data_8ZRF
# 
_entry.id   8ZRF 
# 
_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   8ZRF         pdb_00008zrf 10.2210/pdb8zrf/pdb 
WWPDB D_1300048399 ?            ?                   
# 
_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                        8ZRF 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8ZR6 
_pdbx_database_related.content_type   unspecified 
# 
_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 Carboxylesterase CXE15' 
_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 'Carboxylesterase 15' 35835.363 1  3.1.1.- ? ? ? 
2 non-polymer syn GLYCEROL              92.094    2  ?       ? ? ? 
3 water       nat water                 18.015    50 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'AtCXE15,Strigolactones hydrolase CXE15' 
# 
_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
GPTSPTLESISLEPMLVIVGGSELLRDRAKEYAYKLKKMGGKRVDYIEFENKEHGFYSNYPSSEAAEQVLRIIGDFMNNL
S
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QVAEDCMGLLQLLSNGTVLRSESIDLITQQIPFKNNQTVLFKDSIYHKPNNLHLRLYKPISASNRTALPVVVFFHGGGFC
FGSRSWPHFHNFCLTLASSLNALVVSPDYRLAPEHRLPAAFEDAEAVLTWLWDQAVSDGVNHWFEDGTDVDFDRVFVVGD
SSGGNIAHQLAVRFGSGSIELTPVRVRGYVLMGPFFGGEERTNSENGPSEALLSLDLLDKFWRLSLPNGATRDHHMANPF
GPTSPTLESISLEPMLVIVGGSELLRDRAKEYAYKLKKMGGKRVDYIEFENKEHGFYSNYPSSEAAEQVLRIIGDFMNNL
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 GLU 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 GLU 263 271 271 GLU GLU 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 2 GOL 1  402 402 GOL GOL A . 
D 3 HOH 1  501 38  HOH HOH A . 
D 3 HOH 2  502 26  HOH HOH A . 
D 3 HOH 3  503 24  HOH HOH A . 
D 3 HOH 4  504 45  HOH HOH A . 
D 3 HOH 5  505 1   HOH HOH A . 
D 3 HOH 6  506 21  HOH HOH A . 
D 3 HOH 7  507 56  HOH HOH A . 
D 3 HOH 8  508 78  HOH HOH A . 
D 3 HOH 9  509 87  HOH HOH A . 
D 3 HOH 10 510 68  HOH HOH A . 
D 3 HOH 11 511 5   HOH HOH A . 
D 3 HOH 12 512 41  HOH HOH A . 
D 3 HOH 13 513 55  HOH HOH A . 
D 3 HOH 14 514 82  HOH HOH A . 
D 3 HOH 15 515 53  HOH HOH A . 
D 3 HOH 16 516 35  HOH HOH A . 
D 3 HOH 17 517 58  HOH HOH A . 
D 3 HOH 18 518 8   HOH HOH A . 
D 3 HOH 19 519 17  HOH HOH A . 
D 3 HOH 20 520 84  HOH HOH A . 
D 3 HOH 21 521 42  HOH HOH A . 
D 3 HOH 22 522 3   HOH HOH A . 
D 3 HOH 23 523 67  HOH HOH A . 
D 3 HOH 24 524 30  HOH HOH A . 
D 3 HOH 25 525 37  HOH HOH A . 
D 3 HOH 26 526 19  HOH HOH A . 
D 3 HOH 27 527 10  HOH HOH A . 
D 3 HOH 28 528 28  HOH HOH A . 
D 3 HOH 29 529 13  HOH HOH A . 
D 3 HOH 30 530 31  HOH HOH A . 
D 3 HOH 31 531 6   HOH HOH A . 
D 3 HOH 32 532 4   HOH HOH A . 
D 3 HOH 33 533 11  HOH HOH A . 
D 3 HOH 34 534 46  HOH HOH A . 
D 3 HOH 35 535 57  HOH HOH A . 
D 3 HOH 36 536 60  HOH HOH A . 
D 3 HOH 37 537 51  HOH HOH A . 
D 3 HOH 38 538 14  HOH HOH A . 
D 3 HOH 39 539 29  HOH HOH A . 
D 3 HOH 40 540 80  HOH HOH A . 
D 3 HOH 41 541 16  HOH HOH A . 
D 3 HOH 42 542 43  HOH HOH A . 
D 3 HOH 43 543 50  HOH HOH A . 
D 3 HOH 44 544 75  HOH HOH A . 
D 3 HOH 45 545 15  HOH HOH A . 
D 3 HOH 46 546 86  HOH HOH A . 
D 3 HOH 47 547 70  HOH HOH A . 
D 3 HOH 48 548 61  HOH HOH A . 
D 3 HOH 49 549 69  HOH HOH A . 
D 3 HOH 50 550 85  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          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .    ? 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                     8ZRF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.091 
_cell.length_a_esd                 ? 
_cell.length_b                     84.091 
_cell.length_b_esd                 ? 
_cell.length_c                     117.238 
_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                         8ZRF 
_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                   8ZRF 
_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             2.82 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.35 
_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                          46.73 
_reflns.entry_id                                       8ZRF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.05 
_reflns.d_resolution_low                               48.13 
_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                                     27053 
_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                           99.82 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                14 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.37 
_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                                   0.998 
_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                                    2.05 
_reflns_shell.d_res_low                                     2.12 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.04 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2637 
_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                                  0.82 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.92 
_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]                            -0.39 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.39 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.78 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               42.981 
_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                                 8ZRF 
_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                            2.05 
_refine.ls_d_res_low                             48.13 
_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                     27041 
_refine.ls_number_reflns_R_free                  1365 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20326 
_refine.ls_R_factor_R_free                       0.22988 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20184 
_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                       0.173 
_refine.pdbx_overall_ESU_R_Free                  0.152 
_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                             4.144 
_refine.overall_SU_ML                            0.109 
_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                       2.05 
_refine_hist.d_res_low                        48.13 
_refine_hist.number_atoms_solvent             50 
_refine_hist.number_atoms_total               2591 
_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         12 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_refine_ls_shell.R_factor_R_free                     0.2716 
_refine_ls_shell.R_factor_R_free_error               ? 
_refine_ls_shell.R_factor_R_work                     0.2675 
_refine_ls_shell.R_factor_all                        ? 
_refine_ls_shell.R_factor_obs                        ? 
_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_free   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.d_res_high                          2.05 
_refine_ls_shell.d_res_low                           2.12 
_refine_ls_shell.number_reflns_R_free                ? 
_refine_ls_shell.number_reflns_R_work                ? 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   2637 
_refine_ls_shell.pdbx_R_complete                     ? 
_refine_ls_shell.pdbx_fsc_free                       ? 
_refine_ls_shell.pdbx_fsc_work                       ? 
_refine_ls_shell.pdbx_phase_error                    ? 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used      ? 
_refine_ls_shell.percent_reflns_R_free               ? 
_refine_ls_shell.percent_reflns_obs                  99.92 
_refine_ls_shell.redundancy_reflns_all               ? 
_refine_ls_shell.redundancy_reflns_obs               ? 
_refine_ls_shell.wR_factor_R_free                    ? 
_refine_ls_shell.wR_factor_R_work                    ? 
_refine_ls_shell.wR_factor_all                       ? 
_refine_ls_shell.wR_factor_obs                       ? 
# 
_struct.entry_id                     8ZRF 
_struct.title                        'Arabidopsis Carboxylesterase CXE15' 
_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        8ZRF 
_struct_keywords.text            'CXE15, carboxylesterase, catabolic enzyme, strigolactones, 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 2 ? 
D 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              8ZRF 
_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 
# 
_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)' 7180  ? 
1 MORE         -45   ? 
1 'SSA (A^2)'  24860 ? 
# 
_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,D 
# 
_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 117.2380000000 
# 
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 ASN A 203 ? GLY A 207 ? ASN A 211 GLY A 215 5 ? 5  
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 ? GLY A 280 ? LEU A 273 GLY A 288 1 ? 16 
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               2.184 
_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 -0.51 
2 LEU 117 A . ? LEU 125 A PRO 118 A ? PRO 126 A 1 8.80  
3 THR 182 A . ? THR 190 A PRO 183 A ? PRO 191 A 1 7.96  
# 
_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 LYS A 42  ? N LYS A 50  O LEU A 56  ? O LEU A 64  
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 LEU A 68  ? N LEU A 76  O ASP A 151 ? O ASP A 159 
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                   8ZRF 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    546 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    550 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.15 
# 
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 PRO A 126 ? ? -94.89  31.15   
2 1 SER A 169 ? ? 57.63   -114.50 
3 1 LEU A 220 ? ? -124.61 -52.09  
# 
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 73  ? ? 0.290 'SIDE CHAIN' 
2 1 ARG A 92  ? ? 0.250 'SIDE CHAIN' 
3 1 ARG A 274 ? ? 0.083 'SIDE CHAIN' 
4 1 ARG A 291 ? ? 0.079 'SIDE CHAIN' 
5 1 ARG A 319 ? ? 0.112 'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+1/4  
3 y+1/2,-x+1/2,z+3/4  
4 x+1/2,-y+1/2,-z+3/4 
5 -x+1/2,y+1/2,-z+1/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
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           ? 
_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          ? 
# 
_space_group.name_H-M_alt     'P 41 21 2' 
_space_group.name_Hall        'P 4abw 2nw' 
_space_group.IT_number        92 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8ZRF 
_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]   0.011892 
_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]   0.011892 
_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]   0.008530 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   ? 50.029 47.953 64.054 1.00 75.59  ? 9   GLN A N   1 
ATOM   2    C CA  . GLN A 1 1   ? 50.044 46.839 65.001 1.00 80.08  ? 9   GLN A CA  1 
ATOM   3    C C   . GLN A 1 1   ? 48.733 46.057 64.954 1.00 76.96  ? 9   GLN A C   1 
ATOM   4    O O   . GLN A 1 1   ? 48.743 44.837 64.813 1.00 74.53  ? 9   GLN A O   1 
ATOM   5    C CB  . GLN A 1 1   ? 50.302 47.349 66.430 1.00 83.93  ? 9   GLN A CB  1 
ATOM   6    C CG  . GLN A 1 1   ? 50.588 46.238 67.436 1.00 87.40  ? 9   GLN A CG  1 
ATOM   7    C CD  . GLN A 1 1   ? 51.809 45.445 67.048 1.00 94.76  ? 9   GLN A CD  1 
ATOM   8    O OE1 . GLN A 1 1   ? 51.738 44.242 66.778 1.00 100.91 ? 9   GLN A OE1 1 
ATOM   9    N NE2 . GLN A 1 1   ? 52.958 46.106 66.995 1.00 94.41  ? 9   GLN A NE2 1 
ATOM   10   N N   . VAL A 1 2   ? 47.611 46.775 65.085 1.00 75.06  ? 10  VAL A N   1 
ATOM   11   C CA  . VAL A 1 2   ? 46.287 46.179 64.988 1.00 75.72  ? 10  VAL A CA  1 
ATOM   12   C C   . VAL A 1 2   ? 46.047 45.682 63.562 1.00 74.23  ? 10  VAL A C   1 
ATOM   13   O O   . VAL A 1 2   ? 45.445 44.629 63.357 1.00 66.85  ? 10  VAL A O   1 
ATOM   14   C CB  . VAL A 1 2   ? 45.186 47.178 65.441 1.00 73.85  ? 10  VAL A CB  1 
ATOM   15   C CG1 . VAL A 1 2   ? 43.786 46.585 65.272 1.00 72.60  ? 10  VAL A CG1 1 
ATOM   16   C CG2 . VAL A 1 2   ? 45.413 47.637 66.883 1.00 74.35  ? 10  VAL A CG2 1 
ATOM   17   N N   . ALA A 1 3   ? 46.538 46.453 62.583 1.00 71.84  ? 11  ALA A N   1 
ATOM   18   C CA  . ALA A 1 3   ? 46.404 46.111 61.176 1.00 70.56  ? 11  ALA A CA  1 
ATOM   19   C C   . ALA A 1 3   ? 47.199 44.859 60.804 1.00 70.09  ? 11  ALA A C   1 
ATOM   20   O O   . ALA A 1 3   ? 46.765 44.089 59.950 1.00 71.28  ? 11  ALA A O   1 
ATOM   21   C CB  . ALA A 1 3   ? 46.831 47.288 60.318 1.00 71.43  ? 11  ALA A CB  1 
ATOM   22   N N   . GLU A 1 4   ? 48.359 44.664 61.447 1.00 67.99  ? 12  GLU A N   1 
ATOM   23   C CA  . GLU A 1 4   ? 49.145 43.452 61.270 1.00 68.43  ? 12  GLU A CA  1 
ATOM   24   C C   . GLU A 1 4   ? 48.447 42.247 61.888 1.00 62.58  ? 12  GLU A C   1 
ATOM   25   O O   . GLU A 1 4   ? 48.441 41.169 61.300 1.00 57.65  ? 12  GLU A O   1 
ATOM   26   C CB  . GLU A 1 4   ? 50.546 43.565 61.894 1.00 75.40  ? 12  GLU A CB  1 
ATOM   27   C CG  . GLU A 1 4   ? 51.568 44.264 61.017 1.00 84.29  ? 12  GLU A CG  1 
ATOM   28   C CD  . GLU A 1 4   ? 53.001 43.981 61.422 1.00 90.82  ? 12  GLU A CD  1 
ATOM   29   O OE1 . GLU A 1 4   ? 53.469 42.842 61.193 1.00 92.89  ? 12  GLU A OE1 1 
ATOM   30   O OE2 . GLU A 1 4   ? 53.651 44.889 61.987 1.00 93.14  ? 12  GLU A OE2 1 
ATOM   31   N N   . ASP A 1 5   ? 47.897 42.438 63.092 1.00 59.56  ? 13  ASP A N   1 
ATOM   32   C CA  . ASP A 1 5   ? 47.127 41.406 63.766 1.00 61.00  ? 13  ASP A CA  1 
ATOM   33   C C   . ASP A 1 5   ? 45.905 40.974 62.956 1.00 58.59  ? 13  ASP A C   1 
ATOM   34   O O   . ASP A 1 5   ? 45.516 39.807 62.996 1.00 55.46  ? 13  ASP A O   1 
ATOM   35   C CB  . ASP A 1 5   ? 46.698 41.898 65.156 1.00 65.57  ? 13  ASP A CB  1 
ATOM   36   C CG  . ASP A 1 5   ? 47.802 41.887 66.195 1.00 65.86  ? 13  ASP A CG  1 
ATOM   37   O OD1 . ASP A 1 5   ? 48.800 41.164 65.992 1.00 67.22  ? 13  ASP A OD1 1 
ATOM   38   O OD2 . ASP A 1 5   ? 47.671 42.606 67.210 1.00 66.10  ? 13  ASP A OD2 1 
ATOM   39   N N   . CYS A 1 6   ? 45.319 41.924 62.218 1.00 55.07  ? 14  CYS A N   1 
ATOM   40   C CA  . CYS A 1 6   ? 44.199 41.650 61.331 1.00 57.60  ? 14  CYS A CA  1 
ATOM   41   C C   . CYS A 1 6   ? 44.606 40.801 60.124 1.00 58.64  ? 14  CYS A C   1 
ATOM   42   O O   . CYS A 1 6   ? 43.855 39.924 59.701 1.00 50.53  ? 14  CYS A O   1 
ATOM   43   C CB  . CYS A 1 6   ? 43.544 42.962 60.901 1.00 59.95  ? 14  CYS A CB  1 
ATOM   44   S SG  . CYS A 1 6   ? 42.247 42.772 59.646 1.00 60.91  ? 14  CYS A SG  1 
ATOM   45   N N   . MET A 1 7   ? 45.785 41.078 59.552 1.00 58.48  ? 15  MET A N   1 
ATOM   46   C CA  . MET A 1 7   ? 46.300 40.292 58.441 1.00 56.34  ? 15  MET A CA  1 
ATOM   47   C C   . MET A 1 7   ? 46.589 38.862 58.896 1.00 51.57  ? 15  MET A C   1 
ATOM   48   O O   . MET A 1 7   ? 46.326 37.910 58.166 1.00 55.20  ? 15  MET A O   1 
ATOM   49   C CB  . MET A 1 7   ? 47.572 40.941 57.872 1.00 60.79  ? 15  MET A CB  1 
ATOM   50   C CG  . MET A 1 7   ? 47.309 42.249 57.131 1.00 66.27  ? 15  MET A CG  1 
ATOM   51   S SD  . MET A 1 7   ? 46.363 42.074 55.596 1.00 75.36  ? 15  MET A SD  1 
ATOM   52   C CE  . MET A 1 7   ? 47.364 40.881 54.723 1.00 74.41  ? 15  MET A CE  1 
ATOM   53   N N   . GLY A 1 8   ? 47.110 38.722 60.119 1.00 46.72  ? 16  GLY A N   1 
ATOM   54   C CA  . GLY A 1 8   ? 47.401 37.424 60.703 1.00 46.57  ? 16  GLY A CA  1 
ATOM   55   C C   . GLY A 1 8   ? 46.149 36.645 61.097 1.00 47.55  ? 16  GLY A C   1 
ATOM   56   O O   . GLY A 1 8   ? 46.155 35.413 61.103 1.00 43.79  ? 16  GLY A O   1 
ATOM   57   N N   . LEU A 1 9   ? 45.087 37.380 61.451 1.00 45.87  ? 17  LEU A N   1 
ATOM   58   C CA  . LEU A 1 9   ? 43.803 36.776 61.764 1.00 43.94  ? 17  LEU A CA  1 
ATOM   59   C C   . LEU A 1 9   ? 43.237 36.059 60.538 1.00 40.47  ? 17  LEU A C   1 
ATOM   60   O O   . LEU A 1 9   ? 42.828 34.906 60.638 1.00 38.20  ? 17  LEU A O   1 
ATOM   61   C CB  . LEU A 1 9   ? 42.819 37.846 62.267 1.00 44.22  ? 17  LEU A CB  1 
ATOM   62   C CG  . LEU A 1 9   ? 41.391 37.367 62.535 1.00 45.14  ? 17  LEU A CG  1 
ATOM   63   C CD1 . LEU A 1 9   ? 41.344 36.428 63.717 1.00 44.50  ? 17  LEU A CD1 1 
ATOM   64   C CD2 . LEU A 1 9   ? 40.458 38.542 62.755 1.00 44.04  ? 17  LEU A CD2 1 
ATOM   65   N N   . LEU A 1 10  ? 43.207 36.756 59.394 1.00 40.90  ? 18  LEU A N   1 
ATOM   66   C CA  . LEU A 1 10  ? 42.769 36.160 58.142 1.00 43.81  ? 18  LEU A CA  1 
ATOM   67   C C   . LEU A 1 10  ? 43.485 34.841 57.845 1.00 45.42  ? 18  LEU A C   1 
ATOM   68   O O   . LEU A 1 10  ? 42.851 33.864 57.448 1.00 41.88  ? 18  LEU A O   1 
ATOM   69   C CB  . LEU A 1 10  ? 43.004 37.124 56.978 1.00 46.91  ? 18  LEU A CB  1 
ATOM   70   C CG  . LEU A 1 10  ? 42.195 38.433 56.971 1.00 50.88  ? 18  LEU A CG  1 
ATOM   71   C CD1 . LEU A 1 10  ? 42.192 39.046 55.578 1.00 49.53  ? 18  LEU A CD1 1 
ATOM   72   C CD2 . LEU A 1 10  ? 40.775 38.235 57.462 1.00 49.64  ? 18  LEU A CD2 1 
ATOM   73   N N   . GLN A 1 11  ? 44.809 34.815 58.045 1.00 43.17  ? 19  GLN A N   1 
ATOM   74   C CA  . GLN A 1 11  ? 45.586 33.620 57.762 1.00 43.27  ? 19  GLN A CA  1 
ATOM   75   C C   . GLN A 1 11  ? 45.198 32.480 58.697 1.00 40.49  ? 19  GLN A C   1 
ATOM   76   O O   . GLN A 1 11  ? 44.985 31.360 58.248 1.00 43.13  ? 19  GLN A O   1 
ATOM   77   C CB  . GLN A 1 11  ? 47.086 33.904 57.862 1.00 48.25  ? 19  GLN A CB  1 
ATOM   78   C CG  . GLN A 1 11  ? 47.563 34.908 56.827 1.00 57.80  ? 19  GLN A CG  1 
ATOM   79   C CD  . GLN A 1 11  ? 49.057 35.072 56.860 1.00 64.75  ? 19  GLN A CD  1 
ATOM   80   O OE1 . GLN A 1 11  ? 49.805 34.232 56.352 1.00 73.88  ? 19  GLN A OE1 1 
ATOM   81   N NE2 . GLN A 1 11  ? 49.529 36.160 57.447 1.00 67.70  ? 19  GLN A NE2 1 
ATOM   82   N N   . LEU A 1 12  ? 45.102 32.767 60.000 1.00 38.82  ? 20  LEU A N   1 
ATOM   83   C CA  . LEU A 1 12  ? 44.796 31.732 60.976 1.00 40.75  ? 20  LEU A CA  1 
ATOM   84   C C   . LEU A 1 12  ? 43.375 31.203 60.794 1.00 39.57  ? 20  LEU A C   1 
ATOM   85   O O   . LEU A 1 12  ? 43.127 30.007 60.935 1.00 37.51  ? 20  LEU A O   1 
ATOM   86   C CB  . LEU A 1 12  ? 44.971 32.278 62.395 1.00 43.48  ? 20  LEU A CB  1 
ATOM   87   C CG  . LEU A 1 12  ? 46.405 32.601 62.804 1.00 43.60  ? 20  LEU A CG  1 
ATOM   88   C CD1 . LEU A 1 12  ? 46.430 33.473 64.043 1.00 42.80  ? 20  LEU A CD1 1 
ATOM   89   C CD2 . LEU A 1 12  ? 47.202 31.336 63.038 1.00 43.52  ? 20  LEU A CD2 1 
ATOM   90   N N   . LEU A 1 13  ? 42.452 32.103 60.442 1.00 38.17  ? 21  LEU A N   1 
ATOM   91   C CA  . LEU A 1 13  ? 41.044 31.756 60.344 1.00 41.48  ? 21  LEU A CA  1 
ATOM   92   C C   . LEU A 1 13  ? 40.787 30.694 59.275 1.00 39.54  ? 21  LEU A C   1 
ATOM   93   O O   . LEU A 1 13  ? 39.954 29.802 59.460 1.00 37.07  ? 21  LEU A O   1 
ATOM   94   C CB  . LEU A 1 13  ? 40.244 33.037 60.050 1.00 44.43  ? 21  LEU A CB  1 
ATOM   95   C CG  . LEU A 1 13  ? 38.740 32.923 60.143 1.00 51.52  ? 21  LEU A CG  1 
ATOM   96   C CD1 . LEU A 1 13  ? 38.294 32.716 61.586 1.00 53.76  ? 21  LEU A CD1 1 
ATOM   97   C CD2 . LEU A 1 13  ? 38.075 34.152 59.554 1.00 54.28  ? 21  LEU A CD2 1 
ATOM   98   N N   . SER A 1 14  ? 41.522 30.784 58.161 1.00 36.81  ? 22  SER A N   1 
ATOM   99   C CA  . SER A 1 14  ? 41.274 29.932 57.009 1.00 38.66  ? 22  SER A CA  1 
ATOM   100  C C   . SER A 1 14  ? 42.338 28.858 56.791 1.00 39.17  ? 22  SER A C   1 
ATOM   101  O O   . SER A 1 14  ? 42.367 28.205 55.751 1.00 38.41  ? 22  SER A O   1 
ATOM   102  C CB  . SER A 1 14  ? 41.117 30.798 55.770 1.00 36.78  ? 22  SER A CB  1 
ATOM   103  O OG  . SER A 1 14  ? 39.894 31.511 55.846 1.00 32.71  ? 22  SER A OG  1 
ATOM   104  N N   . ASN A 1 15  ? 43.187 28.665 57.801 1.00 42.37  ? 23  ASN A N   1 
ATOM   105  C CA  . ASN A 1 15  ? 44.249 27.679 57.742 1.00 47.33  ? 23  ASN A CA  1 
ATOM   106  C C   . ASN A 1 15  ? 43.724 26.245 57.820 1.00 46.19  ? 23  ASN A C   1 
ATOM   107  O O   . ASN A 1 15  ? 44.251 25.353 57.162 1.00 47.35  ? 23  ASN A O   1 
ATOM   108  C CB  . ASN A 1 15  ? 45.232 27.939 58.879 1.00 52.26  ? 23  ASN A CB  1 
ATOM   109  C CG  . ASN A 1 15  ? 46.530 27.227 58.693 1.00 57.47  ? 23  ASN A CG  1 
ATOM   110  O OD1 . ASN A 1 15  ? 46.893 26.349 59.477 1.00 63.55  ? 23  ASN A OD1 1 
ATOM   111  N ND2 . ASN A 1 15  ? 47.244 27.580 57.633 1.00 59.07  ? 23  ASN A ND2 1 
ATOM   112  N N   . GLY A 1 16  ? 42.694 26.027 58.643 1.00 45.50  ? 24  GLY A N   1 
ATOM   113  C CA  . GLY A 1 16  ? 42.101 24.708 58.800 1.00 48.46  ? 24  GLY A CA  1 
ATOM   114  C C   . GLY A 1 16  ? 43.044 23.733 59.502 1.00 49.39  ? 24  GLY A C   1 
ATOM   115  O O   . GLY A 1 16  ? 43.968 24.146 60.200 1.00 46.49  ? 24  GLY A O   1 
ATOM   116  N N   . THR A 1 17  ? 42.802 22.434 59.302 1.00 46.43  ? 25  THR A N   1 
ATOM   117  C CA  . THR A 1 17  ? 43.618 21.397 59.908 1.00 44.36  ? 25  THR A CA  1 
ATOM   118  C C   . THR A 1 17  ? 43.713 20.199 58.967 1.00 41.09  ? 25  THR A C   1 
ATOM   119  O O   . THR A 1 17  ? 42.899 20.049 58.060 1.00 42.74  ? 25  THR A O   1 
ATOM   120  C CB  . THR A 1 17  ? 43.038 21.029 61.289 1.00 47.40  ? 25  THR A CB  1 
ATOM   121  O OG1 . THR A 1 17  ? 44.001 20.289 62.035 1.00 46.42  ? 25  THR A OG1 1 
ATOM   122  C CG2 . THR A 1 17  ? 41.748 20.227 61.190 1.00 48.43  ? 25  THR A CG2 1 
ATOM   123  N N   . VAL A 1 18  ? 44.706 19.342 59.219 1.00 38.96  ? 26  VAL A N   1 
ATOM   124  C CA  . VAL A 1 18  ? 44.961 18.160 58.413 1.00 39.15  ? 26  VAL A CA  1 
ATOM   125  C C   . VAL A 1 18  ? 44.721 16.926 59.273 1.00 41.61  ? 26  VAL A C   1 
ATOM   126  O O   . VAL A 1 18  ? 45.331 16.779 60.325 1.00 41.60  ? 26  VAL A O   1 
ATOM   127  C CB  . VAL A 1 18  ? 46.401 18.185 57.852 1.00 40.72  ? 26  VAL A CB  1 
ATOM   128  C CG1 . VAL A 1 18  ? 46.749 16.881 57.123 1.00 41.24  ? 26  VAL A CG1 1 
ATOM   129  C CG2 . VAL A 1 18  ? 46.607 19.398 56.951 1.00 41.13  ? 26  VAL A CG2 1 
ATOM   130  N N   . LEU A 1 19  ? 43.828 16.044 58.819 1.00 42.49  ? 27  LEU A N   1 
ATOM   131  C CA  . LEU A 1 19  ? 43.590 14.789 59.509 1.00 47.06  ? 27  LEU A CA  1 
ATOM   132  C C   . LEU A 1 19  ? 44.786 13.869 59.297 1.00 49.21  ? 27  LEU A C   1 
ATOM   133  O O   . LEU A 1 19  ? 45.262 13.728 58.173 1.00 48.66  ? 27  LEU A O   1 
ATOM   134  C CB  . LEU A 1 19  ? 42.325 14.122 58.984 1.00 48.95  ? 27  LEU A CB  1 
ATOM   135  C CG  . LEU A 1 19  ? 41.036 14.828 59.336 1.00 54.52  ? 27  LEU A CG  1 
ATOM   136  C CD1 . LEU A 1 19  ? 39.869 14.189 58.619 1.00 58.93  ? 27  LEU A CD1 1 
ATOM   137  C CD2 . LEU A 1 19  ? 40.800 14.837 60.838 1.00 53.23  ? 27  LEU A CD2 1 
ATOM   138  N N   . ARG A 1 20  ? 45.239 13.238 60.387 1.00 56.28  ? 28  ARG A N   1 
ATOM   139  C CA  . ARG A 1 20  ? 46.380 12.338 60.350 1.00 66.07  ? 28  ARG A CA  1 
ATOM   140  C C   . ARG A 1 20  ? 46.024 10.988 59.728 1.00 62.47  ? 28  ARG A C   1 
ATOM   141  O O   . ARG A 1 20  ? 46.885 10.344 59.132 1.00 66.19  ? 28  ARG A O   1 
ATOM   142  C CB  . ARG A 1 20  ? 46.945 12.142 61.766 1.00 74.97  ? 28  ARG A CB  1 
ATOM   143  C CG  . ARG A 1 20  ? 47.420 13.440 62.404 1.00 83.81  ? 28  ARG A CG  1 
ATOM   144  C CD  . ARG A 1 20  ? 47.860 13.244 63.839 1.00 94.25  ? 28  ARG A CD  1 
ATOM   145  N NE  . ARG A 1 20  ? 48.075 14.522 64.509 1.00 100.67 ? 28  ARG A NE  1 
ATOM   146  C CZ  . ARG A 1 20  ? 47.277 15.034 65.440 1.00 103.67 ? 28  ARG A CZ  1 
ATOM   147  N NH1 . ARG A 1 20  ? 46.153 14.432 65.796 1.00 107.05 ? 28  ARG A NH1 1 
ATOM   148  N NH2 . ARG A 1 20  ? 47.609 16.183 66.021 1.00 103.83 ? 28  ARG A NH2 1 
ATOM   149  N N   . SER A 1 21  ? 44.753 10.577 59.861 1.00 51.82  ? 29  SER A N   1 
ATOM   150  C CA  . SER A 1 21  ? 44.275 9.333  59.276 1.00 49.64  ? 29  SER A CA  1 
ATOM   151  C C   . SER A 1 21  ? 42.828 9.449  58.799 1.00 43.95  ? 29  SER A C   1 
ATOM   152  O O   . SER A 1 21  ? 42.165 10.444 59.065 1.00 46.32  ? 29  SER A O   1 
ATOM   153  C CB  . SER A 1 21  ? 44.402 8.202  60.290 1.00 51.71  ? 29  SER A CB  1 
