM   1245 C CD2 . PHE A 1 156 ? 15.948 29.052 82.132 1.00 26.61 ? 164 PHE A CD2 1 
ATOM   1246 C CE1 . PHE A 1 156 ? 13.243 29.292 81.680 1.00 26.02 ? 164 PHE A CE1 1 
ATOM   1247 C CE2 . PHE A 1 156 ? 15.037 28.430 82.975 1.00 25.10 ? 164 PHE A CE2 1 
ATOM   1248 C CZ  . PHE A 1 156 ? 13.691 28.554 82.746 1.00 25.03 ? 164 PHE A CZ  1 
ATOM   1249 N N   . VAL A 1 157 ? 19.087 32.484 79.913 1.00 26.77 ? 165 VAL A N   1 
ATOM   1250 C CA  . VAL A 1 157 ? 20.149 32.991 79.060 1.00 29.58 ? 165 VAL A CA  1 
ATOM   1251 C C   . VAL A 1 157 ? 20.922 31.800 78.506 1.00 28.93 ? 165 VAL A C   1 
ATOM   1252 O O   . VAL A 1 157 ? 21.450 31.001 79.273 1.00 32.18 ? 165 VAL A O   1 
ATOM   1253 C CB  . VAL A 1 157 ? 21.079 33.976 79.801 1.00 30.60 ? 165 VAL A CB  1 
ATOM   1254 C CG1 . VAL A 1 157 ? 22.211 34.457 78.894 1.00 31.20 ? 165 VAL A CG1 1 
ATOM   1255 C CG2 . VAL A 1 157 ? 20.294 35.156 80.363 1.00 30.04 ? 165 VAL A CG2 1 
ATOM   1256 N N   . VAL A 1 158 ? 20.958 31.688 77.172 1.00 29.27 ? 166 VAL A N   1 
ATOM   1257 C CA  . VAL A 1 158 ? 21.719 30.653 76.492 1.00 30.95 ? 166 VAL A CA  1 
ATOM   1258 C C   . VAL A 1 158 ? 22.905 31.307 75.788 1.00 32.45 ? 166 VAL A C   1 
ATOM   1259 O O   . VAL A 1 158 ? 22.721 32.134 74.896 1.00 31.79 ? 166 VAL A O   1 
ATOM   1260 C CB  . VAL A 1 158 ? 20.840 29.853 75.506 1.00 33.92 ? 166 VAL A CB  1 
ATOM   1261 C CG1 . VAL A 1 158 ? 21.678 28.878 74.679 1.00 33.45 ? 166 VAL A CG1 1 
ATOM   1262 C CG2 . VAL A 1 158 ? 19.715 29.127 76.239 1.00 35.33 ? 166 VAL A CG2 1 
ATOM   1263 N N   . GLY A 1 159 ? 24.117 30.924 76.205 1.00 31.47 ? 167 GLY A N   1 
ATOM   1264 C CA  . GLY A 1 159 ? 25.342 31.518 75.695 1.00 31.18 ? 167 GLY A CA  1 
ATOM   1265 C C   . GLY A 1 159 ? 26.191 30.533 74.896 1.00 34.97 ? 167 GLY A C   1 
ATOM   1266 O O   . GLY A 1 159 ? 26.466 29.429 75.360 1.00 35.16 ? 167 GLY A O   1 
ATOM   1267 N N   . ASP A 1 160 ? 26.598 30.957 73.695 1.00 36.24 ? 168 ASP A N   1 
ATOM   1268 C CA  . ASP A 1 160 ? 27.452 30.169 72.824 1.00 36.30 ? 168 ASP A CA  1 
ATOM   1269 C C   . ASP A 1 160 ? 28.844 30.792 72.746 1.00 37.18 ? 168 ASP A C   1 
ATOM   1270 O O   . ASP A 1 160 ? 28.981 31.942 72.334 1.00 33.39 ? 168 ASP A O   1 
ATOM   1271 C CB  . ASP A 1 160 ? 26.815 30.080 71.426 1.00 38.67 ? 168 ASP A CB  1 
ATOM   1272 C CG  . ASP A 1 160 ? 27.751 29.648 70.320 1.00 36.61 ? 168 ASP A CG  1 
ATOM   1273 O OD1 . ASP A 1 160 ? 28.430 28.614 70.488 1.00 36.51 ? 168 ASP A OD1 1 
ATOM   1274 O OD2 . ASP A 1 160 ? 27.799 30.341 69.283 1.00 42.18 ? 168 ASP A OD2 1 
ATOM   1275 N N   . SER A 1 161 ? 29.864 30.023 73.152 1.00 44.94 ? 169 SER A N   1 
ATOM   1276 C CA  . SER A 1 161 ? 31.260 30.423 73.027 1.00 42.65 ? 169 SER A CA  1 
ATOM   1277 C C   . SER A 1 161 ? 31.459 31.718 73.817 1.00 34.91 ? 169 SER A C   1 
ATOM   1278 O O   . SER A 1 161 ? 31.216 31.744 75.023 1.00 29.43 ? 169 SER A O   1 
ATOM   1279 C CB  . SER A 1 161 ? 31.640 30.551 71.551 1.00 50.62 ? 169 SER A CB  1 
ATOM   1280 O OG  . SER A 1 161 ? 33.025 30.803 71.372 1.00 63.00 ? 169 SER A OG  1 
ATOM   1281 N N   . SER A 1 162 ? 31.896 32.789 73.141 1.00 29.01 ? 170 SER A N   1 
ATOM   1282 C CA  . SER A 1 162 ? 31.966 34.110 73.744 1.00 27.89 ? 170 SER A CA  1 
ATOM   1283 C C   . SER A 1 162 ? 30.657 34.543 74.402 1.00 29.38 ? 170 SER A C   1 
ATOM   1284 O O   . SER A 1 162 ? 30.671 35.277 75.388 1.00 29.09 ? 170 SER A O   1 
ATOM   1285 C CB  . SER A 1 162 ? 32.421 35.148 72.723 1.00 26.89 ? 170 SER A CB  1 
ATOM   1286 O OG  . SER A 1 162 ? 31.569 35.178 71.589 1.00 25.77 ? 170 SER A OG  1 
ATOM   1287 N N   . GLY A 1 163 ? 29.530 34.085 73.842 1.00 29.14 ? 171 GLY A N   1 
ATOM   1288 C CA  . GLY A 1 163 ? 28.224 34.288 74.445 1.00 28.36 ? 171 GLY A CA  1 
ATOM   1289 C C   . GLY A 1 163 ? 28.071 33.556 75.776 1.00 31.74 ? 171 GLY A C   1 
ATOM   1290 O O   . GLY A 1 163 ? 27.348 34.017 76.657 1.00 32.77 ? 171 GLY A O   1 
ATOM   1291 N N   . GLY A 1 164 ? 28.748 32.405 75.896 1.00 29.05 ? 172 GLY A N   1 
ATOM   1292 C CA  . GLY A 1 164 ? 28.834 31.675 77.151 1.00 30.63 ? 172 GLY A CA  1 
ATOM   1293 C C   . GLY A 1 164 ? 29.560 32.468 78.236 1.00 32.16 ? 172 GLY A C   1 
ATOM   1294 O O   . GLY A 1 164 ? 29.174 32.429 79.403 1.00 27.44 ? 172 GLY A O   1 
ATOM   1295 N N   . ASN A 1 165 ? 30.619 33.182 77.831 1.00 34.39 ? 173 ASN A N   1 
ATOM   1296 C CA  . ASN A 1 165 ? 31.342 34.071 78.725 1.00 33.49 ? 173 ASN A CA  1 
ATOM   1297 C C   . ASN A 1 165 ? 30.424 35.204 79.180 1.00 34.02 ? 173 ASN A C   1 
ATOM   1298 O O   . ASN A 1 165 ? 30.337 35.487 80.372 1.00 32.63 ? 173 ASN A O   1 
ATOM   1299 C CB  . ASN A 1 165 ? 32.594 34.618 78.044 1.00 30.08 ? 173 ASN A CB  1 
ATOM   1300 C CG  . ASN A 1 165 ? 33.470 35.438 78.963 1.00 30.06 ? 173 ASN A CG  1 
ATOM   1301 O OD1 . ASN A 1 165 ? 33.009 36.367 79.631 1.00 28.27 ? 173 ASN A OD1 1 
ATOM   1302 N ND2 . ASN A 1 165 ? 34.760 35.114 79.027 1.00 30.03 ? 173 ASN A ND2 1 
ATOM   1303 N N   . ILE A 1 166 ? 29.739 35.833 78.215 1.00 29.96 ? 174 ILE A N   1 
ATOM   1304 C CA  . ILE A 1 166 ? 28.763 36.875 78.496 1.00 29.93 ? 174 ILE A CA  1 
ATOM   1305 C C   . ILE A 1 166 ? 27.713 36.394 79.497 1.00 29.63 ? 174 ILE A C   1 
ATOM   1306 O O   . ILE A 1 166 ? 27.357 37.123 80.421 1.00 31.13 ? 174 ILE A O   1 
ATOM   1307 C CB  . ILE A 1 166 ? 28.105 37.374 77.180 1.00 28.49 ? 174 ILE A CB  1 
ATOM   1308 C CG1 . ILE A 1 166 ? 29.115 38.143 76.310 1.00 29.76 ? 174 ILE A CG1 1 
ATOM   1309 C CG2 . ILE A 1 166 ? 26.861 38.226 77.459 1.00 27.22 ? 174 ILE A CG2 1 
ATOM   1310 C CD1 . ILE A 1 166 ? 28.627 38.452 74.913 1.00 32.24 ? 174 ILE A CD1 1 
ATOM   1311 N N   . ALA A 1 167 ? 27.223 35.165 79.297 1.00 29.42 ? 175 ALA A N   1 
ATOM   1312 C CA  . ALA A 1 167 ? 26.243 34.564 80.187 1.00 30.20 ? 175 ALA A CA  1 
ATOM   1313 C C   . ALA A 1 167 ? 26.755 34.531 81.624 1.00 30.28 ? 175 ALA A C   1 
ATOM   1314 O O   . ALA A 1 167 ? 26.053 34.943 82.547 1.00 28.40 ? 175 ALA A O   1 
ATOM   1315 C CB  . ALA A 1 167 ? 25.895 33.160 79.719 1.00 30.47 ? 175 ALA A CB  1 
ATOM   1316 N N   . HIS A 1 168 ? 27.989 34.042 81.794 1.00 29.67 ? 176 HIS A N   1 
ATOM   1317 C CA  . HIS A 1 168 ? 28.631 33.993 83.098 1.00 26.59 ? 176 HIS A CA  1 
ATOM   1318 C C   . HIS A 1 168 ? 28.662 35.367 83.763 1.00 25.01 ? 176 HIS A C   1 
ATOM   1319 O O   . HIS A 1 168 ? 28.392 35.482 84.956 1.00 22.41 ? 176 HIS A O   1 
ATOM   1320 C CB  . HIS A 1 168 ? 30.059 33.436 82.984 1.00 27.84 ? 176 HIS A CB  1 
ATOM   1321 C CG  . HIS A 1 168 ? 30.876 33.623 84.227 1.00 30.11 ? 176 HIS A CG  1 
ATOM   1322 N ND1 . HIS A 1 168 ? 30.652 32.865 85.357 1.00 30.15 ? 176 HIS A ND1 1 
ATOM   1323 C CD2 . HIS A 1 168 ? 31.882 34.489 84.477 1.00 27.81 ? 176 HIS A CD2 1 
ATOM   1324 C CE1 . HIS A 1 168 ? 31.525 33.286 86.259 1.00 30.72 ? 176 HIS A CE1 1 
ATOM   1325 N NE2 . HIS A 1 168 ? 32.285 34.268 85.768 1.00 29.39 ? 176 HIS A NE2 1 
ATOM   1326 N N   . GLN A 1 169 ? 28.989 36.403 82.979 1.00 26.12 ? 177 GLN A N   1 
ATOM   1327 C CA  . GLN A 1 169 ? 29.123 37.752 83.507 1.00 25.50 ? 177 GLN A CA  1 
ATOM   1328 C C   . GLN A 1 169 ? 27.788 38.291 84.017 1.00 24.20 ? 177 GLN A C   1 
ATOM   1329 O O   . GLN A 1 169 ? 27.742 38.916 85.074 1.00 23.55 ? 177 GLN A O   1 
ATOM   1330 C CB  . GLN A 1 169 ? 29.700 38.712 82.451 1.00 24.61 ? 177 GLN A CB  1 
ATOM   1331 C CG  . GLN A 1 169 ? 31.054 38.292 81.887 1.00 27.55 ? 177 GLN A CG  1 
ATOM   1332 C CD  . GLN A 1 169 ? 32.138 38.132 82.922 1.00 26.51 ? 177 GLN A CD  1 
ATOM   1333 O OE1 . GLN A 1 169 ? 32.072 38.671 84.030 1.00 26.01 ? 177 GLN A OE1 1 
ATOM   1334 N NE2 . GLN A 1 169 ? 33.184 37.408 82.563 1.00 27.27 ? 177 GLN A NE2 1 
ATOM   1335 N N   . LEU A 1 170 ? 26.715 38.045 83.255 1.00 22.09 ? 178 LEU A N   1 
ATOM   1336 C CA  . LEU A 1 170 ? 25.368 38.396 83.676 1.00 22.40 ? 178 LEU A CA  1 
ATOM   1337 C C   . LEU A 1 170 ? 24.996 37.682 84.973 1.00 22.22 ? 178 LEU A C   1 
ATOM   1338 O O   . LEU A 1 170 ? 24.517 38.312 85.913 1.00 20.49 ? 178 LEU A O   1 
ATOM   1339 C CB  . LEU A 1 170 ? 24.353 38.034 82.581 1.00 22.95 ? 178 LEU A CB  1 
ATOM   1340 C CG  . LEU A 1 170 ? 24.425 38.864 81.309 1.00 23.89 ? 178 LEU A CG  1 
ATOM   1341 C CD1 . LEU A 1 170 ? 23.425 38.370 80.283 1.00 24.62 ? 178 LEU A CD1 1 
ATOM   1342 C CD2 . LEU A 1 170 ? 24.191 40.343 81.603 1.00 23.39 ? 178 LEU A CD2 1 
ATOM   1343 N N   . ALA A 1 171 ? 25.231 36.364 85.010 1.00 24.20 ? 179 ALA A N   1 
ATOM   1344 C CA  . ALA A 1 171 ? 24.959 35.559 86.191 1.00 25.25 ? 179 ALA A CA  1 
ATOM   1345 C C   . ALA A 1 171 ? 25.601 36.145 87.447 1.00 28.42 ? 179 ALA A C   1 
ATOM   1346 O O   . ALA A 1 171 ? 24.956 36.225 88.490 1.00 34.29 ? 179 ALA A O   1 
ATOM   1347 C CB  . ALA A 1 171 ? 25.434 34.130 85.974 1.00 22.74 ? 179 ALA A CB  1 
ATOM   1348 N N   . VAL A 1 172 ? 26.869 36.559 87.330 1.00 27.50 ? 180 VAL A N   1 
ATOM   1349 C CA  . VAL A 1 172 ? 27.596 37.167 88.433 1.00 28.88 ? 180 VAL A CA  1 
ATOM   1350 C C   . VAL A 1 172 ? 26.972 38.507 88.820 1.00 31.31 ? 180 VAL A C   1 
ATOM   1351 O O   . VAL A 1 172 ? 26.796 38.789 90.005 1.00 32.85 ? 180 VAL A O   1 
ATOM   1352 C CB  . VAL A 1 172 ? 29.102 37.326 88.085 1.00 27.19 ? 180 VAL A CB  1 
ATOM   1353 C CG1 . VAL A 1 172 ? 29.828 38.194 89.107 1.00 25.74 ? 180 VAL A CG1 1 
ATOM   1354 C CG2 . VAL A 1 172 ? 29.786 35.968 87.949 1.00 28.55 ? 180 VAL A CG2 1 
ATOM   1355 N N   . ARG A 1 173 ? 26.649 39.323 87.809 1.00 30.67 ? 181 ARG A N   1 
ATOM   1356 C CA  . ARG A 1 173 ? 26.094 40.650 88.027 1.00 33.36 ? 181 ARG A CA  1 
ATOM   1357 C C   . ARG A 1 173 ? 24.737 40.599 88.730 1.00 33.58 ? 181 ARG A C   1 
ATOM   1358 O O   . ARG A 1 173 ? 24.486 41.381 89.646 1.00 28.59 ? 181 ARG A O   1 
ATOM   1359 C CB  . ARG A 1 173 ? 25.986 41.396 86.688 1.00 33.66 ? 181 ARG A CB  1 
ATOM   1360 C CG  . ARG A 1 173 ? 27.338 41.856 86.143 1.00 33.99 ? 181 ARG A CG  1 
ATOM   1361 C CD  . ARG A 1 173 ? 27.810 43.135 86.805 1.00 34.30 ? 181 ARG A CD  1 
ATOM   1362 N NE  . ARG A 1 173 ? 26.985 44.272 86.411 1.00 38.01 ? 181 ARG A NE  1 
ATOM   1363 C CZ  . ARG A 1 173 ? 27.032 45.476 86.966 1.00 36.70 ? 181 ARG A CZ  1 
ATOM   1364 N NH1 . ARG A 1 173 ? 27.667 45.691 88.106 1.00 43.74 ? 181 ARG A NH1 1 
ATOM   1365 N NH2 . ARG A 1 173 ? 26.405 46.488 86.372 1.00 33.13 ? 181 ARG A NH2 1 
ATOM   1366 N N   . PHE A 1 174 ? 23.874 39.673 88.294 1.00 32.68 ? 182 PHE A N   1 
ATOM   1367 C CA  . PHE A 1 174 ? 22.598 39.436 88.951 1.00 29.87 ? 182 PHE A CA  1 
ATOM   1368 C C   . PHE A 1 174 ? 22.798 38.797 90.321 1.00 30.29 ? 182 PHE A C   1 
ATOM   1369 O O   . PHE A 1 174 ? 22.231 39.255 91.310 1.00 33.90 ? 182 PHE A O   1 
ATOM   1370 C CB  . PHE A 1 174 ? 21.686 38.541 88.096 1.00 33.36 ? 182 PHE A CB  1 
ATOM   1371 C CG  . PHE A 1 174 ? 21.016 39.255 86.948 1.00 36.61 ? 182 PHE A CG  1 
ATOM   1372 C CD1 . PHE A 1 174 ? 20.130 40.293 87.181 1.00 39.43 ? 182 PHE A CD1 1 
ATOM   1373 C CD2 . PHE A 1 174 ? 21.272 38.889 85.637 1.00 36.74 ? 182 PHE A CD2 1 
ATOM   1374 C CE1 . PHE A 1 174 ? 19.516 40.954 86.123 1.00 42.06 ? 182 PHE A CE1 1 
ATOM   1375 C CE2 . PHE A 1 174 ? 20.655 39.549 84.582 1.00 41.14 ? 182 PHE A CE2 1 
ATOM   1376 C CZ  . PHE A 1 174 ? 19.781 40.577 84.830 1.00 43.15 ? 182 PHE A CZ  1 
ATOM   1377 N N   . GLY A 1 175 ? 23.615 37.738 90.361 1.00 28.80 ? 183 GLY A N   1 
ATOM   1378 C CA  . GLY A 1 175 ? 23.836 36.972 91.576 1.00 28.88 ? 183 GLY A CA  1 
ATOM   1379 C C   . GLY A 1 175 ? 24.347 37.799 92.753 1.00 29.10 ? 183 GLY A C   1 
ATOM   1380 O O   . GLY A 1 175 ? 23.944 37.570 93.890 1.00 32.43 ? 183 GLY A O   1 
ATOM   1381 N N   . SER A 1 176 ? 25.240 38.753 92.464 1.00 30.95 ? 184 SER A N   1 
ATOM   1382 C CA  . SER A 1 176 ? 25.801 39.626 93.483 1.00 33.51 ? 184 SER A CA  1 
ATOM   1383 C C   . SER A 1 176 ? 24.826 40.706 93.951 1.00 33.82 ? 184 SER A C   1 
ATOM   1384 O O   . SER A 1 176 ? 25.049 41.337 94.980 1.00 34.68 ? 184 SER A O   1 
ATOM   1385 C CB  . SER A 1 176 ? 27.076 40.285 92.967 1.00 35.02 ? 184 SER A CB  1 
ATOM   1386 O OG  . SER A 1 176 ? 26.814 41.072 91.817 1.00 37.23 ? 184 SER A OG  1 
ATOM   1387 N N   . GLY A 1 177 ? 23.754 40.920 93.180 1.00 35.96 ? 185 GLY A N   1 
ATOM   1388 C CA  . GLY A 1 177 ? 22.774 41.949 93.485 1.00 35.67 ? 185 GLY A CA  1 
ATOM   1389 C C   . GLY A 1 177 ? 23.162 43.321 92.938 1.00 37.02 ? 185 GLY A C   1 
ATOM   1390 O O   . GLY A 1 177 ? 22.569 44.327 93.318 1.00 40.68 ? 185 GLY A O   1 
ATOM   1391 N N   . SER A 1 178 ? 24.157 43.344 92.041 1.00 40.74 ? 186 SER A N   1 
ATOM   1392 C CA  . SER A 1 178 ? 24.606 44.572 91.408 1.00 41.21 ? 186 SER A CA  1 
ATOM   1393 C C   . SER A 1 178 ? 23.490 45.173 90.559 1.00 41.60 ? 186 SER A C   1 
ATOM   1394 O O   . SER A 1 178 ? 23.181 46.356 90.683 1.00 43.26 ? 186 SER A O   1 
ATOM   1395 C CB  . SER A 1 178 ? 25.834 44.316 90.541 1.00 41.76 ? 186 SER A CB  1 
ATOM   1396 O OG  . SER A 1 178 ? 26.847 43.644 91.269 1.00 47.47 ? 186 SER A OG  1 
ATOM   1397 N N   . ILE A 1 179 ? 22.899 44.331 89.703 1.00 41.76 ? 187 ILE A N   1 
ATOM   1398 C CA  . ILE A 1 179 ? 21.759 44.712 88.887 1.00 43.62 ? 187 ILE A CA  1 
ATOM   1399 C C   . ILE A 1 179 ? 20.559 43.854 89.273 1.00 42.95 ? 187 ILE A C   1 
ATOM   1400 O O   . ILE A 1 179 ? 20.719 42.713 89.702 1.00 35.10 ? 187 ILE A O   1 
ATOM   1401 C CB  . ILE A 1 179 ? 22.083 44.606 87.377 1.00 48.03 ? 187 ILE A CB  1 
ATOM   1402 C CG1 . ILE A 1 179 ? 22.425 43.164 86.960 1.00 49.23 ? 187 ILE A CG1 1 
ATOM   1403 C CG2 . ILE A 1 179 ? 23.200 45.575 87.001 1.00 52.33 ? 187 ILE A CG2 1 
ATOM   1404 C CD1 . ILE A 1 179 ? 22.592 42.983 85.490 1.00 56.07 ? 187 ILE A CD1 1 
ATOM   1405 N N   . GLU A 1 180 ? 19.360 44.423 89.110 1.00 42.40 ? 188 GLU A N   1 
ATOM   1406 C CA  . GLU A 1 180 ? 18.125 43.779 89.521 1.00 37.64 ? 188 GLU A CA  1 
ATOM   1407 C C   . GLU A 1 180 ? 16.978 44.391 88.720 1.00 32.57 ? 188 GLU A C   1 
ATOM   1408 O O   . GLU A 1 180 ? 16.794 45.606 88.741 1.00 34.02 ? 188 GLU A O   1 
ATOM   1409 C CB  . GLU A 1 180 ? 17.946 43.945 91.040 1.00 36.85 ? 188 GLU A CB  1 
ATOM   1410 C CG  . GLU A 1 180 ? 16.696 43.303 91.607 1.00 40.93 ? 188 GLU A CG  1 
ATOM   1411 C CD  . GLU A 1 180 ? 15.461 44.176 91.538 1.00 41.01 ? 188 GLU A CD  1 
ATOM   1412 O OE1 . GLU A 1 180 ? 15.463 45.256 92.172 1.00 43.34 ? 188 GLU A OE1 1 
ATOM   1413 O OE2 . GLU A 1 180 ? 14.495 43.789 90.844 1.00 44.37 ? 188 GLU A OE2 1 
ATOM   1414 N N   . LEU A 1 181 ? 16.217 43.537 88.020 1.00 27.90 ? 189 LEU A N   1 
ATOM   1415 C CA  . LEU A 1 181 ? 15.293 43.983 86.987 1.00 27.78 ? 189 LEU A CA  1 
ATOM   1416 C C   . LEU A 1 181 ? 13.897 43.368 87.082 1.00 25.80 ? 189 LEU A C   1 
ATOM   1417 O O   . LEU A 1 181 ? 13.357 42.908 86.080 1.00 26.01 ? 189 LEU A O   1 
ATOM   1418 C CB  . LEU A 1 181 ? 15.893 43.630 85.612 1.00 29.34 ? 189 LEU A CB  1 
ATOM   1419 C CG  . LEU A 1 181 ? 17.222 44.278 85.259 1.00 30.11 ? 189 LEU A CG  1 
ATOM   1420 C CD1 . LEU A 1 181 ? 17.705 43.799 83.909 1.00 30.81 ? 189 LEU A CD1 1 
ATOM   1421 C CD2 . LEU A 1 181 ? 17.119 45.793 85.260 1.00 29.03 ? 189 LEU A CD2 1 
ATOM   1422 N N   . THR A 1 182 ? 13.305 43.384 88.282 1.00 25.46 ? 190 THR A N   1 
ATOM   1423 C CA  . THR A 1 182 ? 11.934 42.929 88.463 1.00 27.65 ? 190 THR A CA  1 
ATOM   1424 C C   . THR A 1 182 ? 11.042 43.744 87.529 1.00 30.77 ? 190 THR A C   1 
ATOM   1425 O O   . THR A 1 182 ? 11.205 44.959 87.450 1.00 33.38 ? 190 THR A O   1 
ATOM   1426 C CB  . THR A 1 182 ? 11.527 43.057 89.940 1.00 28.15 ? 190 THR A CB  1 
ATOM   1427 O OG1 . THR A 1 182 ? 12.454 42.326 90.739 1.00 25.50 ? 190 THR A OG1 1 
ATOM   1428 C CG2 . THR A 1 182 ? 10.120 42.545 90.219 1.00 30.57 ? 190 THR A CG2 1 
ATOM   1429 N N   . PRO A 1 183 ? 10.064 43.143 86.803 1.00 35.26 ? 191 PRO A N   1 
ATOM   1430 C CA  . PRO A 1 183 ? 9.639  41.757 86.992 1.00 35.16 ? 191 PRO A CA  1 
ATOM   1431 C C   . PRO A 1 183 ? 10.389 40.704 86.173 1.00 31.97 ? 191 PRO A C   1 
ATOM   1432 O O   . PRO A 1 183 ? 9.935  39.565 86.087 1.00 32.28 ? 191 PRO A O   1 
ATOM   1433 C CB  . PRO A 1 183 ? 8.178  41.823 86.551 1.00 32.67 ? 191 PRO A CB  1 
ATOM   1434 C CG  . PRO A 1 183 ? 8.202  42.810 85.412 1.00 34.25 ? 191 PRO A CG  1 
ATOM   1435 C CD  . PRO A 1 183 ? 9.272  43.824 85.765 1.00 36.22 ? 191 PRO A CD  1 
ATOM   1436 N N   . VAL A 1 184 ? 11.530 41.073 85.579 1.00 29.57 ? 192 VAL A N   1 
ATOM   1437 C CA  . VAL A 1 184 ? 12.337 40.120 84.834 1.00 29.16 ? 192 VAL A CA  1 
ATOM   1438 C C   . VAL A 1 184 ? 13.103 39.239 85.820 1.00 29.12 ? 192 VAL A C   1 
ATOM   1439 O O   . VAL A 1 184 ? 13.806 39.751 86.689 1.00 28.97 ? 192 VAL A O   1 
ATOM   1440 C CB  . VAL A 1 184 ? 13.297 40.808 83.834 1.00 28.49 ? 192 VAL A CB  1 
ATOM   1441 C CG1 . VAL A 1 184 ? 14.048 39.778 83.000 1.00 32.74 ? 192 VAL A CG1 1 
ATOM   1442 C CG2 . VAL A 1 184 ? 12.554 41.789 82.934 1.00 29.50 ? 192 VAL A CG2 1 
ATOM   1443 N N   . ARG A 1 185 ? 12.944 37.916 85.675 1.00 28.23 ? 193 ARG A N   1 
ATOM   1444 C CA  . ARG A 1 185 ? 13.661 36.936 86.477 1.00 29.71 ? 193 ARG A CA  1 
ATOM   1445 C C   . ARG A 1 185 ? 14.382 35.926 85.586 1.00 29.26 ? 193 ARG A C   1 
ATOM   1446 O O   . ARG A 1 185 ? 13.743 35.120 84.914 1.00 25.37 ? 193 ARG A O   1 
ATOM   1447 C CB  . ARG A 1 185 ? 12.698 36.186 87.415 1.00 33.97 ? 193 ARG A CB  1 
ATOM   1448 C CG  . ARG A 1 185 ? 13.345 35.012 88.163 1.00 41.42 ? 193 ARG A CG  1 
ATOM   1449 C CD  . ARG A 1 185 ? 12.345 34.215 88.971 1.00 47.54 ? 193 ARG A CD  1 
ATOM   1450 N NE  . ARG A 1 185 ? 11.819 34.980 90.095 1.00 64.74 ? 193 ARG A NE  1 
ATOM   1451 C CZ  . ARG A 1 185 ? 10.901 34.536 90.944 1.00 71.20 ? 193 ARG A CZ  1 
ATOM   1452 N NH1 . ARG A 1 185 ? 10.361 33.334 90.814 1.00 77.26 ? 193 ARG A NH1 1 
ATOM   1453 N NH2 . ARG A 1 185 ? 10.511 35.319 91.947 1.00 62.10 ? 193 ARG A NH2 1 
ATOM   1454 N N   . VAL A 1 186 ? 15.719 35.968 85.608 1.00 29.33 ? 194 VAL A N   1 
ATOM   1455 C CA  . VAL A 1 186 ? 16.536 34.954 84.964 1.00 28.38 ? 194 VAL A CA  1 
ATOM   1456 C C   . VAL A 1 186 ? 16.643 33.754 85.902 1.00 28.07 ? 194 VAL A C   1 
ATOM   1457 O O   . VAL A 1 186 ? 17.265 33.850 86.956 1.00 30.75 ? 194 VAL A O   1 
ATOM   1458 C CB  . VAL A 1 186 ? 17.926 35.508 84.591 1.00 25.46 ? 194 VAL A CB  1 
ATOM   1459 C CG1 . VAL A 1 186 ? 18.784 34.435 83.921 1.00 28.24 ? 194 VAL A CG1 1 
ATOM   1460 C CG2 . VAL A 1 186 ? 17.800 36.742 83.708 1.00 24.37 ? 194 VAL A CG2 1 
ATOM   1461 N N   . ARG A 1 187 ? 16.035 32.629 85.506 1.00 28.35 ? 195 ARG A N   1 
ATOM   1462 C CA  . ARG A 1 187 ? 15.973 31.444 86.347 1.00 29.17 ? 195 ARG A CA  1 
ATOM   1463 C C   . ARG A 1 187 ? 17.139 30.476 86.154 1.00 28.92 ? 195 ARG A C   1 
ATOM   1464 O O   . ARG A 1 187 ? 17.359 29.606 86.993 1.00 28.84 ? 195 ARG A O   1 
ATOM   1465 C CB  . ARG A 1 187 ? 14.669 30.683 86.090 1.00 32.19 ? 195 ARG A CB  1 
ATOM   1466 C CG  . ARG A 1 187 ? 13.417 31.460 86.458 1.00 33.87 ? 195 ARG A CG  1 
ATOM   1467 C CD  . ARG A 1 187 ? 12.297 30.514 86.809 1.00 36.61 ? 195 ARG A CD  1 
ATOM   1468 N NE  . ARG A 1 187 ? 11.048 31.205 87.102 1.00 41.11 ? 195 ARG A NE  1 
ATOM   1469 C CZ  . ARG A 1 187 ? 9.981  30.635 87.647 1.00 46.61 ? 195 ARG A CZ  1 
ATOM   1470 N NH1 . ARG A 1 187 ? 10.043 29.438 88.210 1.00 48.35 ? 195 ARG A NH1 1 
ATOM   1471 N NH2 . ARG A 1 187 ? 8.825  31.291 87.646 1.00 52.02 ? 195 ARG A NH2 1 
ATOM   1472 N N   . GLY A 1 188 ? 17.865 30.610 85.038 1.00 27.52 ? 196 GLY A N   1 
ATOM   1473 C CA  . GLY A 1 188 ? 18.993 29.737 84.763 1.00 28.61 ? 196 GLY A CA  1 
ATOM   1474 C C   . GLY A 1 188 ? 19.846 30.189 83.582 1.00 26.45 ? 196 GLY A C   1 
ATOM   1475 O O   . GLY A 1 188 ? 19.401 30.987 82.761 1.00 27.13 ? 196 GLY A O   1 
ATOM   1476 N N   . TYR A 1 189 ? 21.074 29.662 83.517 1.00 26.11 ? 197 TYR A N   1 
ATOM   1477 C CA  . TYR A 1 189 ? 22.016 29.993 82.462 1.00 26.62 ? 197 TYR A CA  1 
ATOM   1478 C C   . TYR A 1 189 ? 22.520 28.724 81.781 1.00 29.16 ? 197 TYR A C   1 
ATOM   1479 O O   . TYR A 1 189 ? 22.719 27.702 82.434 1.00 28.22 ? 197 TYR A O   1 
ATOM   1480 C CB  . TYR A 1 189 ? 23.197 30.802 83.021 1.00 25.34 ? 197 TYR A CB  1 
ATOM   1481 C CG  . TYR A 1 189 ? 22.770 32.073 83.715 1.00 28.22 ? 197 TYR A CG  1 
ATOM   1482 C CD1 . TYR A 1 189 ? 22.227 32.043 84.994 1.00 29.57 ? 197 TYR A CD1 1 
ATOM   1483 C CD2 . TYR A 1 189 ? 22.878 33.306 83.083 1.00 28.00 ? 197 TYR A CD2 1 
ATOM   1484 C CE1 . TYR A 1 189 ? 21.819 33.208 85.633 1.00 25.73 ? 197 TYR A CE1 1 
ATOM   1485 C CE2 . TYR A 1 189 ? 22.472 34.478 83.713 1.00 28.65 ? 197 TYR A CE2 1 
ATOM   1486 C CZ  . TYR A 1 189 ? 21.942 34.424 84.989 1.00 26.04 ? 197 TYR A CZ  1 
ATOM   1487 O OH  . TYR A 1 189 ? 21.538 35.573 85.619 1.00 32.84 ? 197 TYR A OH  1 
ATOM   1488 N N   . VAL A 1 190 ? 22.694 28.796 80.458 1.00 32.11 ? 198 VAL A N   1 
ATOM   1489 C CA  . VAL A 1 190 ? 23.233 27.631 79.693 1.00 31.00 ? 198 VAL A CA  1 
ATOM   1490 C C   . VAL A 1 190 ? 24.560 28.068 79.054 1.00 29.39 ? 198 VAL A C   1 
ATOM   1491 O O   . VAL A 1 190 ? 24.526 28.930 78.148 1.00 28.92 ? 198 VAL A O   1 
ATOM   1492 C CB  . VAL A 1 190 ? 22.251 27.105 78.629 1.00 30.22 ? 198 VAL A CB  1 
ATOM   1493 C CG1 . VAL A 1 190 ? 22.879 26.009 77.775 1.00 30.43 ? 198 VAL A CG1 1 
ATOM   1494 C CG2 . VAL A 1 190 ? 20.949 26.617 79.252 1.00 29.38 ? 198 VAL A CG2 1 
ATOM   1495 N N   . LEU A 1 191 ? 25.678 27.508 79.521 1.00 31.19 ? 199 LEU A N   1 
ATOM   1496 C CA  . LEU A 1 191 ? 27.011 27.910 79.003 1.00 30.01 ? 199 LEU A CA  1 
ATOM   1497 C C   . LEU A 1 191 ? 27.496 26.856 77.996 1.00 28.43 ? 199 LEU A C   1 
ATOM   1498 O O   . LEU A 1 191 ? 28.175 25.896 78.420 1.00 26.73 ? 199 LEU A O   1 
ATOM   1499 C CB  . LEU A 1 191 ? 27.978 28.077 80.174 1.00 32.70 ? 199 LEU A CB  1 
ATOM   1500 C CG  . LEU A 1 191 ? 27.954 29.442 80.872 1.00 33.29 ? 199 LEU A CG  1 
ATOM   1501 C CD1 . LEU A 1 191 ? 26.780 29.581 81.828 1.00 35.15 ? 199 LEU A CD1 1 
ATOM   1502 C CD2 . LEU A 1 191 ? 29.259 29.709 81.599 1.00 34.19 ? 199 LEU A CD2 1 
ATOM   1503 N N   . MET A 1 192 ? 27.143 27.027 76.719 1.00 28.22 ? 200 MET A N   1 
ATOM   1504 C CA  . MET A 1 192 ? 27.587 26.076 75.666 1.00 29.20 ? 200 MET A CA  1 
ATOM   1505 C C   . MET A 1 192 ? 29.031 26.418 75.271 1.00 30.59 ? 200 MET A C   1 
ATOM   1506 O O   . MET A 1 192 ? 29.230 27.471 74.624 1.00 35.07 ? 200 MET A O   1 
ATOM   1507 C CB  . MET A 1 192 ? 26.672 26.149 74.440 1.00 28.52 ? 200 MET A CB  1 
ATOM   1508 C CG  . MET A 1 192 ? 25.513 25.172 74.483 1.00 30.43 ? 200 MET A CG  1 
ATOM   1509 S SD  . MET A 1 192 ? 24.171 25.635 73.370 1.00 37.15 ? 200 MET A SD  1 
ATOM   1510 C CE  . MET A 1 192 ? 24.632 27.330 72.989 1.00 39.84 ? 200 MET A CE  1 
ATOM   1511 N N   . GLY A 1 193 ? 29.991 25.569 75.651 1.00 32.85 ? 201 GLY A N   1 
ATOM   1512 C CA  . GLY A 1 193 ? 31.416 25.833 75.361 1.00 32.12 ? 201 GLY A CA  1 
ATOM   1513 C C   . GLY A 1 193 ? 31.844 27.257 75.665 1.00 30.13 ? 201 GLY A C   1 
ATOM   1514 O O   . GLY A 1 193 ? 32.460 27.880 74.780 1.00 28.93 ? 201 GLY A O   1 
ATOM   1515 N N   . PRO A 1 194 ? 31.601 27.800 76.880 1.00 26.13 ? 202 PRO A N   1 
ATOM   1516 C CA  . PRO A 1 194 ? 31.906 29.230 77.203 1.00 27.56 ? 202 PRO A CA  1 
ATOM   1517 C C   . PRO A 1 194 ? 33.350 29.610 76.891 1.00 30.61 ? 202 PRO A C   1 
ATOM   1518 O O   . PRO A 1 194 ? 34.266 28.783 77.106 1.00 30.28 ? 202 PRO A O   1 
ATOM   1519 C CB  . PRO A 1 194 ? 31.548 29.361 78.681 1.00 26.21 ? 202 PRO A CB  1 
ATOM   1520 C CG  . PRO A 1 194 ? 31.740 27.959 79.228 1.00 26.11 ? 202 PRO A CG  1 
ATOM   1521 C CD  . PRO A 1 194 ? 31.316 27.035 78.138 1.00 25.28 ? 202 PRO A CD  1 
ATOM   1522 N N   . PHE A 1 195 ? 33.560 30.836 76.405 1.00 28.12 ? 203 PHE A N   1 
ATOM   1523 C CA  . PHE A 1 195 ? 34.928 31.273 76.013 1.00 29.17 ? 203 PHE A CA  1 
ATOM   1524 C C   . PHE A 1 195 ? 35.675 31.790 77.235 1.00 31.21 ? 203 PHE A C   1 
ATOM   1525 O O   . PHE A 1 195 ? 35.695 33.020 77.454 1.00 30.85 ? 203 PHE A O   1 
ATOM   1526 C CB  . PHE A 1 195 ? 34.860 32.348 74.924 1.00 29.01 ? 203 PHE A CB  1 
ATOM   1527 C CG  . PHE A 1 195 ? 36.186 32.681 74.251 1.00 29.67 ? 203 PHE A CG  1 
ATOM   1528 C CD1 . PHE A 1 195 ? 37.209 31.742 74.180 1.00 29.53 ? 203 PHE A CD1 1 
ATOM   1529 C CD2 . PHE A 1 195 ? 36.403 33.933 73.688 1.00 30.87 ? 203 PHE A CD2 1 
ATOM   1530 C CE1 . PHE A 1 195 ? 38.413 32.052 73.566 1.00 29.15 ? 203 PHE A CE1 1 
ATOM   1531 C CE2 . PHE A 1 195 ? 37.608 34.237 73.075 1.00 32.67 ? 203 PHE A CE2 1 
ATOM   1532 C CZ  . PHE A 1 195 ? 38.609 33.296 73.014 1.00 32.10 ? 203 PHE A CZ  1 
ATOM   1533 N N   . PHE A 1 196 ? 36.265 30.887 78.023 1.00 28.52 ? 204 PHE A N   1 
ATOM   1534 C CA  . PHE A 1 196 ? 37.086 31.332 79.135 1.00 30.72 ? 204 PHE A CA  1 
ATOM   1535 C C   . PHE A 1 196 ? 38.556 31.176 78.764 1.00 29.49 ? 204 PHE A C   1 
ATOM   1536 O O   . PHE A 1 196 ? 38.899 30.394 77.880 1.00 28.34 ? 204 PHE A O   1 
ATOM   1537 C CB  . PHE A 1 196 ? 36.773 30.549 80.415 1.00 30.13 ? 204 PHE A CB  1 
ATOM   1538 C CG  . PHE A 1 196 ? 35.364 30.729 80.920 1.00 31.04 ? 204 PHE A CG  1 
ATOM   1539 C CD1 . PHE A 1 196 ? 34.809 31.994 81.041 1.00 28.81 ? 204 PHE A CD1 1 
ATOM   1540 C CD2 . PHE A 1 196 ? 34.599 29.636 81.292 1.00 31.84 ? 204 PHE A CD2 1 
ATOM   1541 C CE1 . PHE A 1 196 ? 33.511 32.157 81.509 1.00 32.58 ? 204 PHE A CE1 1 
ATOM   1542 C CE2 . PHE A 1 196 ? 33.303 29.803 81.766 1.00 31.76 ? 204 PHE A CE2 1 
ATOM   1543 C CZ  . PHE A 1 196 ? 32.767 31.061 81.871 1.00 34.37 ? 204 PHE A CZ  1 
ATOM   1544 N N   . GLY A 1 197 ? 39.410 31.932 79.460 1.00 30.70 ? 205 GLY A N   1 
ATOM   1545 C CA  . GLY A 1 197 ? 40.822 32.009 79.132 1.00 30.90 ? 205 GLY A CA  1 
ATOM   1546 C C   . GLY A 1 197 ? 41.741 31.794 80.328 1.00 31.98 ? 205 GLY A C   1 
ATOM   1547 O O   . GLY A 1 197 ? 41.289 31.748 81.469 1.00 35.00 ? 205 GLY A O   1 
ATOM   1548 N N   . GLY A 1 198 ? 43.037 31.654 80.037 1.00 34.59 ? 206 GLY A N   1 
ATOM   1549 C CA  . GLY A 1 198 ? 44.057 31.524 81.062 1.00 30.87 ? 206 GLY A CA  1 
ATOM   1550 C C   . GLY A 1 198 ? 45.461 31.544 80.466 1.00 30.55 ? 206 GLY A C   1 
ATOM   1551 O O   . GLY A 1 198 ? 45.697 30.965 79.407 1.00 30.15 ? 206 GLY A O   1 
ATOM   1552 N N   . GLU A 1 199 ? 46.383 32.228 81.154 1.00 31.40 ? 207 GLU A N   1 
ATOM   1553 C CA  . GLU A 1 199 ? 47.782 32.242 80.760 1.00 30.51 ? 207 GLU A CA  1 
ATOM   1554 C C   . GLU A 1 199 ? 48.324 30.816 80.704 1.00 32.59 ? 207 GLU A C   1 
ATOM   1555 O O   . GLU A 1 199 ? 48.937 30.426 79.713 1.00 36.19 ? 207 GLU A O   1 
ATOM   1556 C CB  . GLU A 1 199 ? 48.613 33.102 81.724 1.00 28.34 ? 207 GLU A CB  1 
ATOM   1557 C CG  . GLU A 1 199 ? 48.426 34.593 81.509 1.00 28.76 ? 207 GLU A CG  1 
ATOM   1558 C CD  . GLU A 1 199 ? 48.966 35.102 80.187 1.00 28.25 ? 207 GLU A CD  1 
ATOM   1559 O OE1 . GLU A 1 199 ? 50.198 35.016 79.978 1.00 27.34 ? 207 GLU A OE1 1 
ATOM   1560 O OE2 . GLU A 1 199 ? 48.159 35.581 79.356 1.00 24.36 ? 207 GLU A OE2 1 
ATOM   1561 N N   . GLU A 1 200 ? 48.072 30.045 81.768 1.00 35.58 ? 208 GLU A N   1 
ATOM   1562 C CA  . GLU A 1 200 ? 48.460 28.645 81.816 1.00 38.17 ? 208 GLU A CA  1 
ATOM   1563 C C   . GLU A 1 200 ? 47.496 27.807 80.978 1.00 31.82 ? 208 GLU A C   1 
ATOM   1564 O O   . GLU A 1 200 ? 46.283 27.987 81.064 1.00 34.11 ? 208 GLU A O   1 
ATOM   1565 C CB  . GLU A 1 200 ? 48.489 28.145 83.269 1.00 44.40 ? 208 GLU A CB  1 
ATOM   1566 C CG  . GLU A 1 200 ? 49.088 26.760 83.429 1.00 53.06 ? 208 GLU A CG  1 
ATOM   1567 C CD  . GLU A 1 200 ? 49.183 26.286 84.865 1.00 59.98 ? 208 GLU A CD  1 
ATOM   1568 O OE1 . GLU A 1 200 ? 49.893 26.942 85.660 1.00 63.63 ? 208 GLU A OE1 1 
ATOM   1569 O OE2 . GLU A 1 200 ? 48.546 25.261 85.197 1.00 66.87 ? 208 GLU A OE2 1 
ATOM   1570 N N   . ARG A 1 201 ? 48.054 26.896 80.170 1.00 27.68 ? 209 ARG A N   1 
ATOM   1571 C CA  . ARG A 1 201 ? 47.268 26.026 79.309 1.00 26.61 ? 209 ARG A CA  1 
ATOM   1572 C C   . ARG A 1 201 ? 46.762 24.795 80.056 1.00 26.58 ? 209 ARG A C   1 