ATOM   154  O OG  . SER A 1 21  ? 43.621 8.475  61.440 1.00 55.34  ? 29  SER A OG  1 
ATOM   155  N N   . GLU A 1 22  ? 42.339 8.417  58.104 1.00 39.60  ? 30  GLU A N   1 
ATOM   156  C CA  . GLU A 1 22  ? 40.994 8.462  57.558 1.00 42.49  ? 30  GLU A CA  1 
ATOM   157  C C   . GLU A 1 22  ? 39.960 8.430  58.681 1.00 40.70  ? 30  GLU A C   1 
ATOM   158  O O   . GLU A 1 22  ? 40.205 7.870  59.750 1.00 37.83  ? 30  GLU A O   1 
ATOM   159  C CB  . GLU A 1 22  ? 40.758 7.348  56.531 1.00 43.07  ? 30  GLU A CB  1 
ATOM   160  C CG  . GLU A 1 22  ? 40.879 5.931  57.048 1.00 46.84  ? 30  GLU A CG  1 
ATOM   161  C CD  . GLU A 1 22  ? 40.634 4.886  55.974 1.00 45.64  ? 30  GLU A CD  1 
ATOM   162  O OE1 . GLU A 1 22  ? 41.287 4.961  54.908 1.00 47.22  ? 30  GLU A OE1 1 
ATOM   163  O OE2 . GLU A 1 22  ? 39.804 3.979  56.204 1.00 47.70  ? 30  GLU A OE2 1 
ATOM   164  N N   . SER A 1 23  ? 38.817 9.084  58.438 1.00 39.33  ? 31  SER A N   1 
ATOM   165  C CA  . SER A 1 23  ? 37.726 9.132  59.399 1.00 37.95  ? 31  SER A CA  1 
ATOM   166  C C   . SER A 1 23  ? 36.397 8.856  58.712 1.00 36.94  ? 31  SER A C   1 
ATOM   167  O O   . SER A 1 23  ? 36.322 8.815  57.488 1.00 38.68  ? 31  SER A O   1 
ATOM   168  C CB  . SER A 1 23  ? 37.656 10.485 60.095 1.00 42.92  ? 31  SER A CB  1 
ATOM   169  O OG  . SER A 1 23  ? 38.944 10.958 60.436 1.00 49.01  ? 31  SER A OG  1 
ATOM   170  N N   . ILE A 1 24  ? 35.358 8.662  59.529 1.00 38.36  ? 32  ILE A N   1 
ATOM   171  C CA  . ILE A 1 24  ? 34.018 8.383  59.047 1.00 37.29  ? 32  ILE A CA  1 
ATOM   172  C C   . ILE A 1 24  ? 33.055 9.318  59.770 1.00 34.45  ? 32  ILE A C   1 
ATOM   173  O O   . ILE A 1 24  ? 33.206 9.538  60.966 1.00 37.26  ? 32  ILE A O   1 
ATOM   174  C CB  . ILE A 1 24  ? 33.630 6.910  59.274 1.00 41.35  ? 32  ILE A CB  1 
ATOM   175  C CG1 . ILE A 1 24  ? 34.659 5.956  58.670 1.00 45.52  ? 32  ILE A CG1 1 
ATOM   176  C CG2 . ILE A 1 24  ? 32.228 6.618  58.735 1.00 40.14  ? 32  ILE A CG2 1 
ATOM   177  C CD1 . ILE A 1 24  ? 34.298 4.462  58.821 1.00 45.84  ? 32  ILE A CD1 1 
ATOM   178  N N   . ASP A 1 25  ? 32.091 9.873  59.028 1.00 32.43  ? 33  ASP A N   1 
ATOM   179  C CA  . ASP A 1 25  ? 30.995 10.628 59.612 1.00 34.21  ? 33  ASP A CA  1 
ATOM   180  C C   . ASP A 1 25  ? 29.672 10.013 59.165 1.00 33.94  ? 33  ASP A C   1 
ATOM   181  O O   . ASP A 1 25  ? 29.604 9.374  58.118 1.00 33.26  ? 33  ASP A O   1 
ATOM   182  C CB  . ASP A 1 25  ? 31.068 12.124 59.249 1.00 34.16  ? 33  ASP A CB  1 
ATOM   183  C CG  . ASP A 1 25  ? 31.810 12.996 60.250 1.00 40.89  ? 33  ASP A CG  1 
ATOM   184  O OD1 . ASP A 1 25  ? 31.820 12.645 61.447 1.00 46.97  ? 33  ASP A OD1 1 
ATOM   185  O OD2 . ASP A 1 25  ? 32.410 14.035 59.826 1.00 40.41  ? 33  ASP A OD2 1 
ATOM   186  N N   . LEU A 1 26  ? 28.632 10.249 59.959 1.00 33.96  ? 34  LEU A N   1 
ATOM   187  C CA  . LEU A 1 26  ? 27.264 9.801  59.608 1.00 40.13  ? 34  LEU A CA  1 
ATOM   188  C C   . LEU A 1 26  ? 26.496 11.010 59.061 1.00 41.07  ? 34  LEU A C   1 
ATOM   189  O O   . LEU A 1 26  ? 26.623 12.088 59.646 1.00 49.45  ? 34  LEU A O   1 
ATOM   190  C CB  . LEU A 1 26  ? 26.607 9.251  60.870 1.00 44.39  ? 34  LEU A CB  1 
ATOM   191  C CG  . LEU A 1 26  ? 26.301 7.753  60.897 1.00 49.00  ? 34  LEU A CG  1 
ATOM   192  C CD1 . LEU A 1 26  ? 25.418 7.489  62.100 1.00 49.96  ? 34  LEU A CD1 1 
ATOM   193  C CD2 . LEU A 1 26  ? 25.611 7.311  59.623 1.00 50.89  ? 34  LEU A CD2 1 
ATOM   194  N N   . ILE A 1 27  ? 25.764 10.835 57.970 1.00 38.42  ? 35  ILE A N   1 
ATOM   195  C CA  . ILE A 1 27  ? 25.028 11.962 57.335 1.00 44.76  ? 35  ILE A CA  1 
ATOM   196  C C   . ILE A 1 27  ? 23.558 11.570 57.174 1.00 47.69  ? 35  ILE A C   1 
ATOM   197  O O   . ILE A 1 27  ? 23.293 10.471 56.667 1.00 43.70  ? 35  ILE A O   1 
ATOM   198  C CB  . ILE A 1 27  ? 25.640 12.365 55.981 1.00 45.34  ? 35  ILE A CB  1 
ATOM   199  C CG1 . ILE A 1 27  ? 25.066 13.673 55.462 1.00 47.87  ? 35  ILE A CG1 1 
ATOM   200  C CG2 . ILE A 1 27  ? 25.498 11.235 54.964 1.00 44.02  ? 35  ILE A CG2 1 
ATOM   201  C CD1 . ILE A 1 27  ? 25.421 14.874 56.317 1.00 51.28  ? 35  ILE A CD1 1 
ATOM   202  N N   . THR A 1 28  ? 22.657 12.467 57.569 1.00 52.39  ? 36  THR A N   1 
ATOM   203  C CA  . THR A 1 28  ? 21.207 12.223 57.432 1.00 55.70  ? 36  THR A CA  1 
ATOM   204  C C   . THR A 1 28  ? 20.806 12.405 55.989 1.00 57.71  ? 36  THR A C   1 
ATOM   205  O O   . THR A 1 28  ? 21.118 13.457 55.418 1.00 61.43  ? 36  THR A O   1 
ATOM   206  C CB  . THR A 1 28  ? 20.441 13.157 58.368 1.00 55.55  ? 36  THR A CB  1 
ATOM   207  O OG1 . THR A 1 28  ? 20.927 12.850 59.670 1.00 53.96  ? 36  THR A OG1 1 
ATOM   208  C CG2 . THR A 1 28  ? 18.940 12.953 58.288 1.00 55.00  ? 36  THR A CG2 1 
ATOM   209  N N   . GLN A 1 29  ? 20.160 11.402 55.408 1.00 61.62  ? 37  GLN A N   1 
ATOM   210  C CA  . GLN A 1 29  ? 19.695 11.463 54.033 1.00 67.32  ? 37  GLN A CA  1 
ATOM   211  C C   . GLN A 1 29  ? 18.429 12.306 53.920 1.00 68.21  ? 37  GLN A C   1 
ATOM   212  O O   . GLN A 1 29  ? 17.691 12.462 54.892 1.00 59.92  ? 37  GLN A O   1 
ATOM   213  C CB  . GLN A 1 29  ? 19.423 10.052 53.483 1.00 73.69  ? 37  GLN A CB  1 
ATOM   214  C CG  . GLN A 1 29  ? 20.675 9.200  53.285 1.00 79.58  ? 37  GLN A CG  1 
ATOM   215  C CD  . GLN A 1 29  ? 21.615 9.804  52.268 1.00 84.51  ? 37  GLN A CD  1 
ATOM   216  O OE1 . GLN A 1 29  ? 22.380 10.718 52.575 1.00 89.04  ? 37  GLN A OE1 1 
ATOM   217  N NE2 . GLN A 1 29  ? 21.596 9.299  51.034 1.00 89.76  ? 37  GLN A NE2 1 
ATOM   218  N N   . GLN A 1 30  ? 18.205 12.856 52.720 1.00 73.99  ? 38  GLN A N   1 
ATOM   219  C CA  . GLN A 1 30  ? 16.948 13.504 52.387 1.00 80.26  ? 38  GLN A CA  1 
ATOM   220  C C   . GLN A 1 30  ? 15.839 12.473 52.573 1.00 81.79  ? 38  GLN A C   1 
ATOM   221  O O   . GLN A 1 30  ? 15.972 11.336 52.125 1.00 87.30  ? 38  GLN A O   1 
ATOM   222  C CB  . GLN A 1 30  ? 16.969 14.055 50.941 1.00 82.01  ? 38  GLN A CB  1 
ATOM   223  C CG  . GLN A 1 30  ? 15.619 14.631 50.468 1.00 86.06  ? 38  GLN A CG  1 
ATOM   224  C CD  . GLN A 1 30  ? 14.701 13.622 49.798 1.00 89.18  ? 38  GLN A CD  1 
ATOM   225  O OE1 . GLN A 1 30  ? 15.130 12.578 49.292 1.00 89.49  ? 38  GLN A OE1 1 
ATOM   226  N NE2 . GLN A 1 30  ? 13.407 13.929 49.758 1.00 87.33  ? 38  GLN A NE2 1 
ATOM   227  N N   . ILE A 1 31  ? 14.767 12.872 53.266 1.00 75.49  ? 39  ILE A N   1 
ATOM   228  C CA  . ILE A 1 31  ? 13.612 12.010 53.458 1.00 79.23  ? 39  ILE A CA  1 
ATOM   229  C C   . ILE A 1 31  ? 12.333 12.821 53.247 1.00 74.11  ? 39  ILE A C   1 
ATOM   230  O O   . ILE A 1 31  ? 12.219 13.944 53.740 1.00 63.47  ? 39  ILE A O   1 
ATOM   231  C CB  . ILE A 1 31  ? 13.688 11.305 54.851 1.00 80.28  ? 39  ILE A CB  1 
ATOM   232  C CG1 . ILE A 1 31  ? 14.875 10.312 54.915 1.00 81.14  ? 39  ILE A CG1 1 
ATOM   233  C CG2 . ILE A 1 31  ? 12.391 10.586 55.226 1.00 80.54  ? 39  ILE A CG2 1 
ATOM   234  C CD1 . ILE A 1 31  ? 14.812 9.145  53.857 1.00 81.02  ? 39  ILE A CD1 1 
ATOM   235  N N   . PRO A 1 32  ? 11.343 12.297 52.484 1.00 71.53  ? 40  PRO A N   1 
ATOM   236  C CA  . PRO A 1 32  ? 10.073 12.994 52.318 1.00 66.21  ? 40  PRO A CA  1 
ATOM   237  C C   . PRO A 1 32  ? 9.251  13.004 53.604 1.00 58.39  ? 40  PRO A C   1 
ATOM   238  O O   . PRO A 1 32  ? 9.566  12.279 54.545 1.00 63.93  ? 40  PRO A O   1 
ATOM   239  C CB  . PRO A 1 32  ? 9.397  12.209 51.188 1.00 66.15  ? 40  PRO A CB  1 
ATOM   240  C CG  . PRO A 1 32  ? 9.979  10.826 51.283 1.00 66.66  ? 40  PRO A CG  1 
ATOM   241  C CD  . PRO A 1 32  ? 11.394 11.012 51.762 1.00 70.25  ? 40  PRO A CD  1 
ATOM   242  N N   . PHE A 1 33  ? 8.180  13.790 53.617 1.00 51.82  ? 41  PHE A N   1 
ATOM   243  C CA  . PHE A 1 33  ? 7.241  13.803 54.774 1.00 56.28  ? 41  PHE A CA  1 
ATOM   244  C C   . PHE A 1 33  ? 7.957  14.293 56.035 1.00 56.81  ? 41  PHE A C   1 
ATOM   245  O O   . PHE A 1 33  ? 7.808  13.714 57.123 1.00 55.23  ? 41  PHE A O   1 
ATOM   246  C CB  . PHE A 1 33  ? 6.535  12.446 54.851 1.00 53.85  ? 41  PHE A CB  1 
ATOM   247  C CG  . PHE A 1 33  ? 5.837  12.092 53.548 1.00 52.56  ? 41  PHE A CG  1 
ATOM   248  C CD1 . PHE A 1 33  ? 4.760  12.843 53.097 1.00 51.09  ? 41  PHE A CD1 1 
ATOM   249  C CD2 . PHE A 1 33  ? 6.277  11.033 52.768 1.00 52.56  ? 41  PHE A CD2 1 
ATOM   250  C CE1 . PHE A 1 33  ? 4.132  12.530 51.905 1.00 51.18  ? 41  PHE A CE1 1 
ATOM   251  C CE2 . PHE A 1 33  ? 5.647  10.727 51.576 1.00 54.95  ? 41  PHE A CE2 1 
ATOM   252  C CZ  . PHE A 1 33  ? 4.577  11.474 51.149 1.00 54.20  ? 41  PHE A CZ  1 
ATOM   253  N N   . LYS A 1 34  ? 8.688  15.387 55.886 1.00 58.40  ? 42  LYS A N   1 
ATOM   254  C CA  . LYS A 1 34  ? 9.358  15.994 57.055 1.00 64.28  ? 42  LYS A CA  1 
ATOM   255  C C   . LYS A 1 34  ? 8.318  16.772 57.861 1.00 62.86  ? 42  LYS A C   1 
ATOM   256  O O   . LYS A 1 34  ? 7.320  17.214 57.273 1.00 59.90  ? 42  LYS A O   1 
ATOM   257  C CB  . LYS A 1 34  ? 10.469 16.935 56.582 1.00 68.27  ? 42  LYS A CB  1 
ATOM   258  C CG  . LYS A 1 34  ? 11.798 16.270 56.283 1.00 71.51  ? 42  LYS A CG  1 
ATOM   259  C CD  . LYS A 1 34  ? 12.730 17.142 55.453 1.00 77.03  ? 42  LYS A CD  1 
ATOM   260  C CE  . LYS A 1 34  ? 14.047 16.478 55.211 1.00 79.16  ? 42  LYS A CE  1 
ATOM   261  N NZ  . LYS A 1 34  ? 14.999 17.388 54.570 1.00 80.18  ? 42  LYS A NZ  1 
ATOM   262  N N   . ASN A 1 35  ? 8.536  16.914 59.164 1.00 58.93  ? 43  ASN A N   1 
ATOM   263  C CA  . ASN A 1 35  ? 7.629  17.743 59.990 1.00 56.47  ? 43  ASN A CA  1 
ATOM   264  C C   . ASN A 1 35  ? 8.136  19.184 59.911 1.00 57.74  ? 43  ASN A C   1 
ATOM   265  O O   . ASN A 1 35  ? 9.362  19.378 59.932 1.00 58.77  ? 43  ASN A O   1 
ATOM   266  C CB  . ASN A 1 35  ? 7.510  17.184 61.401 1.00 56.30  ? 43  ASN A CB  1 
ATOM   267  C CG  . ASN A 1 35  ? 6.629  15.961 61.458 1.00 57.34  ? 43  ASN A CG  1 
ATOM   268  O OD1 . ASN A 1 35  ? 6.542  15.209 60.482 1.00 53.80  ? 43  ASN A OD1 1 
ATOM   269  N ND2 . ASN A 1 35  ? 5.974  15.742 62.587 1.00 59.23  ? 43  ASN A ND2 1 
ATOM   270  N N   . ASN A 1 36  ? 7.228  20.145 59.794 1.00 53.62  ? 44  ASN A N   1 
ATOM   271  C CA  . ASN A 1 36  ? 7.658  21.554 59.618 1.00 60.18  ? 44  ASN A CA  1 
ATOM   272  C C   . ASN A 1 36  ? 6.930  22.470 60.606 1.00 57.54  ? 44  ASN A C   1 
ATOM   273  O O   . ASN A 1 36  ? 5.950  22.019 61.225 1.00 50.06  ? 44  ASN A O   1 
ATOM   274  C CB  . ASN A 1 36  ? 7.501  22.021 58.175 1.00 62.91  ? 44  ASN A CB  1 
ATOM   275  C CG  . ASN A 1 36  ? 6.100  21.859 57.645 1.00 69.22  ? 44  ASN A CG  1 
ATOM   276  O OD1 . ASN A 1 36  ? 5.174  22.529 58.112 1.00 74.21  ? 44  ASN A OD1 1 
ATOM   277  N ND2 . ASN A 1 36  ? 5.928  20.992 56.659 1.00 75.06  ? 44  ASN A ND2 1 
ATOM   278  N N   . GLN A 1 37  ? 7.421  23.700 60.747 1.00 52.94  ? 45  GLN A N   1 
ATOM   279  C CA  . GLN A 1 37  ? 6.825  24.699 61.663 1.00 49.33  ? 45  GLN A CA  1 
ATOM   280  C C   . GLN A 1 37  ? 7.208  26.081 61.124 1.00 41.28  ? 45  GLN A C   1 
ATOM   281  O O   . GLN A 1 37  ? 8.282  26.194 60.522 1.00 36.69  ? 45  GLN A O   1 
ATOM   282  C CB  . GLN A 1 37  ? 7.345  24.482 63.083 1.00 55.16  ? 45  GLN A CB  1 
ATOM   283  C CG  . GLN A 1 37  ? 6.582  25.228 64.171 1.00 64.95  ? 45  GLN A CG  1 
ATOM   284  C CD  . GLN A 1 37  ? 7.093  24.914 65.560 1.00 68.34  ? 45  GLN A CD  1 
ATOM   285  O OE1 . GLN A 1 37  ? 7.732  23.883 65.792 1.00 65.47  ? 45  GLN A OE1 1 
ATOM   286  N NE2 . GLN A 1 37  ? 6.814  25.803 66.501 1.00 73.04  ? 45  GLN A NE2 1 
ATOM   287  N N   . THR A 1 38  ? 6.343  27.070 61.312 1.00 33.83  ? 46  THR A N   1 
ATOM   288  C CA  . THR A 1 38  ? 6.630  28.441 60.869 1.00 33.58  ? 46  THR A CA  1 
ATOM   289  C C   . THR A 1 38  ? 7.185  29.233 62.030 1.00 30.70  ? 46  THR A C   1 
ATOM   290  O O   . THR A 1 38  ? 6.752  28.997 63.169 1.00 30.32  ? 46  THR A O   1 
ATOM   291  C CB  . THR A 1 38  ? 5.362  29.075 60.306 1.00 36.00  ? 46  THR A CB  1 
ATOM   292  O OG1 . THR A 1 38  ? 4.341  28.789 61.253 1.00 36.80  ? 46  THR A OG1 1 
ATOM   293  C CG2 . THR A 1 38  ? 5.007  28.517 58.941 1.00 37.39  ? 46  THR A CG2 1 
ATOM   294  N N   . VAL A 1 39  ? 8.121  30.129 61.745 1.00 31.52  ? 47  VAL A N   1 
ATOM   295  C CA  . VAL A 1 39  ? 8.695  31.018 62.792 1.00 29.80  ? 47  VAL A CA  1 
ATOM   296  C C   . VAL A 1 39  ? 8.658  32.455 62.256 1.00 28.48  ? 47  VAL A C   1 
ATOM   297  O O   . VAL A 1 39  ? 9.228  32.707 61.192 1.00 28.89  ? 47  VAL A O   1 
ATOM   298  C CB  . VAL A 1 39  ? 10.103 30.632 63.288 1.00 28.98  ? 47  VAL A CB  1 
ATOM   299  C CG1 . VAL A 1 39  ? 10.643 31.633 64.299 1.00 28.84  ? 47  VAL A CG1 1 
ATOM   300  C CG2 . VAL A 1 39  ? 10.144 29.220 63.859 1.00 29.45  ? 47  VAL A CG2 1 
ATOM   301  N N   . LEU A 1 40  ? 7.982  33.334 62.978 1.00 29.38  ? 48  LEU A N   1 
ATOM   302  C CA  . LEU A 1 40  ? 7.910  34.759 62.602 1.00 31.85  ? 48  LEU A CA  1 
ATOM   303  C C   . LEU A 1 40  ? 9.126  35.475 63.189 1.00 29.96  ? 48  LEU A C   1 
ATOM   304  O O   . LEU A 1 40  ? 9.471  35.194 64.334 1.00 32.32  ? 48  LEU A O   1 
ATOM   305  C CB  . LEU A 1 40  ? 6.602  35.307 63.164 1.00 34.84  ? 48  LEU A CB  1 
ATOM   306  C CG  . LEU A 1 40  ? 6.148  36.683 62.675 1.00 41.52  ? 48  LEU A CG  1 
ATOM   307  C CD1 . LEU A 1 40  ? 6.052  36.736 61.164 1.00 43.43  ? 48  LEU A CD1 1 
ATOM   308  C CD2 . LEU A 1 40  ? 4.803  36.991 63.303 1.00 42.59  ? 48  LEU A CD2 1 
ATOM   309  N N   . PHE A 1 41  ? 9.744  36.357 62.413 1.00 29.66  ? 49  PHE A N   1 
ATOM   310  C CA  . PHE A 1 41  ? 10.843 37.127 62.960 1.00 28.79  ? 49  PHE A CA  1 
ATOM   311  C C   . PHE A 1 41  ? 10.875 38.531 62.376 1.00 30.40  ? 49  PHE A C   1 
ATOM   312  O O   . PHE A 1 41  ? 10.356 38.776 61.291 1.00 29.65  ? 49  PHE A O   1 
ATOM   313  C CB  . PHE A 1 41  ? 12.189 36.419 62.754 1.00 27.54  ? 49  PHE A CB  1 
ATOM   314  C CG  . PHE A 1 41  ? 12.501 36.066 61.319 1.00 27.22  ? 49  PHE A CG  1 
ATOM   315  C CD1 . PHE A 1 41  ? 11.988 34.923 60.746 1.00 28.61  ? 49  PHE A CD1 1 
ATOM   316  C CD2 . PHE A 1 41  ? 13.307 36.881 60.548 1.00 29.71  ? 49  PHE A CD2 1 
ATOM   317  C CE1 . PHE A 1 41  ? 12.280 34.595 59.426 1.00 29.75  ? 49  PHE A CE1 1 
ATOM   318  C CE2 . PHE A 1 41  ? 13.606 36.546 59.231 1.00 30.27  ? 49  PHE A CE2 1 
ATOM   319  C CZ  . PHE A 1 41  ? 13.087 35.406 58.679 1.00 30.48  ? 49  PHE A CZ  1 
ATOM   320  N N   . LYS A 1 42  ? 11.460 39.449 63.143 1.00 30.31  ? 50  LYS A N   1 
ATOM   321  C CA  . LYS A 1 42  ? 11.663 40.805 62.681 1.00 33.09  ? 50  LYS A CA  1 
ATOM   322  C C   . LYS A 1 42  ? 12.827 41.414 63.446 1.00 31.27  ? 50  LYS A C   1 
ATOM   323  O O   . LYS A 1 42  ? 13.141 40.977 64.552 1.00 28.75  ? 50  LYS A O   1 
ATOM   324  C CB  . LYS A 1 42  ? 10.400 41.651 62.872 1.00 37.93  ? 50  LYS A CB  1 
ATOM   325  C CG  . LYS A 1 42  ? 10.122 42.045 64.299 1.00 44.32  ? 50  LYS A CG  1 
ATOM   326  C CD  . LYS A 1 42  ? 8.977  43.017 64.398 1.00 56.75  ? 50  LYS A CD  1 
ATOM   327  C CE  . LYS A 1 42  ? 9.244  44.399 63.839 1.00 57.38  ? 50  LYS A CE  1 
ATOM   328  N NZ  . LYS A 1 42  ? 10.125 45.184 64.739 1.00 61.92  ? 50  LYS A NZ  1 
ATOM   329  N N   . ASP A 1 43  ? 13.424 42.445 62.848 1.00 29.97  ? 51  ASP A N   1 
ATOM   330  C CA  . ASP A 1 43  ? 14.499 43.183 63.480 1.00 31.55  ? 51  ASP A CA  1 
ATOM   331  C C   . ASP A 1 43  ? 13.956 44.446 64.140 1.00 33.31  ? 51  ASP A C   1 
ATOM   332  O O   . ASP A 1 43  ? 12.981 45.028 63.669 1.00 31.66  ? 51  ASP A O   1 
ATOM   333  C CB  . ASP A 1 43  ? 15.571 43.543 62.445 1.00 29.91  ? 51  ASP A CB  1 
ATOM   334  C CG  . ASP A 1 43  ? 16.352 42.350 61.973 1.00 29.96  ? 51  ASP A CG  1 
ATOM   335  O OD1 . ASP A 1 43  ? 16.704 41.496 62.824 1.00 28.30  ? 51  ASP A OD1 1 
ATOM   336  O OD2 . ASP A 1 43  ? 16.648 42.278 60.768 1.00 29.22  ? 51  ASP A OD2 1 
ATOM   337  N N   . SER A 1 44  ? 14.592 44.857 65.238 1.00 35.80  ? 52  SER A N   1 
ATOM   338  C CA  . SER A 1 44  ? 14.377 46.196 65.757 1.00 37.29  ? 52  SER A CA  1 
ATOM   339  C C   . SER A 1 44  ? 15.601 46.704 66.503 1.00 35.92  ? 52  SER A C   1 
ATOM   340  O O   . SER A 1 44  ? 16.434 45.931 66.988 1.00 32.92  ? 52  SER A O   1 
ATOM   341  C CB  . SER A 1 44  ? 13.124 46.271 66.620 1.00 39.40  ? 52  SER A CB  1 
ATOM   342  O OG  . SER A 1 44  ? 13.236 45.434 67.742 1.00 43.27  ? 52  SER A OG  1 
ATOM   343  N N   . ILE A 1 45  ? 15.710 48.033 66.534 1.00 33.11  ? 53  ILE A N   1 
ATOM   344  C CA  . ILE A 1 45  ? 16.832 48.697 67.166 1.00 36.24  ? 53  ILE A CA  1 
ATOM   345  C C   . ILE A 1 45  ? 16.629 48.623 68.675 1.00 32.85  ? 53  ILE A C   1 
ATOM   346  O O   . ILE A 1 45  ? 15.518 48.817 69.156 1.00 37.44  ? 53  ILE A O   1 
ATOM   347  C CB  . ILE A 1 45  ? 16.967 50.138 66.617 1.00 41.80  ? 53  ILE A CB  1 
ATOM   348  C CG1 . ILE A 1 45  ? 18.328 50.742 66.981 1.00 46.06  ? 53  ILE A CG1 1 
ATOM   349  C CG2 . ILE A 1 45  ? 15.804 51.028 67.075 1.00 42.79  ? 53  ILE A CG2 1 
ATOM   350  C CD1 . ILE A 1 45  ? 18.794 51.746 65.996 1.00 53.12  ? 53  ILE A CD1 1 
ATOM   351  N N   . TYR A 1 46  ? 17.691 48.258 69.400 1.00 30.55  ? 54  TYR A N   1 
ATOM   352  C CA  . TYR A 1 46  ? 17.669 48.246 70.853 1.00 30.67  ? 54  TYR A CA  1 
ATOM   353  C C   . TYR A 1 46  ? 18.594 49.300 71.456 1.00 31.10  ? 54  TYR A C   1 
ATOM   354  O O   . TYR A 1 46  ? 18.503 49.584 72.642 1.00 32.35  ? 54  TYR A O   1 
ATOM   355  C CB  . TYR A 1 46  ? 18.009 46.839 71.392 1.00 28.51  ? 54  TYR A CB  1 
ATOM   356  C CG  . TYR A 1 46  ? 19.465 46.413 71.397 1.00 28.07  ? 54  TYR A CG  1 
ATOM   357  C CD1 . TYR A 1 46  ? 20.307 46.753 72.446 1.00 26.29  ? 54  TYR A CD1 1 
ATOM   358  C CD2 . TYR A 1 46  ? 19.983 45.615 70.382 1.00 27.44  ? 54  TYR A CD2 1 
ATOM   359  C CE1 . TYR A 1 46  ? 21.638 46.346 72.470 1.00 27.98  ? 54  TYR A CE1 1 
ATOM   360  C CE2 . TYR A 1 46  ? 21.308 45.183 70.405 1.00 26.30  ? 54  TYR A CE2 1 
ATOM   361  C CZ  . TYR A 1 46  ? 22.133 45.549 71.454 1.00 28.15  ? 54  TYR A CZ  1 
ATOM   362  O OH  . TYR A 1 46  ? 23.445 45.143 71.488 1.00 26.67  ? 54  TYR A OH  1 
ATOM   363  N N   . HIS A 1 47  ? 19.499 49.855 70.644 1.00 32.96  ? 55  HIS A N   1 
ATOM   364  C CA  . HIS A 1 47  ? 20.383 50.912 71.101 1.00 33.66  ? 55  HIS A CA  1 
ATOM   365  C C   . HIS A 1 47  ? 20.608 51.876 69.938 1.00 33.47  ? 55  HIS A C   1 
ATOM   366  O O   . HIS A 1 47  ? 21.357 51.585 69.003 1.00 31.70  ? 55  HIS A O   1 
ATOM   367  C CB  . HIS A 1 47  ? 21.686 50.338 71.655 1.00 34.46  ? 55  HIS A CB  1 
ATOM   368  C CG  . HIS A 1 47  ? 22.524 51.332 72.401 1.00 36.26  ? 55  HIS A CG  1 
ATOM   369  N ND1 . HIS A 1 47  ? 23.318 52.247 71.740 1.00 37.17  ? 55  HIS A ND1 1 
ATOM   370  C CD2 . HIS A 1 47  ? 22.674 51.512 73.730 1.00 36.67  ? 55  HIS A CD2 1 
ATOM   371  C CE1 . HIS A 1 47  ? 23.924 52.952 72.688 1.00 36.50  ? 55  HIS A CE1 1 
ATOM   372  N NE2 . HIS A 1 47  ? 23.558 52.541 73.897 1.00 35.17  ? 55  HIS A NE2 1 
ATOM   373  N N   . LYS A 1 48  ? 19.917 53.017 70.004 1.00 33.95  ? 56  LYS A N   1 
ATOM   374  C CA  . LYS A 1 48  ? 19.899 53.975 68.911 1.00 36.34  ? 56  LYS A CA  1 
ATOM   375  C C   . LYS A 1 48  ? 21.275 54.584 68.642 1.00 33.14  ? 56  LYS A C   1 
ATOM   376  O O   . LYS A 1 48  ? 21.701 54.613 67.494 1.00 35.35  ? 56  LYS A O   1 
ATOM   377  C CB  . LYS A 1 48  ? 18.845 55.049 69.185 1.00 41.92  ? 56  LYS A CB  1 
ATOM   378  C CG  . LYS A 1 48  ? 17.427 54.485 69.206 1.00 49.61  ? 56  LYS A CG  1 
ATOM   379  C CD  . LYS A 1 48  ? 16.363 55.514 69.589 1.00 56.01  ? 56  LYS A CD  1 
ATOM   380  C CE  . LYS A 1 48  ? 14.990 54.895 69.720 1.00 60.47  ? 56  LYS A CE  1 
ATOM   381  N NZ  . LYS A 1 48  ? 14.804 54.245 71.043 1.00 64.93  ? 56  LYS A NZ  1 
ATOM   382  N N   . PRO A 1 49  ? 22.034 55.053 69.664 1.00 35.79  ? 57  PRO A N   1 
ATOM   383  C CA  . PRO A 1 49  ? 23.326 55.689 69.425 1.00 36.17  ? 57  PRO A CA  1 
ATOM   384  C C   . PRO A 1 49  ? 24.330 54.817 68.674 1.00 38.04  ? 57  PRO A C   1 
ATOM   385  O O   . PRO A 1 49  ? 25.024 55.305 67.788 1.00 36.06  ? 57  PRO A O   1 
ATOM   386  C CB  . PRO A 1 49  ? 23.834 56.008 70.836 1.00 36.39  ? 57  PRO A CB  1 
ATOM   387  C CG  . PRO A 1 49  ? 22.613 56.056 71.682 1.00 36.24  ? 57  PRO A CG  1 
ATOM   388  C CD  . PRO A 1 49  ? 21.667 55.045 71.089 1.00 36.28  ? 57  PRO A CD  1 
ATOM   389  N N   . ASN A 1 50  ? 24.417 53.538 69.060 1.00 36.55  ? 58  ASN A N   1 
ATOM   390  C CA  . ASN A 1 50  ? 25.311 52.582 68.421 1.00 36.31  ? 58  ASN A CA  1 
ATOM   391  C C   . ASN A 1 50  ? 24.676 51.850 67.236 1.00 34.65  ? 58  ASN A C   1 
ATOM   392  O O   . ASN A 1 50  ? 25.321 51.024 66.603 1.00 35.65  ? 58  ASN A O   1 
ATOM   393  C CB  . ASN A 1 50  ? 25.810 51.582 69.472 1.00 36.43  ? 58  ASN A CB  1 
ATOM   394  C CG  . ASN A 1 50  ? 26.773 52.194 70.456 1.00 38.63  ? 58  ASN A CG  1 
ATOM   395  O OD1 . ASN A 1 50  ? 27.453 53.157 70.144 1.00 42.54  ? 58  ASN A OD1 1 
ATOM   396  N ND2 . ASN A 1 50  ? 26.892 51.628 71.651 1.00 40.94  ? 58  ASN A ND2 1 
ATOM   397  N N   . ASN A 1 51  ? 23.418 52.173 66.918 1.00 33.21  ? 59  ASN A N   1 
ATOM   398  C CA  . ASN A 1 51  ? 22.722 51.542 65.810 1.00 36.61  ? 59  ASN A CA  1 
ATOM   399  C C   . ASN A 1 51  ? 22.754 50.016 65.931 1.00 36.27  ? 59  ASN A C   1 
ATOM   400  O O   . ASN A 1 51  ? 22.973 49.308 64.952 1.00 37.38  ? 59  ASN A O   1 
ATOM   401  C CB  . ASN A 1 51  ? 23.334 52.009 64.482 1.00 40.36  ? 59  ASN A CB  1 
ATOM   402  C CG  . ASN A 1 51  ? 22.445 51.760 63.293 1.00 43.51  ? 59  ASN A CG  1 
ATOM   403  O OD1 . ASN A 1 51  ? 21.238 52.017 63.322 1.00 47.22  ? 59  ASN A OD1 1 
ATOM   404  N ND2 . ASN A 1 51  ? 23.021 51.247 62.221 1.00 48.25  ? 59  ASN A ND2 1 
ATOM   405  N N   . LEU A 1 52  ? 22.558 49.518 67.155 1.00 33.61  ? 60  LEU A N   1 
ATOM   406  C CA  . LEU A 1 52  ? 22.562 48.089 67.415 1.00 32.97  ? 60  LEU A CA  1 
ATOM   407  C C   . LEU A 1 52  ? 21.141 47.545 67.316 1.00 32.76  ? 60  LEU A C   1 
ATOM   408  O O   . LEU A 1 52  ? 20.219 48.082 67.940 1.00 28.20  ? 60  LEU A O   1 
ATOM   409  C CB  . LEU A 1 52  ? 23.133 47.794 68.793 1.00 32.48  ? 60  LEU A CB  1 
ATOM   410  C CG  . LEU A 1 52  ? 24.621 48.053 68.935 1.00 34.02  ? 60  LEU A CG  1 
ATOM   411  C CD1 . LEU A 1 52  ? 25.062 47.917 70.360 1.00 32.28  ? 60  LEU A CD1 1 
ATOM   412  C CD2 . LEU A 1 52  ? 25.422 47.103 68.054 1.00 37.09  ? 60  LEU A CD2 1 
ATOM   413  N N   . HIS A 1 53  ? 21.006 46.471 66.525 1.00 28.90  ? 61  HIS A N   1 
ATOM   414  C CA  . HIS A 1 53  ? 19.745 45.790 66.298 1.00 27.33  ? 61  HIS A CA  1 
ATOM   415  C C   . HIS A 1 53  ? 19.721 44.397 66.922 1.00 28.39  ? 61  HIS A C   1 
ATOM   416  O O   . HIS A 1 53  ? 20.758 43.767 67.120 1.00 27.31  ? 61  HIS A O   1 
ATOM   417  C CB  . HIS A 1 53  ? 19.470 45.665 64.801 1.00 30.02  ? 61  HIS A CB  1 
ATOM   418  C CG  . HIS A 1 53  ? 19.265 46.970 64.094 1.00 33.02  ? 61  HIS A CG  1 
ATOM   419  N ND1 . HIS A 1 53  ? 20.322 47.810 63.814 1.00 36.20  ? 61  HIS A ND1 1 
ATOM   420  C CD2 . HIS A 1 53  ? 18.131 47.522 63.615 1.00 36.24  ? 61  HIS A CD2 1 
ATOM   421  C CE1 . HIS A 1 53  ? 19.806 48.848 63.179 1.00 38.31  ? 61  HIS A CE1 1 
ATOM   422  N NE2 . HIS A 1 53  ? 18.485 48.717 63.040 1.00 38.65  ? 61  HIS A NE2 1 
ATOM   423  N N   . LEU A 1 54  ? 18.511 43.940 67.243 1.00 26.66  ? 62  LEU A N   1 
ATOM   424  C CA  . LEU A 1 54  ? 18.283 42.565 67.632 1.00 26.88  ? 62  LEU A CA  1 
ATOM   425  C C   . LEU A 1 54  ? 17.148 42.018 66.772 1.00 27.93  ? 62  LEU A C   1 
ATOM   426  O O   . LEU A 1 54  ? 16.358 42.781 66.208 1.00 27.19  ? 62  LEU A O   1 
ATOM   427  C CB  . LEU A 1 54  ? 17.993 42.438 69.140 1.00 28.89  ? 62  LEU A CB  1 
ATOM   428  C CG  . LEU A 1 54  ? 16.872 43.285 69.746 1.00 28.88  ? 62  LEU A CG  1 
ATOM   429  C CD1 . LEU A 1 54  ? 15.491 42.716 69.457 1.00 29.38  ? 62  LEU A CD1 1 