ATOM   1573 O O   . ARG A 1 201 ? 47.442 24.281 80.942 1.00 26.64 ? 209 ARG A O   1 
ATOM   1574 C CB  . ARG A 1 201 ? 48.096 25.554 78.096 1.00 25.04 ? 209 ARG A CB  1 
ATOM   1575 C CG  . ARG A 1 201 ? 48.258 26.584 76.984 1.00 25.34 ? 209 ARG A CG  1 
ATOM   1576 C CD  . ARG A 1 201 ? 49.198 27.710 77.362 1.00 24.89 ? 209 ARG A CD  1 
ATOM   1577 N NE  . ARG A 1 201 ? 49.541 28.538 76.212 1.00 24.93 ? 209 ARG A NE  1 
ATOM   1578 C CZ  . ARG A 1 201 ? 48.685 29.296 75.540 1.00 29.19 ? 209 ARG A CZ  1 
ATOM   1579 N NH1 . ARG A 1 201 ? 47.454 29.511 75.977 1.00 34.91 ? 209 ARG A NH1 1 
ATOM   1580 N NH2 . ARG A 1 201 ? 49.078 29.862 74.403 1.00 30.32 ? 209 ARG A NH2 1 
ATOM   1581 N N   . THR A 1 202 ? 45.567 24.328 79.676 1.00 26.44 ? 210 THR A N   1 
ATOM   1582 C CA  . THR A 1 202 ? 45.084 23.013 80.067 1.00 26.94 ? 210 THR A CA  1 
ATOM   1583 C C   . THR A 1 202 ? 45.671 21.966 79.124 1.00 27.82 ? 210 THR A C   1 
ATOM   1584 O O   . THR A 1 202 ? 46.260 22.312 78.100 1.00 27.07 ? 210 THR A O   1 
ATOM   1585 C CB  . THR A 1 202 ? 43.556 22.952 80.044 1.00 25.66 ? 210 THR A CB  1 
ATOM   1586 O OG1 . THR A 1 202 ? 43.116 23.103 78.694 1.00 26.29 ? 210 THR A OG1 1 
ATOM   1587 C CG2 . THR A 1 202 ? 42.910 24.012 80.924 1.00 22.87 ? 210 THR A CG2 1 
ATOM   1588 N N   . ASN A 1 203 ? 45.489 20.686 79.469 1.00 27.39 ? 211 ASN A N   1 
ATOM   1589 C CA  . ASN A 1 203 ? 45.940 19.594 78.623 1.00 28.20 ? 211 ASN A CA  1 
ATOM   1590 C C   . ASN A 1 203 ? 45.239 19.617 77.267 1.00 30.84 ? 211 ASN A C   1 
ATOM   1591 O O   . ASN A 1 203 ? 45.888 19.440 76.238 1.00 29.21 ? 211 ASN A O   1 
ATOM   1592 C CB  . ASN A 1 203 ? 45.724 18.241 79.301 1.00 32.49 ? 211 ASN A CB  1 
ATOM   1593 C CG  . ASN A 1 203 ? 46.646 18.009 80.472 1.00 38.57 ? 211 ASN A CG  1 
ATOM   1594 O OD1 . ASN A 1 203 ? 46.210 17.821 81.613 1.00 44.99 ? 211 ASN A OD1 1 
ATOM   1595 N ND2 . ASN A 1 203 ? 47.946 18.016 80.217 1.00 40.86 ? 211 ASN A ND2 1 
ATOM   1596 N N   . SER A 1 204 ? 43.918 19.849 77.282 1.00 32.08 ? 212 SER A N   1 
ATOM   1597 C CA  . SER A 1 204 ? 43.122 19.873 76.064 1.00 29.84 ? 212 SER A CA  1 
ATOM   1598 C C   . SER A 1 204 ? 43.512 21.027 75.142 1.00 30.20 ? 212 SER A C   1 
ATOM   1599 O O   . SER A 1 204 ? 43.462 20.887 73.922 1.00 33.22 ? 212 SER A O   1 
ATOM   1600 C CB  . SER A 1 204 ? 41.629 19.938 76.386 1.00 31.48 ? 212 SER A CB  1 
ATOM   1601 O OG  . SER A 1 204 ? 41.263 21.145 77.035 1.00 34.80 ? 212 SER A OG  1 
ATOM   1602 N N   . GLU A 1 205 ? 43.913 22.157 75.736 1.00 30.43 ? 213 GLU A N   1 
ATOM   1603 C CA  . GLU A 1 205 ? 44.358 23.315 74.974 1.00 34.23 ? 213 GLU A CA  1 
ATOM   1604 C C   . GLU A 1 205 ? 45.667 23.047 74.229 1.00 34.72 ? 213 GLU A C   1 
ATOM   1605 O O   . GLU A 1 205 ? 45.896 23.615 73.163 1.00 38.09 ? 213 GLU A O   1 
ATOM   1606 C CB  . GLU A 1 205 ? 44.491 24.537 75.904 1.00 33.30 ? 213 GLU A CB  1 
ATOM   1607 C CG  . GLU A 1 205 ? 43.147 25.107 76.329 1.00 30.07 ? 213 GLU A CG  1 
ATOM   1608 C CD  . GLU A 1 205 ? 43.169 26.087 77.486 1.00 31.54 ? 213 GLU A CD  1 
ATOM   1609 O OE1 . GLU A 1 205 ? 44.273 26.504 77.904 1.00 31.81 ? 213 GLU A OE1 1 
ATOM   1610 O OE2 . GLU A 1 205 ? 42.073 26.429 77.985 1.00 35.60 ? 213 GLU A OE2 1 
ATOM   1611 N N   . ASN A 1 206 ? 46.516 22.175 74.790 1.00 35.30 ? 214 ASN A N   1 
ATOM   1612 C CA  . ASN A 1 206 ? 47.733 21.741 74.120 1.00 35.57 ? 214 ASN A CA  1 
ATOM   1613 C C   . ASN A 1 206 ? 47.499 20.571 73.165 1.00 33.52 ? 214 ASN A C   1 
ATOM   1614 O O   . ASN A 1 206 ? 48.390 20.212 72.398 1.00 31.64 ? 214 ASN A O   1 
ATOM   1615 C CB  . ASN A 1 206 ? 48.808 21.352 75.136 1.00 37.79 ? 214 ASN A CB  1 
ATOM   1616 C CG  . ASN A 1 206 ? 49.283 22.505 75.980 1.00 40.53 ? 214 ASN A CG  1 
ATOM   1617 O OD1 . ASN A 1 206 ? 49.543 23.608 75.484 1.00 41.08 ? 214 ASN A OD1 1 
ATOM   1618 N ND2 . ASN A 1 206 ? 49.401 22.278 77.279 1.00 41.82 ? 214 ASN A ND2 1 
ATOM   1619 N N   . GLY A 1 207 ? 46.300 19.979 73.219 1.00 33.50 ? 215 GLY A N   1 
ATOM   1620 C CA  . GLY A 1 207 ? 45.938 18.882 72.337 1.00 36.38 ? 215 GLY A CA  1 
ATOM   1621 C C   . GLY A 1 207 ? 45.782 19.309 70.879 1.00 37.15 ? 215 GLY A C   1 
ATOM   1622 O O   . GLY A 1 207 ? 46.061 20.454 70.531 1.00 32.34 ? 215 GLY A O   1 
ATOM   1623 N N   . PRO A 1 208 ? 45.318 18.406 69.984 1.00 43.30 ? 216 PRO A N   1 
ATOM   1624 C CA  . PRO A 1 208 ? 45.228 18.723 68.563 1.00 43.35 ? 216 PRO A CA  1 
ATOM   1625 C C   . PRO A 1 208 ? 44.195 19.801 68.250 1.00 38.43 ? 216 PRO A C   1 
ATOM   1626 O O   . PRO A 1 208 ? 43.232 19.978 68.993 1.00 38.50 ? 216 PRO A O   1 
ATOM   1627 C CB  . PRO A 1 208 ? 44.855 17.378 67.930 1.00 47.80 ? 216 PRO A CB  1 
ATOM   1628 C CG  . PRO A 1 208 ? 44.165 16.615 69.035 1.00 48.55 ? 216 PRO A CG  1 
ATOM   1629 C CD  . PRO A 1 208 ? 44.839 17.052 70.308 1.00 44.70 ? 216 PRO A CD  1 
ATOM   1630 N N   . SER A 1 209 ? 44.416 20.518 67.144 1.00 34.97 ? 217 SER A N   1 
ATOM   1631 C CA  . SER A 1 209 ? 43.492 21.540 66.686 1.00 36.83 ? 217 SER A CA  1 
ATOM   1632 C C   . SER A 1 209 ? 42.181 20.923 66.207 1.00 40.19 ? 217 SER A C   1 
ATOM   1633 O O   . SER A 1 209 ? 42.155 19.781 65.754 1.00 47.39 ? 217 SER A O   1 
ATOM   1634 C CB  . SER A 1 209 ? 44.120 22.365 65.567 1.00 36.57 ? 217 SER A CB  1 
ATOM   1635 O OG  . SER A 1 209 ? 45.320 22.982 66.000 1.00 37.11 ? 217 SER A OG  1 
ATOM   1636 N N   . GLU A 1 210 ? 41.099 21.702 66.311 1.00 45.39 ? 218 GLU A N   1 
ATOM   1637 C CA  . GLU A 1 210 ? 39.788 21.297 65.833 1.00 42.27 ? 218 GLU A CA  1 
ATOM   1638 C C   . GLU A 1 210 ? 39.686 21.604 64.340 1.00 43.08 ? 218 GLU A C   1 
ATOM   1639 O O   . GLU A 1 210 ? 40.633 22.113 63.747 1.00 42.12 ? 218 GLU A O   1 
ATOM   1640 C CB  . GLU A 1 210 ? 38.680 22.033 66.610 1.00 37.65 ? 218 GLU A CB  1 
ATOM   1641 C CG  . GLU A 1 210 ? 38.820 21.955 68.121 1.00 38.38 ? 218 GLU A CG  1 
ATOM   1642 C CD  . GLU A 1 210 ? 37.790 22.762 68.884 1.00 38.94 ? 218 GLU A CD  1 
ATOM   1643 O OE1 . GLU A 1 210 ? 36.764 23.142 68.275 1.00 35.60 ? 218 GLU A OE1 1 
ATOM   1644 O OE2 . GLU A 1 210 ? 38.020 23.037 70.084 1.00 39.40 ? 218 GLU A OE2 1 
ATOM   1645 N N   . ALA A 1 211 ? 38.528 21.292 63.747 1.00 40.48 ? 219 ALA A N   1 
ATOM   1646 C CA  . ALA A 1 211 ? 38.235 21.629 62.361 1.00 36.49 ? 219 ALA A CA  1 
ATOM   1647 C C   . ALA A 1 211 ? 38.570 23.082 62.022 1.00 38.34 ? 219 ALA A C   1 
ATOM   1648 O O   . ALA A 1 211 ? 39.159 23.355 60.977 1.00 35.48 ? 219 ALA A O   1 
ATOM   1649 C CB  . ALA A 1 211 ? 36.765 21.352 62.065 1.00 34.72 ? 219 ALA A CB  1 
ATOM   1650 N N   . LEU A 1 212 ? 38.179 24.004 62.912 1.00 39.78 ? 220 LEU A N   1 
ATOM   1651 C CA  . LEU A 1 212 ? 38.383 25.430 62.706 1.00 41.92 ? 220 LEU A CA  1 
ATOM   1652 C C   . LEU A 1 212 ? 39.283 26.031 63.784 1.00 38.06 ? 220 LEU A C   1 
ATOM   1653 O O   . LEU A 1 212 ? 40.254 26.711 63.463 1.00 45.17 ? 220 LEU A O   1 
ATOM   1654 C CB  . LEU A 1 212 ? 37.014 26.143 62.674 1.00 45.39 ? 220 LEU A CB  1 
ATOM   1655 C CG  . LEU A 1 212 ? 36.995 27.582 62.121 1.00 52.13 ? 220 LEU A CG  1 
ATOM   1656 C CD1 . LEU A 1 212 ? 35.609 27.971 61.649 1.00 52.19 ? 220 LEU A CD1 1 
ATOM   1657 C CD2 . LEU A 1 212 ? 37.451 28.601 63.155 1.00 52.69 ? 220 LEU A CD2 1 
ATOM   1658 N N   . LEU A 1 213 ? 38.951 25.778 65.056 1.00 36.39 ? 221 LEU A N   1 
ATOM   1659 C CA  . LEU A 1 213 ? 39.654 26.385 66.176 1.00 32.32 ? 221 LEU A CA  1 
ATOM   1660 C C   . LEU A 1 213 ? 41.050 25.802 66.376 1.00 29.01 ? 221 LEU A C   1 
ATOM   1661 O O   . LEU A 1 213 ? 41.240 24.591 66.294 1.00 28.00 ? 221 LEU A O   1 
ATOM   1662 C CB  . LEU A 1 213 ? 38.869 26.194 67.487 1.00 33.58 ? 221 LEU A CB  1 
ATOM   1663 C CG  . LEU A 1 213 ? 37.517 26.899 67.599 1.00 34.33 ? 221 LEU A CG  1 
ATOM   1664 C CD1 . LEU A 1 213 ? 37.013 26.859 69.026 1.00 35.63 ? 221 LEU A CD1 1 
ATOM   1665 C CD2 . LEU A 1 213 ? 37.589 28.336 67.116 1.00 33.33 ? 221 LEU A CD2 1 
ATOM   1666 N N   . SER A 1 214 ? 42.011 26.693 66.640 1.00 26.87 ? 222 SER A N   1 
ATOM   1667 C CA  . SER A 1 214 ? 43.329 26.323 67.130 1.00 24.87 ? 222 SER A CA  1 
ATOM   1668 C C   . SER A 1 214 ? 43.645 27.190 68.344 1.00 24.59 ? 222 SER A C   1 
ATOM   1669 O O   . SER A 1 214 ? 43.001 28.215 68.557 1.00 23.91 ? 222 SER A O   1 
ATOM   1670 C CB  . SER A 1 214 ? 44.392 26.506 66.053 1.00 22.55 ? 222 SER A CB  1 
ATOM   1671 O OG  . SER A 1 214 ? 44.597 27.879 65.764 1.00 21.96 ? 222 SER A OG  1 
ATOM   1672 N N   . LEU A 1 215 ? 44.645 26.773 69.127 1.00 24.60 ? 223 LEU A N   1 
ATOM   1673 C CA  . LEU A 1 215 ? 45.052 27.518 70.307 1.00 24.54 ? 223 LEU A CA  1 
ATOM   1674 C C   . LEU A 1 215 ? 45.565 28.903 69.916 1.00 27.16 ? 223 LEU A C   1 
ATOM   1675 O O   . LEU A 1 215 ? 45.306 29.881 70.615 1.00 31.31 ? 223 LEU A O   1 
ATOM   1676 C CB  . LEU A 1 215 ? 46.124 26.747 71.081 1.00 22.96 ? 223 LEU A CB  1 
ATOM   1677 C CG  . LEU A 1 215 ? 46.471 27.318 72.444 1.00 24.22 ? 223 LEU A CG  1 
ATOM   1678 C CD1 . LEU A 1 215 ? 45.302 27.180 73.397 1.00 24.36 ? 223 LEU A CD1 1 
ATOM   1679 C CD2 . LEU A 1 215 ? 47.707 26.651 73.011 1.00 23.27 ? 223 LEU A CD2 1 
ATOM   1680 N N   . ASP A 1 216 ? 46.284 28.972 68.790 1.00 25.74 ? 224 ASP A N   1 
ATOM   1681 C CA  . ASP A 1 216 ? 46.740 30.237 68.236 1.00 26.61 ? 224 ASP A CA  1 
ATOM   1682 C C   . ASP A 1 216 ? 45.586 31.189 67.927 1.00 26.07 ? 224 ASP A C   1 
ATOM   1683 O O   . ASP A 1 216 ? 45.688 32.386 68.188 1.00 26.62 ? 224 ASP A O   1 
ATOM   1684 C CB  . ASP A 1 216 ? 47.576 29.997 66.964 1.00 24.63 ? 224 ASP A CB  1 
ATOM   1685 C CG  . ASP A 1 216 ? 48.980 29.491 67.224 1.00 24.74 ? 224 ASP A CG  1 
ATOM   1686 O OD1 . ASP A 1 216 ? 49.408 29.500 68.398 1.00 23.93 ? 224 ASP A OD1 1 
ATOM   1687 O OD2 . ASP A 1 216 ? 49.652 29.088 66.254 1.00 29.83 ? 224 ASP A OD2 1 
ATOM   1688 N N   . LEU A 1 217 ? 44.493 30.651 67.371 1.00 24.83 ? 225 LEU A N   1 
ATOM   1689 C CA  . LEU A 1 217 ? 43.333 31.464 67.042 1.00 26.06 ? 225 LEU A CA  1 
ATOM   1690 C C   . LEU A 1 217 ? 42.691 32.023 68.309 1.00 25.74 ? 225 LEU A C   1 
ATOM   1691 O O   . LEU A 1 217 ? 42.341 33.200 68.360 1.00 25.96 ? 225 LEU A O   1 
ATOM   1692 C CB  . LEU A 1 217 ? 42.306 30.650 66.238 1.00 26.20 ? 225 LEU A CB  1 
ATOM   1693 C CG  . LEU A 1 217 ? 41.075 31.417 65.754 1.00 27.86 ? 225 LEU A CG  1 
ATOM   1694 C CD1 . LEU A 1 217 ? 41.452 32.513 64.778 1.00 29.80 ? 225 LEU A CD1 1 
ATOM   1695 C CD2 . LEU A 1 217 ? 40.079 30.487 65.110 1.00 29.56 ? 225 LEU A CD2 1 
ATOM   1696 N N   . LEU A 1 218 ? 42.551 31.170 69.331 1.00 26.87 ? 226 LEU A N   1 
ATOM   1697 C CA  . LEU A 1 218 ? 41.976 31.581 70.601 1.00 28.27 ? 226 LEU A CA  1 
ATOM   1698 C C   . LEU A 1 218 ? 42.844 32.636 71.285 1.00 29.48 ? 226 LEU A C   1 
ATOM   1699 O O   . LEU A 1 218 ? 42.316 33.577 71.873 1.00 30.05 ? 226 LEU A O   1 
ATOM   1700 C CB  . LEU A 1 218 ? 41.793 30.362 71.520 1.00 31.35 ? 226 LEU A CB  1 
ATOM   1701 C CG  . LEU A 1 218 ? 40.802 29.301 71.037 1.00 35.03 ? 226 LEU A CG  1 
ATOM   1702 C CD1 . LEU A 1 218 ? 40.677 28.174 72.042 1.00 35.65 ? 226 LEU A CD1 1 
ATOM   1703 C CD2 . LEU A 1 218 ? 39.434 29.901 70.761 1.00 39.91 ? 226 LEU A CD2 1 
ATOM   1704 N N   . ASP A 1 219 ? 44.173 32.469 71.203 1.00 26.79 ? 227 ASP A N   1 
ATOM   1705 C CA  . ASP A 1 219 ? 45.110 33.449 71.733 1.00 24.76 ? 227 ASP A CA  1 
ATOM   1706 C C   . ASP A 1 219 ? 44.981 34.792 71.016 1.00 23.37 ? 227 ASP A C   1 
ATOM   1707 O O   . ASP A 1 219 ? 45.053 35.843 71.649 1.00 24.30 ? 227 ASP A O   1 
ATOM   1708 C CB  . ASP A 1 219 ? 46.561 32.943 71.623 1.00 23.82 ? 227 ASP A CB  1 
ATOM   1709 C CG  . ASP A 1 219 ? 46.945 31.826 72.578 1.00 25.16 ? 227 ASP A CG  1 
ATOM   1710 O OD1 . ASP A 1 219 ? 46.146 31.520 73.492 1.00 26.29 ? 227 ASP A OD1 1 
ATOM   1711 O OD2 . ASP A 1 219 ? 48.041 31.254 72.407 1.00 24.59 ? 227 ASP A OD2 1 
ATOM   1712 N N   . LYS A 1 220 ? 44.792 34.740 69.692 1.00 23.07 ? 228 LYS A N   1 
ATOM   1713 C CA  . LYS A 1 220 ? 44.592 35.934 68.887 1.00 25.92 ? 228 LYS A CA  1 
ATOM   1714 C C   . LYS A 1 220 ? 43.302 36.651 69.283 1.00 24.91 ? 228 LYS A C   1 
ATOM   1715 O O   . LYS A 1 220 ? 43.276 37.878 69.365 1.00 23.12 ? 228 LYS A O   1 
ATOM   1716 C CB  . LYS A 1 220 ? 44.566 35.568 67.391 1.00 30.31 ? 228 LYS A CB  1 
ATOM   1717 C CG  . LYS A 1 220 ? 44.552 36.766 66.437 1.00 34.40 ? 228 LYS A CG  1 
ATOM   1718 C CD  . LYS A 1 220 ? 45.855 37.564 66.428 1.00 37.35 ? 228 LYS A CD  1 
ATOM   1719 C CE  . LYS A 1 220 ? 47.000 36.815 65.787 1.00 42.40 ? 228 LYS A CE  1 
ATOM   1720 N NZ  . LYS A 1 220 ? 48.275 37.577 65.878 1.00 47.72 ? 228 LYS A NZ  1 
ATOM   1721 N N   . PHE A 1 221 ? 42.237 35.876 69.527 1.00 23.95 ? 229 PHE A N   1 
ATOM   1722 C CA  . PHE A 1 221 ? 40.978 36.426 70.003 1.00 24.39 ? 229 PHE A CA  1 
ATOM   1723 C C   . PHE A 1 221 ? 41.166 37.259 71.267 1.00 24.93 ? 229 PHE A C   1 
ATOM   1724 O O   . PHE A 1 221 ? 40.655 38.371 71.348 1.00 32.17 ? 229 PHE A O   1 
ATOM   1725 C CB  . PHE A 1 221 ? 39.951 35.314 70.275 1.00 26.65 ? 229 PHE A CB  1 
ATOM   1726 C CG  . PHE A 1 221 ? 39.270 34.703 69.068 1.00 27.27 ? 229 PHE A CG  1 
ATOM   1727 C CD1 . PHE A 1 221 ? 39.097 35.432 67.899 1.00 27.01 ? 229 PHE A CD1 1 
ATOM   1728 C CD2 . PHE A 1 221 ? 38.811 33.398 69.101 1.00 28.05 ? 229 PHE A CD2 1 
ATOM   1729 C CE1 . PHE A 1 221 ? 38.469 34.866 66.797 1.00 29.91 ? 229 PHE A CE1 1 
ATOM   1730 C CE2 . PHE A 1 221 ? 38.189 32.834 67.992 1.00 30.76 ? 229 PHE A CE2 1 
ATOM   1731 C CZ  . PHE A 1 221 ? 38.022 33.571 66.848 1.00 31.97 ? 229 PHE A CZ  1 
ATOM   1732 N N   . TRP A 1 222 ? 41.907 36.717 72.242 1.00 25.86 ? 230 TRP A N   1 
ATOM   1733 C CA  . TRP A 1 222 ? 42.127 37.404 73.506 1.00 26.82 ? 230 TRP A CA  1 
ATOM   1734 C C   . TRP A 1 222 ? 42.980 38.657 73.335 1.00 25.86 ? 230 TRP A C   1 
ATOM   1735 O O   . TRP A 1 222 ? 42.731 39.666 73.991 1.00 24.39 ? 230 TRP A O   1 