ATOM   430  C CD2 . LEU A 1 54  ? 17.043 43.395 71.249 1.00 30.17  ? 62  LEU A CD2 1 
ATOM   431  N N   . ARG A 1 55  ? 17.115 40.689 66.652 1.00 26.53  ? 63  ARG A N   1 
ATOM   432  C CA  . ARG A 1 55  ? 16.058 39.997 65.940 1.00 27.10  ? 63  ARG A CA  1 
ATOM   433  C C   . ARG A 1 55  ? 15.200 39.250 66.954 1.00 26.20  ? 63  ARG A C   1 
ATOM   434  O O   . ARG A 1 55  ? 15.713 38.578 67.853 1.00 25.62  ? 63  ARG A O   1 
ATOM   435  C CB  . ARG A 1 55  ? 16.655 39.042 64.886 1.00 28.45  ? 63  ARG A CB  1 
ATOM   436  C CG  . ARG A 1 55  ? 15.617 38.372 63.993 1.00 28.02  ? 63  ARG A CG  1 
ATOM   437  C CD  . ARG A 1 55  ? 16.269 37.773 62.769 1.00 28.90  ? 63  ARG A CD  1 
ATOM   438  N NE  . ARG A 1 55  ? 16.673 38.818 61.842 1.00 27.90  ? 63  ARG A NE  1 
ATOM   439  C CZ  . ARG A 1 55  ? 17.278 38.619 60.682 1.00 30.51  ? 63  ARG A CZ  1 
ATOM   440  N NH1 . ARG A 1 55  ? 17.607 37.404 60.266 1.00 29.08  ? 63  ARG A NH1 1 
ATOM   441  N NH2 . ARG A 1 55  ? 17.564 39.669 59.918 1.00 29.50  ? 63  ARG A NH2 1 
ATOM   442  N N   . LEU A 1 56  ? 13.884 39.423 66.812 1.00 25.41  ? 64  LEU A N   1 
ATOM   443  C CA  . LEU A 1 56  ? 12.899 38.710 67.600 1.00 25.10  ? 64  LEU A CA  1 
ATOM   444  C C   . LEU A 1 56  ? 12.324 37.547 66.792 1.00 24.58  ? 64  LEU A C   1 
ATOM   445  O O   . LEU A 1 56  ? 11.957 37.719 65.633 1.00 26.22  ? 64  LEU A O   1 
ATOM   446  C CB  . LEU A 1 56  ? 11.781 39.690 67.970 1.00 28.26  ? 64  LEU A CB  1 
ATOM   447  C CG  . LEU A 1 56  ? 12.212 40.907 68.788 1.00 28.50  ? 64  LEU A CG  1 
ATOM   448  C CD1 . LEU A 1 56  ? 11.104 41.919 68.869 1.00 32.14  ? 64  LEU A CD1 1 
ATOM   449  C CD2 . LEU A 1 56  ? 12.636 40.506 70.166 1.00 29.03  ? 64  LEU A CD2 1 
ATOM   450  N N   . TYR A 1 57  ? 12.211 36.385 67.434 1.00 25.42  ? 65  TYR A N   1 
ATOM   451  C CA  . TYR A 1 57  ? 11.642 35.198 66.820 1.00 26.75  ? 65  TYR A CA  1 
ATOM   452  C C   . TYR A 1 57  ? 10.476 34.687 67.654 1.00 27.16  ? 65  TYR A C   1 
ATOM   453  O O   . TYR A 1 57  ? 10.584 34.584 68.867 1.00 26.71  ? 65  TYR A O   1 
ATOM   454  C CB  . TYR A 1 57  ? 12.634 34.048 66.732 1.00 26.60  ? 65  TYR A CB  1 
ATOM   455  C CG  . TYR A 1 57  ? 13.869 34.306 65.918 1.00 25.14  ? 65  TYR A CG  1 
ATOM   456  C CD1 . TYR A 1 57  ? 14.904 35.084 66.416 1.00 28.11  ? 65  TYR A CD1 1 
ATOM   457  C CD2 . TYR A 1 57  ? 14.023 33.748 64.659 1.00 25.13  ? 65  TYR A CD2 1 
ATOM   458  C CE1 . TYR A 1 57  ? 16.066 35.302 65.677 1.00 25.38  ? 65  TYR A CE1 1 
ATOM   459  C CE2 . TYR A 1 57  ? 15.168 33.965 63.910 1.00 25.98  ? 65  TYR A CE2 1 
ATOM   460  C CZ  . TYR A 1 57  ? 16.196 34.737 64.428 1.00 25.64  ? 65  TYR A CZ  1 
ATOM   461  O OH  . TYR A 1 57  ? 17.342 34.939 63.694 1.00 26.48  ? 65  TYR A OH  1 
ATOM   462  N N   . LYS A 1 58  ? 9.392  34.321 66.969 1.00 28.71  ? 66  LYS A N   1 
ATOM   463  C CA  . LYS A 1 58  ? 8.225  33.747 67.605 1.00 31.48  ? 66  LYS A CA  1 
ATOM   464  C C   . LYS A 1 58  ? 7.800  32.513 66.818 1.00 29.30  ? 66  LYS A C   1 
ATOM   465  O O   . LYS A 1 58  ? 7.486  32.618 65.634 1.00 27.67  ? 66  LYS A O   1 
ATOM   466  C CB  . LYS A 1 58  ? 7.098  34.806 67.635 1.00 33.61  ? 66  LYS A CB  1 
ATOM   467  C CG  . LYS A 1 58  ? 5.799  34.299 68.127 1.00 37.58  ? 66  LYS A CG  1 
ATOM   468  C CD  . LYS A 1 58  ? 4.796  35.390 68.469 1.00 38.43  ? 66  LYS A CD  1 
ATOM   469  C CE  . LYS A 1 58  ? 4.185  36.065 67.278 1.00 40.43  ? 66  LYS A CE  1 
ATOM   470  N NZ  . LYS A 1 58  ? 2.966  36.833 67.678 1.00 41.12  ? 66  LYS A NZ  1 
ATOM   471  N N   . PRO A 1 59  ? 7.740  31.314 67.438 1.00 34.03  ? 67  PRO A N   1 
ATOM   472  C CA  . PRO A 1 59  ? 7.087  30.180 66.797 1.00 38.52  ? 67  PRO A CA  1 
ATOM   473  C C   . PRO A 1 59  ? 5.584  30.403 66.738 1.00 38.98  ? 67  PRO A C   1 
ATOM   474  O O   . PRO A 1 59  ? 5.000  30.756 67.754 1.00 39.40  ? 67  PRO A O   1 
ATOM   475  C CB  . PRO A 1 59  ? 7.445  29.018 67.710 1.00 39.79  ? 67  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 59  ? 7.643  29.660 69.066 1.00 38.09  ? 67  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 59  ? 8.197  31.017 68.804 1.00 36.14  ? 67  PRO A CD  1 
ATOM   478  N N   . ILE A 1 60  ? 4.973  30.251 65.560 1.00 43.82  ? 68  ILE A N   1 
ATOM   479  C CA  . ILE A 1 60  ? 3.603  30.711 65.377 1.00 51.74  ? 68  ILE A CA  1 
ATOM   480  C C   . ILE A 1 60  ? 2.563  29.862 66.111 1.00 61.23  ? 68  ILE A C   1 
ATOM   481  O O   . ILE A 1 60  ? 1.773  30.398 66.890 1.00 64.34  ? 68  ILE A O   1 
ATOM   482  C CB  . ILE A 1 60  ? 3.273  30.855 63.885 1.00 51.46  ? 68  ILE A CB  1 
ATOM   483  C CG1 . ILE A 1 60  ? 4.093  31.998 63.286 1.00 50.04  ? 68  ILE A CG1 1 
ATOM   484  C CG2 . ILE A 1 60  ? 1.774  31.063 63.664 1.00 53.48  ? 68  ILE A CG2 1 
ATOM   485  C CD1 . ILE A 1 60  ? 3.843  32.282 61.810 1.00 51.67  ? 68  ILE A CD1 1 
ATOM   486  N N   . SER A 1 61  ? 2.550  28.548 65.860 1.00 65.88  ? 69  SER A N   1 
ATOM   487  C CA  . SER A 1 61  ? 1.522  27.689 66.431 1.00 74.19  ? 69  SER A CA  1 
ATOM   488  C C   . SER A 1 61  ? 1.616  27.597 67.956 1.00 79.06  ? 69  SER A C   1 
ATOM   489  O O   . SER A 1 61  ? 0.595  27.454 68.627 1.00 81.65  ? 69  SER A O   1 
ATOM   490  C CB  . SER A 1 61  ? 1.564  26.296 65.805 1.00 72.36  ? 69  SER A CB  1 
ATOM   491  O OG  . SER A 1 61  ? 2.830  25.684 65.977 1.00 73.78  ? 69  SER A OG  1 
ATOM   492  N N   . ALA A 1 62  ? 2.841  27.695 68.494 1.00 81.98  ? 70  ALA A N   1 
ATOM   493  C CA  . ALA A 1 62  ? 3.080  27.575 69.927 1.00 83.48  ? 70  ALA A CA  1 
ATOM   494  C C   . ALA A 1 62  ? 2.631  28.798 70.728 1.00 86.58  ? 70  ALA A C   1 
ATOM   495  O O   . ALA A 1 62  ? 2.234  28.658 71.884 1.00 87.68  ? 70  ALA A O   1 
ATOM   496  C CB  . ALA A 1 62  ? 4.557  27.295 70.189 1.00 77.75  ? 70  ALA A CB  1 
ATOM   497  N N   . SER A 1 63  ? 2.698  29.987 70.109 1.00 87.46  ? 71  SER A N   1 
ATOM   498  C CA  . SER A 1 63  ? 2.317  31.236 70.758 1.00 90.22  ? 71  SER A CA  1 
ATOM   499  C C   . SER A 1 63  ? 0.805  31.415 70.904 1.00 93.53  ? 71  SER A C   1 
ATOM   500  O O   . SER A 1 63  ? 0.357  32.222 71.718 1.00 89.87  ? 71  SER A O   1 
ATOM   501  C CB  . SER A 1 63  ? 2.911  32.429 70.006 1.00 86.84  ? 71  SER A CB  1 
ATOM   502  O OG  . SER A 1 63  ? 2.300  32.650 68.747 1.00 86.98  ? 71  SER A OG  1 
ATOM   503  N N   . ASN A 1 64  ? 0.032  30.667 70.102 1.00 100.26 ? 72  ASN A N   1 
ATOM   504  C CA  . ASN A 1 64  ? -1.415 30.583 70.247 1.00 101.39 ? 72  ASN A CA  1 
ATOM   505  C C   . ASN A 1 64  ? -1.845 29.864 71.525 1.00 97.82  ? 72  ASN A C   1 
ATOM   506  O O   . ASN A 1 64  ? -2.931 30.121 72.039 1.00 98.76  ? 72  ASN A O   1 
ATOM   507  C CB  . ASN A 1 64  ? -2.045 29.844 69.045 1.00 101.19 ? 72  ASN A CB  1 
ATOM   508  C CG  . ASN A 1 64  ? -1.996 30.597 67.738 1.00 99.08  ? 72  ASN A CG  1 
ATOM   509  O OD1 . ASN A 1 64  ? -1.722 31.799 67.687 1.00 95.78  ? 72  ASN A OD1 1 
ATOM   510  N ND2 . ASN A 1 64  ? -2.282 29.900 66.643 1.00 102.26 ? 72  ASN A ND2 1 
ATOM   511  N N   . ARG A 1 65  ? -1.022 28.912 71.956 1.00 98.18  ? 73  ARG A N   1 
ATOM   512  C CA  . ARG A 1 65  ? -1.413 28.068 73.109 1.00 98.46  ? 73  ARG A CA  1 
ATOM   513  C C   . ARG A 1 65  ? -1.127 28.763 74.441 1.00 91.39  ? 73  ARG A C   1 
ATOM   514  O O   . ARG A 1 65  ? -2.037 28.779 75.294 1.00 91.82  ? 73  ARG A O   1 
ATOM   515  C CB  . ARG A 1 65  ? -0.654 26.740 73.040 1.00 100.15 ? 73  ARG A CB  1 
ATOM   516  C CG  . ARG A 1 65  ? -0.982 25.847 71.853 1.00 102.07 ? 73  ARG A CG  1 
ATOM   517  C CD  . ARG A 1 65  ? -0.091 24.612 71.852 1.00 102.70 ? 73  ARG A CD  1 
ATOM   518  N NE  . ARG A 1 65  ? -0.308 23.746 73.016 1.00 103.19 ? 73  ARG A NE  1 
ATOM   519  C CZ  . ARG A 1 65  ? 0.417  22.674 73.308 1.00 99.61  ? 73  ARG A CZ  1 
ATOM   520  N NH1 . ARG A 1 65  ? 1.579  22.806 73.921 1.00 95.55  ? 73  ARG A NH1 1 
ATOM   521  N NH2 . ARG A 1 65  ? -0.024 21.472 72.986 1.00 96.05  ? 73  ARG A NH2 1 
ATOM   522  N N   . THR A 1 66  ? 0.078  29.302 74.623 1.00 82.14  ? 74  THR A N   1 
ATOM   523  C CA  . THR A 1 66  ? 0.399  29.849 75.956 1.00 74.76  ? 74  THR A CA  1 
ATOM   524  C C   . THR A 1 66  ? 1.333  31.030 75.886 1.00 62.58  ? 74  THR A C   1 
ATOM   525  O O   . THR A 1 66  ? 1.647  31.486 74.769 1.00 60.95  ? 74  THR A O   1 
ATOM   526  C CB  . THR A 1 66  ? 1.021  28.743 76.806 1.00 76.02  ? 74  THR A CB  1 
ATOM   527  O OG1 . THR A 1 66  ? 2.190  28.291 76.128 1.00 76.11  ? 74  THR A OG1 1 
ATOM   528  C CG2 . THR A 1 66  ? 0.069  27.583 77.037 1.00 78.79  ? 74  THR A CG2 1 
ATOM   529  N N   . ALA A 1 67  ? 1.740  31.518 77.056 1.00 53.43  ? 75  ALA A N   1 
ATOM   530  C CA  . ALA A 1 67  ? 2.722  32.612 77.126 1.00 47.66  ? 75  ALA A CA  1 
ATOM   531  C C   . ALA A 1 67  ? 4.099  32.005 76.910 1.00 42.13  ? 75  ALA A C   1 
ATOM   532  O O   . ALA A 1 67  ? 4.431  31.003 77.555 1.00 44.83  ? 75  ALA A O   1 
ATOM   533  C CB  . ALA A 1 67  ? 2.626  33.310 78.447 1.00 45.65  ? 75  ALA A CB  1 
ATOM   534  N N   . LEU A 1 68  ? 4.876  32.614 76.031 1.00 40.45  ? 76  LEU A N   1 
ATOM   535  C CA  . LEU A 1 68  ? 6.171  32.062 75.674 1.00 37.53  ? 76  LEU A CA  1 
ATOM   536  C C   . LEU A 1 68  ? 7.244  32.432 76.693 1.00 37.39  ? 76  LEU A C   1 
ATOM   537  O O   . LEU A 1 68  ? 7.317  33.582 77.130 1.00 34.16  ? 76  LEU A O   1 
ATOM   538  C CB  . LEU A 1 68  ? 6.572  32.604 74.305 1.00 37.44  ? 76  LEU A CB  1 
ATOM   539  C CG  . LEU A 1 68  ? 5.664  32.221 73.152 1.00 39.18  ? 76  LEU A CG  1 
ATOM   540  C CD1 . LEU A 1 68  ? 6.102  32.897 71.882 1.00 41.84  ? 76  LEU A CD1 1 
ATOM   541  C CD2 . LEU A 1 68  ? 5.629  30.720 72.960 1.00 39.34  ? 76  LEU A CD2 1 
ATOM   542  N N   . PRO A 1 69  ? 8.140  31.494 77.077 1.00 34.09  ? 77  PRO A N   1 
ATOM   543  C CA  . PRO A 1 69  ? 9.372  31.883 77.744 1.00 32.83  ? 77  PRO A CA  1 
ATOM   544  C C   . PRO A 1 69  ? 10.272 32.620 76.764 1.00 29.27  ? 77  PRO A C   1 
ATOM   545  O O   . PRO A 1 69  ? 10.044 32.558 75.561 1.00 27.04  ? 77  PRO A O   1 
ATOM   546  C CB  . PRO A 1 69  ? 9.968  30.553 78.205 1.00 32.12  ? 77  PRO A CB  1 
ATOM   547  C CG  . PRO A 1 69  ? 9.439  29.566 77.209 1.00 33.97  ? 77  PRO A CG  1 
ATOM   548  C CD  . PRO A 1 69  ? 8.064  30.048 76.813 1.00 33.74  ? 77  PRO A CD  1 
ATOM   549  N N   . VAL A 1 70  ? 11.273 33.319 77.295 1.00 28.93  ? 78  VAL A N   1 
ATOM   550  C CA  . VAL A 1 70  ? 12.171 34.110 76.480 1.00 27.73  ? 78  VAL A CA  1 
ATOM   551  C C   . VAL A 1 70  ? 13.549 33.463 76.517 1.00 27.87  ? 78  VAL A C   1 
ATOM   552  O O   . VAL A 1 70  ? 14.049 33.132 77.586 1.00 28.89  ? 78  VAL A O   1 
ATOM   553  C CB  . VAL A 1 70  ? 12.250 35.567 76.961 1.00 29.64  ? 78  VAL A CB  1 
ATOM   554  C CG1 . VAL A 1 70  ? 13.173 36.379 76.065 1.00 29.75  ? 78  VAL A CG1 1 
ATOM   555  C CG2 . VAL A 1 70  ? 10.861 36.202 77.047 1.00 31.18  ? 78  VAL A CG2 1 
ATOM   556  N N   . VAL A 1 71  ? 14.144 33.307 75.334 1.00 26.99  ? 79  VAL A N   1 
ATOM   557  C CA  . VAL A 1 71  ? 15.527 32.888 75.207 1.00 27.43  ? 79  VAL A CA  1 
ATOM   558  C C   . VAL A 1 71  ? 16.294 34.039 74.566 1.00 24.83  ? 79  VAL A C   1 
ATOM   559  O O   . VAL A 1 71  ? 16.017 34.424 73.438 1.00 26.59  ? 79  VAL A O   1 
ATOM   560  C CB  . VAL A 1 71  ? 15.654 31.583 74.405 1.00 27.08  ? 79  VAL A CB  1 
ATOM   561  C CG1 . VAL A 1 71  ? 17.108 31.286 74.037 1.00 29.97  ? 79  VAL A CG1 1 
ATOM   562  C CG2 . VAL A 1 71  ? 15.053 30.429 75.175 1.00 29.34  ? 79  VAL A CG2 1 
ATOM   563  N N   . VAL A 1 72  ? 17.249 34.592 75.312 1.00 25.12  ? 80  VAL A N   1 
ATOM   564  C CA  . VAL A 1 72  ? 18.176 35.570 74.768 1.00 25.08  ? 80  VAL A CA  1 
ATOM   565  C C   . VAL A 1 72  ? 19.421 34.820 74.309 1.00 25.94  ? 80  VAL A C   1 
ATOM   566  O O   . VAL A 1 72  ? 20.144 34.252 75.128 1.00 26.86  ? 80  VAL A O   1 
ATOM   567  C CB  . VAL A 1 72  ? 18.525 36.664 75.776 1.00 25.06  ? 80  VAL A CB  1 
ATOM   568  C CG1 . VAL A 1 72  ? 19.346 37.765 75.110 1.00 24.93  ? 80  VAL A CG1 1 
ATOM   569  C CG2 . VAL A 1 72  ? 17.260 37.223 76.429 1.00 26.83  ? 80  VAL A CG2 1 
ATOM   570  N N   . PHE A 1 73  ? 19.631 34.805 72.991 1.00 25.23  ? 81  PHE A N   1 
ATOM   571  C CA  . PHE A 1 73  ? 20.755 34.110 72.387 1.00 25.86  ? 81  PHE A CA  1 
ATOM   572  C C   . PHE A 1 73  ? 21.856 35.086 71.984 1.00 25.44  ? 81  PHE A C   1 
ATOM   573  O O   . PHE A 1 73  ? 21.606 35.984 71.182 1.00 24.69  ? 81  PHE A O   1 
ATOM   574  C CB  . PHE A 1 73  ? 20.303 33.347 71.139 1.00 25.35  ? 81  PHE A CB  1 
ATOM   575  C CG  . PHE A 1 73  ? 21.450 32.716 70.389 1.00 26.21  ? 81  PHE A CG  1 
ATOM   576  C CD1 . PHE A 1 73  ? 22.098 31.597 70.893 1.00 29.33  ? 81  PHE A CD1 1 
ATOM   577  C CD2 . PHE A 1 73  ? 21.902 33.258 69.206 1.00 25.32  ? 81  PHE A CD2 1 
ATOM   578  C CE1 . PHE A 1 73  ? 23.161 31.024 70.208 1.00 28.16  ? 81  PHE A CE1 1 
ATOM   579  C CE2 . PHE A 1 73  ? 22.971 32.689 68.525 1.00 28.12  ? 81  PHE A CE2 1 
ATOM   580  C CZ  . PHE A 1 73  ? 23.592 31.574 69.029 1.00 27.62  ? 81  PHE A CZ  1 
ATOM   581  N N   . PHE A 1 74  ? 23.063 34.871 72.523 1.00 24.40  ? 82  PHE A N   1 
ATOM   582  C CA  . PHE A 1 74  ? 24.254 35.616 72.139 1.00 25.42  ? 82  PHE A CA  1 
ATOM   583  C C   . PHE A 1 74  ? 25.147 34.770 71.240 1.00 23.69  ? 82  PHE A C   1 
ATOM   584  O O   . PHE A 1 74  ? 25.658 33.739 71.667 1.00 23.45  ? 82  PHE A O   1 
ATOM   585  C CB  . PHE A 1 74  ? 25.040 36.062 73.390 1.00 25.96  ? 82  PHE A CB  1 
ATOM   586  C CG  . PHE A 1 74  ? 24.326 37.151 74.149 1.00 25.68  ? 82  PHE A CG  1 
ATOM   587  C CD1 . PHE A 1 74  ? 24.370 38.460 73.713 1.00 26.17  ? 82  PHE A CD1 1 
ATOM   588  C CD2 . PHE A 1 74  ? 23.560 36.853 75.261 1.00 27.03  ? 82  PHE A CD2 1 
ATOM   589  C CE1 . PHE A 1 74  ? 23.681 39.459 74.394 1.00 27.05  ? 82  PHE A CE1 1 
ATOM   590  C CE2 . PHE A 1 74  ? 22.873 37.850 75.941 1.00 29.26  ? 82  PHE A CE2 1 
ATOM   591  C CZ  . PHE A 1 74  ? 22.939 39.151 75.506 1.00 27.10  ? 82  PHE A CZ  1 
ATOM   592  N N   . HIS A 1 75  ? 25.312 35.219 69.994 1.00 25.30  ? 83  HIS A N   1 
ATOM   593  C CA  . HIS A 1 75  ? 26.105 34.512 69.004 1.00 27.36  ? 83  HIS A CA  1 
ATOM   594  C C   . HIS A 1 75  ? 27.599 34.507 69.334 1.00 28.35  ? 83  HIS A C   1 
ATOM   595  O O   . HIS A 1 75  ? 28.080 35.330 70.113 1.00 26.53  ? 83  HIS A O   1 
ATOM   596  C CB  . HIS A 1 75  ? 25.855 35.112 67.610 1.00 26.66  ? 83  HIS A CB  1 
ATOM   597  C CG  . HIS A 1 75  ? 26.399 36.492 67.369 1.00 28.92  ? 83  HIS A CG  1 
ATOM   598  N ND1 . HIS A 1 75  ? 27.763 36.728 67.250 1.00 28.77  ? 83  HIS A ND1 1 
ATOM   599  C CD2 . HIS A 1 75  ? 25.744 37.657 67.166 1.00 28.45  ? 83  HIS A CD2 1 
ATOM   600  C CE1 . HIS A 1 75  ? 27.896 38.026 67.010 1.00 29.39  ? 83  HIS A CE1 1 
ATOM   601  N NE2 . HIS A 1 75  ? 26.701 38.627 66.947 1.00 28.36  ? 83  HIS A NE2 1 
ATOM   602  N N   . GLY A 1 76  ? 28.319 33.564 68.720 1.00 29.19  ? 84  GLY A N   1 
ATOM   603  C CA  . GLY A 1 76  ? 29.758 33.440 68.876 1.00 30.22  ? 84  GLY A CA  1 
ATOM   604  C C   . GLY A 1 76  ? 30.517 34.286 67.859 1.00 30.57  ? 84  GLY A C   1 
ATOM   605  O O   . GLY A 1 76  ? 29.947 35.197 67.266 1.00 30.73  ? 84  GLY A O   1 
ATOM   606  N N   . GLY A 1 77  ? 31.799 33.959 67.657 1.00 28.50  ? 85  GLY A N   1 
ATOM   607  C CA  . GLY A 1 77  ? 32.650 34.680 66.727 1.00 27.27  ? 85  GLY A CA  1 
ATOM   608  C C   . GLY A 1 77  ? 33.873 35.341 67.361 1.00 28.60  ? 85  GLY A C   1 
ATOM   609  O O   . GLY A 1 77  ? 34.475 36.227 66.756 1.00 31.34  ? 85  GLY A O   1 
ATOM   610  N N   . GLY A 1 78  ? 34.233 34.893 68.569 1.00 29.06  ? 86  GLY A N   1 
ATOM   611  C CA  . GLY A 1 78  ? 35.462 35.298 69.230 1.00 31.38  ? 86  GLY A CA  1 
ATOM   612  C C   . GLY A 1 78  ? 35.543 36.784 69.581 1.00 33.08  ? 86  GLY A C   1 
ATOM   613  O O   . GLY A 1 78  ? 36.642 37.304 69.737 1.00 33.35  ? 86  GLY A O   1 
ATOM   614  N N   . PHE A 1 79  ? 34.374 37.439 69.708 1.00 31.32  ? 87  PHE A N   1 
ATOM   615  C CA  . PHE A 1 79  ? 34.252 38.878 69.922 1.00 31.40  ? 87  PHE A CA  1 
ATOM   616  C C   . PHE A 1 79  ? 34.657 39.720 68.710 1.00 33.36  ? 87  PHE A C   1 
ATOM   617  O O   . PHE A 1 79  ? 34.620 40.950 68.775 1.00 32.14  ? 87  PHE A O   1 
ATOM   618  C CB  . PHE A 1 79  ? 35.041 39.340 71.173 1.00 30.38  ? 87  PHE A CB  1 
ATOM   619  C CG  . PHE A 1 79  ? 34.468 38.807 72.464 1.00 30.73  ? 87  PHE A CG  1 
ATOM   620  C CD1 . PHE A 1 79  ? 33.197 39.169 72.878 1.00 30.93  ? 87  PHE A CD1 1 
ATOM   621  C CD2 . PHE A 1 79  ? 35.188 37.928 73.249 1.00 30.78  ? 87  PHE A CD2 1 
ATOM   622  C CE1 . PHE A 1 79  ? 32.664 38.667 74.060 1.00 30.36  ? 87  PHE A CE1 1 
ATOM   623  C CE2 . PHE A 1 79  ? 34.653 37.426 74.431 1.00 32.22  ? 87  PHE A CE2 1 
ATOM   624  C CZ  . PHE A 1 79  ? 33.394 37.798 74.829 1.00 30.55  ? 87  PHE A CZ  1 
ATOM   625  N N   . CYS A 1 80  ? 34.990 39.053 67.595 1.00 30.23  ? 88  CYS A N   1 
ATOM   626  C CA  . CYS A 1 80  ? 35.489 39.719 66.403 1.00 31.22  ? 88  CYS A CA  1 
ATOM   627  C C   . CYS A 1 80  ? 34.591 39.536 65.187 1.00 32.58  ? 88  CYS A C   1 
ATOM   628  O O   . CYS A 1 80  ? 34.653 40.343 64.267 1.00 34.63  ? 88  CYS A O   1 
ATOM   629  C CB  . CYS A 1 80  ? 36.906 39.247 66.088 1.00 33.85  ? 88  CYS A CB  1 
ATOM   630  S SG  . CYS A 1 80  ? 38.107 39.627 67.381 1.00 35.61  ? 88  CYS A SG  1 
ATOM   631  N N   . PHE A 1 81  ? 33.795 38.458 65.184 1.00 30.56  ? 89  PHE A N   1 
ATOM   632  C CA  . PHE A 1 81  ? 32.953 38.101 64.056 1.00 30.11  ? 89  PHE A CA  1 
ATOM   633  C C   . PHE A 1 81  ? 31.499 37.911 64.476 1.00 29.73  ? 89  PHE A C   1 
ATOM   634  O O   . PHE A 1 81  ? 31.211 37.600 65.631 1.00 29.97  ? 89  PHE A O   1 
ATOM   635  C CB  . PHE A 1 81  ? 33.464 36.789 63.411 1.00 31.78  ? 89  PHE A CB  1 
ATOM   636  C CG  . PHE A 1 81  ? 34.803 36.920 62.737 1.00 34.37  ? 89  PHE A CG  1 
ATOM   637  C CD1 . PHE A 1 81  ? 34.911 37.484 61.474 1.00 39.17  ? 89  PHE A CD1 1 
ATOM   638  C CD2 . PHE A 1 81  ? 35.961 36.519 63.377 1.00 35.31  ? 89  PHE A CD2 1 
ATOM   639  C CE1 . PHE A 1 81  ? 36.152 37.616 60.855 1.00 37.18  ? 89  PHE A CE1 1 
ATOM   640  C CE2 . PHE A 1 81  ? 37.202 36.657 62.754 1.00 38.12  ? 89  PHE A CE2 1 
ATOM   641  C CZ  . PHE A 1 81  ? 37.288 37.202 61.499 1.00 36.32  ? 89  PHE A CZ  1 
ATOM   642  N N   . GLY A 1 82  ? 30.593 38.085 63.510 1.00 29.27  ? 90  GLY A N   1 
ATOM   643  C CA  . GLY A 1 82  ? 29.234 37.588 63.630 1.00 28.84  ? 90  GLY A CA  1 
ATOM   644  C C   . GLY A 1 82  ? 28.172 38.671 63.504 1.00 31.79  ? 90  GLY A C   1 
ATOM   645  O O   . GLY A 1 82  ? 28.438 39.856 63.701 1.00 32.10  ? 90  GLY A O   1 
ATOM   646  N N   . SER A 1 83  ? 26.965 38.224 63.162 1.00 32.61  ? 91  SER A N   1 
ATOM   647  C CA  . SER A 1 83  ? 25.790 39.076 63.112 1.00 34.27  ? 91  SER A CA  1 
ATOM   648  C C   . SER A 1 83  ? 24.571 38.186 63.310 1.00 34.63  ? 91  SER A C   1 
ATOM   649  O O   . SER A 1 83  ? 24.585 37.024 62.901 1.00 33.21  ? 91  SER A O   1 
ATOM   650  C CB  . SER A 1 83  ? 25.699 39.809 61.783 1.00 34.78  ? 91  SER A CB  1 
ATOM   651  O OG  . SER A 1 83  ? 24.503 40.564 61.712 1.00 35.40  ? 91  SER A OG  1 
ATOM   652  N N   . ARG A 1 84  ? 23.518 38.747 63.913 1.00 34.38  ? 92  ARG A N   1 
ATOM   653  C CA  . ARG A 1 84  ? 22.280 38.016 64.114 1.00 32.53  ? 92  ARG A CA  1 
ATOM   654  C C   . ARG A 1 84  ? 21.673 37.603 62.773 1.00 29.96  ? 92  ARG A C   1 
ATOM   655  O O   . ARG A 1 84  ? 20.912 36.647 62.723 1.00 31.46  ? 92  ARG A O   1 
ATOM   656  C CB  . ARG A 1 84  ? 21.260 38.854 64.880 1.00 33.39  ? 92  ARG A CB  1 
ATOM   657  C CG  . ARG A 1 84  ? 20.709 39.928 63.998 1.00 36.05  ? 92  ARG A CG  1 
ATOM   658  C CD  . ARG A 1 84  ? 19.871 40.956 64.672 1.00 38.58  ? 92  ARG A CD  1 
ATOM   659  N NE  . ARG A 1 84  ? 20.058 42.229 63.991 1.00 40.75  ? 92  ARG A NE  1 
ATOM   660  C CZ  . ARG A 1 84  ? 20.198 42.372 62.681 1.00 38.93  ? 92  ARG A CZ  1 
ATOM   661  N NH1 . ARG A 1 84  ? 19.245 42.021 61.839 1.00 42.82  ? 92  ARG A NH1 1 
ATOM   662  N NH2 . ARG A 1 84  ? 21.313 42.917 62.207 1.00 38.27  ? 92  ARG A NH2 1 
ATOM   663  N N   . SER A 1 85  ? 21.985 38.343 61.697 1.00 30.10  ? 93  SER A N   1 
ATOM   664  C CA  . SER A 1 85  ? 21.421 38.050 60.387 1.00 33.14  ? 93  SER A CA  1 
ATOM   665  C C   . SER A 1 85  ? 22.179 36.995 59.581 1.00 31.78  ? 93  SER A C   1 
ATOM   666  O O   . SER A 1 85  ? 21.650 36.483 58.600 1.00 33.57  ? 93  SER A O   1 
ATOM   667  C CB  . SER A 1 85  ? 21.263 39.319 59.556 1.00 33.23  ? 93  SER A CB  1 
ATOM   668  O OG  . SER A 1 85  ? 22.498 39.898 59.207 1.00 35.81  ? 93  SER A OG  1 
ATOM   669  N N   . TRP A 1 86  ? 23.400 36.653 60.002 1.00 29.69  ? 94  TRP A N   1 
ATOM   670  C CA  . TRP A 1 86  ? 24.147 35.594 59.347 1.00 30.70  ? 94  TRP A CA  1 
ATOM   671  C C   . TRP A 1 86  ? 23.316 34.316 59.294 1.00 30.82  ? 94  TRP A C   1 
ATOM   672  O O   . TRP A 1 86  ? 22.779 33.881 60.309 1.00 30.81  ? 94  TRP A O   1 
ATOM   673  C CB  . TRP A 1 86  ? 25.453 35.278 60.067 1.00 30.25  ? 94  TRP A CB  1 
ATOM   674  C CG  . TRP A 1 86  ? 26.575 36.221 59.802 1.00 30.85  ? 94  TRP A CG  1 
ATOM   675  C CD1 . TRP A 1 86  ? 26.517 37.439 59.184 1.00 31.06  ? 94  TRP A CD1 1 
ATOM   676  C CD2 . TRP A 1 86  ? 27.943 35.999 60.132 1.00 28.89  ? 94  TRP A CD2 1 
ATOM   677  N NE1 . TRP A 1 86  ? 27.768 37.998 59.136 1.00 30.06  ? 94  TRP A NE1 1 
ATOM   678  C CE2 . TRP A 1 86  ? 28.666 37.131 59.710 1.00 30.69  ? 94  TRP A CE2 1 
ATOM   679  C CE3 . TRP A 1 86  ? 28.635 34.942 60.742 1.00 30.97  ? 94  TRP A CE3 1 
ATOM   680  C CZ2 . TRP A 1 86  ? 30.056 37.230 59.868 1.00 31.46  ? 94  TRP A CZ2 1 
ATOM   681  C CZ3 . TRP A 1 86  ? 30.001 35.050 60.916 1.00 30.78  ? 94  TRP A CZ3 1 
ATOM   682  C CH2 . TRP A 1 86  ? 30.698 36.185 60.483 1.00 31.04  ? 94  TRP A CH2 1 
ATOM   683  N N   . PRO A 1 87  ? 23.194 33.667 58.117 1.00 33.18  ? 95  PRO A N   1 
ATOM   684  C CA  . PRO A 1 87  ? 22.424 32.434 57.999 1.00 34.40  ? 95  PRO A CA  1 
ATOM   685  C C   . PRO A 1 87  ? 22.689 31.416 59.107 1.00 32.71  ? 95  PRO A C   1 
ATOM   686  O O   . PRO A 1 87  ? 21.749 30.842 59.650 1.00 33.07  ? 95  PRO A O   1 
ATOM   687  C CB  . PRO A 1 87  ? 22.830 31.924 56.613 1.00 36.42  ? 95  PRO A CB  1 
ATOM   688  C CG  . PRO A 1 87  ? 23.108 33.163 55.845 1.00 36.14  ? 95  PRO A CG  1 
ATOM   689  C CD  . PRO A 1 87  ? 23.745 34.119 56.831 1.00 34.31  ? 95  PRO A CD  1 
ATOM   690  N N   . HIS A 1 88  ? 23.968 31.207 59.446 1.00 35.96  ? 96  HIS A N   1 
ATOM   691  C CA  . HIS A 1 88  ? 24.361 30.267 60.486 1.00 35.40  ? 96  HIS A CA  1 
ATOM   692  C C   . HIS A 1 88  ? 23.657 30.528 61.819 1.00 35.89  ? 96  HIS A C   1 
ATOM   693  O O   . HIS A 1 88  ? 23.167 29.613 62.475 1.00 32.31  ? 96  HIS A O   1 
ATOM   694  C CB  . HIS A 1 88  ? 25.890 30.340 60.682 1.00 43.02  ? 96  HIS A CB  1 
ATOM   695  C CG  . HIS A 1 88  ? 26.444 29.366 61.682 1.00 50.36  ? 96  HIS A CG  1 
ATOM   696  N ND1 . HIS A 1 88  ? 26.709 29.743 62.993 1.00 55.60  ? 96  HIS A ND1 1 
ATOM   697  C CD2 . HIS A 1 88  ? 26.748 28.055 61.540 1.00 56.14  ? 96  HIS A CD2 1 
ATOM   698  C CE1 . HIS A 1 88  ? 27.176 28.661 63.603 1.00 54.42  ? 96  HIS A CE1 1 
ATOM   699  N NE2 . HIS A 1 88  ? 27.221 27.618 62.764 1.00 54.08  ? 96  HIS A NE2 1 
ATOM   700  N N   . PHE A 1 89  ? 23.621 31.793 62.245 1.00 33.08  ? 97  PHE A N   1 
ATOM   701  C CA  . PHE A 1 89  ? 22.996 32.117 63.515 1.00 32.35  ? 97  PHE A CA  1 
ATOM   702  C C   . PHE A 1 89  ? 21.477 32.192 63.382 1.00 27.64  ? 97  PHE A C   1 
ATOM   703  O O   . PHE A 1 89  ? 20.755 31.758 64.274 1.00 29.77  ? 97  PHE A O   1 
ATOM   704  C CB  . PHE A 1 89  ? 23.596 33.400 64.081 1.00 34.33  ? 97  PHE A CB  1 
ATOM   705  C CG  . PHE A 1 89  ? 25.046 33.226 64.462 1.00 37.36  ? 97  PHE A CG  1 
ATOM   706  C CD1 . PHE A 1 89  ? 25.437 32.211 65.323 1.00 39.74  ? 97  PHE A CD1 1 
ATOM   707  C CD2 . PHE A 1 89  ? 26.013 34.081 63.976 1.00 38.47  ? 97  PHE A CD2 1 
ATOM   708  C CE1 . PHE A 1 89  ? 26.773 32.053 65.675 1.00 39.88  ? 97  PHE A CE1 1 
ATOM   709  C CE2 . PHE A 1 89  ? 27.350 33.918 64.332 1.00 37.76  ? 97  PHE A CE2 1 
ATOM   710  C CZ  . PHE A 1 89  ? 27.719 32.905 65.170 1.00 36.68  ? 97  PHE A CZ  1 
ATOM   711  N N   . HIS A 1 90  ? 21.000 32.722 62.257 1.00 28.61  ? 98  HIS A N   1 
ATOM   712  C CA  . HIS A 1 90  ? 19.572 32.817 62.009 1.00 28.89  ? 98  HIS A CA  1 
ATOM   713  C C   . HIS A 1 90  ? 18.951 31.425 62.028 1.00 30.44  ? 98  HIS A C   1 
ATOM   714  O O   . HIS A 1 90  ? 17.907 31.222 62.645 1.00 29.69  ? 98  HIS A O   1 
ATOM   715  C CB  . HIS A 1 90  ? 19.306 33.529 60.687 1.00 28.05  ? 98  HIS A CB  1 
ATOM   716  C CG  . HIS A 1 90  ? 17.857 33.607 60.313 1.00 27.94  ? 98  HIS A CG  1 
ATOM   717  N ND1 . HIS A 1 90  ? 16.960 34.379 61.036 1.00 28.97  ? 98  HIS A ND1 1 
ATOM   718  C CD2 . HIS A 1 90  ? 17.197 33.006 59.300 1.00 28.36  ? 98  HIS A CD2 1 
ATOM   719  C CE1 . HIS A 1 90  ? 15.790 34.223 60.440 1.00 31.20  ? 98  HIS A CE1 1 
ATOM   720  N NE2 . HIS A 1 90  ? 15.887 33.392 59.392 1.00 29.20  ? 98  HIS A NE2 1 
ATOM   721  N N   . ASN A 1 91  ? 19.630 30.469 61.376 1.00 31.43  ? 99  ASN A N   1 
ATOM   722  C CA  . ASN A 1 91  ? 19.170 29.089 61.319 1.00 32.29  ? 99  ASN A CA  1 
ATOM   723  C C   . ASN A 1 91  ? 19.106 28.487 62.718 1.00 28.58  ? 99  ASN A C   1 
ATOM   724  O O   . ASN A 1 91  ? 18.113 27.860 63.089 1.00 25.46  ? 99  ASN A O   1 
ATOM   725  C CB  . ASN A 1 91  ? 20.064 28.256 60.368 1.00 35.58  ? 99  ASN A CB  1 
ATOM   726  C CG  . ASN A 1 91  ? 19.505 26.893 60.026 1.00 43.96  ? 99  ASN A CG  1 
ATOM   727  O OD1 . ASN A 1 91  ? 18.288 26.714 59.828 1.00 46.15  ? 99  ASN A OD1 1 
ATOM   728  N ND2 . ASN A 1 91  ? 20.385 25.896 59.942 1.00 47.42  ? 99  ASN A ND2 1 
ATOM   729  N N   . PHE A 1 92  ? 20.147 28.738 63.523 1.00 27.58  ? 100 PHE A N   1 
ATOM   730  C CA  . PHE A 1 92  ? 20.169 28.237 64.883 1.00 26.06  ? 100 PHE A CA  1 
ATOM   731  C C   . PHE A 1 92  ? 19.023 28.806 65.727 1.00 27.57  ? 100 PHE A C   1 
ATOM   732  O O   . PHE A 1 92  ? 18.395 28.083 66.500 1.00 27.61  ? 100 PHE A O   1 
ATOM   733  C CB  . PHE A 1 92  ? 21.525 28.521 65.519 1.00 28.51  ? 100 PHE A CB  1 
ATOM   734  C CG  . PHE A 1 92  ? 21.680 27.799 66.825 1.00 32.35  ? 100 PHE A CG  1 
ATOM   735  C CD1 . PHE A 1 92  ? 21.753 26.406 66.864 1.00 32.30  ? 100 PHE A CD1 1 
ATOM   736  C CD2 . PHE A 1 92  ? 21.694 28.497 68.022 1.00 31.30  ? 100 PHE A CD2 1 
ATOM   737  C CE1 . PHE A 1 92  ? 21.868 25.737 68.073 1.00 31.05  ? 100 PHE A CE1 1 
ATOM   738  C CE2 . PHE A 1 92  ? 21.811 27.828 69.228 1.00 32.90  ? 100 PHE A CE2 1 
ATOM   739  C CZ  . PHE A 1 92  ? 21.895 26.448 69.250 1.00 34.54  ? 100 PHE A CZ  1 
ATOM   740  N N   . CYS A 1 93  ? 18.754 30.109 65.585 1.00 26.78  ? 101 CYS A N   1 
ATOM   741  C CA  . CYS A 1 93  ? 17.637 30.741 66.272 1.00 27.16  ? 101 CYS A CA  1 
ATOM   742  C C   . CYS A 1 93  ? 16.270 30.231 65.815 1.00 27.49  ? 101 CYS A C   1 
ATOM   743  O O   . CYS A 1 93  ? 15.360 30.107 66.627 1.00 28.19  ? 101 CYS A O   1 
ATOM   744  C CB  . CYS A 1 93  ? 17.722 32.254 66.136 1.00 28.34  ? 101 CYS A CB  1 
ATOM   745  S SG  . CYS A 1 93  ? 19.034 32.994 67.140 1.00 29.67  ? 101 CYS A SG  1 
ATOM   746  N N   . LEU A 1 94  ? 16.115 29.950 64.517 1.00 28.29  ? 102 LEU A N   1 
ATOM   747  C CA  . LEU A 1 94  ? 14.873 29.356 64.039 1.00 29.10  ? 102 LEU A CA  1 
ATOM   748  C C   . LEU A 1 94  ? 14.646 28.043 64.783 1.00 27.99  ? 102 LEU A C   1 
ATOM   749  O O   . LEU A 1 94  ? 13.550 27.758 65.259 1.00 27.79  ? 102 LEU A O   1 
ATOM   750  C CB  . LEU A 1 94  ? 14.914 29.087 62.531 1.00 30.18  ? 102 LEU A CB  1 
ATOM   751  C CG  . LEU A 1 94  ? 14.872 30.283 61.608 1.00 31.65  ? 102 LEU A CG  1 
ATOM   752  C CD1 . LEU A 1 94  ? 14.985 29.837 60.158 1.00 31.99  ? 102 LEU A CD1 1 
ATOM   753  C CD2 . LEU A 1 94  ? 13.602 31.101 61.811 1.00 30.51  ? 102 LEU A CD2 1 
ATOM   754  N N   . THR A 1 95  ? 15.726 27.270 64.916 1.00 29.59  ? 103 THR A N   1 
ATOM   755  C CA  . THR A 1 95  ? 15.688 26.011 65.636 1.00 30.41  ? 103 THR A CA  1 
ATOM   756  C C   . THR A 1 95  ? 15.376 26.199 67.119 1.00 30.69  ? 103 THR A C   1 
ATOM   757  O O   . THR A 1 95  ? 14.573 25.446 67.670 1.00 30.03  ? 103 THR A O   1 
ATOM   758  C CB  . THR A 1 95  ? 16.999 25.260 65.393 1.00 33.69  ? 103 THR A CB  1 
ATOM   759  O OG1 . THR A 1 95  ? 17.134 25.003 63.995 1.00 37.00  ? 103 THR A OG1 1 
ATOM   760  C CG2 . THR A 1 95  ? 17.054 23.977 66.127 1.00 35.48  ? 103 THR A CG2 1 
ATOM   761  N N   . LEU A 1 96  ? 16.029 27.175 67.771 1.00 28.75  ? 104 LEU A N   1 
ATOM   762  C CA  . LEU A 1 96  ? 15.768 27.452 69.175 1.00 30.98  ? 104 LEU A CA  1 
ATOM   763  C C   . LEU A 1 96  ? 14.297 27.786 69.393 1.00 30.19  ? 104 LEU A C   1 
ATOM   764  O O   . LEU A 1 96  ? 13.673 27.255 70.300 1.00 29.27  ? 104 LEU A O   1 
ATOM   765  C CB  . LEU A 1 96  ? 16.590 28.636 69.718 1.00 31.20  ? 104 LEU A CB  1 
ATOM   766  C CG  . LEU A 1 96  ? 18.087 28.434 69.888 1.00 31.68  ? 104 LEU A CG  1 
ATOM   767  C CD1 . LEU A 1 96  ? 18.776 29.780 70.169 1.00 33.40  ? 104 LEU A CD1 1 
ATOM   768  C CD2 . LEU A 1 96  ? 18.380 27.448 70.988 1.00 31.92  ? 104 LEU A CD2 1 
ATOM   769  N N   . ALA A 1 97  ? 13.769 28.703 68.575 1.00 30.37  ? 105 ALA A N   1 
ATOM   770  C CA  . ALA A 1 97  ? 12.389 29.139 68.711 1.00 30.00  ? 105 ALA A CA  1 
ATOM   771  C C   . ALA A 1 97  ? 11.416 27.969 68.573 1.00 30.69  ? 105 ALA A C   1 
ATOM   772  O O   . ALA A 1 97  ? 10.556 27.764 69.429 1.00 31.38  ? 105 ALA A O   1 
ATOM   773  C CB  . ALA A 1 97  ? 12.068 30.212 67.678 1.00 28.70  ? 105 ALA A CB  1 
ATOM   774  N N   . SER A 1 98  ? 11.555 27.206 67.487 1.00 32.19  ? 106 SER A N   1 
ATOM   775  C CA  . SER A 1 98  ? 10.614 26.136 67.195 1.00 34.26  ? 106 SER A CA  1 
ATOM   776  C C   . SER A 1 98  ? 10.784 24.978 68.171 1.00 33.07  ? 106 SER A C   1 
ATOM   777  O O   . SER A 1 98  ? 9.812  24.472 68.708 1.00 32.49  ? 106 SER A O   1 
ATOM   778  C CB  . SER A 1 98  ? 10.766 25.646 65.755 1.00 36.30  ? 106 SER A CB  1 
ATOM   779  O OG  . SER A 1 98  ? 12.125 25.371 65.457 1.00 39.57  ? 106 SER A OG  1 
ATOM   780  N N   . SER A 1 99  ? 12.034 24.581 68.416 1.00 35.87  ? 107 SER A N   1 
ATOM   781  C CA  . SER A 1 99  ? 12.303 23.444 69.277 1.00 36.88  ? 107 SER A CA  1 
ATOM   782  C C   . SER A 1 99  ? 11.973 23.709 70.745 1.00 37.22  ? 107 SER A C   1 
ATOM   783  O O   . SER A 1 99  ? 11.493 22.817 71.436 1.00 36.38  ? 107 SER A O   1 
ATOM   784  C CB  . SER A 1 99  ? 13.757 23.004 69.122 1.00 36.51  ? 107 SER A CB  1 
ATOM   785  O OG  . SER A 1 99  ? 14.053 22.004 70.073 1.00 44.86  ? 107 SER A OG  1 
ATOM   786  N N   . LEU A 1 100 ? 12.222 24.936 71.225 1.00 36.65  ? 108 LEU A N   1 
ATOM   787  C CA  . LEU A 1 100 ? 12.025 25.253 72.632 1.00 34.05  ? 108 LEU A CA  1 
ATOM   788  C C   . LEU A 1 100 ? 10.667 25.904 72.874 1.00 33.49  ? 108 LEU A C   1 
ATOM   789  O O   . LEU A 1 100 ? 10.311 26.148 74.020 1.00 35.93  ? 108 LEU A O   1 
ATOM   790  C CB  . LEU A 1 100 ? 13.151 26.186 73.136 1.00 33.14  ? 108 LEU A CB  1 
ATOM   791  C CG  . LEU A 1 100 ? 14.567 25.673 72.926 1.00 33.68  ? 108 LEU A CG  1 
ATOM   792  C CD1 . LEU A 1 100 ? 15.607 26.701 73.325 1.00 33.72  ? 108 LEU A CD1 1 
ATOM   793  C CD2 . LEU A 1 100 ? 14.805 24.402 73.706 1.00 35.05  ? 108 LEU A CD2 1 
ATOM   794  N N   . ASN A 1 101 ? 9.927  26.191 71.796 1.00 33.40  ? 109 ASN A N   1 
ATOM   795  C CA  . ASN A 1 101 ? 8.677  26.930 71.883 1.00 38.71  ? 109 ASN A CA  1 
ATOM   796  C C   . ASN A 1 101 ? 8.867  28.213 72.689 1.00 36.30  ? 109 ASN A C   1 
ATOM   797  O O   . ASN A 1 101 ? 8.173  28.448 73.673 1.00 33.68  ? 109 ASN A O   1 
ATOM   798  C CB  . ASN A 1 101 ? 7.558  26.070 72.479 1.00 41.64  ? 109 ASN A CB  1 
ATOM   799  C CG  . ASN A 1 101 ? 7.219  24.923 71.574 1.00 53.81  ? 109 ASN A CG  1 
ATOM   800  O OD1 . ASN A 1 101 ? 6.844  25.121 70.414 1.00 60.72  ? 109 ASN A OD1 1 
ATOM   801  N ND2 . ASN A 1 101 ? 7.360  23.698 72.067 1.00 59.95  ? 109 ASN A ND2 1 
ATOM   802  N N   . ALA A 1 102 ? 9.819  29.037 72.243 1.00 33.14  ? 110 ALA A N   1 
ATOM   803  C CA  . ALA A 1 102 ? 10.234 30.204 72.997 1.00 32.04  ? 110 ALA A CA  1 
ATOM   804  C C   . ALA A 1 102 ? 10.301 31.424 72.087 1.00 31.41  ? 110 ALA A C   1 
ATOM   805  O O   . ALA A 1 102 ? 10.549 31.303 70.888 1.00 31.08  ? 110 ALA A O   1 
ATOM   806  C CB  . ALA A 1 102 ? 11.585 29.954 73.640 1.00 32.09  ? 110 ALA A CB  1 
ATOM   807  N N   . LEU A 1 103 ? 10.079 32.600 72.676 1.00 29.53  ? 111 LEU A N   1 
ATOM   808  C CA  . LEU A 1 103 ? 10.399 33.830 71.985 1.00 29.22  ? 111 LEU A CA  1 
ATOM   809  C C   . LEU A 1 103 ? 11.912 33.994 72.078 1.00 27.73  ? 111 LEU A C   1 
ATOM   810  O O   . LEU A 1 103 ? 12.456 34.064 73.176 1.00 30.02  ? 111 LEU A O   1 
ATOM   811  C CB  . LEU A 1 103 ? 9.719  35.049 72.591 1.00 32.93  ? 111 LEU A CB  1 
ATOM   812  C CG  . LEU A 1 103 ? 9.939  36.271 71.702 1.00 35.95  ? 111 LEU A CG  1 
ATOM   813  C CD1 . LEU A 1 103 ? 8.753  37.172 71.771 1.00 36.86  ? 111 LEU A CD1 1 
ATOM   814  C CD2 . LEU A 1 103 ? 11.283 36.907 72.007 1.00 35.46  ? 111 LEU A CD2 1 
ATOM   815  N N   . VAL A 1 104 ? 12.584 34.043 70.925 1.00 26.86  ? 112 VAL A N   1 
ATOM   816  C CA  . VAL A 1 104 ? 14.031 34.166 70.906 1.00 27.20  ? 112 VAL A CA  1 
ATOM   817  C C   . VAL A 1 104 ? 14.411 35.610 70.591 1.00 27.11  ? 112 VAL A C   1 
ATOM   818  O O   . VAL A 1 104 ? 13.859 36.216 69.673 1.00 24.41  ? 112 VAL A O   1 
ATOM   819  C CB  . VAL A 1 104 ? 14.660 33.154 69.926 1.00 27.07  ? 112 VAL A CB  1 
ATOM   820  C CG1 . VAL A 1 104 ? 16.175 33.302 69.841 1.00 27.56  ? 112 VAL A CG1 1 
ATOM   821  C CG2 . VAL A 1 104 ? 14.286 31.737 70.328 1.00 27.65  ? 112 VAL A CG2 1 
ATOM   822  N N   . VAL A 1 105 ? 15.342 36.140 71.392 1.00 25.27  ? 113 VAL A N   1 
ATOM   823  C CA  . VAL A 1 105 ? 15.924 37.452 71.178 1.00 25.73  ? 113 VAL A CA  1 
ATOM   824  C C   . VAL A 1 105 ? 17.381 37.267 70.772 1.00 25.93  ? 113 VAL A C   1 
ATOM   825  O O   . VAL A 1 105 ? 18.162 36.726 71.547 1.00 26.69  ? 113 VAL A O   1 
ATOM   826  C CB  . VAL A 1 105 ? 15.820 38.311 72.449 1.00 25.13  ? 113 VAL A CB  1 
ATOM   827  C CG1 . VAL A 1 105 ? 16.397 39.705 72.221 1.00 25.97  ? 113 VAL A CG1 1 
ATOM   828  C CG2 . VAL A 1 105 ? 14.387 38.384 72.945 1.00 25.13  ? 113 VAL A CG2 1 
ATOM   829  N N   . SER A 1 106 ? 17.732 37.713 69.562 1.00 26.41  ? 114 SER A N   1 
ATOM   830  C CA  . SER A 1 106 ? 19.078 37.535 69.042 1.00 27.74  ? 114 SER A CA  1 
ATOM   831  C C   . SER A 1 106 ? 19.744 38.866 68.696 1.00 26.01  ? 114 SER A C   1 
ATOM   832  O O   . SER A 1 106 ? 19.517 39.394 67.611 1.00 24.96  ? 114 SER A O   1 
ATOM   833  C CB  . SER A 1 106 ? 19.039 36.628 67.816 1.00 29.43  ? 114 SER A CB  1 
ATOM   834  O OG  . SER A 1 106 ? 20.345 36.289 67.384 1.00 30.85  ? 114 SER A OG  1 
ATOM   835  N N   . PRO A 1 107 ? 20.557 39.459 69.606 1.00 26.37  ? 115 PRO A N   1 
ATOM   836  C CA  . PRO A 1 107 ? 21.161 40.767 69.365 1.00 27.40  ? 115 PRO A CA  1 
ATOM   837  C C   . PRO A 1 107 ? 22.519 40.745 68.672 1.00 27.90  ? 115 PRO A C   1 
ATOM   838  O O   . PRO A 1 107 ? 23.331 39.849 68.896 1.00 28.56  ? 115 PRO A O   1 
ATOM   839  C CB  . PRO A 1 107 ? 21.316 41.333 70.770 1.00 27.97  ? 115 PRO A CB  1 
ATOM   840  C CG  . PRO A 1 107 ? 21.549 40.129 71.626 1.00 28.52  ? 115 PRO A CG  1 
ATOM   841  C CD  . PRO A 1 107 ? 20.832 38.960 70.962 1.00 27.17  ? 115 PRO A CD  1 
ATOM   842  N N   . ASP A 1 108 ? 22.764 41.774 67.852 1.00 27.58  ? 116 ASP A N   1 
ATOM   843  C CA  . ASP A 1 108 ? 24.126 42.148 67.518 1.00 28.95  ? 116 ASP A CA  1 
ATOM   844  C C   . ASP A 1 108 ? 24.762 42.790 68.743 1.00 31.09  ? 116 ASP A C   1 
ATOM   845  O O   . ASP A 1 108 ? 24.066 43.308 69.622 1.00 29.44  ? 116 ASP A O   1 
ATOM   846  C CB  . ASP A 1 108 ? 24.199 43.115 66.342 1.00 32.17  ? 116 ASP A CB  1 
ATOM   847  C CG  . ASP A 1 108 ? 23.845 42.507 65.011 1.00 32.53  ? 116 ASP A CG  1 
ATOM   848  O OD1 . ASP A 1 108 ? 24.117 41.309 64.821 1.00 33.05  ? 116 ASP A OD1 1 
ATOM   849  O OD2 . ASP A 1 108 ? 23.312 43.235 64.156 1.00 33.86  ? 116 ASP A OD2 1 
ATOM   850  N N   . TYR A 1 109 ? 26.092 42.711 68.791 1.00 29.12  ? 117 TYR A N   1 
ATOM   851  C CA  . TYR A 1 109 ? 26.869 43.437 69.771 1.00 28.94  ? 117 TYR A CA  1 
ATOM   852  C C   . TYR A 1 109 ? 28.132 43.929 69.074 1.00 29.77  ? 117 TYR A C   1 
ATOM   853  O O   . TYR A 1 109 ? 28.552 43.360 68.064 1.00 29.08  ? 117 TYR A O   1 
ATOM   854  C CB  . TYR A 1 109 ? 27.153 42.581 70.997 1.00 29.44  ? 117 TYR A CB  1 
ATOM   855  C CG  . TYR A 1 109 ? 27.804 41.230 70.748 1.00 29.73  ? 117 TYR A CG  1 
ATOM   856  C CD1 . TYR A 1 109 ? 29.182 41.114 70.603 1.00 28.98  ? 117 TYR A CD1 1 
ATOM   857  C CD2 . TYR A 1 109 ? 27.040 40.066 70.688 1.00 27.95  ? 117 TYR A CD2 1 
ATOM   858  C CE1 . TYR A 1 109 ? 29.789 39.870 70.420 1.00 30.90  ? 117 TYR A CE1 1 
ATOM   859  C CE2 . TYR A 1 109 ? 27.631 38.821 70.478 1.00 28.54  ? 117 TYR A CE2 1 
ATOM   860  C CZ  . TYR A 1 109 ? 29.006 38.724 70.347 1.00 29.45  ? 117 TYR A CZ  1 
ATOM   861  O OH  . TYR A 1 109 ? 29.590 37.488 70.166 1.00 27.54  ? 117 TYR A OH  1 
ATOM   862  N N   . ARG A 1 110 ? 28.704 45.011 69.607 1.00 29.20  ? 118 ARG A N   1 
ATOM   863  C CA  . ARG A 1 110 ? 29.862 45.636 68.994 1.00 30.52  ? 118 ARG A CA  1 
ATOM   864  C C   . ARG A 1 110 ? 31.031 44.658 69.032 1.00 28.93  ? 118 ARG A C   1 
ATOM   865  O O   . ARG A 1 110 ? 31.199 43.920 70.004 1.00 27.02  ? 118 ARG A O   1 
ATOM   866  C CB  . ARG A 1 110 ? 30.220 46.952 69.700 1.00 31.66  ? 118 ARG A CB  1 
ATOM   867  C CG  . ARG A 1 110 ? 29.261 48.077 69.364 1.00 30.51  ? 118 ARG A CG  1 
ATOM   868  C CD  . ARG A 1 110 ? 29.502 49.298 70.246 1.00 32.59  ? 118 ARG A CD  1 
ATOM   869  N NE  . ARG A 1 110 ? 29.247 49.015 71.655 1.00 31.98  ? 118 ARG A NE  1 
ATOM   870  C CZ  . ARG A 1 110 ? 29.717 49.735 72.669 1.00 33.63  ? 118 ARG A CZ  1 
ATOM   871  N NH1 . ARG A 1 110 ? 30.560 50.734 72.476 1.00 35.06  ? 118 ARG A NH1 1 
ATOM   872  N NH2 . ARG A 1 110 ? 29.346 49.433 73.908 1.00 32.48  ? 118 ARG A NH2 1 
ATOM   873  N N   . LEU A 1 111 ? 31.795 44.659 67.936 1.00 30.15  ? 119 LEU A N   1 
ATOM   874  C CA  . LEU A 1 111 ? 32.887 43.729 67.722 1.00 31.54  ? 119 LEU A CA  1 
ATOM   875  C C   . LEU A 1 111 ? 34.257 44.397 67.790 1.00 32.30  ? 119 LEU A C   1 
ATOM   876  O O   . LEU A 1 111 ? 34.415 45.555 67.401 1.00 32.10  ? 119 LEU A O   1 
ATOM   877  C CB  . LEU A 1 111 ? 32.702 43.109 66.341 1.00 30.10  ? 119 LEU A CB  1 
ATOM   878  C CG  . LEU A 1 111 ? 31.437 42.290 66.189 1.00 30.69  ? 119 LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 111 ? 31.323 41.747 64.803 1.00 33.18  ? 119 LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 111 ? 31.386 41.180 67.208 1.00 29.15  ? 119 LEU A CD2 1 
ATOM   881  N N   . ALA A 1 112 ? 35.227 43.627 68.284 1.00 33.26  ? 120 ALA A N   1 
ATOM   882  C CA  . ALA A 1 112 ? 36.634 43.989 68.279 1.00 32.76  ? 120 ALA A CA  1 
ATOM   883  C C   . ALA A 1 112 ? 37.232 43.742 66.897 1.00 37.25  ? 120 ALA A C   1 
ATOM   884  O O   . ALA A 1 112 ? 36.679 42.951 66.134 1.00 35.63  ? 120 ALA A O   1 
ATOM   885  C CB  . ALA A 1 112 ? 37.353 43.155 69.315 1.00 33.15  ? 120 ALA A CB  1 
ATOM   886  N N   . PRO A 1 113 ? 38.387 44.353 66.526 1.00 42.23  ? 121 PRO A N   1 
ATOM   887  C CA  . PRO A 1 113 ? 39.128 45.279 67.386 1.00 43.36  ? 121 PRO A CA  1 
ATOM   888  C C   . PRO A 1 113 ? 38.604 46.718 67.454 1.00 42.18  ? 121 PRO A C   1 
ATOM   889  O O   . PRO A 1 113 ? 39.055 47.491 68.293 1.00 43.96  ? 121 PRO A O   1 
ATOM   890  C CB  . PRO A 1 113 ? 40.537 45.257 66.764 1.00 42.84  ? 121 PRO A CB  1 
ATOM   891  C CG  . PRO A 1 113 ? 40.304 44.981 65.324 1.00 42.87  ? 121 PRO A CG  1 
ATOM   892  C CD  . PRO A 1 113 ? 39.086 44.079 65.257 1.00 42.33  ? 121 PRO A CD  1 
ATOM   893  N N   . GLU A 1 114 ? 37.678 47.098 66.570 1.00 42.96  ? 122 GLU A N   1 
ATOM   894  C CA  . GLU A 1 114 ? 37.141 48.450 66.593 1.00 43.37  ? 122 GLU A CA  1 
ATOM   895  C C   . GLU A 1 114 ? 36.565 48.774 67.973 1.00 45.01  ? 122 GLU A C   1 
ATOM   896  O O   . GLU A 1 114 ? 36.809 49.850 68.508 1.00 42.26  ? 122 GLU A O   1 
ATOM   897  C CB  . GLU A 1 114 ? 36.079 48.632 65.505 1.00 44.61  ? 122 GLU A CB  1 
ATOM   898  C CG  . GLU A 1 114 ? 35.510 50.042 65.445 1.00 52.62  ? 122 GLU A CG  1 
ATOM   899  C CD  . GLU A 1 114 ? 34.387 50.244 64.445 1.00 56.68  ? 122 GLU A CD  1 
ATOM   900  O OE1 . GLU A 1 114 ? 33.957 49.251 63.817 1.00 62.48  ? 122 GLU A OE1 1 
ATOM   901  O OE2 . GLU A 1 114 ? 33.937 51.403 64.288 1.00 63.22  ? 122 GLU A OE2 1 
ATOM   902  N N   . HIS A 1 115 ? 35.813 47.828 68.552 1.00 41.04  ? 123 HIS A N   1 
ATOM   903  C CA  . HIS A 1 115 ? 35.249 47.989 69.883 1.00 37.78  ? 123 HIS A CA  1 
ATOM   904  C C   . HIS A 1 115 ? 35.722 46.866 70.800 1.00 37.30  ? 123 HIS A C   1 
ATOM   905  O O   . HIS A 1 115 ? 35.155 45.771 70.798 1.00 37.25  ? 123 HIS A O   1 
ATOM   906  C CB  . HIS A 1 115 ? 33.716 48.011 69.810 1.00 36.43  ? 123 HIS A CB  1 
ATOM   907  C CG  . HIS A 1 115 ? 33.163 49.078 68.916 1.00 36.19  ? 123 HIS A CG  1 
ATOM   908  N ND1 . HIS A 1 115 ? 33.214 50.415 69.270 1.00 39.65  ? 123 HIS A ND1 1 
ATOM   909  C CD2 . HIS A 1 115 ? 32.558 48.970 67.716 1.00 37.93  ? 123 HIS A CD2 1 
ATOM   910  C CE1 . HIS A 1 115 ? 32.644 51.078 68.276 1.00 38.54  ? 123 HIS A CE1 1 
ATOM   911  N NE2 . HIS A 1 115 ? 32.231 50.242 67.318 1.00 41.31  ? 123 HIS A NE2 1 
ATOM   912  N N   . ARG A 1 116 ? 36.772 47.149 71.576 1.00 35.44  ? 124 ARG A N   1 
ATOM   913  C CA  . ARG A 1 116 ? 37.334 46.167 72.489 1.00 36.64  ? 124 ARG A CA  1 
ATOM   914  C C   . ARG A 1 116 ? 36.418 45.924 73.681 1.00 34.21  ? 124 ARG A C   1 
ATOM   915  O O   . ARG A 1 116 ? 35.557 46.744 73.994 1.00 36.07  ? 124 ARG A O   1 
ATOM   916  C CB  . ARG A 1 116 ? 38.725 46.606 72.950 1.00 39.80  ? 124 ARG A CB  1 
ATOM   917  C CG  . ARG A 1 116 ? 39.708 46.572 71.801 1.00 44.23  ? 124 ARG A CG  1 
ATOM   918  C CD  . ARG A 1 116 ? 41.111 46.920 72.202 1.00 47.95  ? 124 ARG A CD  1 
ATOM   919  N NE  . ARG A 1 116 ? 41.979 46.923 71.030 1.00 49.88  ? 124 ARG A NE  1 
ATOM   920  C CZ  . ARG A 1 116 ? 42.829 45.957 70.713 1.00 47.55  ? 124 ARG A CZ  1 
ATOM   921  N NH1 . ARG A 1 116 ? 43.085 44.961 71.542 1.00 48.34  ? 124 ARG A NH1 1 
ATOM   922  N NH2 . ARG A 1 116 ? 43.430 45.986 69.528 1.00 48.98  ? 124 ARG A NH2 1 
ATOM   923  N N   . LEU A 1 117 ? 36.598 44.765 74.315 1.00 34.00  ? 125 LEU A N   1 
ATOM   924  C CA  . LEU A 1 117 ? 35.905 44.457 75.550 1.00 34.80  ? 125 LEU A CA  1 
ATOM   925  C C   . LEU A 1 117 ? 36.209 45.600 76.516 1.00 40.56  ? 125 LEU A C   1 
ATOM   926  O O   . LEU A 1 117 ? 37.333 46.103 76.497 1.00 38.59  ? 125 LEU A O   1 
ATOM   927  C CB  . LEU A 1 117 ? 36.378 43.125 76.096 1.00 33.84  ? 125 LEU A CB  1 
ATOM   928  C CG  . LEU A 1 117 ? 35.984 41.896 75.251 1.00 36.15  ? 125 LEU A CG  1 
ATOM   929  C CD1 . LEU A 1 117 ? 36.633 40.647 75.768 1.00 36.91  ? 125 LEU A CD1 1 
ATOM   930  C CD2 . LEU A 1 117 ? 34.471 41.705 75.226 1.00 37.33  ? 125 LEU A CD2 1 
ATOM   931  N N   . PRO A 1 118 ? 35.260 46.032 77.391 1.00 38.06  ? 126 PRO A N   1 
ATOM   932  C CA  . PRO A 1 118 ? 33.985 45.341 77.606 1.00 36.13  ? 126 PRO A CA  1 
ATOM   933  C C   . PRO A 1 118 ? 32.781 45.842 76.798 1.00 31.79  ? 126 PRO A C   1 
ATOM   934  O O   . PRO A 1 118 ? 31.647 45.749 77.264 1.00 36.55  ? 126 PRO A O   1 
ATOM   935  C CB  . PRO A 1 118 ? 33.753 45.609 79.096 1.00 38.00  ? 126 PRO A CB  1 
ATOM   936  C CG  . PRO A 1 118 ? 34.228 47.064 79.246 1.00 39.03  ? 126 PRO A CG  1 
ATOM   937  C CD  . PRO A 1 118 ? 35.418 47.193 78.286 1.00 39.10  ? 126 PRO A CD  1 
ATOM   938  N N   . ALA A 1 119 ? 32.997 46.357 75.584 1.00 31.22  ? 127 ALA A N   1 
ATOM   939  C CA  . ALA A 1 119 ? 31.893 46.831 74.759 1.00 30.84  ? 127 ALA A CA  1 
ATOM   940  C C   . ALA A 1 119 ? 30.769 45.801 74.589 1.00 32.81  ? 127 ALA A C   1 
ATOM   941  O O   . ALA A 1 119 ? 29.593 46.122 74.770 1.00 30.89  ? 127 ALA A O   1 
ATOM   942  C CB  . ALA A 1 119 ? 32.404 47.277 73.402 1.00 31.06  ? 127 ALA A CB  1 
ATOM   943  N N   . ALA A 1 120 ? 31.128 44.551 74.271 1.00 31.18  ? 128 ALA A N   1 
ATOM   944  C CA  . ALA A 1 120 ? 30.131 43.511 74.062 1.00 32.50  ? 128 ALA A CA  1 
ATOM   945  C C   . ALA A 1 120 ? 29.255 43.304 75.299 1.00 32.69  ? 128 ALA A C   1 
ATOM   946  O O   . ALA A 1 120 ? 28.046 43.124 75.169 1.00 31.43  ? 128 ALA A O   1 
ATOM   947  C CB  . ALA A 1 120 ? 30.797 42.202 73.656 1.00 32.09  ? 128 ALA A CB  1 
ATOM   948  N N   . PHE A 1 121 ? 29.868 43.350 76.493 1.00 33.66  ? 129 PHE A N   1 
ATOM   949  C CA  . PHE A 1 121 ? 29.148 43.142 77.742 1.00 30.80  ? 129 PHE A CA  1 
ATOM   950  C C   . PHE A 1 121 ? 28.188 44.287 78.052 1.00 32.15  ? 129 PHE A C   1 
ATOM   951  O O   . PHE A 1 121 ? 27.093 44.061 78.566 1.00 31.64  ? 129 PHE A O   1 
ATOM   952  C CB  . PHE A 1 121 ? 30.109 42.963 78.916 1.00 31.82  ? 129 PHE A CB  1 
ATOM   953  C CG  . PHE A 1 121 ? 31.177 41.912 78.708 1.00 33.44  ? 129 PHE A CG  1 
ATOM   954  C CD1 . PHE A 1 121 ? 30.898 40.739 78.025 1.00 31.62  ? 129 PHE A CD1 1 
ATOM   955  C CD2 . PHE A 1 121 ? 32.452 42.084 79.224 1.00 34.33  ? 129 PHE A CD2 1 
ATOM   956  C CE1 . PHE A 1 121 ? 31.883 39.772 77.836 1.00 33.29  ? 129 PHE A CE1 1 
ATOM   957  C CE2 . PHE A 1 121 ? 33.431 41.111 79.045 1.00 35.07  ? 129 PHE A CE2 1 
ATOM   958  C CZ  . PHE A 1 121 ? 33.143 39.963 78.348 1.00 34.69  ? 129 PHE A CZ  1 
ATOM   959  N N   . GLU A 1 122 ? 28.622 45.510 77.736 1.00 31.31  ? 130 GLU A N   1 
ATOM   960  C CA  . GLU A 1 122 ? 27.784 46.694 77.834 1.00 34.33  ? 130 GLU A CA  1 
ATOM   961  C C   . GLU A 1 122 ? 26.564 46.566 76.922 1.00 32.48  ? 130 GLU A C   1 
ATOM   962  O O   . GLU A 1 122 ? 25.444 46.901 77.307 1.00 28.98  ? 130 GLU A O   1 
ATOM   963  C CB  . GLU A 1 122 ? 28.632 47.938 77.469 1.00 37.90  ? 130 GLU A CB  1 
ATOM   964  C CG  . GLU A 1 122 ? 27.876 49.247 77.416 1.00 43.59  ? 130 GLU A CG  1 
ATOM   965  C CD  . GLU A 1 122 ? 28.752 50.461 77.132 1.00 48.41  ? 130 GLU A CD  1 
ATOM   966  O OE1 . GLU A 1 122 ? 29.973 50.302 76.884 1.00 47.07  ? 130 GLU A OE1 1 
ATOM   967  O OE2 . GLU A 1 122 ? 28.198 51.581 77.163 1.00 50.53  ? 130 GLU A OE2 1 
ATOM   968  N N   . ASP A 1 123 ? 26.787 46.073 75.703 1.00 31.05  ? 131 ASP A N   1 
ATOM   969  C CA  . ASP A 1 123 ? 25.694 45.865 74.769 1.00 31.13  ? 131 ASP A CA  1 
ATOM   970  C C   . ASP A 1 123 ? 24.737 44.794 75.292 1.00 28.90  ? 131 ASP A C   1 
ATOM   971  O O   . ASP A 1 123 ? 23.524 44.970 75.231 1.00 26.97  ? 131 ASP A O   1 
ATOM   972  C CB  . ASP A 1 123 ? 26.242 45.549 73.380 1.00 31.94  ? 131 ASP A CB  1 
ATOM   973  C CG  . ASP A 1 123 ? 27.078 46.687 72.774 1.00 36.33  ? 131 ASP A CG  1 
ATOM   974  O OD1 . ASP A 1 123 ? 26.962 47.846 73.259 1.00 34.38  ? 131 ASP A OD1 1 
ATOM   975  O OD2 . ASP A 1 123 ? 27.859 46.417 71.850 1.00 32.28  ? 131 ASP A OD2 1 
ATOM   976  N N   . ALA A 1 124 ? 25.284 43.717 75.862 1.00 30.13  ? 132 ALA A N   1 
ATOM   977  C CA  . ALA A 1 124 ? 24.456 42.649 76.398 1.00 31.62  ? 132 ALA A CA  1 
ATOM   978  C C   . ALA A 1 124 ? 23.513 43.180 77.478 1.00 32.10  ? 132 ALA A C   1 
ATOM   979  O O   . ALA A 1 124 ? 22.350 42.787 77.527 1.00 28.45  ? 132 ALA A O   1 
ATOM   980  C CB  . ALA A 1 124 ? 25.311 41.525 76.951 1.00 30.36  ? 132 ALA A CB  1 
ATOM   981  N N   . GLU A 1 125 ? 24.019 44.073 78.341 1.00 30.79  ? 133 GLU A N   1 