ATOM   1736 C CB  . TRP A 1 222 ? 42.772 36.476 74.549 1.00 26.52 ? 230 TRP A CB  1 
ATOM   1737 C CG  . TRP A 1 222 ? 41.866 35.395 75.058 1.00 27.01 ? 230 TRP A CG  1 
ATOM   1738 C CD1 . TRP A 1 222 ? 42.095 34.053 75.022 1.00 27.01 ? 230 TRP A CD1 1 
ATOM   1739 C CD2 . TRP A 1 222 ? 40.589 35.569 75.685 1.00 24.31 ? 230 TRP A CD2 1 
ATOM   1740 N NE1 . TRP A 1 222 ? 41.039 33.377 75.586 1.00 25.64 ? 230 TRP A NE1 1 
ATOM   1741 C CE2 . TRP A 1 222 ? 40.099 34.284 76.001 1.00 26.45 ? 230 TRP A CE2 1 
ATOM   1742 C CE3 . TRP A 1 222 ? 39.809 36.684 76.010 1.00 24.42 ? 230 TRP A CE3 1 
ATOM   1743 C CZ2 . TRP A 1 222 ? 38.865 34.088 76.622 1.00 26.75 ? 230 TRP A CZ2 1 
ATOM   1744 C CZ3 . TRP A 1 222 ? 38.585 36.487 76.626 1.00 24.80 ? 230 TRP A CZ3 1 
ATOM   1745 C CH2 . TRP A 1 222 ? 38.126 35.202 76.926 1.00 26.05 ? 230 TRP A CH2 1 
ATOM   1746 N N   . ARG A 1 223 ? 43.980 38.583 72.449 1.00 29.06 ? 231 ARG A N   1 
ATOM   1747 C CA  . ARG A 1 223 ? 44.854 39.713 72.179 1.00 31.52 ? 231 ARG A CA  1 
ATOM   1748 C C   . ARG A 1 223 ? 44.073 40.896 71.610 1.00 28.67 ? 231 ARG A C   1 
ATOM   1749 O O   . ARG A 1 223 ? 44.352 42.044 71.948 1.00 29.40 ? 231 ARG A O   1 
ATOM   1750 C CB  . ARG A 1 223 ? 45.982 39.303 71.221 1.00 35.58 ? 231 ARG A CB  1 
ATOM   1751 C CG  . ARG A 1 223 ? 46.979 40.419 70.953 1.00 44.23 ? 231 ARG A CG  1 
ATOM   1752 C CD  . ARG A 1 223 ? 48.289 39.896 70.392 1.00 54.14 ? 231 ARG A CD  1 
ATOM   1753 N NE  . ARG A 1 223 ? 49.303 40.942 70.301 1.00 61.87 ? 231 ARG A NE  1 
ATOM   1754 C CZ  . ARG A 1 223 ? 49.863 41.545 71.343 1.00 65.69 ? 231 ARG A CZ  1 
ATOM   1755 N NH1 . ARG A 1 223 ? 49.582 41.183 72.585 1.00 69.56 ? 231 ARG A NH1 1 
ATOM   1756 N NH2 . ARG A 1 223 ? 50.730 42.532 71.135 1.00 70.28 ? 231 ARG A NH2 1 
ATOM   1757 N N   . LEU A 1 224 ? 43.086 40.599 70.756 1.00 26.75 ? 232 LEU A N   1 
ATOM   1758 C CA  . LEU A 1 224 ? 42.251 41.618 70.141 1.00 28.15 ? 232 LEU A CA  1 
ATOM   1759 C C   . LEU A 1 224 ? 41.078 42.059 71.017 1.00 27.23 ? 232 LEU A C   1 
ATOM   1760 O O   . LEU A 1 224 ? 40.581 43.170 70.859 1.00 26.73 ? 232 LEU A O   1 
ATOM   1761 C CB  . LEU A 1 224 ? 41.717 41.074 68.807 1.00 29.45 ? 232 LEU A CB  1 
ATOM   1762 C CG  . LEU A 1 224 ? 42.772 40.841 67.727 1.00 29.33 ? 232 LEU A CG  1 
ATOM   1763 C CD1 . LEU A 1 224 ? 42.225 40.011 66.591 1.00 29.17 ? 232 LEU A CD1 1 
ATOM   1764 C CD2 . LEU A 1 224 ? 43.296 42.153 67.185 1.00 30.16 ? 232 LEU A CD2 1 
ATOM   1765 N N   . SER A 1 225 ? 40.644 41.191 71.939 1.00 30.58 ? 233 SER A N   1 
ATOM   1766 C CA  . SER A 1 225 ? 39.452 41.440 72.738 1.00 36.40 ? 233 SER A CA  1 
ATOM   1767 C C   . SER A 1 225 ? 39.732 42.157 74.056 1.00 36.25 ? 233 SER A C   1 
ATOM   1768 O O   . SER A 1 225 ? 39.060 43.131 74.385 1.00 33.95 ? 233 SER A O   1 
ATOM   1769 C CB  . SER A 1 225 ? 38.734 40.131 73.036 1.00 34.41 ? 233 SER A CB  1 
ATOM   1770 O OG  . SER A 1 225 ? 38.294 39.530 71.832 1.00 47.75 ? 233 SER A OG  1 
ATOM   1771 N N   . LEU A 1 226 ? 40.711 41.642 74.807 1.00 36.97 ? 234 LEU A N   1 
ATOM   1772 C CA  . LEU A 1 226 ? 41.059 42.181 76.112 1.00 37.67 ? 234 LEU A CA  1 
ATOM   1773 C C   . LEU A 1 226 ? 41.656 43.578 75.977 1.00 37.35 ? 234 LEU A C   1 
ATOM   1774 O O   . LEU A 1 226 ? 42.269 43.893 74.960 1.00 34.49 ? 234 LEU A O   1 
ATOM   1775 C CB  . LEU A 1 226 ? 42.069 41.261 76.805 1.00 34.42 ? 234 LEU A CB  1 
ATOM   1776 C CG  . LEU A 1 226 ? 41.568 39.871 77.152 1.00 35.96 ? 234 LEU A CG  1 
ATOM   1777 C CD1 . LEU A 1 226 ? 42.701 38.994 77.611 1.00 35.35 ? 234 LEU A CD1 1 
ATOM   1778 C CD2 . LEU A 1 226 ? 40.492 39.925 78.222 1.00 36.57 ? 234 LEU A CD2 1 
ATOM   1779 N N   . PRO A 1 227 ? 41.509 44.456 76.997 1.00 39.35 ? 235 PRO A N   1 
ATOM   1780 C CA  . PRO A 1 227 ? 42.106 45.784 76.936 1.00 36.72 ? 235 PRO A CA  1 
ATOM   1781 C C   . PRO A 1 227 ? 43.624 45.727 76.811 1.00 34.19 ? 235 PRO A C   1 
ATOM   1782 O O   . PRO A 1 227 ? 44.243 44.742 77.209 1.00 30.02 ? 235 PRO A O   1 
ATOM   1783 C CB  . PRO A 1 227 ? 41.647 46.442 78.243 1.00 38.50 ? 235 PRO A CB  1 
ATOM   1784 C CG  . PRO A 1 227 ? 41.285 45.298 79.152 1.00 38.46 ? 235 PRO A CG  1 
ATOM   1785 C CD  . PRO A 1 227 ? 40.788 44.203 78.256 1.00 40.92 ? 235 PRO A CD  1 
ATOM   1786 N N   . ASN A 1 228 ? 44.207 46.787 76.245 1.00 35.23 ? 236 ASN A N   1 
ATOM   1787 C CA  . ASN A 1 228 ? 45.622 46.798 75.923 1.00 37.55 ? 236 ASN A CA  1 
ATOM   1788 C C   . ASN A 1 228 ? 46.439 46.664 77.207 1.00 38.56 ? 236 ASN A C   1 
ATOM   1789 O O   . ASN A 1 228 ? 46.278 47.460 78.130 1.00 40.32 ? 236 ASN A O   1 
ATOM   1790 C CB  . ASN A 1 228 ? 45.989 48.073 75.158 1.00 40.27 ? 236 ASN A CB  1 
ATOM   1791 C CG  . ASN A 1 228 ? 47.110 47.867 74.178 1.00 47.13 ? 236 ASN A CG  1 
ATOM   1792 O OD1 . ASN A 1 228 ? 48.211 48.407 74.329 1.00 50.38 ? 236 ASN A OD1 1 
ATOM   1793 N ND2 . ASN A 1 228 ? 46.850 47.070 73.146 1.00 50.12 ? 236 ASN A ND2 1 
ATOM   1794 N N   . GLY A 1 229 ? 47.286 45.628 77.265 1.00 36.16 ? 237 GLY A N   1 
ATOM   1795 C CA  . GLY A 1 229 ? 48.135 45.376 78.418 1.00 33.95 ? 237 GLY A CA  1 
ATOM   1796 C C   . GLY A 1 229 ? 47.652 44.259 79.343 1.00 33.17 ? 237 GLY A C   1 
ATOM   1797 O O   . GLY A 1 229 ? 48.386 43.839 80.234 1.00 38.08 ? 237 GLY A O   1 
ATOM   1798 N N   . ALA A 1 230 ? 46.419 43.784 79.132 1.00 29.88 ? 238 ALA A N   1 
ATOM   1799 C CA  . ALA A 1 230 ? 45.858 42.714 79.942 1.00 32.53 ? 238 ALA A CA  1 
ATOM   1800 C C   . ALA A 1 230 ? 46.439 41.358 79.547 1.00 32.66 ? 238 ALA A C   1 
ATOM   1801 O O   . ALA A 1 230 ? 46.971 41.202 78.450 1.00 34.30 ? 238 ALA A O   1 
ATOM   1802 C CB  . ALA A 1 230 ? 44.344 42.690 79.810 1.00 32.45 ? 238 ALA A CB  1 
ATOM   1803 N N   . THR A 1 231 ? 46.333 40.389 80.463 1.00 32.69 ? 239 THR A N   1 
ATOM   1804 C CA  . THR A 1 231 ? 46.741 39.017 80.211 1.00 30.79 ? 239 THR A CA  1 
ATOM   1805 C C   . THR A 1 231 ? 45.486 38.151 80.158 1.00 30.30 ? 239 THR A C   1 
ATOM   1806 O O   . THR A 1 231 ? 44.390 38.633 80.432 1.00 30.27 ? 239 THR A O   1 
ATOM   1807 C CB  . THR A 1 231 ? 47.737 38.551 81.280 1.00 33.90 ? 239 THR A CB  1 
ATOM   1808 O OG1 . THR A 1 231 ? 47.054 38.374 82.522 1.00 41.44 ? 239 THR A OG1 1 
ATOM   1809 C CG2 . THR A 1 231 ? 48.891 39.532 81.469 1.00 30.68 ? 239 THR A CG2 1 
ATOM   1810 N N   . ARG A 1 232 ? 45.656 36.868 79.818 1.00 31.00 ? 240 ARG A N   1 
ATOM   1811 C CA  . ARG A 1 232 ? 44.542 35.935 79.754 1.00 30.03 ? 240 ARG A CA  1 
ATOM   1812 C C   . ARG A 1 232 ? 44.004 35.544 81.132 1.00 34.15 ? 240 ARG A C   1 
ATOM   1813 O O   . ARG A 1 232 ? 42.961 34.898 81.221 1.00 35.83 ? 240 ARG A O   1 
ATOM   1814 C CB  . ARG A 1 232 ? 44.947 34.670 78.978 1.00 28.50 ? 240 ARG A CB  1 
ATOM   1815 C CG  . ARG A 1 232 ? 45.253 34.921 77.505 1.00 26.61 ? 240 ARG A CG  1 
ATOM   1816 C CD  . ARG A 1 232 ? 45.319 33.623 76.714 1.00 25.93 ? 240 ARG A CD  1 
ATOM   1817 N NE  . ARG A 1 232 ? 46.450 32.787 77.099 1.00 22.93 ? 240 ARG A NE  1 
ATOM   1818 C CZ  . ARG A 1 232 ? 47.707 33.005 76.730 1.00 23.22 ? 240 ARG A CZ  1 
ATOM   1819 N NH1 . ARG A 1 232 ? 48.014 33.937 75.842 1.00 22.45 ? 240 ARG A NH1 1 
ATOM   1820 N NH2 . ARG A 1 232 ? 48.678 32.259 77.250 1.00 22.68 ? 240 ARG A NH2 1 
ATOM   1821 N N   . ASP A 1 233 ? 44.719 35.933 82.198 1.00 37.00 ? 241 ASP A N   1 
ATOM   1822 C CA  . ASP A 1 233 ? 44.258 35.734 83.565 1.00 36.23 ? 241 ASP A CA  1 
ATOM   1823 C C   . ASP A 1 233 ? 43.399 36.887 84.089 1.00 35.53 ? 241 ASP A C   1 
ATOM   1824 O O   . ASP A 1 233 ? 42.979 36.866 85.245 1.00 37.47 ? 241 ASP A O   1 
ATOM   1825 C CB  . ASP A 1 233 ? 45.463 35.505 84.501 1.00 32.80 ? 241 ASP A CB  1 
ATOM   1826 C CG  . ASP A 1 233 ? 46.107 34.133 84.388 1.00 30.95 ? 241 ASP A CG  1 
ATOM   1827 O OD1 . ASP A 1 233 ? 45.589 33.293 83.621 1.00 27.54 ? 241 ASP A OD1 1 
ATOM   1828 O OD2 . ASP A 1 233 ? 47.126 33.900 85.070 1.00 31.40 ? 241 ASP A OD2 1 
ATOM   1829 N N   . HIS A 1 234 ? 43.142 37.887 83.235 1.00 34.66 ? 242 HIS A N   1 
ATOM   1830 C CA  . HIS A 1 234 ? 42.190 38.946 83.535 1.00 32.60 ? 242 HIS A CA  1 
ATOM   1831 C C   . HIS A 1 234 ? 40.818 38.332 83.805 1.00 32.37 ? 242 HIS A C   1 
ATOM   1832 O O   . HIS A 1 234 ? 40.439 37.359 83.156 1.00 34.49 ? 242 HIS A O   1 
ATOM   1833 C CB  . HIS A 1 234 ? 42.119 39.946 82.365 1.00 32.83 ? 242 HIS A CB  1 
ATOM   1834 C CG  . HIS A 1 234 ? 41.510 41.275 82.697 1.00 32.84 ? 242 HIS A CG  1 
ATOM   1835 N ND1 . HIS A 1 234 ? 40.164 41.411 82.969 1.00 34.29 ? 242 HIS A ND1 1 
ATOM   1836 C CD2 . HIS A 1 234 ? 42.091 42.493 82.761 1.00 31.61 ? 242 HIS A CD2 1 
ATOM   1837 C CE1 . HIS A 1 234 ? 39.968 42.701 83.205 1.00 30.98 ? 242 HIS A CE1 1 
ATOM   1838 N NE2 . HIS A 1 234 ? 41.106 43.388 83.090 1.00 33.29 ? 242 HIS A NE2 1 
ATOM   1839 N N   . HIS A 1 235 ? 40.078 38.911 84.758 1.00 33.68 ? 243 HIS A N   1 
ATOM   1840 C CA  . HIS A 1 235 ? 38.816 38.335 85.198 1.00 33.00 ? 243 HIS A CA  1 
ATOM   1841 C C   . HIS A 1 235 ? 37.783 38.241 84.076 1.00 33.14 ? 243 HIS A C   1 
ATOM   1842 O O   . HIS A 1 235 ? 36.909 37.377 84.110 1.00 32.89 ? 243 HIS A O   1 
ATOM   1843 C CB  . HIS A 1 235 ? 38.226 39.109 86.394 1.00 31.42 ? 243 HIS A CB  1 
ATOM   1844 C CG  . HIS A 1 235 ? 37.906 40.549 86.128 1.00 34.83 ? 243 HIS A CG  1 
ATOM   1845 N ND1 . HIS A 1 235 ? 38.867 41.539 86.251 1.00 40.26 ? 243 HIS A ND1 1 
ATOM   1846 C CD2 . HIS A 1 235 ? 36.728 41.126 85.805 1.00 37.92 ? 243 HIS A CD2 1 
ATOM   1847 C CE1 . HIS A 1 235 ? 38.253 42.681 85.974 1.00 41.24 ? 243 HIS A CE1 1 
ATOM   1848 N NE2 . HIS A 1 235 ? 36.962 42.476 85.694 1.00 43.87 ? 243 HIS A NE2 1 
ATOM   1849 N N   . MET A 1 236 ? 37.893 39.126 83.083 1.00 33.32 ? 244 MET A N   1 
ATOM   1850 C CA  . MET A 1 236 ? 36.940 39.098 81.941 1.00 34.91 ? 244 MET A CA  1 
ATOM   1851 C C   . MET A 1 236 ? 37.172 37.814 81.129 1.00 35.82 ? 244 MET A C   1 
ATOM   1852 O O   . MET A 1 236 ? 36.194 37.305 80.540 1.00 36.99 ? 244 MET A O   1 
ATOM   1853 C CB  . MET A 1 236 ? 37.103 40.340 81.059 1.00 37.41 ? 244 MET A CB  1 
ATOM   1854 C CG  . MET A 1 236 ? 36.365 41.553 81.592 1.00 35.98 ? 244 MET A CG  1 
ATOM   1855 S SD  . MET A 1 236 ? 36.852 43.069 80.746 1.00 44.87 ? 244 MET A SD  1 
ATOM   1856 C CE  . MET A 1 236 ? 38.327 42.439 79.936 1.00 33.60 ? 244 MET A CE  1 
ATOM   1857 N N   . ALA A 1 237 ? 38.411 37.313 81.103 1.00 32.79 ? 245 ALA A N   1 
ATOM   1858 C CA  . ALA A 1 237 ? 38.700 36.066 80.410 1.00 29.60 ? 245 ALA A CA  1 
ATOM   1859 C C   . ALA A 1 237 ? 38.610 34.871 81.356 1.00 28.52 ? 245 ALA A C   1 
ATOM   1860 O O   . ALA A 1 237 ? 37.935 33.890 81.053 1.00 26.03 ? 245 ALA A O   1 
ATOM   1861 C CB  . ALA A 1 237 ? 40.080 36.122 79.775 1.00 27.48 ? 245 ALA A CB  1 
ATOM   1862 N N   . ASN A 1 238 ? 39.308 34.965 82.494 1.00 30.83 ? 246 ASN A N   1 
ATOM   1863 C CA  . ASN A 1 238 ? 39.410 33.869 83.443 1.00 31.36 ? 246 ASN A CA  1 
ATOM   1864 C C   . ASN A 1 238 ? 38.530 34.112 84.667 1.00 31.69 ? 246 ASN A C   1 
ATOM   1865 O O   . ASN A 1 238 ? 38.842 34.969 85.492 1.00 28.13 ? 246 ASN A O   1 
ATOM   1866 C CB  . ASN A 1 238 ? 40.864 33.688 83.877 1.00 34.93 ? 246 ASN A CB  1 
ATOM   1867 C CG  . ASN A 1 238 ? 41.117 32.411 84.642 1.00 33.50 ? 246 ASN A CG  1 
ATOM   1868 O OD1 . ASN A 1 238 ? 40.204 31.624 84.923 1.00 30.51 ? 246 ASN A OD1 1 
ATOM   1869 N ND2 . ASN A 1 238 ? 42.375 32.177 84.993 1.00 32.11 ? 246 ASN A ND2 1 
ATOM   1870 N N   . PRO A 1 239 ? 37.423 33.353 84.845 1.00 34.46 ? 247 PRO A N   1 
ATOM   1871 C CA  . PRO A 1 239 ? 36.553 33.542 86.001 1.00 36.79 ? 247 PRO A CA  1 
ATOM   1872 C C   . PRO A 1 239 ? 37.188 33.113 87.322 1.00 39.96 ? 247 PRO A C   1 
ATOM   1873 O O   . PRO A 1 239 ? 36.720 33.507 88.388 1.00 43.65 ? 247 PRO A O   1 
ATOM   1874 C CB  . PRO A 1 239 ? 35.325 32.700 85.651 1.00 34.90 ? 247 PRO A CB  1 
ATOM   1875 C CG  . PRO A 1 239 ? 35.835 31.647 84.712 1.00 33.71 ? 247 PRO A CG  1 
ATOM   1876 C CD  . PRO A 1 239 ? 36.968 32.275 83.950 1.00 33.60 ? 247 PRO A CD  1 
ATOM   1877 N N   . PHE A 1 240 ? 38.254 32.304 87.236 1.00 46.37 ? 248 PHE A N   1 
ATOM   1878 C CA  . PHE A 1 240 ? 39.002 31.859 88.400 1.00 50.16 ? 248 PHE A CA  1 
ATOM   1879 C C   . PHE A 1 240 ? 40.448 32.346 88.340 1.00 56.50 ? 248 PHE A C   1 
ATOM   1880 O O   . PHE A 1 240 ? 41.371 31.628 88.721 1.00 57.56 ? 248 PHE A O   1 
ATOM   1881 C CB  . PHE A 1 240 ? 38.919 30.330 88.500 1.00 47.83 ? 248 PHE A CB  1 
ATOM   1882 C CG  . PHE A 1 240 ? 37.502 29.865 88.716 1.00 52.04 ? 248 PHE A CG  1 
ATOM   1883 C CD1 . PHE A 1 240 ? 36.855 30.100 89.916 1.00 53.25 ? 248 PHE A CD1 1 
ATOM   1884 C CD2 . PHE A 1 240 ? 36.801 29.231 87.705 1.00 53.62 ? 248 PHE A CD2 1 
ATOM   1885 C CE1 . PHE A 1 240 ? 35.544 29.684 90.110 1.00 56.97 ? 248 PHE A CE1 1 
ATOM   1886 C CE2 . PHE A 1 240 ? 35.490 28.820 87.904 1.00 55.20 ? 248 PHE A CE2 1 
ATOM   1887 C CZ  . PHE A 1 240 ? 34.870 29.048 89.103 1.00 56.42 ? 248 PHE A CZ  1 
ATOM   1888 N N   . GLY A 1 241 ? 40.624 33.586 87.867 1.00 54.55 ? 249 GLY A N   1 
ATOM   1889 C CA  . GLY A 1 241 ? 41.927 34.225 87.822 1.00 54.48 ? 249 GLY A CA  1 
ATOM   1890 C C   . GLY A 1 241 ? 42.331 34.782 89.184 1.00 54.83 ? 249 GLY A C   1 
ATOM   1891 O O   . GLY A 1 241 ? 41.562 34.698 90.139 1.00 52.67 ? 249 GLY A O   1 
ATOM   1892 N N   . PRO A 1 242 ? 43.542 35.375 89.310 1.00 62.12 ? 250 PRO A N   1 
ATOM   1893 C CA  . PRO A 1 242 ? 44.060 35.813 90.603 1.00 54.57 ? 250 PRO A CA  1 
ATOM   1894 C C   . PRO A 1 242 ? 43.260 36.931 91.268 1.00 49.58 ? 250 PRO A C   1 
ATOM   1895 O O   . PRO A 1 242 ? 43.225 37.009 92.494 1.00 60.89 ? 250 PRO A O   1 
ATOM   1896 C CB  . PRO A 1 242 ? 45.486 36.281 90.273 1.00 56.87 ? 250 PRO A CB  1 
ATOM   1897 C CG  . PRO A 1 242 ? 45.795 35.703 88.912 1.00 57.21 ? 250 PRO A CG  1 
ATOM   1898 C CD  . PRO A 1 242 ? 44.480 35.635 88.207 1.00 62.96 ? 250 PRO A CD  1 
ATOM   1899 N N   . THR A 1 243 ? 42.633 37.795 90.457 1.00 44.36 ? 251 THR A N   1 