ATOM   982  C CA  . GLU A 1 125 ? 23.188 44.664 79.382 1.00 30.35  ? 133 GLU A CA  1 
ATOM   983  C C   . GLU A 1 125 ? 22.119 45.579 78.802 1.00 26.45  ? 133 GLU A C   1 
ATOM   984  O O   . GLU A 1 125 ? 21.007 45.615 79.317 1.00 28.54  ? 133 GLU A O   1 
ATOM   985  C CB  . GLU A 1 125 ? 24.020 45.433 80.420 1.00 29.52  ? 133 GLU A CB  1 
ATOM   986  C CG  . GLU A 1 125 ? 24.852 44.489 81.258 1.00 30.69  ? 133 GLU A CG  1 
ATOM   987  C CD  . GLU A 1 125 ? 25.562 45.109 82.444 1.00 34.44  ? 133 GLU A CD  1 
ATOM   988  O OE1 . GLU A 1 125 ? 25.273 46.274 82.806 1.00 35.89  ? 133 GLU A OE1 1 
ATOM   989  O OE2 . GLU A 1 125 ? 26.424 44.408 83.013 1.00 35.05  ? 133 GLU A OE2 1 
ATOM   990  N N   . ALA A 1 126 ? 22.457 46.308 77.735 1.00 25.33  ? 134 ALA A N   1 
ATOM   991  C CA  . ALA A 1 126 ? 21.489 47.160 77.066 1.00 26.72  ? 134 ALA A CA  1 
ATOM   992  C C   . ALA A 1 126 ? 20.363 46.331 76.445 1.00 28.15  ? 134 ALA A C   1 
ATOM   993  O O   . ALA A 1 126 ? 19.219 46.772 76.404 1.00 27.30  ? 134 ALA A O   1 
ATOM   994  C CB  . ALA A 1 126 ? 22.162 48.023 76.021 1.00 27.20  ? 134 ALA A CB  1 
ATOM   995  N N   . VAL A 1 127 ? 20.684 45.115 75.986 1.00 28.48  ? 135 VAL A N   1 
ATOM   996  C CA  . VAL A 1 127 ? 19.667 44.206 75.475 1.00 26.92  ? 135 VAL A CA  1 
ATOM   997  C C   . VAL A 1 127 ? 18.658 43.856 76.567 1.00 25.89  ? 135 VAL A C   1 
ATOM   998  O O   . VAL A 1 127 ? 17.453 43.923 76.344 1.00 25.86  ? 135 VAL A O   1 
ATOM   999  C CB  . VAL A 1 127 ? 20.278 42.917 74.886 1.00 25.73  ? 135 VAL A CB  1 
ATOM   1000 C CG1 . VAL A 1 127 ? 19.185 41.916 74.516 1.00 26.49  ? 135 VAL A CG1 1 
ATOM   1001 C CG2 . VAL A 1 127 ? 21.152 43.224 73.682 1.00 26.01  ? 135 VAL A CG2 1 
ATOM   1002 N N   . LEU A 1 128 ? 19.164 43.455 77.738 1.00 26.96  ? 136 LEU A N   1 
ATOM   1003 C CA  . LEU A 1 128 ? 18.307 43.079 78.852 1.00 30.86  ? 136 LEU A CA  1 
ATOM   1004 C C   . LEU A 1 128 ? 17.495 44.271 79.359 1.00 30.43  ? 136 LEU A C   1 
ATOM   1005 O O   . LEU A 1 128 ? 16.331 44.120 79.712 1.00 30.92  ? 136 LEU A O   1 
ATOM   1006 C CB  . LEU A 1 128 ? 19.139 42.458 79.984 1.00 31.83  ? 136 LEU A CB  1 
ATOM   1007 C CG  . LEU A 1 128 ? 19.339 40.939 79.920 1.00 33.65  ? 136 LEU A CG  1 
ATOM   1008 C CD1 . LEU A 1 128 ? 18.019 40.201 80.088 1.00 34.65  ? 136 LEU A CD1 1 
ATOM   1009 C CD2 . LEU A 1 128 ? 19.960 40.502 78.628 1.00 35.71  ? 136 LEU A CD2 1 
ATOM   1010 N N   . THR A 1 129 ? 18.111 45.456 79.360 1.00 28.72  ? 137 THR A N   1 
ATOM   1011 C CA  . THR A 1 129 ? 17.433 46.690 79.716 1.00 30.66  ? 137 THR A CA  1 
ATOM   1012 C C   . THR A 1 129 ? 16.346 47.050 78.711 1.00 31.07  ? 137 THR A C   1 
ATOM   1013 O O   . THR A 1 129 ? 15.265 47.490 79.097 1.00 31.19  ? 137 THR A O   1 
ATOM   1014 C CB  . THR A 1 129 ? 18.468 47.816 79.848 1.00 34.63  ? 137 THR A CB  1 
ATOM   1015 O OG1 . THR A 1 129 ? 19.400 47.430 80.859 1.00 33.14  ? 137 THR A OG1 1 
ATOM   1016 C CG2 . THR A 1 129 ? 17.835 49.142 80.200 1.00 36.83  ? 137 THR A CG2 1 
ATOM   1017 N N   . TRP A 1 130 ? 16.646 46.871 77.418 1.00 28.45  ? 138 TRP A N   1 
ATOM   1018 C CA  . TRP A 1 130 ? 15.645 47.041 76.385 1.00 28.80  ? 138 TRP A CA  1 
ATOM   1019 C C   . TRP A 1 130 ? 14.459 46.103 76.618 1.00 29.42  ? 138 TRP A C   1 
ATOM   1020 O O   . TRP A 1 130 ? 13.306 46.519 76.507 1.00 31.99  ? 138 TRP A O   1 
ATOM   1021 C CB  . TRP A 1 130 ? 16.255 46.823 75.005 1.00 29.71  ? 138 TRP A CB  1 
ATOM   1022 C CG  . TRP A 1 130 ? 15.280 46.993 73.886 1.00 29.65  ? 138 TRP A CG  1 
ATOM   1023 C CD1 . TRP A 1 130 ? 14.962 48.148 73.245 1.00 31.34  ? 138 TRP A CD1 1 
ATOM   1024 C CD2 . TRP A 1 130 ? 14.460 45.974 73.311 1.00 29.58  ? 138 TRP A CD2 1 
ATOM   1025 N NE1 . TRP A 1 130 ? 14.021 47.905 72.277 1.00 29.17  ? 138 TRP A NE1 1 
ATOM   1026 C CE2 . TRP A 1 130 ? 13.688 46.579 72.303 1.00 29.37  ? 138 TRP A CE2 1 
ATOM   1027 C CE3 . TRP A 1 130 ? 14.304 44.605 73.548 1.00 31.58  ? 138 TRP A CE3 1 
ATOM   1028 C CZ2 . TRP A 1 130 ? 12.788 45.858 71.518 1.00 30.05  ? 138 TRP A CZ2 1 
ATOM   1029 C CZ3 . TRP A 1 130 ? 13.409 43.895 72.772 1.00 30.40  ? 138 TRP A CZ3 1 
ATOM   1030 C CH2 . TRP A 1 130 ? 12.661 44.522 71.777 1.00 29.33  ? 138 TRP A CH2 1 
ATOM   1031 N N   . LEU A 1 131 ? 14.747 44.843 76.958 1.00 29.38  ? 139 LEU A N   1 
ATOM   1032 C CA  . LEU A 1 131 ? 13.702 43.878 77.271 1.00 31.44  ? 139 LEU A CA  1 
ATOM   1033 C C   . LEU A 1 131 ? 12.865 44.302 78.478 1.00 30.08  ? 139 LEU A C   1 
ATOM   1034 O O   . LEU A 1 131 ? 11.649 44.144 78.468 1.00 27.62  ? 139 LEU A O   1 
ATOM   1035 C CB  . LEU A 1 131 ? 14.293 42.512 77.575 1.00 34.12  ? 139 LEU A CB  1 
ATOM   1036 C CG  . LEU A 1 131 ? 14.587 41.625 76.404 1.00 40.56  ? 139 LEU A CG  1 
ATOM   1037 C CD1 . LEU A 1 131 ? 15.216 40.318 76.888 1.00 45.42  ? 139 LEU A CD1 1 
ATOM   1038 C CD2 . LEU A 1 131 ? 13.317 41.333 75.587 1.00 40.26  ? 139 LEU A CD2 1 
ATOM   1039 N N   . TRP A 1 132 ? 13.533 44.802 79.522 1.00 30.02  ? 140 TRP A N   1 
ATOM   1040 C CA  . TRP A 1 132 ? 12.842 45.349 80.677 1.00 31.51  ? 140 TRP A CA  1 
ATOM   1041 C C   . TRP A 1 132 ? 11.869 46.449 80.246 1.00 30.72  ? 140 TRP A C   1 
ATOM   1042 O O   . TRP A 1 132 ? 10.701 46.450 80.636 1.00 30.25  ? 140 TRP A O   1 
ATOM   1043 C CB  . TRP A 1 132 ? 13.833 45.884 81.726 1.00 32.28  ? 140 TRP A CB  1 
ATOM   1044 C CG  . TRP A 1 132 ? 13.142 46.620 82.833 1.00 32.68  ? 140 TRP A CG  1 
ATOM   1045 C CD1 . TRP A 1 132 ? 12.589 46.086 83.959 1.00 34.11  ? 140 TRP A CD1 1 
ATOM   1046 C CD2 . TRP A 1 132 ? 12.857 48.017 82.869 1.00 33.35  ? 140 TRP A CD2 1 
ATOM   1047 N NE1 . TRP A 1 132 ? 12.005 47.075 84.714 1.00 33.17  ? 140 TRP A NE1 1 
ATOM   1048 C CE2 . TRP A 1 132 ? 12.153 48.272 84.066 1.00 33.35  ? 140 TRP A CE2 1 
ATOM   1049 C CE3 . TRP A 1 132 ? 13.141 49.086 82.009 1.00 35.37  ? 140 TRP A CE3 1 
ATOM   1050 C CZ2 . TRP A 1 132 ? 11.727 49.551 84.420 1.00 32.82  ? 140 TRP A CZ2 1 
ATOM   1051 C CZ3 . TRP A 1 132 ? 12.723 50.356 82.366 1.00 34.86  ? 140 TRP A CZ3 1 
ATOM   1052 C CH2 . TRP A 1 132 ? 12.019 50.577 83.553 1.00 34.07  ? 140 TRP A CH2 1 
ATOM   1053 N N   . ASP A 1 133 ? 12.357 47.370 79.416 1.00 29.25  ? 141 ASP A N   1 
ATOM   1054 C CA  . ASP A 1 133 ? 11.566 48.506 78.975 1.00 33.87  ? 141 ASP A CA  1 
ATOM   1055 C C   . ASP A 1 133 ? 10.332 48.055 78.197 1.00 35.01  ? 141 ASP A C   1 
ATOM   1056 O O   . ASP A 1 133 ? 9.242  48.593 78.376 1.00 35.27  ? 141 ASP A O   1 
ATOM   1057 C CB  . ASP A 1 133 ? 12.437 49.454 78.124 1.00 36.58  ? 141 ASP A CB  1 
ATOM   1058 C CG  . ASP A 1 133 ? 11.786 50.796 77.891 1.00 44.27  ? 141 ASP A CG  1 
ATOM   1059 O OD1 . ASP A 1 133 ? 11.439 51.469 78.886 1.00 49.00  ? 141 ASP A OD1 1 
ATOM   1060 O OD2 . ASP A 1 133 ? 11.599 51.166 76.720 1.00 50.80  ? 141 ASP A OD2 1 
ATOM   1061 N N   . GLN A 1 134 ? 10.515 47.049 77.339 1.00 33.05  ? 142 GLN A N   1 
ATOM   1062 C CA  . GLN A 1 134 ? 9.424  46.499 76.556 1.00 32.44  ? 142 GLN A CA  1 
ATOM   1063 C C   . GLN A 1 134 ? 8.406  45.827 77.469 1.00 31.58  ? 142 GLN A C   1 
ATOM   1064 O O   . GLN A 1 134 ? 7.204  45.970 77.263 1.00 31.41  ? 142 GLN A O   1 
ATOM   1065 C CB  . GLN A 1 134 ? 9.960  45.498 75.520 1.00 33.48  ? 142 GLN A CB  1 
ATOM   1066 C CG  . GLN A 1 134 ? 10.844 46.142 74.473 1.00 34.47  ? 142 GLN A CG  1 
ATOM   1067 C CD  . GLN A 1 134 ? 10.069 47.077 73.589 1.00 36.71  ? 142 GLN A CD  1 
ATOM   1068 O OE1 . GLN A 1 134 ? 9.073  46.703 72.958 1.00 34.13  ? 142 GLN A OE1 1 
ATOM   1069 N NE2 . GLN A 1 134 ? 10.497 48.320 73.515 1.00 39.80  ? 142 GLN A NE2 1 
ATOM   1070 N N   . ALA A 1 135 ? 8.908  45.111 78.478 1.00 30.36  ? 143 ALA A N   1 
ATOM   1071 C CA  . ALA A 1 135 ? 8.063  44.362 79.392 1.00 33.41  ? 143 ALA A CA  1 
ATOM   1072 C C   . ALA A 1 135 ? 7.146  45.246 80.239 1.00 35.95  ? 143 ALA A C   1 
ATOM   1073 O O   . ALA A 1 135 ? 5.997  44.887 80.474 1.00 36.13  ? 143 ALA A O   1 
ATOM   1074 C CB  . ALA A 1 135 ? 8.924  43.510 80.301 1.00 33.99  ? 143 ALA A CB  1 
ATOM   1075 N N   . VAL A 1 136 ? 7.664  46.381 80.723 1.00 35.52  ? 144 VAL A N   1 
ATOM   1076 C CA  . VAL A 1 136 ? 6.904  47.246 81.618 1.00 38.17  ? 144 VAL A CA  1 
ATOM   1077 C C   . VAL A 1 136 ? 6.012  48.241 80.877 1.00 38.31  ? 144 VAL A C   1 
ATOM   1078 O O   . VAL A 1 136 ? 5.200  48.917 81.501 1.00 43.18  ? 144 VAL A O   1 
ATOM   1079 C CB  . VAL A 1 136 ? 7.821  48.012 82.608 1.00 36.29  ? 144 VAL A CB  1 
ATOM   1080 C CG1 . VAL A 1 136 ? 8.640  47.046 83.448 1.00 37.67  ? 144 VAL A CG1 1 
ATOM   1081 C CG2 . VAL A 1 136 ? 8.715  49.017 81.893 1.00 37.03  ? 144 VAL A CG2 1 
ATOM   1082 N N   . SER A 1 137 ? 6.162  48.329 79.553 1.00 38.39  ? 145 SER A N   1 
ATOM   1083 C CA  . SER A 1 137 ? 5.426  49.302 78.763 1.00 40.03  ? 145 SER A CA  1 
ATOM   1084 C C   . SER A 1 137 ? 4.446  48.706 77.752 1.00 40.62  ? 145 SER A C   1 
ATOM   1085 O O   . SER A 1 137 ? 3.971  49.423 76.882 1.00 40.06  ? 145 SER A O   1 
ATOM   1086 C CB  . SER A 1 137 ? 6.414  50.175 78.010 1.00 42.06  ? 145 SER A CB  1 
ATOM   1087 O OG  . SER A 1 137 ? 7.118  49.391 77.058 1.00 47.46  ? 145 SER A OG  1 
ATOM   1088 N N   . ASP A 1 138 ? 4.154  47.402 77.860 1.00 39.98  ? 146 ASP A N   1 
ATOM   1089 C CA  . ASP A 1 138 ? 3.376  46.697 76.850 1.00 48.36  ? 146 ASP A CA  1 
ATOM   1090 C C   . ASP A 1 138 ? 3.939  46.868 75.434 1.00 44.73  ? 146 ASP A C   1 
ATOM   1091 O O   . ASP A 1 138 ? 3.192  46.898 74.460 1.00 44.10  ? 146 ASP A O   1 
ATOM   1092 C CB  . ASP A 1 138 ? 1.892  47.145 76.891 1.00 59.61  ? 146 ASP A CB  1 
ATOM   1093 C CG  . ASP A 1 138 ? 1.171  46.809 78.183 1.00 66.26  ? 146 ASP A CG  1 
ATOM   1094 O OD1 . ASP A 1 138 ? 1.082  45.609 78.517 1.00 72.35  ? 146 ASP A OD1 1 
ATOM   1095 O OD2 . ASP A 1 138 ? 0.686  47.747 78.854 1.00 75.16  ? 146 ASP A OD2 1 
ATOM   1096 N N   . GLY A 1 139 ? 5.271  46.950 75.319 1.00 44.81  ? 147 GLY A N   1 
ATOM   1097 C CA  . GLY A 1 139 ? 5.930  46.982 74.024 1.00 42.21  ? 147 GLY A CA  1 
ATOM   1098 C C   . GLY A 1 139 ? 5.700  45.705 73.220 1.00 39.69  ? 147 GLY A C   1 
ATOM   1099 O O   . GLY A 1 139 ? 5.668  45.741 71.993 1.00 38.38  ? 147 GLY A O   1 
ATOM   1100 N N   . VAL A 1 140 ? 5.500  44.588 73.929 1.00 41.52  ? 148 VAL A N   1 
ATOM   1101 C CA  . VAL A 1 140 ? 5.362  43.280 73.313 1.00 44.03  ? 148 VAL A CA  1 
ATOM   1102 C C   . VAL A 1 140 ? 4.231  43.229 72.286 1.00 45.46  ? 148 VAL A C   1 
ATOM   1103 O O   . VAL A 1 140 ? 4.369  42.583 71.247 1.00 42.81  ? 148 VAL A O   1 
ATOM   1104 C CB  . VAL A 1 140 ? 5.206  42.210 74.420 1.00 46.40  ? 148 VAL A CB  1 
ATOM   1105 C CG1 . VAL A 1 140 ? 4.808  40.860 73.851 1.00 49.87  ? 148 VAL A CG1 1 
ATOM   1106 C CG2 . VAL A 1 140 ? 6.485  42.088 75.231 1.00 45.08  ? 148 VAL A CG2 1 
ATOM   1107 N N   . ASN A 1 141 ? 3.132  43.942 72.558 1.00 46.21  ? 149 ASN A N   1 
ATOM   1108 C CA  . ASN A 1 141 ? 1.999  43.975 71.645 1.00 50.17  ? 149 ASN A CA  1 
ATOM   1109 C C   . ASN A 1 141 ? 2.320  44.606 70.292 1.00 46.06  ? 149 ASN A C   1 
ATOM   1110 O O   . ASN A 1 141 ? 1.596  44.375 69.324 1.00 45.92  ? 149 ASN A O   1 
ATOM   1111 C CB  . ASN A 1 141 ? 0.807  44.705 72.279 1.00 58.59  ? 149 ASN A CB  1 
ATOM   1112 C CG  . ASN A 1 141 ? 0.128  43.876 73.332 1.00 66.74  ? 149 ASN A CG  1 
ATOM   1113 O OD1 . ASN A 1 141 ? -0.001 44.292 74.487 1.00 76.83  ? 149 ASN A OD1 1 
ATOM   1114 N ND2 . ASN A 1 141 ? -0.313 42.674 72.953 1.00 67.17  ? 149 ASN A ND2 1 
ATOM   1115 N N   . HIS A 1 142 ? 3.401  45.394 70.235 1.00 41.83  ? 150 HIS A N   1 
ATOM   1116 C CA  . HIS A 1 142 ? 3.831  46.037 69.004 1.00 46.47  ? 150 HIS A CA  1 
ATOM   1117 C C   . HIS A 1 142 ? 5.032  45.359 68.342 1.00 44.10  ? 150 HIS A C   1 
ATOM   1118 O O   . HIS A 1 142 ? 5.511  45.825 67.313 1.00 43.26  ? 150 HIS A O   1 
ATOM   1119 C CB  . HIS A 1 142 ? 4.142  47.514 69.289 1.00 54.32  ? 150 HIS A CB  1 
ATOM   1120 C CG  . HIS A 1 142 ? 2.991  48.274 69.882 1.00 67.21  ? 150 HIS A CG  1 
ATOM   1121 N ND1 . HIS A 1 142 ? 3.137  49.578 70.322 1.00 73.74  ? 150 HIS A ND1 1 
ATOM   1122 C CD2 . HIS A 1 142 ? 1.713  47.884 70.105 1.00 71.87  ? 150 HIS A CD2 1 
ATOM   1123 C CE1 . HIS A 1 142 ? 1.953  49.941 70.792 1.00 76.98  ? 150 HIS A CE1 1 
ATOM   1124 N NE2 . HIS A 1 142 ? 1.066  48.946 70.679 1.00 78.82  ? 150 HIS A NE2 1 
ATOM   1125 N N   . TRP A 1 143 ? 5.514  44.254 68.924 1.00 40.66  ? 151 TRP A N   1 
ATOM   1126 C CA  . TRP A 1 143 ? 6.623  43.512 68.344 1.00 39.96  ? 151 TRP A CA  1 
ATOM   1127 C C   . TRP A 1 143 ? 6.279  42.975 66.958 1.00 42.56  ? 151 TRP A C   1 
ATOM   1128 O O   . TRP A 1 143 ? 7.015  43.207 66.010 1.00 46.51  ? 151 TRP A O   1 
ATOM   1129 C CB  . TRP A 1 143 ? 7.058  42.368 69.272 1.00 37.41  ? 151 TRP A CB  1 
ATOM   1130 C CG  . TRP A 1 143 ? 7.872  42.820 70.443 1.00 35.02  ? 151 TRP A CG  1 
ATOM   1131 C CD1 . TRP A 1 143 ? 8.229  44.102 70.757 1.00 33.70  ? 151 TRP A CD1 1 
ATOM   1132 C CD2 . TRP A 1 143 ? 8.439  41.986 71.456 1.00 33.94  ? 151 TRP A CD2 1 
ATOM   1133 N NE1 . TRP A 1 143 ? 8.982  44.111 71.904 1.00 34.10  ? 151 TRP A NE1 1 
ATOM   1134 C CE2 . TRP A 1 143 ? 9.133  42.826 72.351 1.00 32.74  ? 151 TRP A CE2 1 
ATOM   1135 C CE3 . TRP A 1 143 ? 8.445  40.606 71.688 1.00 35.41  ? 151 TRP A CE3 1 
ATOM   1136 C CZ2 . TRP A 1 143 ? 9.821  42.329 73.455 1.00 33.16  ? 151 TRP A CZ2 1 
ATOM   1137 C CZ3 . TRP A 1 143 ? 9.126  40.120 72.780 1.00 33.54  ? 151 TRP A CZ3 1 
ATOM   1138 C CH2 . TRP A 1 143 ? 9.803  40.976 73.650 1.00 34.13  ? 151 TRP A CH2 1 
ATOM   1139 N N   . PHE A 1 144 ? 5.151  42.269 66.854 1.00 39.24  ? 152 PHE A N   1 
ATOM   1140 C CA  . PHE A 1 144 ? 4.682  41.734 65.588 1.00 41.68  ? 152 PHE A CA  1 
ATOM   1141 C C   . PHE A 1 144 ? 3.352  42.383 65.215 1.00 46.77  ? 152 PHE A C   1 
ATOM   1142 O O   . PHE A 1 144 ? 2.800  43.158 65.992 1.00 46.51  ? 152 PHE A O   1 
ATOM   1143 C CB  . PHE A 1 144 ? 4.580  40.199 65.694 1.00 39.42  ? 152 PHE A CB  1 
ATOM   1144 C CG  . PHE A 1 144 ? 5.936  39.576 65.928 1.00 37.90  ? 152 PHE A CG  1 
ATOM   1145 C CD1 . PHE A 1 144 ? 6.858  39.474 64.897 1.00 36.89  ? 152 PHE A CD1 1 
ATOM   1146 C CD2 . PHE A 1 144 ? 6.318  39.163 67.192 1.00 36.84  ? 152 PHE A CD2 1 
ATOM   1147 C CE1 . PHE A 1 144 ? 8.119  38.925 65.123 1.00 37.05  ? 152 PHE A CE1 1 
ATOM   1148 C CE2 . PHE A 1 144 ? 7.582  38.623 67.414 1.00 36.76  ? 152 PHE A CE2 1 
ATOM   1149 C CZ  . PHE A 1 144 ? 8.472  38.505 66.383 1.00 34.95  ? 152 PHE A CZ  1 
ATOM   1150 N N   . GLU A 1 145 ? 2.861  42.070 64.011 1.00 50.36  ? 153 GLU A N   1 
ATOM   1151 C CA  . GLU A 1 145 ? 1.610  42.621 63.514 1.00 54.32  ? 153 GLU A CA  1 
ATOM   1152 C C   . GLU A 1 145 ? 0.462  42.253 64.449 1.00 53.66  ? 153 GLU A C   1 
ATOM   1153 O O   . GLU A 1 145 ? -0.341 43.105 64.825 1.00 53.89  ? 153 GLU A O   1 
ATOM   1154 C CB  . GLU A 1 145 ? 1.314  42.097 62.102 1.00 60.77  ? 153 GLU A CB  1 
ATOM   1155 C CG  . GLU A 1 145 ? 0.567  43.085 61.231 1.00 71.66  ? 153 GLU A CG  1 
ATOM   1156 C CD  . GLU A 1 145 ? 1.410  44.271 60.804 1.00 78.44  ? 153 GLU A CD  1 
ATOM   1157 O OE1 . GLU A 1 145 ? 2.501  44.042 60.232 1.00 76.88  ? 153 GLU A OE1 1 
ATOM   1158 O OE2 . GLU A 1 145 ? 0.981  45.424 61.038 1.00 81.78  ? 153 GLU A OE2 1 
ATOM   1159 N N   . ASP A 1 146 ? 0.407  40.970 64.823 1.00 49.57  ? 154 ASP A N   1 
ATOM   1160 C CA  . ASP A 1 146 ? -0.575 40.477 65.773 1.00 47.40  ? 154 ASP A CA  1 
ATOM   1161 C C   . ASP A 1 146 ? -0.061 40.672 67.200 1.00 46.56  ? 154 ASP A C   1 
ATOM   1162 O O   . ASP A 1 146 ? 0.987  41.279 67.413 1.00 50.94  ? 154 ASP A O   1 
ATOM   1163 C CB  . ASP A 1 146 ? -0.902 39.002 65.465 1.00 50.44  ? 154 ASP A CB  1 
ATOM   1164 C CG  . ASP A 1 146 ? 0.221  38.015 65.726 1.00 54.10  ? 154 ASP A CG  1 
ATOM   1165 O OD1 . ASP A 1 146 ? 1.362  38.288 65.302 1.00 56.98  ? 154 ASP A OD1 1 
ATOM   1166 O OD2 . ASP A 1 146 ? -0.047 36.960 66.346 1.00 58.95  ? 154 ASP A OD2 1 
ATOM   1167 N N   . GLY A 1 147 ? -0.825 40.179 68.177 1.00 44.18  ? 155 GLY A N   1 
ATOM   1168 C CA  . GLY A 1 147 ? -0.405 40.209 69.568 1.00 45.67  ? 155 GLY A CA  1 
ATOM   1169 C C   . GLY A 1 147 ? 0.582  39.088 69.881 1.00 44.12  ? 155 GLY A C   1 
ATOM   1170 O O   . GLY A 1 147 ? 0.628  38.081 69.179 1.00 41.84  ? 155 GLY A O   1 
ATOM   1171 N N   . THR A 1 148 ? 1.371  39.285 70.940 1.00 42.46  ? 156 THR A N   1 
ATOM   1172 C CA  . THR A 1 148 ? 2.292  38.271 71.424 1.00 41.35  ? 156 THR A CA  1 
ATOM   1173 C C   . THR A 1 148 ? 2.205  38.233 72.942 1.00 39.88  ? 156 THR A C   1 
ATOM   1174 O O   . THR A 1 148 ? 2.248  39.280 73.579 1.00 38.51  ? 156 THR A O   1 
ATOM   1175 C CB  . THR A 1 148 ? 3.732  38.573 70.994 1.00 41.71  ? 156 THR A CB  1 
ATOM   1176 O OG1 . THR A 1 148 ? 3.772  38.787 69.587 1.00 38.51  ? 156 THR A OG1 1 
ATOM   1177 C CG2 . THR A 1 148 ? 4.684  37.460 71.370 1.00 42.69  ? 156 THR A CG2 1 
ATOM   1178 N N   . ASP A 1 149 ? 2.108  37.024 73.503 1.00 38.86  ? 157 ASP A N   1 
ATOM   1179 C CA  . ASP A 1 149 ? 2.081  36.843 74.944 1.00 42.84  ? 157 ASP A CA  1 
ATOM   1180 C C   . ASP A 1 149 ? 3.412  36.258 75.421 1.00 41.38  ? 157 ASP A C   1 
ATOM   1181 O O   . ASP A 1 149 ? 3.789  35.156 75.025 1.00 38.36  ? 157 ASP A O   1 
ATOM   1182 C CB  . ASP A 1 149 ? 0.903  35.936 75.338 1.00 49.32  ? 157 ASP A CB  1 
ATOM   1183 C CG  . ASP A 1 149 ? 0.574  35.913 76.824 1.00 60.70  ? 157 ASP A CG  1 
ATOM   1184 O OD1 . ASP A 1 149 ? 1.193  36.694 77.590 1.00 67.36  ? 157 ASP A OD1 1 
ATOM   1185 O OD2 . ASP A 1 149 ? -0.301 35.113 77.225 1.00 70.39  ? 157 ASP A OD2 1 
ATOM   1186 N N   . VAL A 1 150 ? 4.113  37.008 76.281 1.00 38.01  ? 158 VAL A N   1 
ATOM   1187 C CA  . VAL A 1 150 ? 5.452  36.655 76.726 1.00 37.48  ? 158 VAL A CA  1 
ATOM   1188 C C   . VAL A 1 150 ? 5.492  36.562 78.244 1.00 37.09  ? 158 VAL A C   1 
ATOM   1189 O O   . VAL A 1 150 ? 4.962  37.430 78.932 1.00 35.16  ? 158 VAL A O   1 
ATOM   1190 C CB  . VAL A 1 150 ? 6.490  37.693 76.261 1.00 39.92  ? 158 VAL A CB  1 
ATOM   1191 C CG1 . VAL A 1 150 ? 7.853  37.423 76.894 1.00 39.41  ? 158 VAL A CG1 1 
ATOM   1192 C CG2 . VAL A 1 150 ? 6.575  37.741 74.746 1.00 40.14  ? 158 VAL A CG2 1 
ATOM   1193 N N   . ASP A 1 151 ? 6.160  35.524 78.753 1.00 33.29  ? 159 ASP A N   1 
ATOM   1194 C CA  . ASP A 1 151 ? 6.364  35.394 80.182 1.00 33.58  ? 159 ASP A CA  1 
ATOM   1195 C C   . ASP A 1 151 ? 7.767  35.871 80.551 1.00 33.40  ? 159 ASP A C   1 
ATOM   1196 O O   . ASP A 1 151 ? 8.738  35.123 80.444 1.00 32.02  ? 159 ASP A O   1 
ATOM   1197 C CB  . ASP A 1 151 ? 6.119  33.954 80.599 1.00 34.36  ? 159 ASP A CB  1 
ATOM   1198 C CG  . ASP A 1 151 ? 6.171  33.728 82.074 1.00 35.24  ? 159 ASP A CG  1 
ATOM   1199 O OD1 . ASP A 1 151 ? 6.447  34.695 82.814 1.00 37.77  ? 159 ASP A OD1 1 
ATOM   1200 O OD2 . ASP A 1 151 ? 5.956  32.591 82.493 1.00 39.06  ? 159 ASP A OD2 1 
ATOM   1201 N N   . PHE A 1 152 ? 7.859  37.132 80.992 1.00 30.88  ? 160 PHE A N   1 
ATOM   1202 C CA  . PHE A 1 152 ? 9.129  37.726 81.376 1.00 31.62  ? 160 PHE A CA  1 
ATOM   1203 C C   . PHE A 1 152 ? 9.667  37.172 82.691 1.00 31.27  ? 160 PHE A C   1 
ATOM   1204 O O   . PHE A 1 152 ? 10.808 37.439 83.041 1.00 30.96  ? 160 PHE A O   1 
ATOM   1205 C CB  . PHE A 1 152 ? 9.010  39.247 81.457 1.00 33.72  ? 160 PHE A CB  1 
ATOM   1206 C CG  . PHE A 1 152 ? 8.944  39.884 80.097 1.00 33.53  ? 160 PHE A CG  1 
ATOM   1207 C CD1 . PHE A 1 152 ? 10.073 39.980 79.305 1.00 34.30  ? 160 PHE A CD1 1 
ATOM   1208 C CD2 . PHE A 1 152 ? 7.747  40.355 79.596 1.00 31.46  ? 160 PHE A CD2 1 
ATOM   1209 C CE1 . PHE A 1 152 ? 10.008 40.559 78.044 1.00 34.66  ? 160 PHE A CE1 1 
ATOM   1210 C CE2 . PHE A 1 152 ? 7.684  40.929 78.343 1.00 33.12  ? 160 PHE A CE2 1 
ATOM   1211 C CZ  . PHE A 1 152 ? 8.814  41.031 77.570 1.00 33.73  ? 160 PHE A CZ  1 
ATOM   1212 N N   . ASP A 1 153 ? 8.850  36.391 83.403 1.00 31.85  ? 161 ASP A N   1 
ATOM   1213 C CA  . ASP A 1 153 ? 9.315  35.694 84.588 1.00 33.74  ? 161 ASP A CA  1 
ATOM   1214 C C   . ASP A 1 153 ? 10.105 34.422 84.271 1.00 33.78  ? 161 ASP A C   1 
ATOM   1215 O O   . ASP A 1 153 ? 10.662 33.811 85.179 1.00 35.87  ? 161 ASP A O   1 
ATOM   1216 C CB  . ASP A 1 153 ? 8.123  35.359 85.491 1.00 37.26  ? 161 ASP A CB  1 
ATOM   1217 C CG  . ASP A 1 153 ? 8.541  35.111 86.909 1.00 37.69  ? 161 ASP A CG  1 
ATOM   1218 O OD1 . ASP A 1 153 ? 9.181  35.999 87.497 1.00 39.44  ? 161 ASP A OD1 1 
ATOM   1219 O OD2 . ASP A 1 153 ? 8.260  34.022 87.420 1.00 42.15  ? 161 ASP A OD2 1 
ATOM   1220 N N   . ARG A 1 154 ? 10.171 34.048 82.982 1.00 33.02  ? 162 ARG A N   1 
ATOM   1221 C CA  . ARG A 1 154 ? 10.898 32.867 82.538 1.00 34.20  ? 162 ARG A CA  1 
ATOM   1222 C C   . ARG A 1 154 ? 11.843 33.222 81.392 1.00 31.43  ? 162 ARG A C   1 
ATOM   1223 O O   . ARG A 1 154 ? 11.600 32.875 80.241 1.00 31.02  ? 162 ARG A O   1 
ATOM   1224 C CB  . ARG A 1 154 ? 9.917  31.761 82.094 1.00 37.45  ? 162 ARG A CB  1 
ATOM   1225 C CG  . ARG A 1 154 ? 9.115  31.134 83.236 1.00 42.41  ? 162 ARG A CG  1 
ATOM   1226 C CD  . ARG A 1 154 ? 8.308  29.923 82.773 1.00 48.41  ? 162 ARG A CD  1 
ATOM   1227 N NE  . ARG A 1 154 ? 7.158  30.309 81.958 1.00 57.01  ? 162 ARG A NE  1 
ATOM   1228 C CZ  . ARG A 1 154 ? 6.863  29.810 80.759 1.00 61.09  ? 162 ARG A CZ  1 
ATOM   1229 N NH1 . ARG A 1 154 ? 7.502  28.756 80.268 1.00 58.13  ? 162 ARG A NH1 1 
ATOM   1230 N NH2 . ARG A 1 154 ? 5.890  30.373 80.043 1.00 53.39  ? 162 ARG A NH2 1 
ATOM   1231 N N   . VAL A 1 155 ? 12.912 33.952 81.714 1.00 29.68  ? 163 VAL A N   1 
ATOM   1232 C CA  . VAL A 1 155 ? 13.910 34.315 80.723 1.00 28.96  ? 163 VAL A CA  1 
ATOM   1233 C C   . VAL A 1 155 ? 15.108 33.395 80.919 1.00 29.73  ? 163 VAL A C   1 
ATOM   1234 O O   . VAL A 1 155 ? 15.457 33.060 82.051 1.00 30.19  ? 163 VAL A O   1 
ATOM   1235 C CB  . VAL A 1 155 ? 14.316 35.806 80.810 1.00 28.71  ? 163 VAL A CB  1 
ATOM   1236 C CG1 . VAL A 1 155 ? 15.376 36.148 79.763 1.00 28.77  ? 163 VAL A CG1 1 
ATOM   1237 C CG2 . VAL A 1 155 ? 13.100 36.708 80.675 1.00 29.06  ? 163 VAL A CG2 1 
ATOM   1238 N N   . PHE A 1 156 ? 15.711 32.980 79.802 1.00 29.11  ? 164 PHE A N   1 
ATOM   1239 C CA  . PHE A 1 156 ? 16.919 32.173 79.827 1.00 28.92  ? 164 PHE A CA  1 
ATOM   1240 C C   . PHE A 1 156 ? 17.918 32.795 78.859 1.00 29.20  ? 164 PHE A C   1 
ATOM   1241 O O   . PHE A 1 156 ? 17.526 33.292 77.806 1.00 27.59  ? 164 PHE A O   1 
ATOM   1242 C CB  . PHE A 1 156 ? 16.624 30.721 79.435 1.00 29.04  ? 164 PHE A CB  1 
ATOM   1243 C CG  . PHE A 1 156 ? 15.642 30.041 80.348 1.00 29.29  ? 164 PHE A CG  1 
ATOM   1244 C CD1 . PHE A 1 156 ? 14.282 30.211 80.176 1.00 31.84  ? 164 PHE A CD1 1 
ATOM   1245 C CD2 . PHE A 1 156 ? 16.080 29.273 81.410 1.00 30.74  ? 164 PHE A CD2 1 
ATOM   1246 C CE1 . PHE A 1 156 ? 13.374 29.594 81.035 1.00 33.62  ? 164 PHE A CE1 1 
ATOM   1247 C CE2 . PHE A 1 156 ? 15.169 28.663 82.272 1.00 31.80  ? 164 PHE A CE2 1 
ATOM   1248 C CZ  . PHE A 1 156 ? 13.826 28.822 82.075 1.00 32.69  ? 164 PHE A CZ  1 
ATOM   1249 N N   . VAL A 1 157 ? 19.199 32.771 79.238 1.00 28.87  ? 165 VAL A N   1 
ATOM   1250 C CA  . VAL A 1 157 ? 20.261 33.276 78.388 1.00 28.82  ? 165 VAL A CA  1 
ATOM   1251 C C   . VAL A 1 157 ? 21.050 32.095 77.840 1.00 28.46  ? 165 VAL A C   1 
ATOM   1252 O O   . VAL A 1 157 ? 21.509 31.254 78.609 1.00 29.56  ? 165 VAL A O   1 
ATOM   1253 C CB  . VAL A 1 157 ? 21.181 34.250 79.129 1.00 29.10  ? 165 VAL A CB  1 
ATOM   1254 C CG1 . VAL A 1 157 ? 22.388 34.613 78.276 1.00 29.82  ? 165 VAL A CG1 1 
ATOM   1255 C CG2 . VAL A 1 157 ? 20.416 35.497 79.565 1.00 30.90  ? 165 VAL A CG2 1 
ATOM   1256 N N   . VAL A 1 158 ? 21.177 32.048 76.510 1.00 28.24  ? 166 VAL A N   1 
ATOM   1257 C CA  . VAL A 1 158 ? 21.898 30.989 75.824 1.00 27.50  ? 166 VAL A CA  1 
ATOM   1258 C C   . VAL A 1 158 ? 23.059 31.656 75.098 1.00 27.84  ? 166 VAL A C   1 
ATOM   1259 O O   . VAL A 1 158 ? 22.846 32.497 74.232 1.00 26.54  ? 166 VAL A O   1 
ATOM   1260 C CB  . VAL A 1 158 ? 21.005 30.191 74.863 1.00 26.67  ? 166 VAL A CB  1 
ATOM   1261 C CG1 . VAL A 1 158 ? 21.817 29.152 74.088 1.00 28.26  ? 166 VAL A CG1 1 
ATOM   1262 C CG2 . VAL A 1 158 ? 19.850 29.521 75.613 1.00 29.58  ? 166 VAL A CG2 1 
ATOM   1263 N N   . GLY A 1 159 ? 24.270 31.277 75.483 1.00 27.79  ? 167 GLY A N   1 
ATOM   1264 C CA  . GLY A 1 159 ? 25.463 31.902 74.913 1.00 28.37  ? 167 GLY A CA  1 
ATOM   1265 C C   . GLY A 1 159 ? 26.326 30.928 74.155 1.00 28.81  ? 167 GLY A C   1 
ATOM   1266 O O   . GLY A 1 159 ? 26.679 29.884 74.714 1.00 30.61  ? 167 GLY A O   1 
ATOM   1267 N N   . ASP A 1 160 ? 26.679 31.292 72.933 1.00 30.48  ? 168 ASP A N   1 
ATOM   1268 C CA  . ASP A 1 160 ? 27.570 30.449 72.104 1.00 31.98  ? 168 ASP A CA  1 
ATOM   1269 C C   . ASP A 1 160 ? 28.966 31.071 72.086 1.00 30.67  ? 168 ASP A C   1 
ATOM   1270 O O   . ASP A 1 160 ? 29.072 32.212 71.642 1.00 28.02  ? 168 ASP A O   1 
ATOM   1271 C CB  . ASP A 1 160 ? 26.978 30.247 70.721 1.00 34.31  ? 168 ASP A CB  1 
ATOM   1272 C CG  . ASP A 1 160 ? 27.917 29.691 69.666 1.00 39.05  ? 168 ASP A CG  1 
ATOM   1273 O OD1 . ASP A 1 160 ? 28.638 28.728 69.974 1.00 39.69  ? 168 ASP A OD1 1 
ATOM   1274 O OD2 . ASP A 1 160 ? 27.909 30.230 68.547 1.00 45.91  ? 168 ASP A OD2 1 
ATOM   1275 N N   . SER A 1 161 ? 29.967 30.348 72.587 1.00 31.34  ? 169 SER A N   1 
ATOM   1276 C CA  . SER A 1 161 ? 31.383 30.801 72.516 1.00 34.94  ? 169 SER A CA  1 
ATOM   1277 C C   . SER A 1 161 ? 31.561 32.169 73.190 1.00 30.80  ? 169 SER A C   1 
ATOM   1278 O O   . SER A 1 161 ? 31.448 32.225 74.410 1.00 27.82  ? 169 SER A O   1 
ATOM   1279 C CB  . SER A 1 161 ? 31.859 30.781 71.079 1.00 38.08  ? 169 SER A CB  1 
ATOM   1280 O OG  . SER A 1 161 ? 33.062 31.509 70.882 1.00 49.09  ? 169 SER A OG  1 
ATOM   1281 N N   . SER A 1 162 ? 31.906 33.195 72.421 1.00 30.50  ? 170 SER A N   1 
ATOM   1282 C CA  . SER A 1 162 ? 32.010 34.573 72.949 1.00 30.29  ? 170 SER A CA  1 
ATOM   1283 C C   . SER A 1 162 ? 30.702 34.880 73.682 1.00 30.98  ? 170 SER A C   1 
ATOM   1284 O O   . SER A 1 162 ? 30.753 35.509 74.739 1.00 29.57  ? 170 SER A O   1 
ATOM   1285 C CB  . SER A 1 162 ? 32.275 35.536 71.826 1.00 30.48  ? 170 SER A CB  1 
ATOM   1286 O OG  . SER A 1 162 ? 31.386 35.372 70.736 1.00 29.38  ? 170 SER A OG  1 
ATOM   1287 N N   . GLY A 1 163 ? 29.585 34.426 73.122 1.00 29.37  ? 171 GLY A N   1 
ATOM   1288 C CA  . GLY A 1 163 ? 28.286 34.610 73.744 1.00 30.43  ? 171 GLY A CA  1 
ATOM   1289 C C   . GLY A 1 163 ? 28.143 33.901 75.088 1.00 27.79  ? 171 GLY A C   1 
ATOM   1290 O O   . GLY A 1 163 ? 27.420 34.365 75.959 1.00 28.68  ? 171 GLY A O   1 
ATOM   1291 N N   . GLY A 1 164 ? 28.811 32.756 75.238 1.00 27.03  ? 172 GLY A N   1 
ATOM   1292 C CA  . GLY A 1 164 ? 28.864 32.061 76.512 1.00 29.03  ? 172 GLY A CA  1 
ATOM   1293 C C   . GLY A 1 164 ? 29.593 32.869 77.584 1.00 29.89  ? 172 GLY A C   1 
ATOM   1294 O O   . GLY A 1 164 ? 29.185 32.884 78.744 1.00 29.08  ? 172 GLY A O   1 
ATOM   1295 N N   . ASN A 1 165 ? 30.665 33.559 77.174 1.00 28.94  ? 173 ASN A N   1 
ATOM   1296 C CA  . ASN A 1 165 ? 31.379 34.452 78.065 1.00 28.87  ? 173 ASN A CA  1 
ATOM   1297 C C   . ASN A 1 165 ? 30.429 35.582 78.462 1.00 28.68  ? 173 ASN A C   1 
ATOM   1298 O O   . ASN A 1 165 ? 30.246 35.843 79.647 1.00 28.96  ? 173 ASN A O   1 
ATOM   1299 C CB  . ASN A 1 165 ? 32.665 34.938 77.399 1.00 28.78  ? 173 ASN A CB  1 
ATOM   1300 C CG  . ASN A 1 165 ? 33.471 35.880 78.257 1.00 32.49  ? 173 ASN A CG  1 
ATOM   1301 O OD1 . ASN A 1 165 ? 32.919 36.774 78.904 1.00 32.39  ? 173 ASN A OD1 1 
ATOM   1302 N ND2 . ASN A 1 165 ? 34.808 35.706 78.283 1.00 32.97  ? 173 ASN A ND2 1 
ATOM   1303 N N   . ILE A 1 166 ? 29.786 36.212 77.467 1.00 29.96  ? 174 ILE A N   1 
ATOM   1304 C CA  . ILE A 1 166 ? 28.782 37.237 77.724 1.00 30.27  ? 174 ILE A CA  1 
ATOM   1305 C C   . ILE A 1 166 ? 27.741 36.743 78.728 1.00 29.29  ? 174 ILE A C   1 
ATOM   1306 O O   . ILE A 1 166 ? 27.382 37.465 79.651 1.00 28.92  ? 174 ILE A O   1 
ATOM   1307 C CB  . ILE A 1 166 ? 28.099 37.722 76.417 1.00 30.30  ? 174 ILE A CB  1 
ATOM   1308 C CG1 . ILE A 1 166 ? 29.091 38.426 75.495 1.00 28.56  ? 174 ILE A CG1 1 
ATOM   1309 C CG2 . ILE A 1 166 ? 26.895 38.636 76.720 1.00 31.18  ? 174 ILE A CG2 1 
ATOM   1310 C CD1 . ILE A 1 166 ? 28.561 38.733 74.148 1.00 28.43  ? 174 ILE A CD1 1 
ATOM   1311 N N   . ALA A 1 167 ? 27.273 35.503 78.556 1.00 28.90  ? 175 ALA A N   1 
ATOM   1312 C CA  . ALA A 1 167 ? 26.282 34.939 79.459 1.00 30.10  ? 175 ALA A CA  1 
ATOM   1313 C C   . ALA A 1 167 ? 26.803 34.865 80.895 1.00 33.34  ? 175 ALA A C   1 
ATOM   1314 O O   . ALA A 1 167 ? 26.091 35.207 81.837 1.00 31.77  ? 175 ALA A O   1 
ATOM   1315 C CB  . ALA A 1 167 ? 25.849 33.560 78.986 1.00 29.95  ? 175 ALA A CB  1 
ATOM   1316 N N   . HIS A 1 168 ? 28.051 34.419 81.058 1.00 31.87  ? 176 HIS A N   1 
ATOM   1317 C CA  . HIS A 1 168 ? 28.678 34.409 82.369 1.00 32.40  ? 176 HIS A CA  1 
ATOM   1318 C C   . HIS A 1 168 ? 28.744 35.802 82.995 1.00 30.72  ? 176 HIS A C   1 
ATOM   1319 O O   . HIS A 1 168 ? 28.423 35.967 84.169 1.00 30.22  ? 176 HIS A O   1 
ATOM   1320 C CB  . HIS A 1 168 ? 30.081 33.818 82.291 1.00 35.43  ? 176 HIS A CB  1 
ATOM   1321 C CG  . HIS A 1 168 ? 30.888 34.064 83.527 1.00 33.77  ? 176 HIS A CG  1 
ATOM   1322 N ND1 . HIS A 1 168 ? 30.663 33.361 84.680 1.00 35.56  ? 176 HIS A ND1 1 
ATOM   1323 C CD2 . HIS A 1 168 ? 31.878 34.954 83.739 1.00 35.04  ? 176 HIS A CD2 1 
ATOM   1324 C CE1 . HIS A 1 168 ? 31.534 33.834 85.562 1.00 36.01  ? 176 HIS A CE1 1 
ATOM   1325 N NE2 . HIS A 1 168 ? 32.283 34.795 85.024 1.00 34.61  ? 176 HIS A NE2 1 
ATOM   1326 N N   . GLN A 1 169 ? 29.151 36.803 82.207 1.00 30.39  ? 177 GLN A N   1 
ATOM   1327 C CA  . GLN A 1 169 ? 29.276 38.164 82.711 1.00 32.47  ? 177 GLN A CA  1 
ATOM   1328 C C   . GLN A 1 169 ? 27.933 38.695 83.214 1.00 35.29  ? 177 GLN A C   1 
ATOM   1329 O O   . GLN A 1 169 ? 27.875 39.356 84.255 1.00 31.72  ? 177 GLN A O   1 
ATOM   1330 C CB  . GLN A 1 169 ? 29.837 39.119 81.642 1.00 31.69  ? 177 GLN A CB  1 
ATOM   1331 C CG  . GLN A 1 169 ? 31.201 38.723 81.080 1.00 32.61  ? 177 GLN A CG  1 
ATOM   1332 C CD  . GLN A 1 169 ? 32.294 38.666 82.119 1.00 35.50  ? 177 GLN A CD  1 
ATOM   1333 O OE1 . GLN A 1 169 ? 32.181 39.224 83.207 1.00 36.86  ? 177 GLN A OE1 1 
ATOM   1334 N NE2 . GLN A 1 169 ? 33.392 38.009 81.786 1.00 34.60  ? 177 GLN A NE2 1 
ATOM   1335 N N   . LEU A 1 170 ? 26.859 38.387 82.475 1.00 31.39  ? 178 LEU A N   1 
ATOM   1336 C CA  . LEU A 1 170 ? 25.512 38.738 82.893 1.00 32.10  ? 178 LEU A CA  1 
ATOM   1337 C C   . LEU A 1 170 ? 25.120 37.997 84.169 1.00 30.99  ? 178 LEU A C   1 
ATOM   1338 O O   . LEU A 1 170 ? 24.507 38.583 85.064 1.00 33.08  ? 178 LEU A O   1 
ATOM   1339 C CB  . LEU A 1 170 ? 24.480 38.416 81.793 1.00 32.45  ? 178 LEU A CB  1 
ATOM   1340 C CG  . LEU A 1 170 ? 24.508 39.286 80.564 1.00 34.23  ? 178 LEU A CG  1 
ATOM   1341 C CD1 . LEU A 1 170 ? 23.488 38.802 79.543 1.00 34.47  ? 178 LEU A CD1 1 
ATOM   1342 C CD2 . LEU A 1 170 ? 24.240 40.751 80.904 1.00 34.55  ? 178 LEU A CD2 1 
ATOM   1343 N N   . ALA A 1 171 ? 25.445 36.700 84.226 1.00 30.85  ? 179 ALA A N   1 
ATOM   1344 C CA  . ALA A 1 171 ? 25.122 35.880 85.383 1.00 34.47  ? 179 ALA A CA  1 
ATOM   1345 C C   . ALA A 1 171 ? 25.715 36.468 86.665 1.00 35.70  ? 179 ALA A C   1 
ATOM   1346 O O   . ALA A 1 171 ? 25.059 36.468 87.706 1.00 38.83  ? 179 ALA A O   1 
ATOM   1347 C CB  . ALA A 1 171 ? 25.602 34.450 85.180 1.00 33.06  ? 179 ALA A CB  1 
ATOM   1348 N N   . VAL A 1 172 ? 26.949 36.974 86.566 1.00 35.66  ? 180 VAL A N   1 
ATOM   1349 C CA  . VAL A 1 172 ? 27.639 37.611 87.679 1.00 37.11  ? 180 VAL A CA  1 
ATOM   1350 C C   . VAL A 1 172 ? 26.998 38.947 88.055 1.00 38.40  ? 180 VAL A C   1 
ATOM   1351 O O   . VAL A 1 172 ? 26.799 39.234 89.232 1.00 39.71  ? 180 VAL A O   1 
ATOM   1352 C CB  . VAL A 1 172 ? 29.139 37.814 87.349 1.00 37.37  ? 180 VAL A CB  1 
ATOM   1353 C CG1 . VAL A 1 172 ? 29.824 38.737 88.363 1.00 40.58  ? 180 VAL A CG1 1 
ATOM   1354 C CG2 . VAL A 1 172 ? 29.870 36.480 87.249 1.00 37.89  ? 180 VAL A CG2 1 
ATOM   1355 N N   . ARG A 1 173 ? 26.708 39.774 87.049 1.00 36.82  ? 181 ARG A N   1 
ATOM   1356 C CA  . ARG A 1 173 ? 26.122 41.080 87.290 1.00 38.72  ? 181 ARG A CA  1 
ATOM   1357 C C   . ARG A 1 173 ? 24.744 40.971 87.943 1.00 39.69  ? 181 ARG A C   1 
ATOM   1358 O O   . ARG A 1 173 ? 24.441 41.742 88.850 1.00 38.40  ? 181 ARG A O   1 
ATOM   1359 C CB  . ARG A 1 173 ? 26.079 41.875 85.986 1.00 37.98  ? 181 ARG A CB  1 
ATOM   1360 C CG  . ARG A 1 173 ? 27.468 42.352 85.563 1.00 38.26  ? 181 ARG A CG  1 
ATOM   1361 C CD  . ARG A 1 173 ? 27.819 43.682 86.224 1.00 39.42  ? 181 ARG A CD  1 
ATOM   1362 N NE  . ARG A 1 173 ? 27.076 44.770 85.602 1.00 39.02  ? 181 ARG A NE  1 
ATOM   1363 C CZ  . ARG A 1 173 ? 26.863 45.965 86.139 1.00 40.95  ? 181 ARG A CZ  1 
ATOM   1364 N NH1 . ARG A 1 173 ? 27.290 46.268 87.354 1.00 43.73  ? 181 ARG A NH1 1 
ATOM   1365 N NH2 . ARG A 1 173 ? 26.188 46.876 85.442 1.00 40.84  ? 181 ARG A NH2 1 
ATOM   1366 N N   . PHE A 1 174 ? 23.928 40.007 87.495 1.00 37.49  ? 182 PHE A N   1 
ATOM   1367 C CA  . PHE A 1 174 ? 22.637 39.749 88.115 1.00 38.50  ? 182 PHE A CA  1 
ATOM   1368 C C   . PHE A 1 174 ? 22.790 39.113 89.493 1.00 40.91  ? 182 PHE A C   1 
ATOM   1369 O O   . PHE A 1 174 ? 22.148 39.540 90.450 1.00 42.65  ? 182 PHE A O   1 
ATOM   1370 C CB  . PHE A 1 174 ? 21.753 38.834 87.253 1.00 38.42  ? 182 PHE A CB  1 
ATOM   1371 C CG  . PHE A 1 174 ? 21.085 39.551 86.115 1.00 40.75  ? 182 PHE A CG  1 
ATOM   1372 C CD1 . PHE A 1 174 ? 20.164 40.555 86.356 1.00 42.95  ? 182 PHE A CD1 1 
ATOM   1373 C CD2 . PHE A 1 174 ? 21.394 39.242 84.804 1.00 39.87  ? 182 PHE A CD2 1 
ATOM   1374 C CE1 . PHE A 1 174 ? 19.559 41.227 85.311 1.00 47.34  ? 182 PHE A CE1 1 
ATOM   1375 C CE2 . PHE A 1 174 ? 20.787 39.918 83.754 1.00 45.54  ? 182 PHE A CE2 1 
ATOM   1376 C CZ  . PHE A 1 174 ? 19.872 40.906 84.012 1.00 48.61  ? 182 PHE A CZ  1 
ATOM   1377 N N   . GLY A 1 175 ? 23.638 38.084 89.573 1.00 40.38  ? 183 GLY A N   1 
ATOM   1378 C CA  . GLY A 1 175 ? 23.839 37.333 90.800 1.00 40.73  ? 183 GLY A CA  1 
ATOM   1379 C C   . GLY A 1 175 ? 24.424 38.152 91.949 1.00 42.98  ? 183 GLY A C   1 
ATOM   1380 O O   . GLY A 1 175 ? 24.170 37.847 93.109 1.00 46.11  ? 183 GLY A O   1 
ATOM   1381 N N   . SER A 1 176 ? 25.196 39.193 91.613 1.00 41.51  ? 184 SER A N   1 
ATOM   1382 C CA  . SER A 1 176 ? 25.763 40.095 92.600 1.00 41.67  ? 184 SER A CA  1 
ATOM   1383 C C   . SER A 1 176 ? 24.772 41.154 93.079 1.00 43.35  ? 184 SER A C   1 
ATOM   1384 O O   . SER A 1 176 ? 25.074 41.918 93.989 1.00 43.55  ? 184 SER A O   1 
ATOM   1385 C CB  . SER A 1 176 ? 27.002 40.780 92.038 1.00 42.71  ? 184 SER A CB  1 
ATOM   1386 O OG  . SER A 1 176 ? 26.671 41.734 91.037 1.00 43.63  ? 184 SER A OG  1 
ATOM   1387 N N   . GLY A 1 177 ? 23.602 41.216 92.435 1.00 43.61  ? 185 GLY A N   1 
ATOM   1388 C CA  . GLY A 1 177 ? 22.611 42.231 92.739 1.00 44.12  ? 185 GLY A CA  1 
ATOM   1389 C C   . GLY A 1 177 ? 22.979 43.612 92.203 1.00 44.90  ? 185 GLY A C   1 
ATOM   1390 O O   . GLY A 1 177 ? 22.354 44.599 92.578 1.00 43.97  ? 185 GLY A O   1 
ATOM   1391 N N   . SER A 1 178 ? 23.981 43.673 91.315 1.00 43.44  ? 186 SER A N   1 
ATOM   1392 C CA  . SER A 1 178 ? 24.445 44.941 90.775 1.00 43.73  ? 186 SER A CA  1 
ATOM   1393 C C   . SER A 1 178 ? 23.398 45.545 89.846 1.00 43.22  ? 186 SER A C   1 
ATOM   1394 O O   . SER A 1 178 ? 23.139 46.744 89.891 1.00 43.89  ? 186 SER A O   1 
ATOM   1395 C CB  . SER A 1 178 ? 25.762 44.762 90.029 1.00 45.92  ? 186 SER A CB  1 
ATOM   1396 O OG  . SER A 1 178 ? 26.755 44.257 90.907 1.00 50.90  ? 186 SER A OG  1 
ATOM   1397 N N   . ILE A 1 179 ? 22.825 44.694 88.990 1.00 41.65  ? 187 ILE A N   1 
ATOM   1398 C CA  . ILE A 1 179 ? 21.702 45.085 88.157 1.00 41.82  ? 187 ILE A CA  1 
ATOM   1399 C C   . ILE A 1 179 ? 20.519 44.194 88.519 1.00 37.08  ? 187 ILE A C   1 
ATOM   1400 O O   . ILE A 1 179 ? 20.678 43.047 88.935 1.00 34.61  ? 187 ILE A O   1 
ATOM   1401 C CB  . ILE A 1 179 ? 22.019 45.056 86.643 1.00 42.02  ? 187 ILE A CB  1 
ATOM   1402 C CG1 . ILE A 1 179 ? 22.459 43.663 86.178 1.00 41.98  ? 187 ILE A CG1 1 
ATOM   1403 C CG2 . ILE A 1 179 ? 23.052 46.133 86.282 1.00 44.36  ? 187 ILE A CG2 1 
ATOM   1404 C CD1 . ILE A 1 179 ? 22.864 43.613 84.742 1.00 43.73  ? 187 ILE A CD1 1 
ATOM   1405 N N   . GLU A 1 180 ? 19.326 44.763 88.375 1.00 35.46  ? 188 GLU A N   1 
ATOM   1406 C CA  . GLU A 1 180 ? 18.111 44.096 88.794 1.00 38.04  ? 188 GLU A CA  1 
ATOM   1407 C C   . GLU A 1 180 ? 17.011 44.669 87.908 1.00 33.45  ? 188 GLU A C   1 
ATOM   1408 O O   . GLU A 1 180 ? 16.877 45.885 87.812 1.00 37.10  ? 188 GLU A O   1 
ATOM   1409 C CB  . GLU A 1 180 ? 17.929 44.314 90.308 1.00 43.05  ? 188 GLU A CB  1 
ATOM   1410 C CG  . GLU A 1 180 ? 16.747 43.583 90.916 1.00 48.25  ? 188 GLU A CG  1 
ATOM   1411 C CD  . GLU A 1 180 ? 15.451 44.364 90.810 1.00 53.31  ? 188 GLU A CD  1 
ATOM   1412 O OE1 . GLU A 1 180 ? 15.399 45.509 91.325 1.00 54.12  ? 188 GLU A OE1 1 
ATOM   1413 O OE2 . GLU A 1 180 ? 14.492 43.832 90.205 1.00 48.87  ? 188 GLU A OE2 1 
ATOM   1414 N N   . LEU A 1 181 ? 16.268 43.783 87.231 1.00 30.97  ? 189 LEU A N   1 
ATOM   1415 C CA  . LEU A 1 181 ? 15.349 44.177 86.175 1.00 32.19  ? 189 LEU A CA  1 
ATOM   1416 C C   . LEU A 1 181 ? 13.950 43.568 86.269 1.00 31.21  ? 189 LEU A C   1 
ATOM   1417 O O   . LEU A 1 181 ? 13.323 43.310 85.244 1.00 30.53  ? 189 LEU A O   1 
ATOM   1418 C CB  . LEU A 1 181 ? 15.987 43.810 84.820 1.00 34.00  ? 189 LEU A CB  1 
ATOM   1419 C CG  . LEU A 1 181 ? 17.244 44.593 84.446 1.00 38.26  ? 189 LEU A CG  1 
ATOM   1420 C CD1 . LEU A 1 181 ? 17.784 44.153 83.111 1.00 38.79  ? 189 LEU A CD1 1 
ATOM   1421 C CD2 . LEU A 1 181 ? 16.976 46.082 84.402 1.00 38.23  ? 189 LEU A CD2 1 
ATOM   1422 N N   . THR A 1 182 ? 13.443 43.388 87.497 1.00 32.08  ? 190 THR A N   1 
ATOM   1423 C CA  . THR A 1 182 ? 12.061 42.985 87.708 1.00 34.22  ? 190 THR A CA  1 
ATOM   1424 C C   . THR A 1 182 ? 11.173 43.837 86.805 1.00 35.03  ? 190 THR A C   1 
ATOM   1425 O O   . THR A 1 182 ? 11.352 45.053 86.764 1.00 35.21  ? 190 THR A O   1 
ATOM   1426 C CB  . THR A 1 182 ? 11.675 43.126 89.194 1.00 37.46  ? 190 THR A CB  1 
ATOM   1427 O OG1 . THR A 1 182 ? 12.544 42.318 89.984 1.00 40.05  ? 190 THR A OG1 1 
ATOM   1428 C CG2 . THR A 1 182 ? 10.206 42.728 89.476 1.00 37.01  ? 190 THR A CG2 1 
ATOM   1429 N N   . PRO A 1 183 ? 10.186 43.271 86.064 1.00 36.83  ? 191 PRO A N   1 
ATOM   1430 C CA  . PRO A 1 183 ? 9.777  41.871 86.182 1.00 37.28  ? 191 PRO A CA  1 
ATOM   1431 C C   . PRO A 1 183 ? 10.534 40.876 85.299 1.00 36.84  ? 191 PRO A C   1 
ATOM   1432 O O   . PRO A 1 183 ? 10.151 39.710 85.228 1.00 37.55  ? 191 PRO A O   1 
ATOM   1433 C CB  . PRO A 1 183 ? 8.303  41.926 85.768 1.00 37.48  ? 191 PRO A CB  1 
ATOM   1434 C CG  . PRO A 1 183 ? 8.264  43.011 84.711 1.00 38.13  ? 191 PRO A CG  1 
ATOM   1435 C CD  . PRO A 1 183 ? 9.375  44.006 85.081 1.00 38.73  ? 191 PRO A CD  1 
ATOM   1436 N N   . VAL A 1 184 ? 11.603 41.312 84.622 1.00 35.74  ? 192 VAL A N   1 
ATOM   1437 C CA  . VAL A 1 184 ? 12.450 40.368 83.909 1.00 35.33  ? 192 VAL A CA  1 
ATOM   1438 C C   . VAL A 1 184 ? 13.131 39.504 84.966 1.00 37.44  ? 192 VAL A C   1 
ATOM   1439 O O   . VAL A 1 184 ? 13.730 40.026 85.904 1.00 39.44  ? 192 VAL A O   1 
ATOM   1440 C CB  . VAL A 1 184 ? 13.459 41.055 82.968 1.00 35.85  ? 192 VAL A CB  1 
ATOM   1441 C CG1 . VAL A 1 184 ? 14.406 40.049 82.331 1.00 38.34  ? 192 VAL A CG1 1 
ATOM   1442 C CG2 . VAL A 1 184 ? 12.739 41.864 81.896 1.00 37.84  ? 192 VAL A CG2 1 
ATOM   1443 N N   . ARG A 1 185 ? 12.986 38.181 84.834 1.00 36.31  ? 193 ARG A N   1 
ATOM   1444 C CA  . ARG A 1 185 ? 13.683 37.239 85.693 1.00 35.67  ? 193 ARG A CA  1 
ATOM   1445 C C   . ARG A 1 185 ? 14.398 36.177 84.857 1.00 34.39  ? 193 ARG A C   1 
ATOM   1446 O O   . ARG A 1 185 ? 13.754 35.355 84.205 1.00 33.38  ? 193 ARG A O   1 
ATOM   1447 C CB  . ARG A 1 185 ? 12.709 36.583 86.670 1.00 39.22  ? 193 ARG A CB  1 
ATOM   1448 C CG  . ARG A 1 185 ? 13.358 35.543 87.568 1.00 44.75  ? 193 ARG A CG  1 
ATOM   1449 C CD  . ARG A 1 185 ? 12.361 34.950 88.530 1.00 50.18  ? 193 ARG A CD  1 
ATOM   1450 N NE  . ARG A 1 185 ? 12.891 33.775 89.212 1.00 56.74  ? 193 ARG A NE  1 
ATOM   1451 C CZ  . ARG A 1 185 ? 12.158 32.738 89.603 1.00 62.97  ? 193 ARG A CZ  1 
ATOM   1452 N NH1 . ARG A 1 185 ? 10.834 32.793 89.627 1.00 63.96  ? 193 ARG A NH1 1 
ATOM   1453 N NH2 . ARG A 1 185 ? 12.768 31.628 90.008 1.00 63.86  ? 193 ARG A NH2 1 
ATOM   1454 N N   . VAL A 1 186 ? 15.735 36.216 84.896 1.00 33.19  ? 194 VAL A N   1 
ATOM   1455 C CA  . VAL A 1 186 ? 16.577 35.241 84.225 1.00 34.60  ? 194 VAL A CA  1 
ATOM   1456 C C   . VAL A 1 186 ? 16.745 34.041 85.149 1.00 33.77  ? 194 VAL A C   1 
ATOM   1457 O O   . VAL A 1 186 ? 17.453 34.121 86.152 1.00 36.50  ? 194 VAL A O   1 
ATOM   1458 C CB  . VAL A 1 186 ? 17.944 35.850 83.831 1.00 35.92  ? 194 VAL A CB  1 
ATOM   1459 C CG1 . VAL A 1 186 ? 18.835 34.822 83.137 1.00 38.08  ? 194 VAL A CG1 1 
ATOM   1460 C CG2 . VAL A 1 186 ? 17.754 37.085 82.964 1.00 37.28  ? 194 VAL A CG2 1 
ATOM   1461 N N   . ARG A 1 187 ? 16.075 32.938 84.802 1.00 32.07  ? 195 ARG A N   1 
ATOM   1462 C CA  . ARG A 1 187 ? 16.045 31.754 85.645 1.00 31.79  ? 195 ARG A CA  1 
ATOM   1463 C C   . ARG A 1 187 ? 17.220 30.807 85.418 1.00 32.71  ? 195 ARG A C   1 
ATOM   1464 O O   . ARG A 1 187 ? 17.437 29.892 86.205 1.00 34.52  ? 195 ARG A O   1 
ATOM   1465 C CB  . ARG A 1 187 ? 14.752 30.988 85.404 1.00 34.28  ? 195 ARG A CB  1 
ATOM   1466 C CG  . ARG A 1 187 ? 13.500 31.664 85.978 1.00 37.95  ? 195 ARG A CG  1 
ATOM   1467 C CD  . ARG A 1 187 ? 12.301 30.748 85.821 1.00 39.96  ? 195 ARG A CD  1 
ATOM   1468 N NE  . ARG A 1 187 ? 11.053 31.370 86.253 1.00 43.38  ? 195 ARG A NE  1 
ATOM   1469 C CZ  . ARG A 1 187 ? 10.126 30.778 87.004 1.00 47.89  ? 195 ARG A CZ  1 
ATOM   1470 N NH1 . ARG A 1 187 ? 10.255 29.523 87.408 1.00 44.45  ? 195 ARG A NH1 1 
ATOM   1471 N NH2 . ARG A 1 187 ? 9.042  31.465 87.360 1.00 48.66  ? 195 ARG A NH2 1 
ATOM   1472 N N   . GLY A 1 188 ? 17.960 30.994 84.322 1.00 30.12  ? 196 GLY A N   1 
ATOM   1473 C CA  . GLY A 1 188 ? 19.041 30.076 84.010 1.00 29.94  ? 196 GLY A CA  1 
ATOM   1474 C C   . GLY A 1 188 ? 19.916 30.526 82.851 1.00 30.55  ? 196 GLY A C   1 
ATOM   1475 O O   . GLY A 1 188 ? 19.479 31.319 82.021 1.00 28.97  ? 196 GLY A O   1 
ATOM   1476 N N   . TYR A 1 189 ? 21.142 29.985 82.825 1.00 31.11  ? 197 TYR A N   1 
ATOM   1477 C CA  . TYR A 1 189 ? 22.144 30.315 81.828 1.00 30.15  ? 197 TYR A CA  1 
ATOM   1478 C C   . TYR A 1 189 ? 22.652 29.046 81.154 1.00 29.00  ? 197 TYR A C   1 
ATOM   1479 O O   . TYR A 1 189 ? 22.965 28.066 81.828 1.00 29.63  ? 197 TYR A O   1 
ATOM   1480 C CB  . TYR A 1 189 ? 23.326 31.081 82.465 1.00 31.33  ? 197 TYR A CB  1 
ATOM   1481 C CG  . TYR A 1 189 ? 22.907 32.402 83.061 1.00 32.12  ? 197 TYR A CG  1 
ATOM   1482 C CD1 . TYR A 1 189 ? 22.313 32.465 84.315 1.00 33.33  ? 197 TYR A CD1 1 
ATOM   1483 C CD2 . TYR A 1 189 ? 23.043 33.583 82.347 1.00 30.84  ? 197 TYR A CD2 1 
ATOM   1484 C CE1 . TYR A 1 189 ? 21.892 33.676 84.854 1.00 31.81  ? 197 TYR A CE1 1 
ATOM   1485 C CE2 . TYR A 1 189 ? 22.625 34.800 82.877 1.00 32.46  ? 197 TYR A CE2 1 
ATOM   1486 C CZ  . TYR A 1 189 ? 22.046 34.839 84.130 1.00 32.35  ? 197 TYR A CZ  1 
ATOM   1487 O OH  . TYR A 1 189 ? 21.629 36.037 84.661 1.00 35.86  ? 197 TYR A OH  1 
ATOM   1488 N N   . VAL A 1 190 ? 22.736 29.091 79.820 1.00 28.25  ? 198 VAL A N   1 
ATOM   1489 C CA  . VAL A 1 190 ? 23.318 28.023 79.028 1.00 28.68  ? 198 VAL A CA  1 
ATOM   1490 C C   . VAL A 1 190 ? 24.576 28.559 78.355 1.00 28.83  ? 198 VAL A C   1 
ATOM   1491 O O   . VAL A 1 190 ? 24.490 29.479 77.545 1.00 28.09  ? 198 VAL A O   1 
ATOM   1492 C CB  . VAL A 1 190 ? 22.329 27.486 77.986 1.00 28.04  ? 198 VAL A CB  1 
ATOM   1493 C CG1 . VAL A 1 190 ? 22.950 26.343 77.185 1.00 28.26  ? 198 VAL A CG1 1 
ATOM   1494 C CG2 . VAL A 1 190 ? 21.018 27.058 78.639 1.00 30.37  ? 198 VAL A CG2 1 
ATOM   1495 N N   . LEU A 1 191 ? 25.726 27.975 78.718 1.00 29.12  ? 199 LEU A N   1 
ATOM   1496 C CA  . LEU A 1 191 ? 27.024 28.335 78.170 1.00 29.84  ? 199 LEU A CA  1 
ATOM   1497 C C   . LEU A 1 191 ? 27.499 27.223 77.240 1.00 30.41  ? 199 LEU A C   1 
ATOM   1498 O O   . LEU A 1 191 ? 27.809 26.125 77.696 1.00 32.34  ? 199 LEU A O   1 
ATOM   1499 C CB  . LEU A 1 191 ? 28.046 28.526 79.301 1.00 31.86  ? 199 LEU A CB  1 
ATOM   1500 C CG  . LEU A 1 191 ? 28.035 29.858 80.069 1.00 33.83  ? 199 LEU A CG  1 
ATOM   1501 C CD1 . LEU A 1 191 ? 26.667 30.217 80.581 1.00 33.78  ? 199 LEU A CD1 1 
ATOM   1502 C CD2 . LEU A 1 191 ? 28.997 29.801 81.230 1.00 31.85  ? 199 LEU A CD2 1 
ATOM   1503 N N   . MET A 1 192 ? 27.548 27.514 75.935 1.00 29.02  ? 200 MET A N   1 
ATOM   1504 C CA  . MET A 1 192 ? 27.905 26.518 74.938 1.00 30.89  ? 200 MET A CA  1 
ATOM   1505 C C   . MET A 1 192 ? 29.309 26.823 74.426 1.00 29.88  ? 200 MET A C   1 
ATOM   1506 O O   . MET A 1 192 ? 29.542 27.887 73.865 1.00 27.54  ? 200 MET A O   1 
ATOM   1507 C CB  . MET A 1 192 ? 26.891 26.541 73.804 1.00 31.71  ? 200 MET A CB  1 
ATOM   1508 C CG  . MET A 1 192 ? 25.481 26.254 74.288 1.00 33.72  ? 200 MET A CG  1 
ATOM   1509 S SD  . MET A 1 192 ? 24.262 26.119 72.961 1.00 37.45  ? 200 MET A SD  1 
ATOM   1510 C CE  . MET A 1 192 ? 24.545 27.575 72.083 1.00 41.07  ? 200 MET A CE  1 
ATOM   1511 N N   . GLY A 1 193 ? 30.244 25.892 74.645 1.00 28.86  ? 201 GLY A N   1 
ATOM   1512 C CA  . GLY A 1 193 ? 31.638 26.118 74.299 1.00 29.62  ? 201 GLY A CA  1 
ATOM   1513 C C   . GLY A 1 193 ? 32.125 27.508 74.702 1.00 27.28  ? 201 GLY A C   1 
ATOM   1514 O O   . GLY A 1 193 ? 32.680 28.226 73.878 1.00 27.85  ? 201 GLY A O   1 
ATOM   1515 N N   . PRO A 1 194 ? 31.927 27.933 75.971 1.00 27.55  ? 202 PRO A N   1 
ATOM   1516 C CA  . PRO A 1 194 ? 32.185 29.314 76.370 1.00 28.64  ? 202 PRO A CA  1 
ATOM   1517 C C   . PRO A 1 194 ? 33.622 29.763 76.118 1.00 29.55  ? 202 PRO A C   1 
ATOM   1518 O O   . PRO A 1 194 ? 34.563 29.053 76.460 1.00 29.47  ? 202 PRO A O   1 
ATOM   1519 C CB  . PRO A 1 194 ? 31.863 29.317 77.856 1.00 27.23  ? 202 PRO A CB  1 
ATOM   1520 C CG  . PRO A 1 194 ? 31.945 27.898 78.275 1.00 27.77  ? 202 PRO A CG  1 
ATOM   1521 C CD  . PRO A 1 194 ? 31.500 27.090 77.098 1.00 27.60  ? 202 PRO A CD  1 
ATOM   1522 N N   . PHE A 1 195 ? 33.776 30.946 75.519 1.00 29.73  ? 203 PHE A N   1 
ATOM   1523 C CA  . PHE A 1 195 ? 35.089 31.463 75.181 1.00 30.44  ? 203 PHE A CA  1 
ATOM   1524 C C   . PHE A 1 195 ? 35.687 32.131 76.417 1.00 31.31  ? 203 PHE A C   1 
ATOM   1525 O O   . PHE A 1 195 ? 35.556 33.339 76.619 1.00 31.27  ? 203 PHE A O   1 
ATOM   1526 C CB  . PHE A 1 195 ? 35.010 32.403 73.967 1.00 31.30  ? 203 PHE A CB  1 
ATOM   1527 C CG  . PHE A 1 195 ? 36.346 32.894 73.465 1.00 31.82  ? 203 PHE A CG  1 
ATOM   1528 C CD1 . PHE A 1 195 ? 37.454 32.068 73.469 1.00 32.65  ? 203 PHE A CD1 1 
ATOM   1529 C CD2 . PHE A 1 195 ? 36.484 34.169 72.959 1.00 32.79  ? 203 PHE A CD2 1 
ATOM   1530 C CE1 . PHE A 1 195 ? 38.678 32.522 73.001 1.00 30.66  ? 203 PHE A CE1 1 
ATOM   1531 C CE2 . PHE A 1 195 ? 37.707 34.616 72.493 1.00 31.93  ? 203 PHE A CE2 1 
ATOM   1532 C CZ  . PHE A 1 195 ? 38.797 33.791 72.521 1.00 30.39  ? 203 PHE A CZ  1 
ATOM   1533 N N   . PHE A 1 196 ? 36.273 31.289 77.273 1.00 34.10  ? 204 PHE A N   1 
ATOM   1534 C CA  . PHE A 1 196 ? 37.073 31.727 78.401 1.00 34.69  ? 204 PHE A CA  1 