ATOM   1900 C CA  . THR A 1 243 ? 41.915 38.951 90.972 1.00 46.79 ? 251 THR A CA  1 
ATOM   1901 C C   . THR A 1 243 ? 40.449 38.971 90.543 1.00 46.45 ? 251 THR A C   1 
ATOM   1902 O O   . THR A 1 243 ? 39.850 40.041 90.438 1.00 43.48 ? 251 THR A O   1 
ATOM   1903 C CB  . THR A 1 243 ? 42.623 40.236 90.527 1.00 52.97 ? 251 THR A CB  1 
ATOM   1904 O OG1 . THR A 1 243 ? 42.207 40.565 89.201 1.00 55.46 ? 251 THR A OG1 1 
ATOM   1905 C CG2 . THR A 1 243 ? 44.145 40.116 90.582 1.00 53.12 ? 251 THR A CG2 1 
ATOM   1906 N N   . SER A 1 244 ? 39.923 37.769 90.320 1.00 45.86 ? 252 SER A N   1 
ATOM   1907 C CA  . SER A 1 244 ? 38.513 37.629 89.901 1.00 47.95 ? 252 SER A CA  1 
ATOM   1908 C C   . SER A 1 244 ? 37.632 37.527 91.144 1.00 43.63 ? 252 SER A C   1 
ATOM   1909 O O   . SER A 1 244 ? 38.142 37.114 92.199 1.00 42.41 ? 252 SER A O   1 
ATOM   1910 C CB  . SER A 1 244 ? 38.354 36.419 89.027 1.00 53.88 ? 252 SER A CB  1 
ATOM   1911 O OG  . SER A 1 244 ? 39.316 36.401 87.983 1.00 53.86 ? 252 SER A OG  1 
ATOM   1912 N N   . PRO A 1 245 ? 36.324 37.875 91.086 1.00 55.28 ? 253 PRO A N   1 
ATOM   1913 C CA  . PRO A 1 245 ? 35.403 37.723 92.246 1.00 56.93 ? 253 PRO A CA  1 
ATOM   1914 C C   . PRO A 1 245 ? 35.509 36.351 92.896 1.00 55.10 ? 253 PRO A C   1 
ATOM   1915 O O   . PRO A 1 245 ? 35.874 35.357 92.233 1.00 50.73 ? 253 PRO A O   1 
ATOM   1916 C CB  . PRO A 1 245 ? 34.023 37.969 91.657 1.00 62.16 ? 253 PRO A CB  1 
ATOM   1917 C CG  . PRO A 1 245 ? 34.300 38.983 90.571 1.00 61.25 ? 253 PRO A CG  1 
ATOM   1918 C CD  . PRO A 1 245 ? 35.559 38.495 89.942 1.00 59.60 ? 253 PRO A CD  1 
ATOM   1919 N N   . THR A 1 246 ? 35.141 36.285 94.175 1.00 54.61 ? 254 THR A N   1 
ATOM   1920 C CA  . THR A 1 246 ? 35.281 35.023 94.922 1.00 52.17 ? 254 THR A CA  1 
ATOM   1921 C C   . THR A 1 246 ? 34.227 34.048 94.454 1.00 51.05 ? 254 THR A C   1 
ATOM   1922 O O   . THR A 1 246 ? 34.585 32.866 94.289 1.00 54.04 ? 254 THR A O   1 
ATOM   1923 C CB  . THR A 1 246 ? 35.205 35.305 96.420 1.00 46.07 ? 254 THR A CB  1 
ATOM   1924 O OG1 . THR A 1 246 ? 35.404 36.706 96.571 1.00 46.69 ? 254 THR A OG1 1 
ATOM   1925 C CG2 . THR A 1 246 ? 36.272 34.555 97.193 1.00 46.33 ? 254 THR A CG2 1 
ATOM   1926 N N   . LEU A 1 247 ? 32.984 34.499 94.296 1.00 43.59 ? 255 LEU A N   1 
ATOM   1927 C CA  . LEU A 1 247 ? 31.890 33.650 93.746 1.00 48.42 ? 255 LEU A CA  1 
ATOM   1928 C C   . LEU A 1 247 ? 31.355 32.701 94.829 1.00 48.82 ? 255 LEU A C   1 
ATOM   1929 O O   . LEU A 1 247 ? 30.231 32.203 94.662 1.00 52.85 ? 255 LEU A O   1 
ATOM   1930 C CB  . LEU A 1 247 ? 32.280 32.883 92.479 1.00 46.74 ? 255 LEU A CB  1 
ATOM   1931 C CG  . LEU A 1 247 ? 31.805 33.460 91.144 1.00 46.24 ? 255 LEU A CG  1 
ATOM   1932 C CD1 . LEU A 1 247 ? 32.275 34.887 90.970 1.00 47.46 ? 255 LEU A CD1 1 
ATOM   1933 C CD2 . LEU A 1 247 ? 32.338 32.594 90.020 1.00 45.54 ? 255 LEU A CD2 1 
ATOM   1934 N N   . GLU A 1 248 ? 32.112 32.477 95.899 1.00 51.04 ? 256 GLU A N   1 
ATOM   1935 C CA  . GLU A 1 248 ? 31.621 31.623 97.010 1.00 53.09 ? 256 GLU A CA  1 
ATOM   1936 C C   . GLU A 1 248 ? 30.579 32.412 97.806 1.00 52.92 ? 256 GLU A C   1 
ATOM   1937 O O   . GLU A 1 248 ? 29.712 31.791 98.443 1.00 49.89 ? 256 GLU A O   1 
ATOM   1938 C CB  . GLU A 1 248 ? 32.772 31.189 97.913 1.00 54.97 ? 256 GLU A CB  1 
ATOM   1939 C CG  . GLU A 1 248 ? 34.144 31.550 97.355 1.00 58.68 ? 256 GLU A CG  1 
ATOM   1940 C CD  . GLU A 1 248 ? 34.932 30.345 96.887 1.00 63.56 ? 256 GLU A CD  1 
ATOM   1941 O OE1 . GLU A 1 248 ? 34.855 29.297 97.560 1.00 60.59 ? 256 GLU A OE1 1 
ATOM   1942 O OE2 . GLU A 1 248 ? 35.617 30.452 95.852 1.00 62.88 ? 256 GLU A OE2 1 
ATOM   1943 N N   . SER A 1 249 ? 30.666 33.734 97.749 1.00 55.93 ? 257 SER A N   1 
ATOM   1944 C CA  . SER A 1 249 ? 29.721 34.598 98.488 1.00 56.11 ? 257 SER A CA  1 
ATOM   1945 C C   . SER A 1 249 ? 28.533 34.931 97.587 1.00 54.47 ? 257 SER A C   1 
ATOM   1946 O O   . SER A 1 249 ? 27.472 35.284 98.127 1.00 61.59 ? 257 SER A O   1 
ATOM   1947 C CB  . SER A 1 249 ? 30.427 35.847 98.876 1.00 57.11 ? 257 SER A CB  1 
ATOM   1948 O OG  . SER A 1 249 ? 31.247 36.304 97.809 1.00 60.24 ? 257 SER A OG  1 
ATOM   1949 N N   . ILE A 1 250 ? 28.715 34.833 96.273 1.00 49.15 ? 258 ILE A N   1 
ATOM   1950 C CA  . ILE A 1 250 ? 27.651 35.231 95.308 1.00 45.74 ? 258 ILE A CA  1 
ATOM   1951 C C   . ILE A 1 250 ? 26.646 34.088 95.143 1.00 48.26 ? 258 ILE A C   1 
ATOM   1952 O O   . ILE A 1 250 ? 27.080 32.927 95.061 1.00 47.22 ? 258 ILE A O   1 
ATOM   1953 C CB  . ILE A 1 250 ? 28.290 35.624 93.965 1.00 45.11 ? 258 ILE A CB  1 
ATOM   1954 C CG1 . ILE A 1 250 ? 29.145 36.876 94.105 1.00 49.54 ? 258 ILE A CG1 1 
ATOM   1955 C CG2 . ILE A 1 250 ? 27.244 35.780 92.865 1.00 47.96 ? 258 ILE A CG2 1 
ATOM   1956 C CD1 . ILE A 1 250 ? 29.944 37.217 92.863 1.00 50.62 ? 258 ILE A CD1 1 
ATOM   1957 N N   . SER A 1 251 ? 25.356 34.407 95.144 1.00 50.20 ? 259 SER A N   1 
ATOM   1958 C CA  . SER A 1 251 ? 24.322 33.418 94.877 1.00 49.67 ? 259 SER A CA  1 
ATOM   1959 C C   . SER A 1 251 ? 24.011 33.348 93.384 1.00 48.66 ? 259 SER A C   1 
ATOM   1960 O O   . SER A 1 251 ? 23.344 34.229 92.848 1.00 56.28 ? 259 SER A O   1 
ATOM   1961 C CB  . SER A 1 251 ? 23.052 33.743 95.657 1.00 47.55 ? 259 SER A CB  1 
ATOM   1962 O OG  . SER A 1 251 ? 23.255 33.594 97.052 1.00 59.67 ? 259 SER A OG  1 
ATOM   1963 N N   . LEU A 1 252 ? 24.502 32.292 92.724 1.00 44.11 ? 260 LEU A N   1 
ATOM   1964 C CA  . LEU A 1 252 ? 24.250 32.078 91.308 1.00 42.24 ? 260 LEU A CA  1 
ATOM   1965 C C   . LEU A 1 252 ? 23.011 31.215 91.094 1.00 36.82 ? 260 LEU A C   1 
ATOM   1966 O O   . LEU A 1 252 ? 22.746 30.296 91.865 1.00 34.91 ? 260 LEU A O   1 
ATOM   1967 C CB  . LEU A 1 252 ? 25.454 31.397 90.644 1.00 41.57 ? 260 LEU A CB  1 
ATOM   1968 C CG  . LEU A 1 252 ? 26.735 32.218 90.564 1.00 45.15 ? 260 LEU A CG  1 
ATOM   1969 C CD1 . LEU A 1 252 ? 27.746 31.543 89.662 1.00 46.46 ? 260 LEU A CD1 1 
ATOM   1970 C CD2 . LEU A 1 252 ? 26.467 33.633 90.074 1.00 46.61 ? 260 LEU A CD2 1 
ATOM   1971 N N   . GLU A 1 253 ? 22.266 31.522 90.027 1.00 36.00 ? 261 GLU A N   1 
ATOM   1972 C CA  . GLU A 1 253 ? 21.138 30.705 89.616 1.00 36.05 ? 261 GLU A CA  1 
ATOM   1973 C C   . GLU A 1 253 ? 21.681 29.424 88.992 1.00 33.03 ? 261 GLU A C   1 
ATOM   1974 O O   . GLU A 1 253 ? 22.859 29.364 88.642 1.00 28.71 ? 261 GLU A O   1 
ATOM   1975 C CB  . GLU A 1 253 ? 20.244 31.464 88.625 1.00 45.34 ? 261 GLU A CB  1 
ATOM   1976 C CG  . GLU A 1 253 ? 19.745 32.800 89.142 1.00 51.90 ? 261 GLU A CG  1 
ATOM   1977 C CD  . GLU A 1 253 ? 19.062 32.726 90.491 1.00 59.63 ? 261 GLU A CD  1 
ATOM   1978 O OE1 . GLU A 1 253 ? 18.119 31.914 90.636 1.00 55.90 ? 261 GLU A OE1 1 
ATOM   1979 O OE2 . GLU A 1 253 ? 19.475 33.475 91.406 1.00 64.49 ? 261 GLU A OE2 1 
ATOM   1980 N N   . PRO A 1 254 ? 20.859 28.357 88.851 1.00 33.29 ? 262 PRO A N   1 
ATOM   1981 C CA  . PRO A 1 254 ? 21.331 27.103 88.278 1.00 32.64 ? 262 PRO A CA  1 
ATOM   1982 C C   . PRO A 1 254 ? 21.971 27.286 86.906 1.00 36.28 ? 262 PRO A C   1 
ATOM   1983 O O   . PRO A 1 254 ? 21.530 28.124 86.120 1.00 33.11 ? 262 PRO A O   1 
ATOM   1984 C CB  . PRO A 1 254 ? 20.061 26.251 88.209 1.00 33.28 ? 262 PRO A CB  1 
ATOM   1985 C CG  . PRO A 1 254 ? 19.169 26.827 89.268 1.00 35.47 ? 262 PRO A CG  1 
ATOM   1986 C CD  . PRO A 1 254 ? 19.444 28.299 89.251 1.00 34.60 ? 262 PRO A CD  1 
ATOM   1987 N N   . MET A 1 255 ? 23.024 26.506 86.642 1.00 39.41 ? 263 MET A N   1 
ATOM   1988 C CA  . MET A 1 255 ? 23.777 26.644 85.409 1.00 39.42 ? 263 MET A CA  1 
ATOM   1989 C C   . MET A 1 255 ? 24.000 25.288 84.747 1.00 35.26 ? 263 MET A C   1 
ATOM   1990 O O   . MET A 1 255 ? 24.115 24.265 85.418 1.00 37.65 ? 263 MET A O   1 
ATOM   1991 C CB  . MET A 1 255 ? 25.109 27.338 85.686 1.00 44.61 ? 263 MET A CB  1 
ATOM   1992 C CG  . MET A 1 255 ? 24.927 28.723 86.290 1.00 51.86 ? 263 MET A CG  1 
ATOM   1993 S SD  . MET A 1 255 ? 26.244 29.892 85.904 1.00 58.88 ? 263 MET A SD  1 
ATOM   1994 C CE  . MET A 1 255 ? 27.630 28.814 85.878 1.00 65.71 ? 263 MET A CE  1 
ATOM   1995 N N   . LEU A 1 256 ? 24.034 25.312 83.413 1.00 36.51 ? 264 LEU A N   1 
ATOM   1996 C CA  . LEU A 1 256 ? 24.227 24.127 82.599 1.00 32.76 ? 264 LEU A CA  1 
ATOM   1997 C C   . LEU A 1 256 ? 25.423 24.403 81.694 1.00 32.13 ? 264 LEU A C   1 
ATOM   1998 O O   . LEU A 1 256 ? 25.377 25.310 80.865 1.00 27.49 ? 264 LEU A O   1 
ATOM   1999 C CB  . LEU A 1 256 ? 22.951 23.852 81.796 1.00 36.11 ? 264 LEU A CB  1 
ATOM   2000 C CG  . LEU A 1 256 ? 22.950 22.623 80.903 1.00 38.59 ? 264 LEU A CG  1 
ATOM   2001 C CD1 . LEU A 1 256 ? 22.974 21.354 81.719 1.00 39.54 ? 264 LEU A CD1 1 
ATOM   2002 C CD2 . LEU A 1 256 ? 21.742 22.632 79.987 1.00 37.51 ? 264 LEU A CD2 1 
ATOM   2003 N N   . VAL A 1 257 ? 26.504 23.642 81.900 1.00 31.64 ? 265 VAL A N   1 
ATOM   2004 C CA  . VAL A 1 257 ? 27.708 23.769 81.098 1.00 28.58 ? 265 VAL A CA  1 
ATOM   2005 C C   . VAL A 1 257 ? 27.742 22.599 80.117 1.00 27.35 ? 265 VAL A C   1 
ATOM   2006 O O   . VAL A 1 257 ? 27.843 21.445 80.527 1.00 28.55 ? 265 VAL A O   1 
ATOM   2007 C CB  . VAL A 1 257 ? 28.972 23.835 81.989 1.00 29.78 ? 265 VAL A CB  1 
ATOM   2008 C CG1 . VAL A 1 257 ? 30.243 23.968 81.154 1.00 32.19 ? 265 VAL A CG1 1 
ATOM   2009 C CG2 . VAL A 1 257 ? 28.869 24.974 82.994 1.00 31.77 ? 265 VAL A CG2 1 
ATOM   2010 N N   . ILE A 1 258 ? 27.632 22.916 78.823 1.00 27.29 ? 266 ILE A N   1 
ATOM   2011 C CA  . ILE A 1 258 ? 27.671 21.920 77.766 1.00 28.63 ? 266 ILE A CA  1 
ATOM   2012 C C   . ILE A 1 258 ? 28.942 22.135 76.953 1.00 30.41 ? 266 ILE A C   1 
ATOM   2013 O O   . ILE A 1 258 ? 29.264 23.268 76.605 1.00 29.27 ? 266 ILE A O   1 
ATOM   2014 C CB  . ILE A 1 258 ? 26.416 22.000 76.873 1.00 28.02 ? 266 ILE A CB  1 
ATOM   2015 C CG1 . ILE A 1 258 ? 25.134 21.826 77.703 1.00 27.28 ? 266 ILE A CG1 1 
ATOM   2016 C CG2 . ILE A 1 258 ? 26.493 20.982 75.730 1.00 29.16 ? 266 ILE A CG2 1 
ATOM   2017 C CD1 . ILE A 1 258 ? 23.885 22.194 76.969 1.00 30.67 ? 266 ILE A CD1 1 
ATOM   2018 N N   . VAL A 1 259 ? 29.645 21.039 76.646 1.00 33.28 ? 267 VAL A N   1 
ATOM   2019 C CA  . VAL A 1 259 ? 30.889 21.119 75.898 1.00 34.15 ? 267 VAL A CA  1 
ATOM   2020 C C   . VAL A 1 259 ? 31.145 19.823 75.131 1.00 33.11 ? 267 VAL A C   1 
ATOM   2021 O O   . VAL A 1 259 ? 30.662 18.761 75.519 1.00 33.67 ? 267 VAL A O   1 
ATOM   2022 C CB  . VAL A 1 259 ? 32.057 21.471 76.854 1.00 35.61 ? 267 VAL A CB  1 
ATOM   2023 C CG1 . VAL A 1 259 ? 32.394 20.304 77.783 1.00 36.88 ? 267 VAL A CG1 1 
ATOM   2024 C CG2 . VAL A 1 259 ? 33.287 21.924 76.080 1.00 39.65 ? 267 VAL A CG2 1 
ATOM   2025 N N   . GLY A 1 260 ? 31.895 19.936 74.028 1.00 31.12 ? 268 GLY A N   1 
ATOM   2026 C CA  . GLY A 1 260 ? 32.316 18.785 73.247 1.00 28.16 ? 268 GLY A CA  1 
ATOM   2027 C C   . GLY A 1 260 ? 33.560 18.125 73.837 1.00 31.39 ? 268 GLY A C   1 
ATOM   2028 O O   . GLY A 1 260 ? 34.435 18.808 74.365 1.00 30.51 ? 268 GLY A O   1 
ATOM   2029 N N   . GLY A 1 261 ? 33.625 16.793 73.735 1.00 32.37 ? 269 GLY A N   1 
ATOM   2030 C CA  . GLY A 1 261 ? 34.737 16.025 74.268 1.00 30.27 ? 269 GLY A CA  1 
ATOM   2031 C C   . GLY A 1 261 ? 36.072 16.339 73.599 1.00 30.36 ? 269 GLY A C   1 
ATOM   2032 O O   . GLY A 1 261 ? 37.114 16.308 74.249 1.00 30.08 ? 269 GLY A O   1 
ATOM   2033 N N   . SER A 1 262 ? 36.026 16.649 72.297 1.00 30.54 ? 270 SER A N   1 
ATOM   2034 C CA  . SER A 1 262 ? 37.224 16.958 71.532 1.00 32.85 ? 270 SER A CA  1 
ATOM   2035 C C   . SER A 1 262 ? 37.521 18.453 71.427 1.00 31.95 ? 270 SER A C   1 
ATOM   2036 O O   . SER A 1 262 ? 38.362 18.853 70.626 1.00 33.98 ? 270 SER A O   1 
ATOM   2037 C CB  . SER A 1 262 ? 37.118 16.360 70.132 1.00 31.99 ? 270 SER A CB  1 
ATOM   2038 O OG  . SER A 1 262 ? 37.045 14.946 70.197 1.00 34.25 ? 270 SER A OG  1 
ATOM   2039 N N   . GLN A 1 263 ? 36.837 19.269 72.242 1.00 33.96 ? 271 GLN A N   1 
ATOM   2040 C CA  . GLN A 1 263 ? 37.079 20.703 72.276 1.00 32.65 ? 271 GLN A CA  1 
ATOM   2041 C C   . GLN A 1 263 ? 38.378 21.049 73.000 1.00 31.73 ? 271 GLN A C   1 
ATOM   2042 O O   . GLN A 1 263 ? 38.742 20.404 73.980 1.00 38.04 ? 271 GLN A O   1 
ATOM   2043 C CB  . GLN A 1 263 ? 35.929 21.458 72.965 1.00 34.32 ? 271 GLN A CB  1 
ATOM   2044 C CG  . GLN A 1 263 ? 34.711 21.666 72.083 1.00 37.56 ? 271 GLN A CG  1 
ATOM   2045 C CD  . GLN A 1 263 ? 33.776 22.712 72.643 1.00 37.39 ? 271 GLN A CD  1 
ATOM   2046 O OE1 . GLN A 1 263 ? 32.619 22.429 72.975 1.00 35.52 ? 271 GLN A OE1 1 
ATOM   2047 N NE2 . GLN A 1 263 ? 34.253 23.948 72.755 1.00 36.49 ? 271 GLN A NE2 1 
ATOM   2048 N N   . LEU A 1 264 ? 39.055 22.089 72.500 1.00 30.28 ? 272 LEU A N   1 
ATOM   2049 C CA  . LEU A 1 264 ? 40.187 22.695 73.181 1.00 29.97 ? 272 LEU A CA  1 
ATOM   2050 C C   . LEU A 1 264 ? 39.775 23.285 74.529 1.00 31.51 ? 272 LEU A C   1 
ATOM   2051 O O   . LEU A 1 264 ? 40.530 23.213 75.498 1.00 33.32 ? 272 LEU A O   1 
ATOM   2052 C CB  . LEU A 1 264 ? 40.777 23.801 72.290 1.00 31.84 ? 272 LEU A CB  1 
ATOM   2053 C CG  . LEU A 1 264 ? 41.442 23.337 70.998 1.00 31.23 ? 272 LEU A CG  1 
ATOM   2054 C CD1 . LEU A 1 264 ? 41.731 24.503 70.088 1.00 34.69 ? 272 LEU A CD1 1 
ATOM   2055 C CD2 . LEU A 1 264 ? 42.726 22.583 71.283 1.00 27.29 ? 272 LEU A CD2 1 
ATOM   2056 N N   . LEU A 1 265 ? 38.563 23.855 74.581 1.00 31.62 ? 273 LEU A N   1 
ATOM   2057 C CA  . LEU A 1 265 ? 38.047 24.504 75.777 1.00 32.66 ? 273 LEU A CA  1 
ATOM   2058 C C   . LEU A 1 265 ? 37.411 23.548 76.788 1.00 30.59 ? 273 LEU A C   1 
ATOM   2059 O O   . LEU A 1 265 ? 36.847 23.994 77.785 1.00 29.59 ? 273 LEU A O   1 
ATOM   2060 C CB  . LEU A 1 265 ? 37.005 25.560 75.351 1.00 33.80 ? 273 LEU A CB  1 
ATOM   2061 C CG  . LEU A 1 265 ? 37.565 26.814 74.689 1.00 36.16 ? 273 LEU A CG  1 
ATOM   2062 C CD1 . LEU A 1 265 ? 36.463 27.645 74.066 1.00 41.74 ? 273 LEU A CD1 1 
ATOM   2063 C CD2 . LEU A 1 265 ? 38.331 27.662 75.684 1.00 39.14 ? 273 LEU A CD2 1 