ATOM   1535 C C   . PHE A 1 196 ? 38.542 31.533 78.047 1.00 36.80  ? 204 PHE A C   1 
ATOM   1536 O O   . PHE A 1 196 ? 38.884 30.694 77.213 1.00 33.78  ? 204 PHE A O   1 
ATOM   1537 C CB  . PHE A 1 196 ? 36.743 30.931 79.663 1.00 35.19  ? 204 PHE A CB  1 
ATOM   1538 C CG  . PHE A 1 196 ? 35.338 31.096 80.191 1.00 33.38  ? 204 PHE A CG  1 
ATOM   1539 C CD1 . PHE A 1 196 ? 34.769 32.353 80.314 1.00 32.49  ? 204 PHE A CD1 1 
ATOM   1540 C CD2 . PHE A 1 196 ? 34.608 30.000 80.615 1.00 33.05  ? 204 PHE A CD2 1 
ATOM   1541 C CE1 . PHE A 1 196 ? 33.482 32.501 80.815 1.00 33.04  ? 204 PHE A CE1 1 
ATOM   1542 C CE2 . PHE A 1 196 ? 33.330 30.152 81.129 1.00 33.84  ? 204 PHE A CE2 1 
ATOM   1543 C CZ  . PHE A 1 196 ? 32.773 31.402 81.220 1.00 34.67  ? 204 PHE A CZ  1 
ATOM   1544 N N   . GLY A 1 197 ? 39.401 32.317 78.703 1.00 37.67  ? 205 GLY A N   1 
ATOM   1545 C CA  . GLY A 1 197 ? 40.817 32.326 78.396 1.00 38.85  ? 205 GLY A CA  1 
ATOM   1546 C C   . GLY A 1 197 ? 41.679 32.361 79.653 1.00 41.07  ? 205 GLY A C   1 
ATOM   1547 O O   . GLY A 1 197 ? 41.187 32.623 80.749 1.00 39.05  ? 205 GLY A O   1 
ATOM   1548 N N   . GLY A 1 198 ? 42.972 32.086 79.462 1.00 43.34  ? 206 GLY A N   1 
ATOM   1549 C CA  . GLY A 1 198 ? 43.952 32.168 80.529 1.00 44.69  ? 206 GLY A CA  1 
ATOM   1550 C C   . GLY A 1 198 ? 45.356 32.297 79.949 1.00 45.19  ? 206 GLY A C   1 
ATOM   1551 O O   . GLY A 1 198 ? 45.631 31.805 78.852 1.00 44.15  ? 206 GLY A O   1 
ATOM   1552 N N   . GLU A 1 199 ? 46.230 32.982 80.689 1.00 45.35  ? 207 GLU A N   1 
ATOM   1553 C CA  . GLU A 1 199 ? 47.604 33.152 80.255 1.00 47.94  ? 207 GLU A CA  1 
ATOM   1554 C C   . GLU A 1 199 ? 48.248 31.767 80.173 1.00 44.16  ? 207 GLU A C   1 
ATOM   1555 O O   . GLU A 1 199 ? 48.833 31.411 79.153 1.00 48.54  ? 207 GLU A O   1 
ATOM   1556 C CB  . GLU A 1 199 ? 48.349 34.116 81.190 1.00 49.31  ? 207 GLU A CB  1 
ATOM   1557 C CG  . GLU A 1 199 ? 49.605 34.695 80.572 1.00 54.78  ? 207 GLU A CG  1 
ATOM   1558 C CD  . GLU A 1 199 ? 49.410 35.627 79.391 1.00 56.76  ? 207 GLU A CD  1 
ATOM   1559 O OE1 . GLU A 1 199 ? 48.252 35.979 79.051 1.00 52.74  ? 207 GLU A OE1 1 
ATOM   1560 O OE2 . GLU A 1 199 ? 50.445 36.005 78.797 1.00 58.66  ? 207 GLU A OE2 1 
ATOM   1561 N N   . GLU A 1 200 ? 48.079 30.972 81.231 1.00 43.88  ? 208 GLU A N   1 
ATOM   1562 C CA  . GLU A 1 200 ? 48.519 29.585 81.250 1.00 49.40  ? 208 GLU A CA  1 
ATOM   1563 C C   . GLU A 1 200 ? 47.523 28.681 80.522 1.00 48.89  ? 208 GLU A C   1 
ATOM   1564 O O   . GLU A 1 200 ? 46.313 28.865 80.644 1.00 44.96  ? 208 GLU A O   1 
ATOM   1565 C CB  . GLU A 1 200 ? 48.698 29.143 82.713 1.00 58.42  ? 208 GLU A CB  1 
ATOM   1566 C CG  . GLU A 1 200 ? 48.982 27.664 82.923 1.00 67.46  ? 208 GLU A CG  1 
ATOM   1567 C CD  . GLU A 1 200 ? 49.151 27.277 84.380 1.00 79.24  ? 208 GLU A CD  1 
ATOM   1568 O OE1 . GLU A 1 200 ? 49.085 28.178 85.249 1.00 82.96  ? 208 GLU A OE1 1 
ATOM   1569 O OE2 . GLU A 1 200 ? 49.344 26.071 84.654 1.00 86.04  ? 208 GLU A OE2 1 
ATOM   1570 N N   . ARG A 1 201 ? 48.051 27.692 79.786 1.00 45.51  ? 209 ARG A N   1 
ATOM   1571 C CA  . ARG A 1 201 ? 47.244 26.808 78.958 1.00 44.94  ? 209 ARG A CA  1 
ATOM   1572 C C   . ARG A 1 201 ? 46.751 25.584 79.726 1.00 45.07  ? 209 ARG A C   1 
ATOM   1573 O O   . ARG A 1 201 ? 47.436 25.087 80.614 1.00 49.26  ? 209 ARG A O   1 
ATOM   1574 C CB  . ARG A 1 201 ? 48.043 26.316 77.732 1.00 44.01  ? 209 ARG A CB  1 
ATOM   1575 C CG  . ARG A 1 201 ? 48.219 27.336 76.607 1.00 42.42  ? 209 ARG A CG  1 
ATOM   1576 C CD  . ARG A 1 201 ? 49.062 28.511 77.007 1.00 41.37  ? 209 ARG A CD  1 
ATOM   1577 N NE  . ARG A 1 201 ? 49.566 29.226 75.842 1.00 41.84  ? 209 ARG A NE  1 
ATOM   1578 C CZ  . ARG A 1 201 ? 48.828 29.960 75.023 1.00 43.13  ? 209 ARG A CZ  1 
ATOM   1579 N NH1 . ARG A 1 201 ? 47.564 30.248 75.294 1.00 46.42  ? 209 ARG A NH1 1 
ATOM   1580 N NH2 . ARG A 1 201 ? 49.373 30.420 73.903 1.00 41.56  ? 209 ARG A NH2 1 
ATOM   1581 N N   . THR A 1 202 ? 45.564 25.094 79.356 1.00 42.62  ? 210 THR A N   1 
ATOM   1582 C CA  . THR A 1 202 ? 45.086 23.794 79.799 1.00 41.54  ? 210 THR A CA  1 
ATOM   1583 C C   . THR A 1 202 ? 45.686 22.720 78.898 1.00 42.52  ? 210 THR A C   1 
ATOM   1584 O O   . THR A 1 202 ? 46.277 23.032 77.864 1.00 43.89  ? 210 THR A O   1 
ATOM   1585 C CB  . THR A 1 202 ? 43.555 23.704 79.743 1.00 41.96  ? 210 THR A CB  1 
ATOM   1586 O OG1 . THR A 1 202 ? 43.149 23.699 78.360 1.00 38.38  ? 210 THR A OG1 1 
ATOM   1587 C CG2 . THR A 1 202 ? 42.872 24.839 80.507 1.00 39.44  ? 210 THR A CG2 1 
ATOM   1588 N N   . ASN A 1 203 ? 45.487 21.455 79.277 1.00 44.11  ? 211 ASN A N   1 
ATOM   1589 C CA  . ASN A 1 203 ? 45.918 20.338 78.454 1.00 46.36  ? 211 ASN A CA  1 
ATOM   1590 C C   . ASN A 1 203 ? 45.214 20.323 77.100 1.00 47.92  ? 211 ASN A C   1 
ATOM   1591 O O   . ASN A 1 203 ? 45.869 20.172 76.073 1.00 47.50  ? 211 ASN A O   1 
ATOM   1592 C CB  . ASN A 1 203 ? 45.706 19.012 79.187 1.00 49.97  ? 211 ASN A CB  1 
ATOM   1593 C CG  . ASN A 1 203 ? 46.707 18.769 80.305 1.00 59.01  ? 211 ASN A CG  1 
ATOM   1594 O OD1 . ASN A 1 203 ? 47.786 19.389 80.387 1.00 59.92  ? 211 ASN A OD1 1 
ATOM   1595 N ND2 . ASN A 1 203 ? 46.383 17.837 81.186 1.00 62.27  ? 211 ASN A ND2 1 
ATOM   1596 N N   . SER A 1 204 ? 43.882 20.489 77.097 1.00 45.99  ? 212 SER A N   1 
ATOM   1597 C CA  . SER A 1 204 ? 43.129 20.484 75.851 1.00 41.26  ? 212 SER A CA  1 
ATOM   1598 C C   . SER A 1 204 ? 43.582 21.626 74.942 1.00 38.32  ? 212 SER A C   1 
ATOM   1599 O O   . SER A 1 204 ? 43.664 21.451 73.730 1.00 41.24  ? 212 SER A O   1 
ATOM   1600 C CB  . SER A 1 204 ? 41.614 20.525 76.089 1.00 43.30  ? 212 SER A CB  1 
ATOM   1601 O OG  . SER A 1 204 ? 41.165 21.708 76.733 1.00 40.21  ? 212 SER A OG  1 
ATOM   1602 N N   . GLU A 1 205 ? 43.914 22.782 75.528 1.00 39.52  ? 213 GLU A N   1 
ATOM   1603 C CA  . GLU A 1 205 ? 44.375 23.921 74.747 1.00 40.47  ? 213 GLU A CA  1 
ATOM   1604 C C   . GLU A 1 205 ? 45.692 23.655 74.017 1.00 41.56  ? 213 GLU A C   1 
ATOM   1605 O O   . GLU A 1 205 ? 45.906 24.193 72.930 1.00 40.28  ? 213 GLU A O   1 
ATOM   1606 C CB  . GLU A 1 205 ? 44.485 25.172 75.628 1.00 41.79  ? 213 GLU A CB  1 
ATOM   1607 C CG  . GLU A 1 205 ? 43.125 25.772 75.928 1.00 41.08  ? 213 GLU A CG  1 
ATOM   1608 C CD  . GLU A 1 205 ? 43.065 26.777 77.058 1.00 44.81  ? 213 GLU A CD  1 
ATOM   1609 O OE1 . GLU A 1 205 ? 44.137 27.252 77.503 1.00 41.59  ? 213 GLU A OE1 1 
ATOM   1610 O OE2 . GLU A 1 205 ? 41.933 27.072 77.513 1.00 42.49  ? 213 GLU A OE2 1 
ATOM   1611 N N   . ASN A 1 206 ? 46.553 22.812 74.607 1.00 44.93  ? 214 ASN A N   1 
ATOM   1612 C CA  . ASN A 1 206 ? 47.784 22.378 73.958 1.00 48.71  ? 214 ASN A CA  1 
ATOM   1613 C C   . ASN A 1 206 ? 47.608 21.147 73.067 1.00 48.85  ? 214 ASN A C   1 
ATOM   1614 O O   . ASN A 1 206 ? 48.584 20.624 72.535 1.00 49.27  ? 214 ASN A O   1 
ATOM   1615 C CB  . ASN A 1 206 ? 48.876 22.070 75.003 1.00 47.52  ? 214 ASN A CB  1 
ATOM   1616 C CG  . ASN A 1 206 ? 49.424 23.273 75.716 1.00 48.06  ? 214 ASN A CG  1 
ATOM   1617 O OD1 . ASN A 1 206 ? 49.537 23.293 76.945 1.00 51.35  ? 214 ASN A OD1 1 
ATOM   1618 N ND2 . ASN A 1 206 ? 49.820 24.291 74.974 1.00 51.19  ? 214 ASN A ND2 1 
ATOM   1619 N N   . GLY A 1 207 ? 46.363 20.689 72.901 1.00 47.32  ? 215 GLY A N   1 
ATOM   1620 C CA  . GLY A 1 207 ? 46.081 19.489 72.133 1.00 45.90  ? 215 GLY A CA  1 
ATOM   1621 C C   . GLY A 1 207 ? 46.030 19.745 70.630 1.00 47.69  ? 215 GLY A C   1 
ATOM   1622 O O   . GLY A 1 207 ? 46.464 20.790 70.151 1.00 43.87  ? 215 GLY A O   1 
ATOM   1623 N N   . PRO A 1 208 ? 45.500 18.793 69.832 1.00 48.44  ? 216 PRO A N   1 
ATOM   1624 C CA  . PRO A 1 208 ? 45.375 18.999 68.395 1.00 48.65  ? 216 PRO A CA  1 
ATOM   1625 C C   . PRO A 1 208 ? 44.424 20.139 68.043 1.00 46.83  ? 216 PRO A C   1 
ATOM   1626 O O   . PRO A 1 208 ? 43.407 20.324 68.707 1.00 47.38  ? 216 PRO A O   1 
ATOM   1627 C CB  . PRO A 1 208 ? 44.833 17.653 67.887 1.00 51.60  ? 216 PRO A CB  1 
ATOM   1628 C CG  . PRO A 1 208 ? 45.036 16.670 69.034 1.00 51.76  ? 216 PRO A CG  1 
ATOM   1629 C CD  . PRO A 1 208 ? 45.003 17.484 70.284 1.00 49.65  ? 216 PRO A CD  1 
ATOM   1630 N N   . SER A 1 209 ? 44.774 20.900 67.001 1.00 43.03  ? 217 SER A N   1 
ATOM   1631 C CA  . SER A 1 209 ? 43.877 21.895 66.441 1.00 43.36  ? 217 SER A CA  1 
ATOM   1632 C C   . SER A 1 209 ? 42.584 21.246 65.952 1.00 45.47  ? 217 SER A C   1 
ATOM   1633 O O   . SER A 1 209 ? 42.553 20.041 65.717 1.00 44.35  ? 217 SER A O   1 
ATOM   1634 C CB  . SER A 1 209 ? 44.554 22.638 65.300 1.00 41.71  ? 217 SER A CB  1 
ATOM   1635 O OG  . SER A 1 209 ? 45.620 23.435 65.779 1.00 46.78  ? 217 SER A OG  1 
ATOM   1636 N N   . GLU A 1 210 ? 41.531 22.062 65.798 1.00 46.05  ? 218 GLU A N   1 
ATOM   1637 C CA  . GLU A 1 210 ? 40.229 21.604 65.331 1.00 44.51  ? 218 GLU A CA  1 
ATOM   1638 C C   . GLU A 1 210 ? 40.024 21.924 63.850 1.00 41.42  ? 218 GLU A C   1 
ATOM   1639 O O   . GLU A 1 210 ? 40.862 22.560 63.218 1.00 44.05  ? 218 GLU A O   1 
ATOM   1640 C CB  . GLU A 1 210 ? 39.091 22.278 66.140 1.00 41.94  ? 218 GLU A CB  1 
ATOM   1641 C CG  . GLU A 1 210 ? 39.161 22.114 67.651 1.00 39.46  ? 218 GLU A CG  1 
ATOM   1642 C CD  . GLU A 1 210 ? 38.006 22.777 68.388 1.00 38.48  ? 218 GLU A CD  1 
ATOM   1643 O OE1 . GLU A 1 210 ? 36.940 22.985 67.757 1.00 33.27  ? 218 GLU A OE1 1 
ATOM   1644 O OE2 . GLU A 1 210 ? 38.180 23.125 69.582 1.00 36.42  ? 218 GLU A OE2 1 
ATOM   1645 N N   . ALA A 1 211 ? 38.882 21.488 63.311 1.00 41.57  ? 219 ALA A N   1 
ATOM   1646 C CA  . ALA A 1 211 ? 38.473 21.800 61.950 1.00 40.26  ? 219 ALA A CA  1 
ATOM   1647 C C   . ALA A 1 211 ? 38.607 23.286 61.604 1.00 41.83  ? 219 ALA A C   1 
ATOM   1648 O O   . ALA A 1 211 ? 38.996 23.631 60.486 1.00 40.27  ? 219 ALA A O   1 
ATOM   1649 C CB  . ALA A 1 211 ? 37.038 21.333 61.739 1.00 37.99  ? 219 ALA A CB  1 
ATOM   1650 N N   . LEU A 1 212 ? 38.291 24.161 62.572 1.00 38.06  ? 220 LEU A N   1 
ATOM   1651 C CA  . LEU A 1 212 ? 38.440 25.596 62.380 1.00 38.81  ? 220 LEU A CA  1 
ATOM   1652 C C   . LEU A 1 212 ? 39.317 26.226 63.462 1.00 38.90  ? 220 LEU A C   1 
ATOM   1653 O O   . LEU A 1 212 ? 40.272 26.926 63.135 1.00 38.47  ? 220 LEU A O   1 
ATOM   1654 C CB  . LEU A 1 212 ? 37.055 26.288 62.303 1.00 40.08  ? 220 LEU A CB  1 
ATOM   1655 C CG  . LEU A 1 212 ? 37.076 27.755 61.803 1.00 41.10  ? 220 LEU A CG  1 
ATOM   1656 C CD1 . LEU A 1 212 ? 35.810 28.120 61.063 1.00 42.34  ? 220 LEU A CD1 1 
ATOM   1657 C CD2 . LEU A 1 212 ? 37.268 28.734 62.951 1.00 43.85  ? 220 LEU A CD2 1 
ATOM   1658 N N   . LEU A 1 213 ? 39.004 25.979 64.740 1.00 36.34  ? 221 LEU A N   1 
ATOM   1659 C CA  . LEU A 1 213 ? 39.738 26.594 65.837 1.00 38.21  ? 221 LEU A CA  1 
ATOM   1660 C C   . LEU A 1 213 ? 41.149 26.025 65.988 1.00 37.36  ? 221 LEU A C   1 
ATOM   1661 O O   . LEU A 1 213 ? 41.350 24.818 65.886 1.00 37.13  ? 221 LEU A O   1 
ATOM   1662 C CB  . LEU A 1 213 ? 39.006 26.395 67.175 1.00 37.57  ? 221 LEU A CB  1 
ATOM   1663 C CG  . LEU A 1 213 ? 37.646 27.064 67.324 1.00 39.77  ? 221 LEU A CG  1 
ATOM   1664 C CD1 . LEU A 1 213 ? 37.134 26.900 68.747 1.00 39.77  ? 221 LEU A CD1 1 
ATOM   1665 C CD2 . LEU A 1 213 ? 37.703 28.535 66.935 1.00 42.04  ? 221 LEU A CD2 1 
ATOM   1666 N N   . SER A 1 214 ? 42.110 26.922 66.232 1.00 36.01  ? 222 SER A N   1 
ATOM   1667 C CA  . SER A 1 214 ? 43.419 26.565 66.757 1.00 36.08  ? 222 SER A CA  1 
ATOM   1668 C C   . SER A 1 214 ? 43.709 27.444 67.968 1.00 35.39  ? 222 SER A C   1 
ATOM   1669 O O   . SER A 1 214 ? 43.066 28.478 68.148 1.00 33.02  ? 222 SER A O   1 
ATOM   1670 C CB  . SER A 1 214 ? 44.509 26.751 65.707 1.00 32.32  ? 222 SER A CB  1 
ATOM   1671 O OG  . SER A 1 214 ? 44.614 28.126 65.382 1.00 33.44  ? 222 SER A OG  1 
ATOM   1672 N N   . LEU A 1 215 ? 44.694 27.037 68.775 1.00 35.84  ? 223 LEU A N   1 
ATOM   1673 C CA  . LEU A 1 215 ? 45.106 27.825 69.919 1.00 36.56  ? 223 LEU A CA  1 
ATOM   1674 C C   . LEU A 1 215 ? 45.625 29.188 69.465 1.00 36.98  ? 223 LEU A C   1 
ATOM   1675 O O   . LEU A 1 215 ? 45.324 30.205 70.085 1.00 37.21  ? 223 LEU A O   1 
ATOM   1676 C CB  . LEU A 1 215 ? 46.161 27.091 70.747 1.00 39.48  ? 223 LEU A CB  1 
ATOM   1677 C CG  . LEU A 1 215 ? 46.625 27.848 72.007 1.00 40.79  ? 223 LEU A CG  1 
ATOM   1678 C CD1 . LEU A 1 215 ? 45.469 28.059 72.980 1.00 43.56  ? 223 LEU A CD1 1 
ATOM   1679 C CD2 . LEU A 1 215 ? 47.760 27.119 72.690 1.00 41.23  ? 223 LEU A CD2 1 
ATOM   1680 N N   . ASP A 1 216 ? 46.393 29.205 68.372 1.00 35.26  ? 224 ASP A N   1 
ATOM   1681 C CA  . ASP A 1 216 ? 46.829 30.456 67.778 1.00 34.75  ? 224 ASP A CA  1 
ATOM   1682 C C   . ASP A 1 216 ? 45.657 31.382 67.441 1.00 34.35  ? 224 ASP A C   1 
ATOM   1683 O O   . ASP A 1 216 ? 45.725 32.584 67.678 1.00 34.31  ? 224 ASP A O   1 
ATOM   1684 C CB  . ASP A 1 216 ? 47.667 30.180 66.522 1.00 36.56  ? 224 ASP A CB  1 
ATOM   1685 C CG  . ASP A 1 216 ? 49.094 29.707 66.787 1.00 38.08  ? 224 ASP A CG  1 
ATOM   1686 O OD1 . ASP A 1 216 ? 49.544 29.774 67.953 1.00 40.04  ? 224 ASP A OD1 1 
ATOM   1687 O OD2 . ASP A 1 216 ? 49.739 29.264 65.846 1.00 39.80  ? 224 ASP A OD2 1 
ATOM   1688 N N   . LEU A 1 217 ? 44.579 30.828 66.879 1.00 33.42  ? 225 LEU A N   1 
ATOM   1689 C CA  . LEU A 1 217 ? 43.435 31.647 66.509 1.00 35.11  ? 225 LEU A CA  1 
ATOM   1690 C C   . LEU A 1 217 ? 42.771 32.223 67.758 1.00 32.45  ? 225 LEU A C   1 
ATOM   1691 O O   . LEU A 1 217 ? 42.422 33.403 67.788 1.00 33.45  ? 225 LEU A O   1 
ATOM   1692 C CB  . LEU A 1 217 ? 42.423 30.852 65.673 1.00 35.15  ? 225 LEU A CB  1 
ATOM   1693 C CG  . LEU A 1 217 ? 41.151 31.604 65.274 1.00 35.68  ? 225 LEU A CG  1 
ATOM   1694 C CD1 . LEU A 1 217 ? 41.464 32.821 64.409 1.00 35.01  ? 225 LEU A CD1 1 
ATOM   1695 C CD2 . LEU A 1 217 ? 40.192 30.688 64.547 1.00 37.18  ? 225 LEU A CD2 1 
ATOM   1696 N N   . LEU A 1 218 ? 42.622 31.385 68.786 1.00 32.36  ? 226 LEU A N   1 
ATOM   1697 C CA  . LEU A 1 218 ? 41.993 31.800 70.028 1.00 34.84  ? 226 LEU A CA  1 
ATOM   1698 C C   . LEU A 1 218 ? 42.791 32.917 70.698 1.00 35.07  ? 226 LEU A C   1 
ATOM   1699 O O   . LEU A 1 218 ? 42.205 33.896 71.156 1.00 32.48  ? 226 LEU A O   1 
ATOM   1700 C CB  . LEU A 1 218 ? 41.839 30.606 70.980 1.00 33.61  ? 226 LEU A CB  1 
ATOM   1701 C CG  . LEU A 1 218 ? 40.860 29.516 70.548 1.00 34.92  ? 226 LEU A CG  1 
ATOM   1702 C CD1 . LEU A 1 218 ? 40.765 28.444 71.584 1.00 32.61  ? 226 LEU A CD1 1 
ATOM   1703 C CD2 . LEU A 1 218 ? 39.458 30.074 70.259 1.00 36.39  ? 226 LEU A CD2 1 
ATOM   1704 N N   . ASP A 1 219 ? 44.126 32.764 70.735 1.00 34.61  ? 227 ASP A N   1 
ATOM   1705 C CA  . ASP A 1 219 ? 45.014 33.788 71.268 1.00 33.59  ? 227 ASP A CA  1 
ATOM   1706 C C   . ASP A 1 219 ? 44.871 35.114 70.536 1.00 34.01  ? 227 ASP A C   1 
ATOM   1707 O O   . ASP A 1 219 ? 44.927 36.172 71.158 1.00 37.10  ? 227 ASP A O   1 
ATOM   1708 C CB  . ASP A 1 219 ? 46.493 33.359 71.168 1.00 35.21  ? 227 ASP A CB  1 
ATOM   1709 C CG  . ASP A 1 219 ? 46.915 32.264 72.111 1.00 35.13  ? 227 ASP A CG  1 
ATOM   1710 O OD1 . ASP A 1 219 ? 46.165 31.978 73.067 1.00 38.58  ? 227 ASP A OD1 1 
ATOM   1711 O OD2 . ASP A 1 219 ? 47.991 31.671 71.884 1.00 43.46  ? 227 ASP A OD2 1 
ATOM   1712 N N   . LYS A 1 220 ? 44.709 35.033 69.212 1.00 35.06  ? 228 LYS A N   1 
ATOM   1713 C CA  . LYS A 1 220 ? 44.567 36.212 68.378 1.00 35.01  ? 228 LYS A CA  1 
ATOM   1714 C C   . LYS A 1 220 ? 43.257 36.939 68.685 1.00 35.03  ? 228 LYS A C   1 
ATOM   1715 O O   . LYS A 1 220 ? 43.210 38.170 68.691 1.00 33.16  ? 228 LYS A O   1 
ATOM   1716 C CB  . LYS A 1 220 ? 44.660 35.810 66.905 1.00 37.96  ? 228 LYS A CB  1 
ATOM   1717 C CG  . LYS A 1 220 ? 44.622 36.973 65.908 1.00 42.02  ? 228 LYS A CG  1 
ATOM   1718 C CD  . LYS A 1 220 ? 45.853 37.902 65.981 1.00 49.55  ? 228 LYS A CD  1 
ATOM   1719 C CE  . LYS A 1 220 ? 47.142 37.245 65.513 1.00 54.10  ? 228 LYS A CE  1 
ATOM   1720 N NZ  . LYS A 1 220 ? 48.332 38.083 65.838 1.00 58.93  ? 228 LYS A NZ  1 
ATOM   1721 N N   . PHE A 1 221 ? 42.188 36.176 68.943 1.00 33.09  ? 229 PHE A N   1 
ATOM   1722 C CA  . PHE A 1 221 ? 40.922 36.781 69.322 1.00 31.81  ? 229 PHE A CA  1 
ATOM   1723 C C   . PHE A 1 221 ? 41.086 37.616 70.588 1.00 31.54  ? 229 PHE A C   1 
ATOM   1724 O O   . PHE A 1 221 ? 40.638 38.760 70.626 1.00 33.05  ? 229 PHE A O   1 
ATOM   1725 C CB  . PHE A 1 221 ? 39.816 35.740 69.551 1.00 33.16  ? 229 PHE A CB  1 
ATOM   1726 C CG  . PHE A 1 221 ? 39.242 35.063 68.333 1.00 31.95  ? 229 PHE A CG  1 
ATOM   1727 C CD1 . PHE A 1 221 ? 38.977 35.779 67.180 1.00 31.54  ? 229 PHE A CD1 1 
ATOM   1728 C CD2 . PHE A 1 221 ? 38.908 33.721 68.363 1.00 35.13  ? 229 PHE A CD2 1 
ATOM   1729 C CE1 . PHE A 1 221 ? 38.421 35.158 66.074 1.00 33.97  ? 229 PHE A CE1 1 
ATOM   1730 C CE2 . PHE A 1 221 ? 38.350 33.102 67.257 1.00 33.83  ? 229 PHE A CE2 1 
ATOM   1731 C CZ  . PHE A 1 221 ? 38.104 33.820 66.122 1.00 34.11  ? 229 PHE A CZ  1 
ATOM   1732 N N   . TRP A 1 222 ? 41.728 37.036 71.611 1.00 32.97  ? 230 TRP A N   1 
ATOM   1733 C CA  . TRP A 1 222 ? 42.003 37.750 72.850 1.00 35.47  ? 230 TRP A CA  1 
ATOM   1734 C C   . TRP A 1 222 ? 42.889 38.974 72.642 1.00 39.28  ? 230 TRP A C   1 
ATOM   1735 O O   . TRP A 1 222 ? 42.676 40.012 73.268 1.00 37.92  ? 230 TRP A O   1 
ATOM   1736 C CB  . TRP A 1 222 ? 42.675 36.846 73.889 1.00 34.61  ? 230 TRP A CB  1 
ATOM   1737 C CG  . TRP A 1 222 ? 41.808 35.762 74.430 1.00 33.22  ? 230 TRP A CG  1 
ATOM   1738 C CD1 . TRP A 1 222 ? 42.093 34.435 74.475 1.00 34.27  ? 230 TRP A CD1 1 
ATOM   1739 C CD2 . TRP A 1 222 ? 40.517 35.917 75.025 1.00 33.06  ? 230 TRP A CD2 1 
ATOM   1740 N NE1 . TRP A 1 222 ? 41.057 33.747 75.055 1.00 33.18  ? 230 TRP A NE1 1 
ATOM   1741 C CE2 . TRP A 1 222 ? 40.077 34.635 75.409 1.00 33.05  ? 230 TRP A CE2 1 
ATOM   1742 C CE3 . TRP A 1 222 ? 39.682 37.016 75.265 1.00 31.64  ? 230 TRP A CE3 1 
ATOM   1743 C CZ2 . TRP A 1 222 ? 38.836 34.420 76.014 1.00 34.12  ? 230 TRP A CZ2 1 
ATOM   1744 C CZ3 . TRP A 1 222 ? 38.457 36.801 75.870 1.00 34.19  ? 230 TRP A CZ3 1 
ATOM   1745 C CH2 . TRP A 1 222 ? 38.045 35.517 76.238 1.00 33.52  ? 230 TRP A CH2 1 
ATOM   1746 N N   . ARG A 1 223 ? 43.889 38.839 71.768 1.00 39.80  ? 231 ARG A N   1 
ATOM   1747 C CA  . ARG A 1 223 ? 44.777 39.948 71.460 1.00 43.39  ? 231 ARG A CA  1 
ATOM   1748 C C   . ARG A 1 223 ? 43.987 41.098 70.839 1.00 38.00  ? 231 ARG A C   1 
ATOM   1749 O O   . ARG A 1 223 ? 44.227 42.255 71.159 1.00 38.50  ? 231 ARG A O   1 
ATOM   1750 C CB  . ARG A 1 223 ? 45.923 39.490 70.536 1.00 48.27  ? 231 ARG A CB  1 
ATOM   1751 C CG  . ARG A 1 223 ? 46.936 40.581 70.209 1.00 58.10  ? 231 ARG A CG  1 
ATOM   1752 C CD  . ARG A 1 223 ? 48.249 40.001 69.683 1.00 67.28  ? 231 ARG A CD  1 
ATOM   1753 N NE  . ARG A 1 223 ? 49.127 41.021 69.113 1.00 73.96  ? 231 ARG A NE  1 
ATOM   1754 C CZ  . ARG A 1 223 ? 49.705 41.998 69.804 1.00 77.38  ? 231 ARG A CZ  1 
ATOM   1755 N NH1 . ARG A 1 223 ? 49.783 41.960 71.124 1.00 76.31  ? 231 ARG A NH1 1 
ATOM   1756 N NH2 . ARG A 1 223 ? 50.234 43.031 69.152 1.00 77.25  ? 231 ARG A NH2 1 
ATOM   1757 N N   . LEU A 1 224 ? 43.034 40.773 69.959 1.00 35.10  ? 232 LEU A N   1 
ATOM   1758 C CA  . LEU A 1 224 ? 42.224 41.788 69.303 1.00 34.81  ? 232 LEU A CA  1 
ATOM   1759 C C   . LEU A 1 224 ? 41.073 42.312 70.164 1.00 32.08  ? 232 LEU A C   1 
ATOM   1760 O O   . LEU A 1 224 ? 40.584 43.410 69.921 1.00 34.87  ? 232 LEU A O   1 
ATOM   1761 C CB  . LEU A 1 224 ? 41.662 41.221 67.992 1.00 35.45  ? 232 LEU A CB  1 
ATOM   1762 C CG  . LEU A 1 224 ? 42.698 40.979 66.904 1.00 37.46  ? 232 LEU A CG  1 
ATOM   1763 C CD1 . LEU A 1 224 ? 42.111 40.233 65.735 1.00 38.73  ? 232 LEU A CD1 1 
ATOM   1764 C CD2 . LEU A 1 224 ? 43.284 42.283 66.430 1.00 39.17  ? 232 LEU A CD2 1 
ATOM   1765 N N   . SER A 1 225 ? 40.641 41.517 71.150 1.00 32.48  ? 233 SER A N   1 
ATOM   1766 C CA  . SER A 1 225 ? 39.430 41.785 71.916 1.00 36.63  ? 233 SER A CA  1 
ATOM   1767 C C   . SER A 1 225 ? 39.668 42.445 73.269 1.00 36.94  ? 233 SER A C   1 
ATOM   1768 O O   . SER A 1 225 ? 38.884 43.293 73.688 1.00 37.62  ? 233 SER A O   1 
ATOM   1769 C CB  . SER A 1 225 ? 38.667 40.483 72.161 1.00 35.88  ? 233 SER A CB  1 
ATOM   1770 O OG  . SER A 1 225 ? 38.187 39.996 70.923 1.00 47.04  ? 233 SER A OG  1 
ATOM   1771 N N   . LEU A 1 226 ? 40.728 42.011 73.959 1.00 36.71  ? 234 LEU A N   1 
ATOM   1772 C CA  . LEU A 1 226 ? 41.046 42.552 75.269 1.00 39.17  ? 234 LEU A CA  1 
ATOM   1773 C C   . LEU A 1 226 ? 41.613 43.963 75.142 1.00 40.68  ? 234 LEU A C   1 
ATOM   1774 O O   . LEU A 1 226 ? 42.150 44.330 74.098 1.00 40.21  ? 234 LEU A O   1 
ATOM   1775 C CB  . LEU A 1 226 ? 42.024 41.648 75.997 1.00 39.69  ? 234 LEU A CB  1 
ATOM   1776 C CG  . LEU A 1 226 ? 41.450 40.307 76.417 1.00 39.54  ? 234 LEU A CG  1 
ATOM   1777 C CD1 . LEU A 1 226 ? 42.527 39.405 76.961 1.00 40.02  ? 234 LEU A CD1 1 
ATOM   1778 C CD2 . LEU A 1 226 ? 40.356 40.474 77.453 1.00 38.89  ? 234 LEU A CD2 1 
ATOM   1779 N N   . PRO A 1 227 ? 41.472 44.814 76.184 1.00 44.26  ? 235 PRO A N   1 
ATOM   1780 C CA  . PRO A 1 227 ? 42.061 46.144 76.145 1.00 49.09  ? 235 PRO A CA  1 
ATOM   1781 C C   . PRO A 1 227 ? 43.570 46.071 75.953 1.00 44.60  ? 235 PRO A C   1 
ATOM   1782 O O   . PRO A 1 227 ? 44.203 45.110 76.391 1.00 42.88  ? 235 PRO A O   1 
ATOM   1783 C CB  . PRO A 1 227 ? 41.680 46.764 77.500 1.00 47.14  ? 235 PRO A CB  1 
ATOM   1784 C CG  . PRO A 1 227 ? 40.641 45.871 78.086 1.00 47.10  ? 235 PRO A CG  1 
ATOM   1785 C CD  . PRO A 1 227 ? 40.783 44.520 77.448 1.00 44.73  ? 235 PRO A CD  1 
ATOM   1786 N N   . ASN A 1 228 ? 44.117 47.077 75.270 1.00 51.10  ? 236 ASN A N   1 
ATOM   1787 C CA  . ASN A 1 228 ? 45.536 47.121 74.970 1.00 56.64  ? 236 ASN A CA  1 
ATOM   1788 C C   . ASN A 1 228 ? 46.341 46.898 76.247 1.00 53.55  ? 236 ASN A C   1 
ATOM   1789 O O   . ASN A 1 228 ? 46.121 47.581 77.246 1.00 56.43  ? 236 ASN A O   1 
ATOM   1790 C CB  . ASN A 1 228 ? 45.896 48.456 74.328 1.00 65.56  ? 236 ASN A CB  1 
ATOM   1791 C CG  . ASN A 1 228 ? 47.069 48.342 73.405 1.00 74.37  ? 236 ASN A CG  1 
ATOM   1792 O OD1 . ASN A 1 228 ? 48.193 48.042 73.823 1.00 81.03  ? 236 ASN A OD1 1 
ATOM   1793 N ND2 . ASN A 1 228 ? 46.821 48.564 72.120 1.00 77.92  ? 236 ASN A ND2 1 
ATOM   1794 N N   . GLY A 1 229 ? 47.239 45.908 76.216 1.00 52.66  ? 237 GLY A N   1 
ATOM   1795 C CA  . GLY A 1 229 ? 48.130 45.633 77.331 1.00 50.54  ? 237 GLY A CA  1 
ATOM   1796 C C   . GLY A 1 229 ? 47.606 44.614 78.338 1.00 51.03  ? 237 GLY A C   1 
ATOM   1797 O O   . GLY A 1 229 ? 48.358 44.163 79.197 1.00 49.94  ? 237 GLY A O   1 
ATOM   1798 N N   . ALA A 1 230 ? 46.321 44.246 78.231 1.00 51.30  ? 238 ALA A N   1 
ATOM   1799 C CA  . ALA A 1 230 ? 45.748 43.243 79.116 1.00 48.96  ? 238 ALA A CA  1 
ATOM   1800 C C   . ALA A 1 230 ? 46.323 41.881 78.753 1.00 44.73  ? 238 ALA A C   1 
ATOM   1801 O O   . ALA A 1 230 ? 46.731 41.667 77.618 1.00 47.18  ? 238 ALA A O   1 
ATOM   1802 C CB  . ALA A 1 230 ? 44.236 43.218 79.011 1.00 51.64  ? 238 ALA A CB  1 
ATOM   1803 N N   . THR A 1 231 ? 46.373 40.979 79.733 1.00 44.66  ? 239 THR A N   1 
ATOM   1804 C CA  . THR A 1 231 ? 46.754 39.601 79.488 1.00 44.88  ? 239 THR A CA  1 
ATOM   1805 C C   . THR A 1 231 ? 45.470 38.779 79.441 1.00 42.54  ? 239 THR A C   1 
ATOM   1806 O O   . THR A 1 231 ? 44.391 39.293 79.725 1.00 41.86  ? 239 THR A O   1 
ATOM   1807 C CB  . THR A 1 231 ? 47.712 39.092 80.564 1.00 45.69  ? 239 THR A CB  1 
ATOM   1808 O OG1 . THR A 1 231 ? 46.994 38.985 81.799 1.00 48.73  ? 239 THR A OG1 1 
ATOM   1809 C CG2 . THR A 1 231 ? 48.938 39.994 80.731 1.00 46.54  ? 239 THR A CG2 1 
ATOM   1810 N N   . ARG A 1 232 ? 45.614 37.494 79.120 1.00 41.85  ? 240 ARG A N   1 