ATOM   2064 N N   . ARG A 1 266 ? 37.519 22.237 76.538 1.00 33.84 ? 274 ARG A N   1 
ATOM   2065 C CA  . ARG A 1 266 ? 36.850 21.235 77.353 1.00 37.08 ? 274 ARG A CA  1 
ATOM   2066 C C   . ARG A 1 266 ? 37.311 21.280 78.808 1.00 38.12 ? 274 ARG A C   1 
ATOM   2067 O O   . ARG A 1 266 ? 36.489 21.420 79.711 1.00 37.36 ? 274 ARG A O   1 
ATOM   2068 C CB  . ARG A 1 266 ? 37.077 19.831 76.760 1.00 38.03 ? 274 ARG A CB  1 
ATOM   2069 C CG  . ARG A 1 266 ? 36.187 18.745 77.362 1.00 45.05 ? 274 ARG A CG  1 
ATOM   2070 C CD  . ARG A 1 266 ? 36.713 18.174 78.667 1.00 50.35 ? 274 ARG A CD  1 
ATOM   2071 N NE  . ARG A 1 266 ? 37.885 17.330 78.462 1.00 58.05 ? 274 ARG A NE  1 
ATOM   2072 C CZ  . ARG A 1 266 ? 37.967 16.049 78.803 1.00 66.40 ? 274 ARG A CZ  1 
ATOM   2073 N NH1 . ARG A 1 266 ? 36.974 15.429 79.421 1.00 66.16 ? 274 ARG A NH1 1 
ATOM   2074 N NH2 . ARG A 1 266 ? 39.078 15.375 78.521 1.00 71.12 ? 274 ARG A NH2 1 
ATOM   2075 N N   . ASP A 1 267 ? 38.628 21.149 79.019 1.00 36.70 ? 275 ASP A N   1 
ATOM   2076 C CA  . ASP A 1 267 ? 39.194 21.069 80.356 1.00 37.33 ? 275 ASP A CA  1 
ATOM   2077 C C   . ASP A 1 267 ? 38.867 22.302 81.192 1.00 36.16 ? 275 ASP A C   1 
ATOM   2078 O O   . ASP A 1 267 ? 38.517 22.180 82.363 1.00 34.76 ? 275 ASP A O   1 
ATOM   2079 C CB  . ASP A 1 267 ? 40.720 20.874 80.290 1.00 35.83 ? 275 ASP A CB  1 
ATOM   2080 C CG  . ASP A 1 267 ? 41.167 19.505 79.812 1.00 36.01 ? 275 ASP A CG  1 
ATOM   2081 O OD1 . ASP A 1 267 ? 40.296 18.626 79.625 1.00 38.11 ? 275 ASP A OD1 1 
ATOM   2082 O OD2 . ASP A 1 267 ? 42.387 19.314 79.620 1.00 34.44 ? 275 ASP A OD2 1 
ATOM   2083 N N   . ARG A 1 268 ? 38.976 23.484 80.575 1.00 36.80 ? 276 ARG A N   1 
ATOM   2084 C CA  . ARG A 1 268 ? 38.726 24.738 81.265 1.00 34.40 ? 276 ARG A CA  1 
ATOM   2085 C C   . ARG A 1 268 ? 37.248 24.879 81.627 1.00 34.45 ? 276 ARG A C   1 
ATOM   2086 O O   . ARG A 1 268 ? 36.918 25.442 82.669 1.00 35.16 ? 276 ARG A O   1 
ATOM   2087 C CB  . ARG A 1 268 ? 39.203 25.917 80.402 1.00 32.16 ? 276 ARG A CB  1 
ATOM   2088 C CG  . ARG A 1 268 ? 39.300 27.238 81.153 1.00 29.93 ? 276 ARG A CG  1 
ATOM   2089 C CD  . ARG A 1 268 ? 39.956 28.314 80.310 1.00 30.63 ? 276 ARG A CD  1 
ATOM   2090 N NE  . ARG A 1 268 ? 41.385 28.085 80.126 1.00 33.29 ? 276 ARG A NE  1 
ATOM   2091 C CZ  . ARG A 1 268 ? 42.304 28.251 81.071 1.00 31.98 ? 276 ARG A CZ  1 
ATOM   2092 N NH1 . ARG A 1 268 ? 41.986 28.691 82.277 1.00 29.75 ? 276 ARG A NH1 1 
ATOM   2093 N NH2 . ARG A 1 268 ? 43.577 27.981 80.793 1.00 32.23 ? 276 ARG A NH2 1 
ATOM   2094 N N   . ALA A 1 269 ? 36.367 24.352 80.766 1.00 30.73 ? 277 ALA A N   1 
ATOM   2095 C CA  . ALA A 1 269 ? 34.936 24.335 81.030 1.00 28.78 ? 277 ALA A CA  1 
ATOM   2096 C C   . ALA A 1 269 ? 34.577 23.374 82.164 1.00 31.86 ? 277 ALA A C   1 
ATOM   2097 O O   . ALA A 1 269 ? 33.668 23.649 82.946 1.00 28.16 ? 277 ALA A O   1 
ATOM   2098 C CB  . ALA A 1 269 ? 34.175 23.965 79.772 1.00 27.28 ? 277 ALA A CB  1 
ATOM   2099 N N   . LYS A 1 270 ? 35.298 22.249 82.246 1.00 29.41 ? 278 LYS A N   1 
ATOM   2100 C CA  . LYS A 1 270 ? 35.077 21.273 83.301 1.00 30.54 ? 278 LYS A CA  1 
ATOM   2101 C C   . LYS A 1 270 ? 35.619 21.780 84.636 1.00 31.58 ? 278 LYS A C   1 
ATOM   2102 O O   . LYS A 1 270 ? 34.979 21.597 85.669 1.00 33.21 ? 278 LYS A O   1 
ATOM   2103 C CB  . LYS A 1 270 ? 35.711 19.922 82.934 1.00 31.02 ? 278 LYS A CB  1 
ATOM   2104 C CG  . LYS A 1 270 ? 35.234 18.774 83.815 1.00 30.16 ? 278 LYS A CG  1 
ATOM   2105 C CD  . LYS A 1 270 ? 35.690 17.420 83.312 1.00 33.91 ? 278 LYS A CD  1 
ATOM   2106 C CE  . LYS A 1 270 ? 35.196 16.290 84.177 1.00 36.99 ? 278 LYS A CE  1 
ATOM   2107 N NZ  . LYS A 1 270 ? 35.707 14.976 83.704 1.00 37.98 ? 278 LYS A NZ  1 
ATOM   2108 N N   . GLU A 1 271 ? 36.802 22.409 84.609 1.00 33.97 ? 279 GLU A N   1 
ATOM   2109 C CA  . GLU A 1 271 ? 37.335 23.095 85.777 1.00 35.53 ? 279 GLU A CA  1 
ATOM   2110 C C   . GLU A 1 271 ? 36.315 24.088 86.325 1.00 35.83 ? 279 GLU A C   1 
ATOM   2111 O O   . GLU A 1 271 ? 36.031 24.094 87.521 1.00 36.28 ? 279 GLU A O   1 
ATOM   2112 C CB  . GLU A 1 271 ? 38.623 23.867 85.454 1.00 40.28 ? 279 GLU A CB  1 
ATOM   2113 C CG  . GLU A 1 271 ? 39.876 23.017 85.387 1.00 43.96 ? 279 GLU A CG  1 
ATOM   2114 C CD  . GLU A 1 271 ? 41.159 23.823 85.325 1.00 48.27 ? 279 GLU A CD  1 
ATOM   2115 O OE1 . GLU A 1 271 ? 41.093 25.066 85.471 1.00 46.44 ? 279 GLU A OE1 1 
ATOM   2116 O OE2 . GLU A 1 271 ? 42.233 23.211 85.127 1.00 53.43 ? 279 GLU A OE2 1 
ATOM   2117 N N   . TYR A 1 272 ? 35.787 24.927 85.424 1.00 31.59 ? 280 TYR A N   1 
ATOM   2118 C CA  . TYR A 1 272 ? 34.781 25.920 85.760 1.00 28.15 ? 280 TYR A CA  1 
ATOM   2119 C C   . TYR A 1 272 ? 33.609 25.302 86.517 1.00 29.60 ? 280 TYR A C   1 
ATOM   2120 O O   . TYR A 1 272 ? 33.307 25.711 87.636 1.00 25.71 ? 280 TYR A O   1 
ATOM   2121 C CB  . TYR A 1 272 ? 34.278 26.598 84.476 1.00 28.19 ? 280 TYR A CB  1 
ATOM   2122 C CG  . TYR A 1 272 ? 33.172 27.607 84.685 1.00 30.35 ? 280 TYR A CG  1 
ATOM   2123 C CD1 . TYR A 1 272 ? 33.449 28.888 85.143 1.00 30.51 ? 280 TYR A CD1 1 
ATOM   2124 C CD2 . TYR A 1 272 ? 31.848 27.280 84.429 1.00 30.99 ? 280 TYR A CD2 1 
ATOM   2125 C CE1 . TYR A 1 272 ? 32.437 29.820 85.334 1.00 32.01 ? 280 TYR A CE1 1 
ATOM   2126 C CE2 . TYR A 1 272 ? 30.826 28.205 84.616 1.00 30.51 ? 280 TYR A CE2 1 
ATOM   2127 C CZ  . TYR A 1 272 ? 31.125 29.476 85.067 1.00 31.83 ? 280 TYR A CZ  1 
ATOM   2128 O OH  . TYR A 1 272 ? 30.124 30.397 85.253 1.00 31.71 ? 280 TYR A OH  1 
ATOM   2129 N N   . ALA A 1 273 ? 32.975 24.304 85.888 1.00 34.88 ? 281 ALA A N   1 
ATOM   2130 C CA  . ALA A 1 273 ? 31.793 23.652 86.428 1.00 34.90 ? 281 ALA A CA  1 
ATOM   2131 C C   . ALA A 1 273 ? 32.043 23.041 87.804 1.00 32.62 ? 281 ALA A C   1 
ATOM   2132 O O   . ALA A 1 273 ? 31.275 23.277 88.734 1.00 30.43 ? 281 ALA A O   1 
ATOM   2133 C CB  . ALA A 1 273 ? 31.310 22.576 85.467 1.00 35.23 ? 281 ALA A CB  1 
ATOM   2134 N N   . TYR A 1 274 ? 33.123 22.260 87.920 1.00 30.02 ? 282 TYR A N   1 
ATOM   2135 C CA  . TYR A 1 274 ? 33.388 21.503 89.133 1.00 37.37 ? 282 TYR A CA  1 
ATOM   2136 C C   . TYR A 1 274 ? 33.925 22.359 90.280 1.00 35.44 ? 282 TYR A C   1 
ATOM   2137 O O   . TYR A 1 274 ? 33.775 21.982 91.439 1.00 38.88 ? 282 TYR A O   1 
ATOM   2138 C CB  . TYR A 1 274 ? 34.325 20.312 88.842 1.00 41.19 ? 282 TYR A CB  1 
ATOM   2139 C CG  . TYR A 1 274 ? 33.589 19.128 88.251 1.00 45.80 ? 282 TYR A CG  1 
ATOM   2140 C CD1 . TYR A 1 274 ? 33.053 19.184 86.971 1.00 47.00 ? 282 TYR A CD1 1 
ATOM   2141 C CD2 . TYR A 1 274 ? 33.391 17.967 88.987 1.00 48.17 ? 282 TYR A CD2 1 
ATOM   2142 C CE1 . TYR A 1 274 ? 32.363 18.106 86.427 1.00 45.85 ? 282 TYR A CE1 1 
ATOM   2143 C CE2 . TYR A 1 274 ? 32.701 16.882 88.455 1.00 51.84 ? 282 TYR A CE2 1 
ATOM   2144 C CZ  . TYR A 1 274 ? 32.188 16.956 87.173 1.00 48.83 ? 282 TYR A CZ  1 
ATOM   2145 O OH  . TYR A 1 274 ? 31.503 15.893 86.635 1.00 45.00 ? 282 TYR A OH  1 
ATOM   2146 N N   . LYS A 1 275 ? 34.538 23.507 89.964 1.00 34.23 ? 283 LYS A N   1 
ATOM   2147 C CA  . LYS A 1 275 ? 34.899 24.474 90.991 1.00 34.98 ? 283 LYS A CA  1 
ATOM   2148 C C   . LYS A 1 275 ? 33.648 25.071 91.633 1.00 32.21 ? 283 LYS A C   1 
ATOM   2149 O O   . LYS A 1 275 ? 33.613 25.280 92.843 1.00 29.13 ? 283 LYS A O   1 
ATOM   2150 C CB  . LYS A 1 275 ? 35.783 25.603 90.435 1.00 36.40 ? 283 LYS A CB  1 
ATOM   2151 C CG  . LYS A 1 275 ? 37.253 25.237 90.248 1.00 35.82 ? 283 LYS A CG  1 
ATOM   2152 C CD  . LYS A 1 275 ? 38.103 26.476 89.963 1.00 39.43 ? 283 LYS A CD  1 
ATOM   2153 C CE  . LYS A 1 275 ? 39.342 26.197 89.144 1.00 42.17 ? 283 LYS A CE  1 
ATOM   2154 N NZ  . LYS A 1 275 ? 40.364 25.439 89.906 1.00 46.55 ? 283 LYS A NZ  1 
ATOM   2155 N N   . LEU A 1 276 ? 32.627 25.345 90.810 1.00 32.61 ? 284 LEU A N   1 
ATOM   2156 C CA  . LEU A 1 276 ? 31.341 25.821 91.297 1.00 32.38 ? 284 LEU A CA  1 
ATOM   2157 C C   . LEU A 1 276 ? 30.583 24.740 92.067 1.00 34.90 ? 284 LEU A C   1 
ATOM   2158 O O   . LEU A 1 276 ? 30.012 25.024 93.118 1.00 34.94 ? 284 LEU A O   1 
ATOM   2159 C CB  . LEU A 1 276 ? 30.485 26.321 90.123 1.00 33.78 ? 284 LEU A CB  1 
ATOM   2160 C CG  . LEU A 1 276 ? 30.990 27.573 89.404 1.00 32.36 ? 284 LEU A CG  1 
ATOM   2161 C CD1 . LEU A 1 276 ? 30.047 27.982 88.298 1.00 32.22 ? 284 LEU A CD1 1 
ATOM   2162 C CD2 . LEU A 1 276 ? 31.168 28.730 90.361 1.00 33.76 ? 284 LEU A CD2 1 
ATOM   2163 N N   . LYS A 1 277 ? 30.580 23.506 91.541 1.00 35.97 ? 285 LYS A N   1 
ATOM   2164 C CA  . LYS A 1 277 ? 29.952 22.376 92.211 1.00 36.76 ? 285 LYS A CA  1 
ATOM   2165 C C   . LYS A 1 277 ? 30.399 22.246 93.665 1.00 40.81 ? 285 LYS A C   1 
ATOM   2166 O O   . LYS A 1 277 ? 29.567 22.160 94.565 1.00 44.19 ? 285 LYS A O   1 
ATOM   2167 C CB  . LYS A 1 277 ? 30.270 21.051 91.499 1.00 39.37 ? 285 LYS A CB  1 
ATOM   2168 C CG  . LYS A 1 277 ? 29.415 20.748 90.282 1.00 44.31 ? 285 LYS A CG  1 
ATOM   2169 C CD  . LYS A 1 277 ? 29.734 19.368 89.703 1.00 48.75 ? 285 LYS A CD  1 
ATOM   2170 C CE  . LYS A 1 277 ? 28.827 18.969 88.561 1.00 49.94 ? 285 LYS A CE  1 
ATOM   2171 N NZ  . LYS A 1 277 ? 27.431 18.730 89.016 1.00 52.70 ? 285 LYS A NZ  1 
ATOM   2172 N N   . LYS A 1 278 ? 31.722 22.232 93.874 1.00 45.41 ? 286 LYS A N   1 
ATOM   2173 C CA  . LYS A 1 278 ? 32.304 22.037 95.193 1.00 46.83 ? 286 LYS A CA  1 
ATOM   2174 C C   . LYS A 1 278 ? 31.991 23.182 96.155 1.00 47.23 ? 286 LYS A C   1 
ATOM   2175 O O   . LYS A 1 278 ? 32.126 23.022 97.366 1.00 48.09 ? 286 LYS A O   1 
ATOM   2176 C CB  . LYS A 1 278 ? 33.826 21.838 95.076 1.00 47.90 ? 286 LYS A CB  1 
ATOM   2177 C CG  . LYS A 1 278 ? 34.217 20.558 94.340 1.00 54.21 ? 286 LYS A CG  1 
ATOM   2178 C CD  . LYS A 1 278 ? 35.722 20.299 94.340 1.00 61.94 ? 286 LYS A CD  1 
ATOM   2179 C CE  . LYS A 1 278 ? 36.121 19.131 93.461 1.00 64.62 ? 286 LYS A CE  1 
ATOM   2180 N NZ  . LYS A 1 278 ? 36.151 19.495 92.016 1.00 62.99 ? 286 LYS A NZ  1 
ATOM   2181 N N   . MET A 1 279 ? 31.514 24.293 95.580 1.00 50.66 ? 287 MET A N   1 
ATOM   2182 C CA  . MET A 1 279 ? 31.099 25.455 96.404 1.00 56.37 ? 287 MET A CA  1 
ATOM   2183 C C   . MET A 1 279 ? 29.623 25.274 96.780 1.00 58.40 ? 287 MET A C   1 
ATOM   2184 O O   . MET A 1 279 ? 28.824 24.912 95.889 1.00 60.82 ? 287 MET A O   1 
ATOM   2185 C CB  . MET A 1 279 ? 31.313 26.771 95.648 1.00 52.72 ? 287 MET A CB  1 
ATOM   2186 C CG  . MET A 1 279 ? 32.762 27.218 95.619 1.00 54.51 ? 287 MET A CG  1 
ATOM   2187 S SD  . MET A 1 279 ? 33.157 28.300 94.231 1.00 55.49 ? 287 MET A SD  1 
ATOM   2188 C CE  . MET A 1 279 ? 31.588 29.161 94.079 1.00 53.91 ? 287 MET A CE  1 
ATOM   2189 N N   . GLY A 1 280 ? 29.279 25.524 98.041 1.00 57.96 ? 288 GLY A N   1 
ATOM   2190 C CA  . GLY A 1 280 ? 27.930 25.334 98.548 1.00 58.93 ? 288 GLY A CA  1 
ATOM   2191 C C   . GLY A 1 280 ? 26.929 26.324 97.956 1.00 59.97 ? 288 GLY A C   1 
ATOM   2192 O O   . GLY A 1 280 ? 27.274 27.474 97.693 1.00 63.57 ? 288 GLY A O   1 
ATOM   2193 N N   . GLY A 1 281 ? 25.693 25.855 97.741 1.00 61.76 ? 289 GLY A N   1 
ATOM   2194 C CA  . GLY A 1 281 ? 24.626 26.683 97.202 1.00 61.88 ? 289 GLY A CA  1 
ATOM   2195 C C   . GLY A 1 281 ? 24.504 26.655 95.680 1.00 60.03 ? 289 GLY A C   1 
ATOM   2196 O O   . GLY A 1 281 ? 23.453 26.996 95.141 1.00 67.79 ? 289 GLY A O   1 
ATOM   2197 N N   . LYS A 1 282 ? 25.581 26.246 94.997 1.00 57.46 ? 290 LYS A N   1 
ATOM   2198 C CA  . LYS A 1 282 ? 25.628 26.241 93.544 1.00 58.20 ? 290 LYS A CA  1 
ATOM   2199 C C   . LYS A 1 282 ? 25.067 24.937 92.982 1.00 51.66 ? 290 LYS A C   1 
ATOM   2200 O O   . LYS A 1 282 ? 25.515 23.857 93.363 1.00 57.45 ? 290 LYS A O   1 
ATOM   2201 C CB  . LYS A 1 282 ? 27.074 26.409 93.055 1.00 60.28 ? 290 LYS A CB  1 
ATOM   2202 C CG  . LYS A 1 282 ? 27.822 27.604 93.639 1.00 61.34 ? 290 LYS A CG  1 
ATOM   2203 C CD  . LYS A 1 282 ? 27.262 28.941 93.191 1.00 57.48 ? 290 LYS A CD  1 
ATOM   2204 C CE  . LYS A 1 282 ? 28.118 30.100 93.644 1.00 55.20 ? 290 LYS A CE  1 
ATOM   2205 N NZ  . LYS A 1 282 ? 28.109 30.254 95.120 1.00 56.74 ? 290 LYS A NZ  1 
ATOM   2206 N N   . ARG A 1 283 ? 24.083 25.051 92.080 1.00 45.97 ? 291 ARG A N   1 
ATOM   2207 C CA  . ARG A 1 283 ? 23.628 23.924 91.284 1.00 45.08 ? 291 ARG A CA  1 
ATOM   2208 C C   . ARG A 1 283 ? 24.210 24.086 89.883 1.00 35.16 ? 291 ARG A C   1 
ATOM   2209 O O   . ARG A 1 283 ? 23.844 25.011 89.165 1.00 34.33 ? 291 ARG A O   1 
ATOM   2210 C CB  . ARG A 1 283 ? 22.091 23.846 91.232 1.00 51.82 ? 291 ARG A CB  1 
ATOM   2211 C CG  . ARG A 1 283 ? 21.570 22.539 90.621 1.00 67.49 ? 291 ARG A CG  1 
ATOM   2212 C CD  . ARG A 1 283 ? 20.101 22.613 90.234 1.00 79.84 ? 291 ARG A CD  1 
ATOM   2213 N NE  . ARG A 1 283 ? 19.642 21.377 89.607 1.00 85.76 ? 291 ARG A NE  1 
ATOM   2214 C CZ  . ARG A 1 283 ? 19.152 21.282 88.375 1.00 80.08 ? 291 ARG A CZ  1 
ATOM   2215 N NH1 . ARG A 1 283 ? 18.989 22.348 87.608 1.00 66.54 ? 291 ARG A NH1 1 
ATOM   2216 N NH2 . ARG A 1 283 ? 18.814 20.086 87.902 1.00 77.75 ? 291 ARG A NH2 1 
ATOM   2217 N N   . VAL A 1 284 ? 25.136 23.193 89.514 1.00 36.98 ? 292 VAL A N   1 
ATOM   2218 C CA  . VAL A 1 284 ? 25.770 23.231 88.206 1.00 38.20 ? 292 VAL A CA  1 
ATOM   2219 C C   . VAL A 1 284 ? 25.806 21.831 87.604 1.00 34.61 ? 292 VAL A C   1 
ATOM   2220 O O   . VAL A 1 284 ? 26.412 20.927 88.173 1.00 32.23 ? 292 VAL A O   1 
ATOM   2221 C CB  . VAL A 1 284 ? 27.192 23.830 88.272 1.00 37.04 ? 292 VAL A CB  1 
ATOM   2222 C CG1 . VAL A 1 284 ? 27.856 23.825 86.894 1.00 36.23 ? 292 VAL A CG1 1 
ATOM   2223 C CG2 . VAL A 1 284 ? 27.171 25.234 88.867 1.00 38.32 ? 292 VAL A CG2 1 
ATOM   2224 N N   . ASP A 1 285 ? 25.151 21.673 86.450 1.00 33.85 ? 293 ASP A N   1 
ATOM   2225 C CA  . ASP A 1 285 ? 25.200 20.439 85.685 1.00 37.10 ? 293 ASP A CA  1 
ATOM   2226 C C   . ASP A 1 285 ? 26.242 20.587 84.580 1.00 33.00 ? 293 ASP A C   1 
ATOM   2227 O O   . ASP A 1 285 ? 26.305 21.623 83.922 1.00 38.01 ? 293 ASP A O   1 
ATOM   2228 C CB  . ASP A 1 285 ? 23.817 20.109 85.099 1.00 41.46 ? 293 ASP A CB  1 
ATOM   2229 C CG  . ASP A 1 285 ? 22.723 19.966 86.142 1.00 46.39 ? 293 ASP A CG  1 
ATOM   2230 O OD1 . ASP A 1 285 ? 22.863 19.102 87.033 1.00 43.50 ? 293 ASP A OD1 1 
ATOM   2231 O OD2 . ASP A 1 285 ? 21.727 20.723 86.068 1.00 51.71 ? 293 ASP A OD2 1 
ATOM   2232 N N   . TYR A 1 286 ? 27.062 19.546 84.401 1.00 32.60 ? 294 TYR A N   1 
ATOM   2233 C CA  . TYR A 1 286 ? 28.098 19.521 83.381 1.00 28.25 ? 294 TYR A CA  1 
ATOM   2234 C C   . TYR A 1 286 ? 27.835 18.351 82.439 1.00 28.72 ? 294 TYR A C   1 
ATOM   2235 O O   . TYR A 1 286 ? 27.745 17.208 82.884 1.00 26.70 ? 294 TYR A O   1 
ATOM   2236 C CB  . TYR A 1 286 ? 29.484 19.392 84.023 1.00 28.75 ? 294 TYR A CB  1 
ATOM   2237 C CG  . TYR A 1 286 ? 30.613 19.208 83.031 1.00 30.40 ? 294 TYR A CG  1 
ATOM   2238 C CD1 . TYR A 1 286 ? 31.120 20.284 82.315 1.00 29.87 ? 294 TYR A CD1 1 
ATOM   2239 C CD2 . TYR A 1 286 ? 31.163 17.955 82.798 1.00 26.69 ? 294 TYR A CD2 1 
ATOM   2240 C CE1 . TYR A 1 286 ? 32.157 20.120 81.402 1.00 28.35 ? 294 TYR A CE1 1 
ATOM   2241 C CE2 . TYR A 1 286 ? 32.196 17.777 81.887 1.00 27.25 ? 294 TYR A CE2 1 
ATOM   2242 C CZ  . TYR A 1 286 ? 32.693 18.862 81.190 1.00 28.41 ? 294 TYR A CZ  1 
ATOM   2243 O OH  . TYR A 1 286 ? 33.716 18.683 80.291 1.00 27.27 ? 294 TYR A OH  1 
ATOM   2244 N N   . ILE A 1 287 ? 27.706 18.651 81.141 1.00 30.74 ? 295 ILE A N   1 
ATOM   2245 C CA  . ILE A 1 287 ? 27.394 17.642 80.144 1.00 30.44 ? 295 ILE A CA  1 
ATOM   2246 C C   . ILE A 1 287 ? 28.423 17.704 79.021 1.00 32.09 ? 295 ILE A C   1 
ATOM   2247 O O   . ILE A 1 287 ? 28.593 18.742 78.387 1.00 35.30 ? 295 ILE A O   1 
ATOM   2248 C CB  . ILE A 1 287 ? 25.948 17.811 79.633 1.00 33.76 ? 295 ILE A CB  1 
ATOM   2249 C CG1 . ILE A 1 287 ? 24.954 17.673 80.800 1.00 37.14 ? 295 ILE A CG1 1 
ATOM   2250 C CG2 . ILE A 1 287 ? 25.626 16.822 78.503 1.00 35.21 ? 295 ILE A CG2 1 
ATOM   2251 C CD1 . ILE A 1 287 ? 23.572 17.925 80.442 1.00 44.52 ? 295 ILE A CD1 1 
ATOM   2252 N N   . GLU A 1 288 ? 29.098 16.571 78.796 1.00 35.48 ? 296 GLU A N   1 
ATOM   2253 C CA  . GLU A 1 288 ? 30.152 16.463 77.803 1.00 34.94 ? 296 GLU A CA  1 
ATOM   2254 C C   . GLU A 1 288 ? 29.727 15.504 76.695 1.00 35.92 ? 296 GLU A C   1 
ATOM   2255 O O   . GLU A 1 288 ? 29.477 14.330 76.959 1.00 37.40 ? 296 GLU A O   1 
ATOM   2256 C CB  . GLU A 1 288 ? 31.440 15.966 78.467 1.00 32.88 ? 296 GLU A CB  1 
ATOM   2257 C CG  . GLU A 1 288 ? 32.650 15.994 77.555 1.00 34.91 ? 296 GLU A CG  1 
ATOM   2258 C CD  . GLU A 1 288 ? 33.927 15.547 78.230 1.00 35.54 ? 296 GLU A CD  1 
ATOM   2259 O OE1 . GLU A 1 288 ? 34.224 16.069 79.328 1.00 33.23 ? 296 GLU A OE1 1 
ATOM   2260 O OE2 . GLU A 1 288 ? 34.632 14.679 77.663 1.00 36.34 ? 296 GLU A OE2 1 
ATOM   2261 N N   . PHE A 1 289 ? 29.646 16.015 75.461 1.00 35.01 ? 297 PHE A N   1 
ATOM   2262 C CA  . PHE A 1 289 ? 29.342 15.185 74.308 1.00 34.10 ? 297 PHE A CA  1 
ATOM   2263 C C   . PHE A 1 289 ? 30.640 14.651 73.708 1.00 38.29 ? 297 PHE A C   1 
ATOM   2264 O O   . PHE A 1 289 ? 31.450 15.416 73.188 1.00 33.69 ? 297 PHE A O   1 
ATOM   2265 C CB  . PHE A 1 289 ? 28.517 15.956 73.272 1.00 30.46 ? 297 PHE A CB  1 
ATOM   2266 C CG  . PHE A 1 289 ? 27.085 16.166 73.696 1.00 28.52 ? 297 PHE A CG  1 
ATOM   2267 C CD1 . PHE A 1 289 ? 26.754 17.140 74.623 1.00 30.14 ? 297 PHE A CD1 1 
ATOM   2268 C CD2 . PHE A 1 289 ? 26.071 15.368 73.191 1.00 27.55 ? 297 PHE A CD2 1 
ATOM   2269 C CE1 . PHE A 1 289 ? 25.434 17.329 75.015 1.00 28.19 ? 297 PHE A CE1 1 
ATOM   2270 C CE2 . PHE A 1 289 ? 24.754 15.554 73.590 1.00 27.08 ? 297 PHE A CE2 1 
ATOM   2271 C CZ  . PHE A 1 289 ? 24.443 16.533 74.501 1.00 28.40 ? 297 PHE A CZ  1 
ATOM   2272 N N   . GLU A 1 290 ? 30.813 13.326 73.784 1.00 42.15 ? 298 GLU A N   1 
ATOM   2273 C CA  . GLU A 1 290 ? 32.060 12.676 73.421 1.00 44.37 ? 298 GLU A CA  1 
ATOM   2274 C C   . GLU A 1 290 ? 32.389 12.886 71.945 1.00 41.91 ? 298 GLU A C   1 
ATOM   2275 O O   . GLU A 1 290 ? 31.499 12.840 71.099 1.00 39.75 ? 298 GLU A O   1 
ATOM   2276 C CB  . GLU A 1 290 ? 31.982 11.170 73.720 1.00 46.24 ? 298 GLU A CB  1 
ATOM   2277 C CG  . GLU A 1 290 ? 31.713 10.841 75.177 1.00 52.70 ? 298 GLU A CG  1 
ATOM   2278 C CD  . GLU A 1 290 ? 31.626 9.357  75.468 1.00 57.96 ? 298 GLU A CD  1 
ATOM   2279 O OE1 . GLU A 1 290 ? 32.627 8.645  75.228 1.00 49.61 ? 298 GLU A OE1 1 
ATOM   2280 O OE2 . GLU A 1 290 ? 30.555 8.904  75.934 1.00 65.54 ? 298 GLU A OE2 1 
ATOM   2281 N N   . ASN A 1 291 ? 33.676 13.130 71.663 1.00 41.59 ? 299 ASN A N   1 
ATOM   2282 C CA  . ASN A 1 291 ? 34.198 13.196 70.305 1.00 42.59 ? 299 ASN A CA  1 
ATOM   2283 C C   . ASN A 1 291 ? 33.598 14.322 69.468 1.00 39.37 ? 299 ASN A C   1 
ATOM   2284 O O   . ASN A 1 291 ? 33.531 14.212 68.245 1.00 48.03 ? 299 ASN A O   1 
ATOM   2285 C CB  . ASN A 1 291 ? 33.984 11.861 69.587 1.00 44.69 ? 299 ASN A CB  1 
ATOM   2286 C CG  . ASN A 1 291 ? 34.400 10.685 70.429 1.00 48.99 ? 299 ASN A CG  1 
ATOM   2287 O OD1 . ASN A 1 291 ? 35.541 10.609 70.900 1.00 48.49 ? 299 ASN A OD1 1 
ATOM   2288 N ND2 . ASN A 1 291 ? 33.485 9.750  70.657 1.00 49.49 ? 299 ASN A ND2 1 
ATOM   2289 N N   . LYS A 1 292 ? 33.171 15.401 70.134 1.00 37.92 ? 300 LYS A N   1 
ATOM   2290 C CA  . LYS A 1 292 ? 32.602 16.553 69.455 1.00 32.85 ? 300 LYS A CA  1 
ATOM   2291 C C   . LYS A 1 292 ? 33.502 17.768 69.650 1.00 32.59 ? 300 LYS A C   1 
ATOM   2292 O O   . LYS A 1 292 ? 34.195 17.880 70.658 1.00 36.71 ? 300 LYS A O   1 
ATOM   2293 C CB  . LYS A 1 292 ? 31.183 16.865 69.962 1.00 30.28 ? 300 LYS A CB  1 
ATOM   2294 C CG  . LYS A 1 292 ? 30.163 15.769 69.697 1.00 32.54 ? 300 LYS A CG  1 
ATOM   2295 C CD  . LYS A 1 292 ? 30.026 15.404 68.222 1.00 35.98 ? 300 LYS A CD  1 
ATOM   2296 C CE  . LYS A 1 292 ? 29.031 14.299 67.992 1.00 38.94 ? 300 LYS A CE  1 
ATOM   2297 N NZ  . LYS A 1 292 ? 28.882 13.996 66.547 1.00 42.72 ? 300 LYS A NZ  1 
ATOM   2298 N N   . GLU A 1 293 ? 33.472 18.666 68.661 1.00 35.11 ? 301 GLU A N   1 
ATOM   2299 C CA  . GLU A 1 293 ? 34.260 19.885 68.678 1.00 34.36 ? 301 GLU A CA  1 
ATOM   2300 C C   . GLU A 1 293 ? 33.330 21.083 68.839 1.00 31.58 ? 301 GLU A C   1 
ATOM   2301 O O   . GLU A 1 293 ? 32.122 20.914 68.990 1.00 28.36 ? 301 GLU A O   1 
ATOM   2302 C CB  . GLU A 1 293 ? 35.088 19.967 67.395 1.00 37.08 ? 301 GLU A CB  1 
ATOM   2303 C CG  . GLU A 1 293 ? 36.115 18.854 67.295 1.00 35.33 ? 301 GLU A CG  1 
ATOM   2304 C CD  . GLU A 1 293 ? 36.915 18.864 66.014 1.00 35.15 ? 301 GLU A CD  1 
ATOM   2305 O OE1 . GLU A 1 293 ? 36.536 19.610 65.082 1.00 35.53 ? 301 GLU A OE1 1 
ATOM   2306 O OE2 . GLU A 1 293 ? 37.931 18.135 65.946 1.00 38.47 ? 301 GLU A OE2 1 
ATOM   2307 N N   . HIS A 1 294 ? 33.907 22.288 68.819 1.00 33.66 ? 302 HIS A N   1 
ATOM   2308 C CA  . HIS A 1 294 ? 33.153 23.501 69.080 1.00 38.43 ? 302 HIS A CA  1 
ATOM   2309 C C   . HIS A 1 294 ? 31.981 23.670 68.116 1.00 32.49 ? 302 HIS A C   1 
ATOM   2310 O O   . HIS A 1 294 ? 32.126 23.461 66.914 1.00 30.94 ? 302 HIS A O   1 
ATOM   2311 C CB  . HIS A 1 294 ? 34.064 24.728 68.994 1.00 49.79 ? 302 HIS A CB  1 
ATOM   2312 C CG  . HIS A 1 294 ? 33.432 25.977 69.530 1.00 75.17 ? 302 HIS A CG  1 
ATOM   2313 N ND1 . HIS A 1 294 ? 33.236 26.158 70.888 1.00 87.54 ? 302 HIS A ND1 1 
ATOM   2314 C CD2 . HIS A 1 294 ? 32.973 27.064 68.874 1.00 72.67 ? 302 HIS A CD2 1 
ATOM   2315 C CE1 . HIS A 1 294 ? 32.665 27.345 71.017 1.00 94.79 ? 302 HIS A CE1 1 
ATOM   2316 N NE2 . HIS A 1 294 ? 32.489 27.925 69.824 1.00 93.33 ? 302 HIS A NE2 1 
ATOM   2317 N N   . GLY A 1 295 ? 30.821 24.035 68.672 1.00 29.43 ? 303 GLY A N   1 
ATOM   2318 C CA  . GLY A 1 295 ? 29.670 24.444 67.886 1.00 30.04 ? 303 GLY A CA  1 
ATOM   2319 C C   . GLY A 1 295 ? 28.905 23.311 67.206 1.00 34.28 ? 303 GLY A C   1 
ATOM   2320 O O   . GLY A 1 295 ? 28.141 23.564 66.279 1.00 40.86 ? 303 GLY A O   1 
ATOM   2321 N N   . PHE A 1 296 ? 29.095 22.075 67.683 1.00 34.05 ? 304 PHE A N   1 
ATOM   2322 C CA  . PHE A 1 296 ? 28.469 20.911 67.073 1.00 33.90 ? 304 PHE A CA  1 
ATOM   2323 C C   . PHE A 1 296 ? 26.945 21.031 67.033 1.00 34.83 ? 304 PHE A C   1 
ATOM   2324 O O   . PHE A 1 296 ? 26.311 20.586 66.080 1.00 38.09 ? 304 PHE A O   1 
ATOM   2325 C CB  . PHE A 1 296 ? 28.880 19.611 67.799 1.00 34.91 ? 304 PHE A CB  1 
ATOM   2326 C CG  . PHE A 1 296 ? 28.419 19.486 69.234 1.00 36.23 ? 304 PHE A CG  1 
ATOM   2327 C CD1 . PHE A 1 296 ? 29.150 20.049 70.269 1.00 35.81 ? 304 PHE A CD1 1 
ATOM   2328 C CD2 . PHE A 1 296 ? 27.246 18.818 69.545 1.00 34.83 ? 304 PHE A CD2 1 
ATOM   2329 C CE1 . PHE A 1 296 ? 28.724 19.933 71.586 1.00 34.60 ? 304 PHE A CE1 1 
ATOM   2330 C CE2 . PHE A 1 296 ? 26.820 18.708 70.863 1.00 38.12 ? 304 PHE A CE2 1 
ATOM   2331 C CZ  . PHE A 1 296 ? 27.561 19.267 71.876 1.00 41.15 ? 304 PHE A CZ  1 
ATOM   2332 N N   . TYR A 1 297 ? 26.373 21.639 68.079 1.00 35.21 ? 305 TYR A N   1 
ATOM   2333 C CA  . TYR A 1 297 ? 24.941 21.886 68.163 1.00 37.74 ? 305 TYR A CA  1 
ATOM   2334 C C   . TYR A 1 297 ? 24.410 22.768 67.032 1.00 39.78 ? 305 TYR A C   1 
ATOM   2335 O O   . TYR A 1 297 ? 23.283 22.575 66.582 1.00 46.36 ? 305 TYR A O   1 
ATOM   2336 C CB  . TYR A 1 297 ? 24.568 22.511 69.532 1.00 38.79 ? 305 TYR A CB  1 
ATOM   2337 C CG  . TYR A 1 297 ? 25.580 23.507 70.059 1.00 43.44 ? 305 TYR A CG  1 
ATOM   2338 C CD1 . TYR A 1 297 ? 26.645 23.094 70.851 1.00 39.51 ? 305 TYR A CD1 1 
ATOM   2339 C CD2 . TYR A 1 297 ? 25.495 24.854 69.734 1.00 37.75 ? 305 TYR A CD2 1 
ATOM   2340 C CE1 . TYR A 1 297 ? 27.587 23.998 71.324 1.00 37.40 ? 305 TYR A CE1 1 
ATOM   2341 C CE2 . TYR A 1 297 ? 26.435 25.768 70.198 1.00 38.25 ? 305 TYR A CE2 1 
ATOM   2342 C CZ  . TYR A 1 297 ? 27.481 25.335 70.993 1.00 38.70 ? 305 TYR A CZ  1 
ATOM   2343 O OH  . TYR A 1 297 ? 28.419 26.224 71.463 1.00 42.75 ? 305 TYR A OH  1 
ATOM   2344 N N   . SER A 1 298 ? 25.225 23.731 66.580 1.00 41.48 ? 306 SER A N   1 
ATOM   2345 C CA  . SER A 1 298 ? 24.823 24.671 65.544 1.00 39.21 ? 306 SER A CA  1 
ATOM   2346 C C   . SER A 1 298 ? 25.458 24.405 64.177 1.00 44.24 ? 306 SER A C   1 
ATOM   2347 O O   . SER A 1 298 ? 24.828 24.647 63.150 1.00 52.16 ? 306 SER A O   1 
ATOM   2348 C CB  . SER A 1 298 ? 25.131 26.097 65.990 1.00 36.08 ? 306 SER A CB  1 
ATOM   2349 O OG  . SER A 1 298 ? 26.498 26.249 66.332 1.00 41.60 ? 306 SER A OG  1 
ATOM   2350 N N   . ASN A 1 299 ? 26.705 23.915 64.169 1.00 46.02 ? 307 ASN A N   1 
ATOM   2351 C CA  . ASN A 1 299 ? 27.402 23.577 62.936 1.00 45.93 ? 307 ASN A CA  1 
ATOM   2352 C C   . ASN A 1 299 ? 26.766 22.404 62.193 1.00 47.10 ? 307 ASN A C   1 
ATOM   2353 O O   . ASN A 1 299 ? 26.836 22.343 60.967 1.00 54.79 ? 307 ASN A O   1 
ATOM   2354 C CB  . ASN A 1 299 ? 28.877 23.249 63.215 1.00 42.80 ? 307 ASN A CB  1 
ATOM   2355 C CG  . ASN A 1 299 ? 29.713 24.452 63.577 1.00 49.44 ? 307 ASN A CG  1 
ATOM   2356 O OD1 . ASN A 1 299 ? 29.353 25.602 63.306 1.00 53.76 ? 307 ASN A OD1 1 
ATOM   2357 N ND2 . ASN A 1 299 ? 30.869 24.214 64.179 1.00 54.47 ? 307 ASN A ND2 1 
ATOM   2358 N N   . TYR A 1 300 ? 26.163 21.477 62.949 1.00 45.74 ? 308 TYR A N   1 
ATOM   2359 C CA  . TYR A 1 300 ? 25.499 20.311 62.387 1.00 46.35 ? 308 TYR A CA  1 
ATOM   2360 C C   . TYR A 1 300 ? 24.045 20.286 62.858 1.00 53.07 ? 308 TYR A C   1 
ATOM   2361 O O   . TYR A 1 300 ? 23.688 19.500 63.732 1.00 55.95 ? 308 TYR A O   1 
ATOM   2362 C CB  . TYR A 1 300 ? 26.262 19.040 62.788 1.00 42.87 ? 308 TYR A CB  1 
ATOM   2363 C CG  . TYR A 1 300 ? 27.704 19.048 62.326 1.00 41.28 ? 308 TYR A CG  1 
ATOM   2364 C CD1 . TYR A 1 300 ? 28.029 18.850 60.990 1.00 40.41 ? 308 TYR A CD1 1 
ATOM   2365 C CD2 . TYR A 1 300 ? 28.741 19.285 63.219 1.00 42.12 ? 308 TYR A CD2 1 
ATOM   2366 C CE1 . TYR A 1 300 ? 29.352 18.866 60.557 1.00 43.13 ? 308 TYR A CE1 1 
ATOM   2367 C CE2 . TYR A 1 300 ? 30.067 19.307 62.799 1.00 38.42 ? 308 TYR A CE2 1 
ATOM   2368 C CZ  . TYR A 1 300 ? 30.370 19.096 61.467 1.00 40.06 ? 308 TYR A CZ  1 
ATOM   2369 O OH  . TYR A 1 300 ? 31.679 19.115 61.055 1.00 38.32 ? 308 TYR A OH  1 
ATOM   2370 N N   . PRO A 1 301 ? 23.164 21.139 62.278 1.00 61.20 ? 309 PRO A N   1 
ATOM   2371 C CA  . PRO A 1 301 ? 21.840 21.400 62.840 1.00 55.79 ? 309 PRO A CA  1 
ATOM   2372 C C   . PRO A 1 301 ? 20.940 20.174 62.993 1.00 59.20 ? 309 PRO A C   1 
ATOM   2373 O O   . PRO A 1 301 ? 20.173 20.094 63.950 1.00 66.19 ? 309 PRO A O   1 
ATOM   2374 C CB  . PRO A 1 301 ? 21.225 22.391 61.842 1.00 56.21 ? 309 PRO A CB  1 
ATOM   2375 C CG  . PRO A 1 301 ? 22.387 22.975 61.100 1.00 55.93 ? 309 PRO A CG  1 
ATOM   2376 C CD  . PRO A 1 301 ? 23.403 21.888 61.034 1.00 59.08 ? 309 PRO A CD  1 
ATOM   2377 N N   . SER A 1 302 ? 21.029 19.236 62.041 1.00 60.07 ? 310 SER A N   1 
ATOM   2378 C CA  . SER A 1 302 ? 20.157 18.071 62.014 1.00 65.37 ? 310 SER A CA  1 
ATOM   2379 C C   . SER A 1 302 ? 20.811 16.795 62.547 1.00 55.56 ? 310 SER A C   1 
ATOM   2380 O O   . SER A 1 302 ? 20.279 15.702 62.357 1.00 50.73 ? 310 SER A O   1 
ATOM   2381 C CB  . SER A 1 302 ? 19.660 17.834 60.589 1.00 78.04 ? 310 SER A CB  1 
ATOM   2382 O OG  . SER A 1 302 ? 20.735 17.565 59.704 1.00 84.48 ? 310 SER A OG  1 
ATOM   2383 N N   . SER A 1 303 ? 21.962 16.940 63.216 1.00 44.58 ? 311 SER A N   1 
ATOM   2384 C CA  . SER A 1 303 ? 22.655 15.805 63.804 1.00 38.42 ? 311 SER A CA  1 
ATOM   2385 C C   . SER A 1 303 ? 21.988 15.375 65.107 1.00 36.07 ? 311 SER A C   1 
ATOM   2386 O O   . SER A 1 303 ? 21.227 16.136 65.703 1.00 37.24 ? 311 SER A O   1 
ATOM   2387 C CB  . SER A 1 303 ? 24.124 16.135 64.050 1.00 39.97 ? 311 SER A CB  1 
ATOM   2388 O OG  . SER A 1 303 ? 24.270 17.199 64.976 1.00 39.84 ? 311 SER A OG  1 
ATOM   2389 N N   . GLU A 1 304 ? 22.293 14.146 65.537 1.00 32.74 ? 312 GLU A N   1 
ATOM   2390 C CA  . GLU A 1 304 ? 21.761 13.590 66.771 1.00 33.20 ? 312 GLU A CA  1 
ATOM   2391 C C   . GLU A 1 304 ? 22.200 14.401 67.989 1.00 30.93 ? 312 GLU A C   1 
ATOM   2392 O O   . GLU A 1 304 ? 21.409 14.629 68.900 1.00 29.39 ? 312 GLU A O   1 
ATOM   2393 C CB  . GLU A 1 304 ? 22.203 12.117 66.913 1.00 36.41 ? 312 GLU A CB  1 
ATOM   2394 C CG  . GLU A 1 304 ? 21.768 11.443 68.207 1.00 40.60 ? 312 GLU A CG  1 
ATOM   2395 C CD  . GLU A 1 304 ? 20.271 11.339 68.427 1.00 46.69 ? 312 GLU A CD  1 
ATOM   2396 O OE1 . GLU A 1 304 ? 19.507 11.482 67.446 1.00 53.39 ? 312 GLU A OE1 1 
ATOM   2397 O OE2 . GLU A 1 304 ? 19.859 11.131 69.592 1.00 51.79 ? 312 GLU A OE2 1 
ATOM   2398 N N   . ALA A 1 305 ? 23.466 14.833 67.994 1.00 31.37 ? 313 ALA A N   1 
ATOM   2399 C CA  . ALA A 1 305 ? 24.016 15.598 69.101 1.00 31.80 ? 313 ALA A CA  1 
ATOM   2400 C C   . ALA A 1 305 ? 23.278 16.919 69.309 1.00 31.47 ? 313 ALA A C   1 
ATOM   2401 O O   . ALA A 1 305 ? 22.924 17.258 70.436 1.00 28.66 ? 313 ALA A O   1 
ATOM   2402 C CB  . ALA A 1 305 ? 25.496 15.851 68.874 1.00 32.76 ? 313 ALA A CB  1 
ATOM   2403 N N   . ALA A 1 306 ? 23.047 17.653 68.214 1.00 33.53 ? 314 ALA A N   1 
ATOM   2404 C CA  . ALA A 1 306 ? 22.340 18.924 68.264 1.00 31.90 ? 314 ALA A CA  1 
ATOM   2405 C C   . ALA A 1 306 ? 20.933 18.763 68.836 1.00 32.28 ? 314 ALA A C   1 
ATOM   2406 O O   . ALA A 1 306 ? 20.516 19.541 69.693 1.00 30.38 ? 314 ALA A O   1 
ATOM   2407 C CB  . ALA A 1 306 ? 22.276 19.546 66.874 1.00 27.78 ? 314 ALA A CB  1 
ATOM   2408 N N   . GLU A 1 307 ? 20.213 17.745 68.350 1.00 33.22 ? 315 GLU A N   1 
ATOM   2409 C CA  . GLU A 1 307 ? 18.889 17.405 68.848 1.00 35.59 ? 315 GLU A CA  1 
ATOM   2410 C C   . GLU A 1 307 ? 18.902 17.157 70.358 1.00 31.21 ? 315 GLU A C   1 
ATOM   2411 O O   . GLU A 1 307 ? 17.995 17.586 71.068 1.00 30.64 ? 315 GLU A O   1 
ATOM   2412 C CB  . GLU A 1 307 ? 18.373 16.161 68.101 1.00 38.50 ? 315 GLU A CB  1 
ATOM   2413 C CG  . GLU A 1 307 ? 17.007 15.660 68.539 1.00 52.02 ? 315 GLU A CG  1 
ATOM   2414 C CD  . GLU A 1 307 ? 16.766 14.198 68.211 1.00 66.56 ? 315 GLU A CD  1 
ATOM   2415 O OE1 . GLU A 1 307 ? 16.773 13.849 67.009 1.00 74.86 ? 315 GLU A OE1 1 
ATOM   2416 O OE2 . GLU A 1 307 ? 16.588 13.397 69.158 1.00 66.93 ? 315 GLU A OE2 1 
ATOM   2417 N N   . GLN A 1 308 ? 19.941 16.461 70.837 1.00 28.14 ? 316 GLN A N   1 
ATOM   2418 C CA  . GLN A 1 308 ? 20.069 16.134 72.248 1.00 25.94 ? 316 GLN A CA  1 
ATOM   2419 C C   . GLN A 1 308 ? 20.318 17.366 73.116 1.00 27.15 ? 316 GLN A C   1 
ATOM   2420 O O   . GLN A 1 308 ? 19.778 17.467 74.214 1.00 23.84 ? 316 GLN A O   1 
ATOM   2421 C CB  . GLN A 1 308 ? 21.191 15.106 72.461 1.00 24.04 ? 316 GLN A CB  1 
ATOM   2422 C CG  . GLN A 1 308 ? 20.791 13.708 72.046 1.00 23.71 ? 316 GLN A CG  1 
ATOM   2423 C CD  . GLN A 1 308 ? 21.816 12.680 72.432 1.00 25.88 ? 316 GLN A CD  1 
ATOM   2424 O OE1 . GLN A 1 308 ? 22.455 12.761 73.488 1.00 29.11 ? 316 GLN A OE1 1 
ATOM   2425 N NE2 . GLN A 1 308 ? 22.002 11.691 71.576 1.00 24.72 ? 316 GLN A NE2 1 
ATOM   2426 N N   . VAL A 1 309 ? 21.139 18.296 72.615 1.00 31.27 ? 317 VAL A N   1 
ATOM   2427 C CA  . VAL A 1 309 ? 21.388 19.548 73.309 1.00 32.21 ? 317 VAL A CA  1 
ATOM   2428 C C   . VAL A 1 309 ? 20.075 20.303 73.514 1.00 32.10 ? 317 VAL A C   1 
ATOM   2429 O O   . VAL A 1 309 ? 19.807 20.800 74.605 1.00 38.78 ? 317 VAL A O   1 
ATOM   2430 C CB  . VAL A 1 309 ? 22.434 20.408 72.560 1.00 28.89 ? 317 VAL A CB  1 
ATOM   2431 C CG1 . VAL A 1 309 ? 22.531 21.813 73.153 1.00 28.59 ? 317 VAL A CG1 1 
ATOM   2432 C CG2 . VAL A 1 309 ? 23.798 19.727 72.554 1.00 29.06 ? 317 VAL A CG2 1 
ATOM   2433 N N   . LEU A 1 310 ? 19.262 20.372 72.455 1.00 30.25 ? 318 LEU A N   1 
ATOM   2434 C CA  . LEU A 1 310 ? 17.971 21.041 72.505 1.00 33.62 ? 318 LEU A CA  1 
ATOM   2435 C C   . LEU A 1 310 ? 17.025 20.390 73.511 1.00 28.53 ? 318 LEU A C   1 
ATOM   2436 O O   . LEU A 1 310 ? 16.291 21.081 74.212 1.00 26.32 ? 318 LEU A O   1 
ATOM   2437 C CB  . LEU A 1 310 ? 17.334 21.020 71.115 1.00 34.32 ? 318 LEU A CB  1 
ATOM   2438 C CG  . LEU A 1 310 ? 18.033 21.878 70.075 1.00 40.43 ? 318 LEU A CG  1 
ATOM   2439 C CD1 . LEU A 1 310 ? 17.633 21.462 68.684 1.00 46.23 ? 318 LEU A CD1 1 
ATOM   2440 C CD2 . LEU A 1 310 ? 17.733 23.351 70.294 1.00 40.53 ? 318 LEU A CD2 1 
ATOM   2441 N N   . ARG A 1 311 ? 17.050 19.056 73.568 1.00 27.58 ? 319 ARG A N   1 
ATOM   2442 C CA  . ARG A 1 311 ? 16.249 18.319 74.531 1.00 31.66 ? 319 ARG A CA  1 
ATOM   2443 C C   . ARG A 1 311 ? 16.697 18.614 75.962 1.00 27.38 ? 319 ARG A C   1 
ATOM   2444 O O   . ARG A 1 311 ? 15.863 18.810 76.842 1.00 28.63 ? 319 ARG A O   1 
ATOM   2445 C CB  . ARG A 1 311 ? 16.320 16.812 74.226 1.00 35.62 ? 319 ARG A CB  1 
ATOM   2446 C CG  . ARG A 1 311 ? 15.637 15.922 75.255 1.00 46.07 ? 319 ARG A CG  1 
ATOM   2447 C CD  . ARG A 1 311 ? 14.138 16.141 75.340 1.00 50.15 ? 319 ARG A CD  1 
ATOM   2448 N NE  . ARG A 1 311 ? 13.565 15.466 76.499 1.00 57.34 ? 319 ARG A NE  1 
ATOM   2449 C CZ  . ARG A 1 311 ? 13.536 14.150 76.674 1.00 57.70 ? 319 ARG A CZ  1 
ATOM   2450 N NH1 . ARG A 1 311 ? 13.847 13.313 75.696 1.00 51.21 ? 319 ARG A NH1 1 
ATOM   2451 N NH2 . ARG A 1 311 ? 13.168 13.661 77.855 1.00 61.81 ? 319 ARG A NH2 1 
ATOM   2452 N N   . ILE A 1 312 ? 18.017 18.652 76.181 1.00 28.03 ? 320 ILE A N   1 
ATOM   2453 C CA  . ILE A 1 312 ? 18.582 18.892 77.501 1.00 28.55 ? 320 ILE A CA  1 
ATOM   2454 C C   . ILE A 1 312 ? 18.289 20.306 78.002 1.00 29.58 ? 320 ILE A C   1 
ATOM   2455 O O   . ILE A 1 312 ? 17.942 20.485 79.168 1.00 29.86 ? 320 ILE A O   1 
ATOM   2456 C CB  . ILE A 1 312 ? 20.100 18.577 77.495 1.00 29.94 ? 320 ILE A CB  1 
ATOM   2457 C CG1 . ILE A 1 312 ? 20.344 17.066 77.331 1.00 33.50 ? 320 ILE A CG1 1 
ATOM   2458 C CG2 . ILE A 1 312 ? 20.801 19.090 78.746 1.00 29.18 ? 320 ILE A CG2 1 
ATOM   2459 C CD1 . ILE A 1 312 ? 21.764 16.705 77.053 1.00 33.64 ? 320 ILE A CD1 1 
ATOM   2460 N N   . ILE A 1 313 ? 18.435 21.304 77.121 1.00 27.59 ? 321 ILE A N   1 
ATOM   2461 C CA  . ILE A 1 313 ? 18.084 22.675 77.456 1.00 27.10 ? 321 ILE A CA  1 
ATOM   2462 C C   . ILE A 1 313 ? 16.601 22.774 77.811 1.00 29.08 ? 321 ILE A C   1 
ATOM   2463 O O   . ILE A 1 313 ? 16.231 23.504 78.728 1.00 33.29 ? 321 ILE A O   1 
ATOM   2464 C CB  . ILE A 1 313 ? 18.461 23.651 76.310 1.00 27.75 ? 321 ILE A CB  1 
ATOM   2465 C CG1 . ILE A 1 313 ? 19.987 23.703 76.095 1.00 26.55 ? 321 ILE A CG1 1 
ATOM   2466 C CG2 . ILE A 1 313 ? 17.893 25.055 76.566 1.00 27.64 ? 321 ILE A CG2 1 
ATOM   2467 C CD1 . ILE A 1 313 ? 20.426 24.494 74.856 1.00 26.69 ? 321 ILE A CD1 1 
ATOM   2468 N N   . GLY A 1 314 ? 15.761 22.037 77.073 1.00 29.59 ? 322 GLY A N   1 
ATOM   2469 C CA  . GLY A 1 314 ? 14.327 22.011 77.314 1.00 29.04 ? 322 GLY A CA  1 
ATOM   2470 C C   . GLY A 1 314 ? 13.946 21.465 78.689 1.00 28.89 ? 322 GLY A C   1 
ATOM   2471 O O   . GLY A 1 314 ? 13.133 22.064 79.389 1.00 32.63 ? 322 GLY A O   1 
ATOM   2472 N N   . ASP A 1 315 ? 14.539 20.323 79.058 1.00 29.13 ? 323 ASP A N   1 
ATOM   2473 C CA  . ASP A 1 315 ? 14.321 19.712 80.360 1.00 28.22 ? 323 ASP A CA  1 
ATOM   2474 C C   . ASP A 1 315 ? 14.803 20.622 81.488 1.00 26.80 ? 323 ASP A C   1 
ATOM   2475 O O   . ASP A 1 315 ? 14.134 20.763 82.509 1.00 30.40 ? 323 ASP A O   1 
ATOM   2476 C CB  . ASP A 1 315 ? 15.043 18.357 80.442 1.00 29.62 ? 323 ASP A CB  1 
ATOM   2477 C CG  . ASP A 1 315 ? 14.509 17.294 79.504 1.00 32.77 ? 323 ASP A CG  1 
ATOM   2478 O OD1 . ASP A 1 315 ? 13.409 17.491 78.945 1.00 35.09 ? 323 ASP A OD1 1 
ATOM   2479 O OD2 . ASP A 1 315 ? 15.198 16.271 79.317 1.00 37.24 ? 323 ASP A OD2 1 
ATOM   2480 N N   . PHE A 1 316 ? 15.979 21.223 81.285 1.00 25.40 ? 324 PHE A N   1 
ATOM   2481 C CA  . PHE A 1 316 ? 16.535 22.209 82.195 1.00 24.21 ? 324 PHE A CA  1 
ATOM   2482 C C   . PHE A 1 316 ? 15.543 23.340 82.463 1.00 25.02 ? 324 PHE A C   1 
ATOM   2483 O O   . PHE A 1 316 ? 15.365 23.755 83.604 1.00 26.69 ? 324 PHE A O   1 
ATOM   2484 C CB  . PHE A 1 316 ? 17.839 22.753 81.592 1.00 24.22 ? 324 PHE A CB  1 
ATOM   2485 C CG  . PHE A 1 316 ? 18.566 23.804 82.392 1.00 23.75 ? 324 PHE A CG  1 
ATOM   2486 C CD1 . PHE A 1 316 ? 19.241 23.470 83.554 1.00 23.79 ? 324 PHE A CD1 1 
ATOM   2487 C CD2 . PHE A 1 316 ? 18.595 25.124 81.970 1.00 22.32 ? 324 PHE A CD2 1 
ATOM   2488 C CE1 . PHE A 1 316 ? 19.926 24.437 84.280 1.00 24.91 ? 324 PHE A CE1 1 
ATOM   2489 C CE2 . PHE A 1 316 ? 19.277 26.089 82.699 1.00 24.17 ? 324 PHE A CE2 1 
ATOM   2490 C CZ  . PHE A 1 316 ? 19.940 25.741 83.849 1.00 25.82 ? 324 PHE A CZ  1 
ATOM   2491 N N   . MET A 1 317 ? 14.889 23.820 81.399 1.00 27.78 ? 325 MET A N   1 
ATOM   2492 C CA  . MET A 1 317 ? 13.923 24.902 81.507 1.00 30.75 ? 325 MET A CA  1 
ATOM   2493 C C   . MET A 1 317 ? 12.676 24.462 82.272 1.00 29.03 ? 325 MET A C   1 
ATOM   2494 O O   . MET A 1 317 ? 12.173 25.207 83.110 1.00 29.45 ? 325 MET A O   1 
ATOM   2495 C CB  . MET A 1 317 ? 13.538 25.410 80.110 1.00 29.08 ? 325 MET A CB  1 
ATOM   2496 C CG  . MET A 1 317 ? 14.539 26.376 79.534 1.00 29.81 ? 325 MET A CG  1 
ATOM   2497 S SD  . MET A 1 317 ? 14.225 26.709 77.787 1.00 33.24 ? 325 MET A SD  1 
ATOM   2498 C CE  . MET A 1 317 ? 12.856 27.838 77.921 1.00 29.64 ? 325 MET A CE  1 
ATOM   2499 N N   . ASN A 1 318 ? 12.188 23.251 81.975 1.00 26.91 ? 326 ASN A N   1 
ATOM   2500 C CA  . ASN A 1 318 ? 11.047 22.682 82.675 1.00 32.03 ? 326 ASN A CA  1 
ATOM   2501 C C   . ASN A 1 318 ? 11.310 22.536 84.173 1.00 35.32 ? 326 ASN A C   1 
ATOM   2502 O O   . ASN A 1 318 ? 10.467 22.903 84.987 1.00 37.60 ? 326 ASN A O   1 
ATOM   2503 C CB  . ASN A 1 318 ? 10.665 21.316 82.090 1.00 33.72 ? 326 ASN A CB  1 
ATOM   2504 C CG  . ASN A 1 318 ? 10.125 21.373 80.680 1.00 37.50 ? 326 ASN A CG  1 
ATOM   2505 O OD1 . ASN A 1 318 ? 9.950  22.442 80.081 1.00 38.99 ? 326 ASN A OD1 1 
ATOM   2506 N ND2 . ASN A 1 318 ? 9.847  20.211 80.113 1.00 40.58 ? 326 ASN A ND2 1 
ATOM   2507 N N   . ASN A 1 319 ? 12.485 21.996 84.521 1.00 37.30 ? 327 ASN A N   1 
ATOM   2508 C CA  . ASN A 1 319 ? 12.854 21.768 85.910 1.00 36.55 ? 327 ASN A CA  1 
ATOM   2509 C C   . ASN A 1 319 ? 12.871 23.053 86.736 1.00 33.94 ? 327 ASN A C   1 
ATOM   2510 O O   . ASN A 1 319 ? 12.492 23.037 87.903 1.00 35.82 ? 327 ASN A O   1 
ATOM   2511 C CB  . ASN A 1 319 ? 14.224 21.082 86.000 1.00 38.50 ? 327 ASN A CB  1 
ATOM   2512 C CG  . ASN A 1 319 ? 14.217 19.641 85.544 1.00 41.06 ? 327 ASN A CG  1 
ATOM   2513 O OD1 . ASN A 1 319 ? 13.169 19.032 85.309 1.00 42.81 ? 327 ASN A OD1 1 
ATOM   2514 N ND2 . ASN A 1 319 ? 15.397 19.054 85.420 1.00 43.80 ? 327 ASN A ND2 1 
ATOM   2515 N N   . LEU A 1 320 ? 13.305 24.156 86.114 1.00 34.28 ? 328 LEU A N   1 
ATOM   2516 C CA  . LEU A 1 320 ? 13.470 25.427 86.801 1.00 35.01 ? 328 LEU A CA  1 
ATOM   2517 C C   . LEU A 1 320 ? 12.244 26.336 86.740 1.00 32.83 ? 328 LEU A C   1 
ATOM   2518 O O   . LEU A 1 320 ? 12.224 27.383 87.381 1.00 33.62 ? 328 LEU A O   1 
ATOM   2519 C CB  . LEU A 1 320 ? 14.669 26.170 86.192 1.00 36.02 ? 328 LEU A CB  1 
ATOM   2520 C CG  . LEU A 1 320 ? 16.015 25.472 86.338 1.00 37.49 ? 328 LEU A CG  1 
ATOM   2521 C CD1 . LEU A 1 320 ? 17.121 26.308 85.738 1.00 37.72 ? 328 LEU A CD1 1 
ATOM   2522 C CD2 . LEU A 1 320 ? 16.315 25.158 87.791 1.00 35.28 ? 328 LEU A CD2 1 
ATOM   2523 N N   . SER A 1 321 ? 11.225 25.933 85.972 1.00 36.09 ? 329 SER A N   1 
ATOM   2524 C CA  . SER A 1 321 ? 10.033 26.746 85.794 1.00 41.59 ? 329 SER A CA  1 
ATOM   2525 C C   . SER A 1 321 ? 8.810  26.113 86.459 1.00 38.67 ? 329 SER A C   1 
ATOM   2526 O O   . SER A 1 321 ? 8.918  25.054 87.073 1.00 38.71 ? 329 SER A O   1 
ATOM   2527 C CB  . SER A 1 321 ? 9.777  26.991 84.311 1.00 42.70 ? 329 SER A CB  1 
ATOM   2528 O OG  . SER A 1 321 ? 9.788  25.781 83.576 1.00 46.40 ? 329 SER A OG  1 
ATOM   2529 O OXT . SER A 1 321 ? 7.717  26.672 86.396 1.00 39.78 ? 329 SER A OXT 1 
HETATM 2530 C C1  . GOL B 2 .   ? 43.611 29.901 74.721 1.00 64.21 ? 401 GOL A C1  1 
HETATM 2531 O O1  . GOL B 2 .   ? 43.667 31.324 74.731 1.00 52.34 ? 401 GOL A O1  1 
HETATM 2532 C C2  . GOL B 2 .   ? 43.086 29.346 76.029 1.00 67.35 ? 401 GOL A C2  1 
HETATM 2533 O O2  . GOL B 2 .   ? 44.056 29.537 77.058 1.00 79.95 ? 401 GOL A O2  1 
HETATM 2534 C C3  . GOL B 2 .   ? 41.772 29.957 76.464 1.00 64.57 ? 401 GOL A C3  1 
HETATM 2535 O O3  . GOL B 2 .   ? 40.814 29.989 75.410 1.00 44.42 ? 401 GOL A O3  1 
HETATM 2536 O O   . HOH C 3 .   ? 20.065 41.093 91.247 1.00 41.39 ? 501 HOH A O   1 
HETATM 2537 O O   . HOH C 3 .   ? 40.357 34.185 56.562 1.00 33.31 ? 502 HOH A O   1 
HETATM 2538 O O   . HOH C 3 .   ? 20.047 35.041 65.733 1.00 24.05 ? 503 HOH A O   1 
HETATM 2539 O O   . HOH C 3 .   ? 15.928 29.716 89.222 1.00 41.96 ? 504 HOH A O   1 
HETATM 2540 O O   . HOH C 3 .   ? 1.859  34.471 72.969 1.00 54.96 ? 505 HOH A O   1 
HETATM 2541 O O   . HOH C 3 .   ? 3.194  41.379 70.022 1.00 39.79 ? 506 HOH A O   1 
HETATM 2542 O O   . HOH C 3 .   ? 31.783 37.432 69.032 1.00 35.41 ? 507 HOH A O   1 
HETATM 2543 O O   . HOH C 3 .   ? 23.145 36.885 69.741 1.00 33.38 ? 508 HOH A O   1 
HETATM 2544 O O   . HOH C 3 .   ? 42.180 27.611 53.344 1.00 24.88 ? 509 HOH A O   1 
HETATM 2545 O O   . HOH C 3 .   ? 27.281 41.100 67.195 1.00 35.16 ? 510 HOH A O   1 
HETATM 2546 O O   . HOH C 3 .   ? 16.384 40.627 88.088 1.00 39.39 ? 511 HOH A O   1 
HETATM 2547 O O   . HOH C 3 .   ? 5.230  38.351 82.451 1.00 41.09 ? 512 HOH A O   1 
HETATM 2548 O O   . HOH C 3 .   ? 23.193 45.933 65.216 1.00 37.90 ? 513 HOH A O   1 
HETATM 2549 O O   . HOH C 3 .   ? 3.185  39.847 77.858 1.00 50.60 ? 514 HOH A O   1 
HETATM 2550 O O   . HOH C 3 .   ? 30.629 45.862 66.251 1.00 40.83 ? 515 HOH A O   1 
HETATM 2551 O O   . HOH C 3 .   ? -2.594 43.137 71.696 1.00 59.77 ? 516 HOH A O   1 
HETATM 2552 O O   . HOH C 3 .   ? 27.943 44.702 65.920 1.00 43.24 ? 517 HOH A O   1 
HETATM 2553 O O   . HOH C 3 .   ? 26.066 32.199 99.026 1.00 56.05 ? 518 HOH A O   1 
HETATM 2554 O O   . HOH C 3 .   ? 8.667  29.977 91.789 1.00 45.73 ? 519 HOH A O   1 
# 