ATOM   1811 C CA  . ARG A 1 232 ? 44.491 36.572 79.098 1.00 43.76  ? 240 ARG A CA  1 
ATOM   1812 C C   . ARG A 1 232 ? 43.988 36.182 80.485 1.00 45.01  ? 240 ARG A C   1 
ATOM   1813 O O   . ARG A 1 232 ? 43.023 35.427 80.595 1.00 41.80  ? 240 ARG A O   1 
ATOM   1814 C CB  . ARG A 1 232 ? 44.875 35.307 78.333 1.00 38.86  ? 240 ARG A CB  1 
ATOM   1815 C CG  . ARG A 1 232 ? 45.155 35.556 76.873 1.00 39.81  ? 240 ARG A CG  1 
ATOM   1816 C CD  . ARG A 1 232 ? 45.282 34.249 76.132 1.00 42.34  ? 240 ARG A CD  1 
ATOM   1817 N NE  . ARG A 1 232 ? 46.467 33.507 76.541 1.00 42.70  ? 240 ARG A NE  1 
ATOM   1818 C CZ  . ARG A 1 232 ? 47.689 33.731 76.074 1.00 41.71  ? 240 ARG A CZ  1 
ATOM   1819 N NH1 . ARG A 1 232 ? 47.910 34.609 75.110 1.00 40.76  ? 240 ARG A NH1 1 
ATOM   1820 N NH2 . ARG A 1 232 ? 48.712 33.046 76.577 1.00 41.04  ? 240 ARG A NH2 1 
ATOM   1821 N N   . ASP A 1 233 ? 44.648 36.675 81.545 1.00 44.47  ? 241 ASP A N   1 
ATOM   1822 C CA  . ASP A 1 233 ? 44.142 36.476 82.896 1.00 43.12  ? 241 ASP A CA  1 
ATOM   1823 C C   . ASP A 1 233 ? 43.257 37.633 83.356 1.00 37.14  ? 241 ASP A C   1 
ATOM   1824 O O   . ASP A 1 233 ? 42.695 37.582 84.445 1.00 38.58  ? 241 ASP A O   1 
ATOM   1825 C CB  . ASP A 1 233 ? 45.296 36.218 83.889 1.00 46.99  ? 241 ASP A CB  1 
ATOM   1826 C CG  . ASP A 1 233 ? 45.854 34.804 83.857 1.00 50.51  ? 241 ASP A CG  1 
ATOM   1827 O OD1 . ASP A 1 233 ? 45.197 33.913 83.266 1.00 48.47  ? 241 ASP A OD1 1 
ATOM   1828 O OD2 . ASP A 1 233 ? 46.949 34.585 84.415 1.00 51.39  ? 241 ASP A OD2 1 
ATOM   1829 N N   . HIS A 1 234 ? 43.101 38.660 82.512 1.00 38.03  ? 242 HIS A N   1 
ATOM   1830 C CA  . HIS A 1 234 ? 42.118 39.701 82.768 1.00 40.17  ? 242 HIS A CA  1 
ATOM   1831 C C   . HIS A 1 234 ? 40.766 39.037 83.030 1.00 42.47  ? 242 HIS A C   1 
ATOM   1832 O O   . HIS A 1 234 ? 40.465 38.002 82.434 1.00 40.81  ? 242 HIS A O   1 
ATOM   1833 C CB  . HIS A 1 234 ? 42.052 40.678 81.594 1.00 40.10  ? 242 HIS A CB  1 
ATOM   1834 C CG  . HIS A 1 234 ? 41.319 41.949 81.896 1.00 42.90  ? 242 HIS A CG  1 
ATOM   1835 N ND1 . HIS A 1 234 ? 39.970 41.953 82.212 1.00 43.03  ? 242 HIS A ND1 1 
ATOM   1836 C CD2 . HIS A 1 234 ? 41.776 43.220 81.919 1.00 43.52  ? 242 HIS A CD2 1 
ATOM   1837 C CE1 . HIS A 1 234 ? 39.649 43.223 82.421 1.00 46.89  ? 242 HIS A CE1 1 
ATOM   1838 N NE2 . HIS A 1 234 ? 40.712 44.022 82.247 1.00 47.02  ? 242 HIS A NE2 1 
ATOM   1839 N N   . HIS A 1 235 ? 39.965 39.594 83.941 1.00 41.29  ? 243 HIS A N   1 
ATOM   1840 C CA  . HIS A 1 235 ? 38.674 38.973 84.361 1.00 44.35  ? 243 HIS A CA  1 
ATOM   1841 C C   . HIS A 1 235 ? 37.652 38.840 83.223 1.00 41.11  ? 243 HIS A C   1 
ATOM   1842 O O   . HIS A 1 235 ? 36.739 38.013 83.325 1.00 41.68  ? 243 HIS A O   1 
ATOM   1843 C CB  . HIS A 1 235 ? 38.074 39.759 85.531 1.00 46.69  ? 243 HIS A CB  1 
ATOM   1844 C CG  . HIS A 1 235 ? 37.645 41.148 85.222 1.00 49.69  ? 243 HIS A CG  1 
ATOM   1845 N ND1 . HIS A 1 235 ? 38.438 42.241 85.484 1.00 58.81  ? 243 HIS A ND1 1 
ATOM   1846 C CD2 . HIS A 1 235 ? 36.512 41.628 84.705 1.00 52.30  ? 243 HIS A CD2 1 
ATOM   1847 C CE1 . HIS A 1 235 ? 37.796 43.339 85.120 1.00 59.10  ? 243 HIS A CE1 1 
ATOM   1848 N NE2 . HIS A 1 235 ? 36.627 42.989 84.640 1.00 52.95  ? 243 HIS A NE2 1 
ATOM   1849 N N   . MET A 1 236 ? 37.803 39.629 82.170 1.00 39.65  ? 244 MET A N   1 
ATOM   1850 C CA  . MET A 1 236 ? 36.856 39.599 81.029 1.00 41.90  ? 244 MET A CA  1 
ATOM   1851 C C   . MET A 1 236 ? 37.127 38.352 80.176 1.00 39.96  ? 244 MET A C   1 
ATOM   1852 O O   . MET A 1 236 ? 36.282 38.025 79.333 1.00 39.04  ? 244 MET A O   1 
ATOM   1853 C CB  . MET A 1 236 ? 37.007 40.887 80.217 1.00 39.66  ? 244 MET A CB  1 
ATOM   1854 C CG  . MET A 1 236 ? 36.499 42.118 80.935 1.00 39.18  ? 244 MET A CG  1 
ATOM   1855 S SD  . MET A 1 236 ? 36.717 43.616 79.958 1.00 42.03  ? 244 MET A SD  1 
ATOM   1856 C CE  . MET A 1 236 ? 38.267 43.152 79.184 1.00 46.06  ? 244 MET A CE  1 
ATOM   1857 N N   . ALA A 1 237 ? 38.257 37.691 80.410 1.00 38.78  ? 245 ALA A N   1 
ATOM   1858 C CA  . ALA A 1 237 ? 38.619 36.460 79.681 1.00 38.13  ? 245 ALA A CA  1 
ATOM   1859 C C   . ALA A 1 237 ? 38.627 35.284 80.645 1.00 37.36  ? 245 ALA A C   1 
ATOM   1860 O O   . ALA A 1 237 ? 38.081 34.228 80.323 1.00 33.12  ? 245 ALA A O   1 
ATOM   1861 C CB  . ALA A 1 237 ? 39.984 36.646 79.095 1.00 37.70  ? 245 ALA A CB  1 
ATOM   1862 N N   . ASN A 1 238 ? 39.202 35.499 81.818 1.00 37.73  ? 246 ASN A N   1 
ATOM   1863 C CA  . ASN A 1 238 ? 39.373 34.427 82.779 1.00 39.05  ? 246 ASN A CA  1 
ATOM   1864 C C   . ASN A 1 238 ? 38.432 34.614 83.965 1.00 39.80  ? 246 ASN A C   1 
ATOM   1865 O O   . ASN A 1 238 ? 38.661 35.485 84.796 1.00 39.88  ? 246 ASN A O   1 
ATOM   1866 C CB  . ASN A 1 238 ? 40.811 34.406 83.252 1.00 39.52  ? 246 ASN A CB  1 
ATOM   1867 C CG  . ASN A 1 238 ? 41.151 33.181 84.039 1.00 41.34  ? 246 ASN A CG  1 
ATOM   1868 O OD1 . ASN A 1 238 ? 40.279 32.451 84.552 1.00 40.19  ? 246 ASN A OD1 1 
ATOM   1869 N ND2 . ASN A 1 238 ? 42.439 32.930 84.155 1.00 42.01  ? 246 ASN A ND2 1 
ATOM   1870 N N   . PRO A 1 239 ? 37.360 33.800 84.106 1.00 41.74  ? 247 PRO A N   1 
ATOM   1871 C CA  . PRO A 1 239 ? 36.423 33.975 85.209 1.00 43.22  ? 247 PRO A CA  1 
ATOM   1872 C C   . PRO A 1 239 ? 37.065 33.858 86.589 1.00 46.88  ? 247 PRO A C   1 
ATOM   1873 O O   . PRO A 1 239 ? 36.499 34.348 87.561 1.00 45.63  ? 247 PRO A O   1 
ATOM   1874 C CB  . PRO A 1 239 ? 35.410 32.853 85.004 1.00 44.10  ? 247 PRO A CB  1 
ATOM   1875 C CG  . PRO A 1 239 ? 35.613 32.374 83.617 1.00 43.99  ? 247 PRO A CG  1 
ATOM   1876 C CD  . PRO A 1 239 ? 37.019 32.661 83.241 1.00 42.28  ? 247 PRO A CD  1 
ATOM   1877 N N   . PHE A 1 240 ? 38.224 33.182 86.659 1.00 52.24  ? 248 PHE A N   1 
ATOM   1878 C CA  . PHE A 1 240 ? 38.967 32.997 87.897 1.00 58.59  ? 248 PHE A CA  1 
ATOM   1879 C C   . PHE A 1 240 ? 40.336 33.674 87.900 1.00 63.93  ? 248 PHE A C   1 
ATOM   1880 O O   . PHE A 1 240 ? 41.282 33.148 88.480 1.00 69.73  ? 248 PHE A O   1 
ATOM   1881 C CB  . PHE A 1 240 ? 39.161 31.499 88.162 1.00 57.57  ? 248 PHE A CB  1 
ATOM   1882 C CG  . PHE A 1 240 ? 37.855 30.766 88.206 1.00 57.62  ? 248 PHE A CG  1 
ATOM   1883 C CD1 . PHE A 1 240 ? 36.964 30.967 89.248 1.00 57.75  ? 248 PHE A CD1 1 
ATOM   1884 C CD2 . PHE A 1 240 ? 37.489 29.914 87.183 1.00 57.14  ? 248 PHE A CD2 1 
ATOM   1885 C CE1 . PHE A 1 240 ? 35.743 30.306 89.274 1.00 59.07  ? 248 PHE A CE1 1 
ATOM   1886 C CE2 . PHE A 1 240 ? 36.270 29.256 87.212 1.00 55.68  ? 248 PHE A CE2 1 
ATOM   1887 C CZ  . PHE A 1 240 ? 35.402 29.456 88.253 1.00 56.43  ? 248 PHE A CZ  1 
ATOM   1888 N N   . GLY A 1 241 ? 40.434 34.845 87.263 1.00 68.47  ? 249 GLY A N   1 
ATOM   1889 C CA  . GLY A 1 241 ? 41.621 35.678 87.382 1.00 76.47  ? 249 GLY A CA  1 
ATOM   1890 C C   . GLY A 1 241 ? 41.776 36.212 88.806 1.00 81.02  ? 249 GLY A C   1 
ATOM   1891 O O   . GLY A 1 241 ? 40.814 36.219 89.574 1.00 73.14  ? 249 GLY A O   1 
ATOM   1892 N N   . PRO A 1 242 ? 42.976 36.693 89.205 1.00 85.46  ? 250 PRO A N   1 
ATOM   1893 C CA  . PRO A 1 242 ? 43.203 37.124 90.580 1.00 87.63  ? 250 PRO A CA  1 
ATOM   1894 C C   . PRO A 1 242 ? 42.363 38.329 90.992 1.00 88.83  ? 250 PRO A C   1 
ATOM   1895 O O   . PRO A 1 242 ? 42.155 38.560 92.183 1.00 96.96  ? 250 PRO A O   1 
ATOM   1896 C CB  . PRO A 1 242 ? 44.700 37.435 90.599 1.00 93.24  ? 250 PRO A CB  1 
ATOM   1897 C CG  . PRO A 1 242 ? 45.037 37.750 89.189 1.00 90.94  ? 250 PRO A CG  1 
ATOM   1898 C CD  . PRO A 1 242 ? 44.159 36.867 88.349 1.00 88.87  ? 250 PRO A CD  1 
ATOM   1899 N N   . THR A 1 243 ? 41.897 39.093 89.998 1.00 90.84  ? 251 THR A N   1 
ATOM   1900 C CA  . THR A 1 243 ? 40.921 40.150 90.214 1.00 99.00  ? 251 THR A CA  1 
ATOM   1901 C C   . THR A 1 243 ? 39.475 39.668 90.129 1.00 96.01  ? 251 THR A C   1 
ATOM   1902 O O   . THR A 1 243 ? 38.596 40.232 90.776 1.00 99.16  ? 251 THR A O   1 
ATOM   1903 C CB  . THR A 1 243 ? 41.126 41.246 89.190 1.00 104.19 ? 251 THR A CB  1 
ATOM   1904 O OG1 . THR A 1 243 ? 42.383 41.863 89.464 1.00 105.96 ? 251 THR A OG1 1 
ATOM   1905 C CG2 . THR A 1 243 ? 39.995 42.290 89.197 1.00 103.65 ? 251 THR A CG2 1 
ATOM   1906 N N   . SER A 1 244 ? 39.243 38.640 89.305 1.00 94.65  ? 252 SER A N   1 
ATOM   1907 C CA  . SER A 1 244 ? 37.899 38.172 89.009 1.00 94.38  ? 252 SER A CA  1 
ATOM   1908 C C   . SER A 1 244 ? 37.043 38.014 90.265 1.00 89.76  ? 252 SER A C   1 
ATOM   1909 O O   . SER A 1 244 ? 37.508 37.466 91.265 1.00 81.12  ? 252 SER A O   1 
ATOM   1910 C CB  . SER A 1 244 ? 37.956 36.857 88.241 1.00 91.23  ? 252 SER A CB  1 
ATOM   1911 O OG  . SER A 1 244 ? 38.752 36.980 87.073 1.00 83.26  ? 252 SER A OG  1 
ATOM   1912 N N   . PRO A 1 245 ? 35.771 38.483 90.250 1.00 87.13  ? 253 PRO A N   1 
ATOM   1913 C CA  . PRO A 1 245 ? 34.945 38.486 91.454 1.00 87.39  ? 253 PRO A CA  1 
ATOM   1914 C C   . PRO A 1 245 ? 34.922 37.145 92.186 1.00 84.41  ? 253 PRO A C   1 
ATOM   1915 O O   . PRO A 1 245 ? 34.901 36.090 91.554 1.00 78.20  ? 253 PRO A O   1 
ATOM   1916 C CB  . PRO A 1 245 ? 33.553 38.859 90.928 1.00 87.51  ? 253 PRO A CB  1 
ATOM   1917 C CG  . PRO A 1 245 ? 33.801 39.576 89.630 1.00 86.74  ? 253 PRO A CG  1 
ATOM   1918 C CD  . PRO A 1 245 ? 35.069 39.008 89.065 1.00 85.58  ? 253 PRO A CD  1 
ATOM   1919 N N   . THR A 1 246 ? 34.941 37.206 93.523 1.00 81.62  ? 254 THR A N   1 
ATOM   1920 C CA  . THR A 1 246 ? 34.835 36.020 94.355 1.00 78.34  ? 254 THR A CA  1 
ATOM   1921 C C   . THR A 1 246 ? 33.409 35.496 94.244 1.00 74.85  ? 254 THR A C   1 
ATOM   1922 O O   . THR A 1 246 ? 32.481 36.077 94.807 1.00 74.93  ? 254 THR A O   1 
ATOM   1923 C CB  . THR A 1 246 ? 35.229 36.335 95.790 1.00 78.69  ? 254 THR A CB  1 
ATOM   1924 O OG1 . THR A 1 246 ? 36.568 36.832 95.784 1.00 83.08  ? 254 THR A OG1 1 
ATOM   1925 C CG2 . THR A 1 246 ? 35.132 35.125 96.705 1.00 77.41  ? 254 THR A CG2 1 
ATOM   1926 N N   . LEU A 1 247 ? 33.257 34.386 93.518 1.00 67.30  ? 255 LEU A N   1 
ATOM   1927 C CA  . LEU A 1 247 ? 31.943 33.877 93.167 1.00 69.71  ? 255 LEU A CA  1 
ATOM   1928 C C   . LEU A 1 247 ? 31.292 33.097 94.311 1.00 70.81  ? 255 LEU A C   1 
ATOM   1929 O O   . LEU A 1 247 ? 30.118 32.741 94.218 1.00 65.77  ? 255 LEU A O   1 
ATOM   1930 C CB  . LEU A 1 247 ? 32.071 33.018 91.893 1.00 70.12  ? 255 LEU A CB  1 
ATOM   1931 C CG  . LEU A 1 247 ? 32.727 33.717 90.672 1.00 69.60  ? 255 LEU A CG  1 
ATOM   1932 C CD1 . LEU A 1 247 ? 32.672 32.847 89.438 1.00 67.89  ? 255 LEU A CD1 1 
ATOM   1933 C CD2 . LEU A 1 247 ? 32.077 35.056 90.371 1.00 66.74  ? 255 LEU A CD2 1 
ATOM   1934 N N   . GLU A 1 248 ? 32.044 32.857 95.397 1.00 75.09  ? 256 GLU A N   1 
ATOM   1935 C CA  . GLU A 1 248 ? 31.491 32.277 96.614 1.00 77.26  ? 256 GLU A CA  1 
ATOM   1936 C C   . GLU A 1 248 ? 30.385 33.158 97.189 1.00 73.68  ? 256 GLU A C   1 
ATOM   1937 O O   . GLU A 1 248 ? 29.338 32.664 97.598 1.00 66.30  ? 256 GLU A O   1 
ATOM   1938 C CB  . GLU A 1 248 ? 32.569 32.090 97.704 1.00 82.71  ? 256 GLU A CB  1 
ATOM   1939 C CG  . GLU A 1 248 ? 33.534 30.940 97.472 1.00 86.64  ? 256 GLU A CG  1 
ATOM   1940 C CD  . GLU A 1 248 ? 34.656 31.196 96.481 1.00 93.49  ? 256 GLU A CD  1 
ATOM   1941 O OE1 . GLU A 1 248 ? 34.687 32.286 95.864 1.00 86.36  ? 256 GLU A OE1 1 
ATOM   1942 O OE2 . GLU A 1 248 ? 35.515 30.297 96.328 1.00 99.05  ? 256 GLU A OE2 1 
ATOM   1943 N N   . SER A 1 249 ? 30.648 34.469 97.213 1.00 77.20  ? 257 SER A N   1 
ATOM   1944 C CA  . SER A 1 249 ? 29.734 35.448 97.779 1.00 78.59  ? 257 SER A CA  1 
ATOM   1945 C C   . SER A 1 249 ? 28.582 35.842 96.852 1.00 80.45  ? 257 SER A C   1 
ATOM   1946 O O   . SER A 1 249 ? 27.648 36.510 97.289 1.00 81.94  ? 257 SER A O   1 
ATOM   1947 C CB  . SER A 1 249 ? 30.528 36.684 98.191 1.00 74.77  ? 257 SER A CB  1 
ATOM   1948 O OG  . SER A 1 249 ? 31.494 37.008 97.205 1.00 74.99  ? 257 SER A OG  1 
ATOM   1949 N N   . ILE A 1 250 ? 28.652 35.417 95.581 1.00 74.77  ? 258 ILE A N   1 
ATOM   1950 C CA  . ILE A 1 250 ? 27.640 35.727 94.582 1.00 66.76  ? 258 ILE A CA  1 
ATOM   1951 C C   . ILE A 1 250 ? 26.603 34.612 94.460 1.00 67.42  ? 258 ILE A C   1 
ATOM   1952 O O   . ILE A 1 250 ? 26.948 33.437 94.535 1.00 64.85  ? 258 ILE A O   1 
ATOM   1953 C CB  . ILE A 1 250 ? 28.353 36.002 93.236 1.00 67.24  ? 258 ILE A CB  1 
ATOM   1954 C CG1 . ILE A 1 250 ? 29.044 37.373 93.279 1.00 70.13  ? 258 ILE A CG1 1 
ATOM   1955 C CG2 . ILE A 1 250 ? 27.400 35.883 92.042 1.00 67.82  ? 258 ILE A CG2 1 
ATOM   1956 C CD1 . ILE A 1 250 ? 30.006 37.619 92.172 1.00 70.65  ? 258 ILE A CD1 1 
ATOM   1957 N N   . SER A 1 251 ? 25.335 34.998 94.259 1.00 68.01  ? 259 SER A N   1 
ATOM   1958 C CA  . SER A 1 251 ? 24.240 34.055 94.083 1.00 70.51  ? 259 SER A CA  1 
ATOM   1959 C C   . SER A 1 251 ? 23.948 33.817 92.604 1.00 63.97  ? 259 SER A C   1 
ATOM   1960 O O   . SER A 1 251 ? 23.087 34.481 92.030 1.00 69.49  ? 259 SER A O   1 
ATOM   1961 C CB  . SER A 1 251 ? 22.967 34.566 94.759 1.00 74.45  ? 259 SER A CB  1 
ATOM   1962 O OG  . SER A 1 251 ? 23.117 34.675 96.163 1.00 81.58  ? 259 SER A OG  1 
ATOM   1963 N N   . LEU A 1 252 ? 24.662 32.864 91.997 1.00 55.26  ? 260 LEU A N   1 
ATOM   1964 C CA  . LEU A 1 252 ? 24.469 32.556 90.589 1.00 52.85  ? 260 LEU A CA  1 
ATOM   1965 C C   . LEU A 1 252 ? 23.212 31.714 90.414 1.00 46.37  ? 260 LEU A C   1 
ATOM   1966 O O   . LEU A 1 252 ? 22.949 30.824 91.209 1.00 48.15  ? 260 LEU A O   1 
ATOM   1967 C CB  . LEU A 1 252 ? 25.660 31.795 90.005 1.00 51.64  ? 260 LEU A CB  1 
ATOM   1968 C CG  . LEU A 1 252 ? 26.954 32.561 89.890 1.00 53.23  ? 260 LEU A CG  1 
ATOM   1969 C CD1 . LEU A 1 252 ? 28.004 31.716 89.205 1.00 57.99  ? 260 LEU A CD1 1 
ATOM   1970 C CD2 . LEU A 1 252 ? 26.765 33.870 89.141 1.00 53.64  ? 260 LEU A CD2 1 
ATOM   1971 N N   . GLU A 1 253 ? 22.443 32.013 89.364 1.00 45.99  ? 261 GLU A N   1 
ATOM   1972 C CA  . GLU A 1 253 ? 21.308 31.191 88.989 1.00 42.48  ? 261 GLU A CA  1 
ATOM   1973 C C   . GLU A 1 253 ? 21.837 29.896 88.381 1.00 38.75  ? 261 GLU A C   1 
ATOM   1974 O O   . GLU A 1 253 ? 23.020 29.798 88.069 1.00 35.35  ? 261 GLU A O   1 
ATOM   1975 C CB  . GLU A 1 253 ? 20.394 31.935 87.997 1.00 47.26  ? 261 GLU A CB  1 
ATOM   1976 C CG  . GLU A 1 253 ? 19.817 33.239 88.531 1.00 51.66  ? 261 GLU A CG  1 
ATOM   1977 C CD  . GLU A 1 253 ? 19.130 33.112 89.874 1.00 59.96  ? 261 GLU A CD  1 
ATOM   1978 O OE1 . GLU A 1 253 ? 18.301 32.185 90.040 1.00 58.65  ? 261 GLU A OE1 1 
ATOM   1979 O OE2 . GLU A 1 253 ? 19.432 33.938 90.766 1.00 69.55  ? 261 GLU A OE2 1 
ATOM   1980 N N   . PRO A 1 254 ? 20.985 28.860 88.224 1.00 38.80  ? 262 PRO A N   1 
ATOM   1981 C CA  . PRO A 1 254 ? 21.393 27.618 87.585 1.00 39.95  ? 262 PRO A CA  1 
ATOM   1982 C C   . PRO A 1 254 ? 22.092 27.813 86.242 1.00 40.47  ? 262 PRO A C   1 
ATOM   1983 O O   . PRO A 1 254 ? 21.702 28.659 85.437 1.00 34.28  ? 262 PRO A O   1 
ATOM   1984 C CB  . PRO A 1 254 ? 20.064 26.889 87.427 1.00 40.38  ? 262 PRO A CB  1 
ATOM   1985 C CG  . PRO A 1 254 ? 19.265 27.361 88.605 1.00 40.51  ? 262 PRO A CG  1 
ATOM   1986 C CD  . PRO A 1 254 ? 19.590 28.815 88.694 1.00 38.04  ? 262 PRO A CD  1 
ATOM   1987 N N   . MET A 1 255 ? 23.123 26.997 86.014 1.00 39.67  ? 263 MET A N   1 
ATOM   1988 C CA  . MET A 1 255 ? 23.923 27.083 84.810 1.00 40.91  ? 263 MET A CA  1 
ATOM   1989 C C   . MET A 1 255 ? 24.068 25.703 84.179 1.00 39.67  ? 263 MET A C   1 
ATOM   1990 O O   . MET A 1 255 ? 24.151 24.687 84.869 1.00 36.94  ? 263 MET A O   1 
ATOM   1991 C CB  . MET A 1 255 ? 25.258 27.711 85.145 1.00 44.46  ? 263 MET A CB  1 
ATOM   1992 C CG  . MET A 1 255 ? 25.075 29.136 85.611 1.00 53.29  ? 263 MET A CG  1 
ATOM   1993 S SD  . MET A 1 255 ? 26.574 30.074 85.677 1.00 66.18  ? 263 MET A SD  1 
ATOM   1994 C CE  . MET A 1 255 ? 26.895 30.247 83.969 1.00 69.72  ? 263 MET A CE  1 
ATOM   1995 N N   . LEU A 1 256 ? 24.034 25.705 82.848 1.00 36.14  ? 264 LEU A N   1 
ATOM   1996 C CA  . LEU A 1 256 ? 24.295 24.536 82.035 1.00 35.70  ? 264 LEU A CA  1 
ATOM   1997 C C   . LEU A 1 256 ? 25.494 24.863 81.149 1.00 35.28  ? 264 LEU A C   1 
ATOM   1998 O O   . LEU A 1 256 ? 25.471 25.849 80.416 1.00 34.52  ? 264 LEU A O   1 
ATOM   1999 C CB  . LEU A 1 256 ? 23.028 24.242 81.242 1.00 37.93  ? 264 LEU A CB  1 
ATOM   2000 C CG  . LEU A 1 256 ? 23.061 23.117 80.265 1.00 37.25  ? 264 LEU A CG  1 
ATOM   2001 C CD1 . LEU A 1 256 ? 23.370 21.785 80.953 1.00 40.20  ? 264 LEU A CD1 1 
ATOM   2002 C CD2 . LEU A 1 256 ? 21.731 23.042 79.526 1.00 37.72  ? 264 LEU A CD2 1 
ATOM   2003 N N   . VAL A 1 257 ? 26.558 24.062 81.272 1.00 33.71  ? 265 VAL A N   1 
ATOM   2004 C CA  . VAL A 1 257 ? 27.750 24.205 80.455 1.00 34.49  ? 265 VAL A CA  1 
ATOM   2005 C C   . VAL A 1 257 ? 27.785 23.007 79.507 1.00 34.53  ? 265 VAL A C   1 
ATOM   2006 O O   . VAL A 1 257 ? 27.744 21.859 79.947 1.00 33.06  ? 265 VAL A O   1 
ATOM   2007 C CB  . VAL A 1 257 ? 29.047 24.331 81.307 1.00 35.35  ? 265 VAL A CB  1 
ATOM   2008 C CG1 . VAL A 1 257 ? 30.291 24.472 80.426 1.00 34.56  ? 265 VAL A CG1 1 
ATOM   2009 C CG2 . VAL A 1 257 ? 28.960 25.500 82.282 1.00 36.72  ? 265 VAL A CG2 1 
ATOM   2010 N N   . ILE A 1 258 ? 27.823 23.297 78.202 1.00 33.48  ? 266 ILE A N   1 
ATOM   2011 C CA  . ILE A 1 258 ? 27.803 22.274 77.170 1.00 33.62  ? 266 ILE A CA  1 
ATOM   2012 C C   . ILE A 1 258 ? 29.050 22.463 76.321 1.00 33.17  ? 266 ILE A C   1 
ATOM   2013 O O   . ILE A 1 258 ? 29.296 23.567 75.838 1.00 31.18  ? 266 ILE A O   1 
ATOM   2014 C CB  . ILE A 1 258 ? 26.531 22.340 76.302 1.00 32.40  ? 266 ILE A CB  1 
ATOM   2015 C CG1 . ILE A 1 258 ? 25.282 22.112 77.143 1.00 33.20  ? 266 ILE A CG1 1 
ATOM   2016 C CG2 . ILE A 1 258 ? 26.608 21.347 75.126 1.00 34.77  ? 266 ILE A CG2 1 
ATOM   2017 C CD1 . ILE A 1 258 ? 24.011 22.369 76.402 1.00 35.47  ? 266 ILE A CD1 1 
ATOM   2018 N N   . VAL A 1 259 ? 29.808 21.374 76.125 1.00 33.22  ? 267 VAL A N   1 
ATOM   2019 C CA  . VAL A 1 259 ? 31.049 21.436 75.372 1.00 32.93  ? 267 VAL A CA  1 
ATOM   2020 C C   . VAL A 1 259 ? 31.284 20.143 74.587 1.00 35.55  ? 267 VAL A C   1 
ATOM   2021 O O   . VAL A 1 259 ? 30.750 19.089 74.930 1.00 34.43  ? 267 VAL A O   1 
ATOM   2022 C CB  . VAL A 1 259 ? 32.206 21.787 76.351 1.00 38.82  ? 267 VAL A CB  1 
ATOM   2023 C CG1 . VAL A 1 259 ? 32.644 20.576 77.169 1.00 38.53  ? 267 VAL A CG1 1 
ATOM   2024 C CG2 . VAL A 1 259 ? 33.385 22.392 75.623 1.00 42.47  ? 267 VAL A CG2 1 
ATOM   2025 N N   . GLY A 1 260 ? 32.052 20.250 73.499 1.00 33.32  ? 268 GLY A N   1 
ATOM   2026 C CA  . GLY A 1 260 ? 32.503 19.092 72.748 1.00 36.96  ? 268 GLY A CA  1 
ATOM   2027 C C   . GLY A 1 260 ? 33.729 18.465 73.409 1.00 37.46  ? 268 GLY A C   1 
ATOM   2028 O O   . GLY A 1 260 ? 34.628 19.181 73.856 1.00 36.08  ? 268 GLY A O   1 
ATOM   2029 N N   . GLY A 1 261 ? 33.747 17.129 73.459 1.00 37.65  ? 269 GLY A N   1 
ATOM   2030 C CA  . GLY A 1 261 ? 34.845 16.374 74.040 1.00 38.53  ? 269 GLY A CA  1 
ATOM   2031 C C   . GLY A 1 261 ? 36.200 16.629 73.385 1.00 36.78  ? 269 GLY A C   1 
ATOM   2032 O O   . GLY A 1 261 ? 37.227 16.555 74.051 1.00 40.56  ? 269 GLY A O   1 
ATOM   2033 N N   . SER A 1 262 ? 36.187 16.947 72.087 1.00 36.41  ? 270 SER A N   1 
ATOM   2034 C CA  . SER A 1 262 ? 37.402 17.233 71.341 1.00 39.46  ? 270 SER A CA  1 
ATOM   2035 C C   . SER A 1 262 ? 37.718 18.724 71.202 1.00 40.87  ? 270 SER A C   1 
ATOM   2036 O O   . SER A 1 262 ? 38.557 19.105 70.390 1.00 38.75  ? 270 SER A O   1 
ATOM   2037 C CB  . SER A 1 262 ? 37.303 16.586 69.960 1.00 39.78  ? 270 SER A CB  1 
ATOM   2038 O OG  . SER A 1 262 ? 37.055 15.195 70.100 1.00 40.15  ? 270 SER A OG  1 
ATOM   2039 N N   . GLU A 1 263 ? 37.055 19.569 72.004 1.00 40.04  ? 271 GLU A N   1 
ATOM   2040 C CA  . GLU A 1 263 ? 37.255 21.009 71.933 1.00 37.76  ? 271 GLU A CA  1 
ATOM   2041 C C   . GLU A 1 263 ? 38.519 21.443 72.660 1.00 34.99  ? 271 GLU A C   1 
ATOM   2042 O O   . GLU A 1 263 ? 38.779 20.976 73.762 1.00 36.13  ? 271 GLU A O   1 
ATOM   2043 C CB  . GLU A 1 263 ? 36.113 21.804 72.607 1.00 38.64  ? 271 GLU A CB  1 
ATOM   2044 C CG  . GLU A 1 263 ? 34.888 21.996 71.763 1.00 40.66  ? 271 GLU A CG  1 
ATOM   2045 C CD  . GLU A 1 263 ? 33.978 23.090 72.299 1.00 38.77  ? 271 GLU A CD  1 
ATOM   2046 O OE1 . GLU A 1 263 ? 34.426 24.256 72.375 1.00 32.79  ? 271 GLU A OE1 1 
ATOM   2047 O OE2 . GLU A 1 263 ? 32.823 22.769 72.651 1.00 34.75  ? 271 GLU A OE2 1 
ATOM   2048 N N   . LEU A 1 264 ? 39.229 22.405 72.066 1.00 33.16  ? 272 LEU A N   1 
ATOM   2049 C CA  . LEU A 1 264 ? 40.331 23.072 72.733 1.00 37.06  ? 272 LEU A CA  1 
ATOM   2050 C C   . LEU A 1 264 ? 39.868 23.678 74.059 1.00 38.42  ? 272 LEU A C   1 
ATOM   2051 O O   . LEU A 1 264 ? 40.597 23.640 75.047 1.00 40.78  ? 272 LEU A O   1 
ATOM   2052 C CB  . LEU A 1 264 ? 40.890 24.163 71.816 1.00 36.20  ? 272 LEU A CB  1 
ATOM   2053 C CG  . LEU A 1 264 ? 41.572 23.684 70.543 1.00 40.04  ? 272 LEU A CG  1 
ATOM   2054 C CD1 . LEU A 1 264 ? 41.747 24.821 69.566 1.00 40.94  ? 272 LEU A CD1 1 
ATOM   2055 C CD2 . LEU A 1 264 ? 42.923 23.059 70.843 1.00 42.54  ? 272 LEU A CD2 1 
ATOM   2056 N N   . LEU A 1 265 ? 38.639 24.191 74.100 1.00 35.68  ? 273 LEU A N   1 
ATOM   2057 C CA  . LEU A 1 265 ? 38.132 24.909 75.296 1.00 35.35  ? 273 LEU A CA  1 
ATOM   2058 C C   . LEU A 1 265 ? 37.485 23.979 76.338 1.00 35.99  ? 273 LEU A C   1 
ATOM   2059 O O   . LEU A 1 265 ? 36.991 24.505 77.339 1.00 36.41  ? 273 LEU A O   1 
ATOM   2060 C CB  . LEU A 1 265 ? 37.130 25.918 74.741 1.00 34.60  ? 273 LEU A CB  1 
ATOM   2061 C CG  . LEU A 1 265 ? 37.698 27.188 74.103 1.00 33.37  ? 273 LEU A CG  1 
ATOM   2062 C CD1 . LEU A 1 265 ? 36.604 27.876 73.312 1.00 34.29  ? 273 LEU A CD1 1 
ATOM   2063 C CD2 . LEU A 1 265 ? 38.244 28.113 75.168 1.00 33.12  ? 273 LEU A CD2 1 
ATOM   2064 N N   . ARG A 1 266 ? 37.517 22.664 76.130 1.00 38.69  ? 274 ARG A N   1 
ATOM   2065 C CA  . ARG A 1 266 ? 36.833 21.699 77.037 1.00 43.83  ? 274 ARG A CA  1 
ATOM   2066 C C   . ARG A 1 266 ? 37.358 21.786 78.480 1.00 44.37  ? 274 ARG A C   1 
ATOM   2067 O O   . ARG A 1 266 ? 36.536 21.869 79.392 1.00 40.18  ? 274 ARG A O   1 
ATOM   2068 C CB  . ARG A 1 266 ? 36.994 20.266 76.520 1.00 48.48  ? 274 ARG A CB  1 
ATOM   2069 C CG  . ARG A 1 266 ? 36.526 19.144 77.433 1.00 55.38  ? 274 ARG A CG  1 
ATOM   2070 C CD  . ARG A 1 266 ? 37.690 18.232 77.773 1.00 64.95  ? 274 ARG A CD  1 
ATOM   2071 N NE  . ARG A 1 266 ? 37.284 16.970 78.398 1.00 72.64  ? 274 ARG A NE  1 
ATOM   2072 C CZ  . ARG A 1 266 ? 37.556 16.615 79.646 1.00 75.45  ? 274 ARG A CZ  1 
ATOM   2073 N NH1 . ARG A 1 266 ? 38.502 17.238 80.322 1.00 79.24  ? 274 ARG A NH1 1 
ATOM   2074 N NH2 . ARG A 1 266 ? 36.875 15.637 80.214 1.00 71.42  ? 274 ARG A NH2 1 
ATOM   2075 N N   . ASP A 1 267 ? 38.673 21.753 78.672 1.00 42.02  ? 275 ASP A N   1 
ATOM   2076 C CA  . ASP A 1 267 ? 39.240 21.726 80.048 1.00 42.20  ? 275 ASP A CA  1 
ATOM   2077 C C   . ASP A 1 267 ? 38.858 22.991 80.827 1.00 38.77  ? 275 ASP A C   1 
ATOM   2078 O O   . ASP A 1 267 ? 38.424 22.863 81.969 1.00 37.51  ? 275 ASP A O   1 
ATOM   2079 C CB  . ASP A 1 267 ? 40.738 21.476 80.010 1.00 43.55  ? 275 ASP A CB  1 
ATOM   2080 C CG  . ASP A 1 267 ? 41.164 20.073 79.609 1.00 43.87  ? 275 ASP A CG  1 
ATOM   2081 O OD1 . ASP A 1 267 ? 40.285 19.198 79.520 1.00 43.94  ? 275 ASP A OD1 1 
ATOM   2082 O OD2 . ASP A 1 267 ? 42.371 19.874 79.385 1.00 46.25  ? 275 ASP A OD2 1 
ATOM   2083 N N   . ARG A 1 268 ? 39.049 24.161 80.229 1.00 37.99  ? 276 ARG A N   1 
ATOM   2084 C CA  . ARG A 1 268 ? 38.738 25.437 80.915 1.00 38.35  ? 276 ARG A CA  1 
ATOM   2085 C C   . ARG A 1 268 ? 37.244 25.446 81.253 1.00 38.30  ? 276 ARG A C   1 
ATOM   2086 O O   . ARG A 1 268 ? 36.888 25.896 82.344 1.00 37.50  ? 276 ARG A O   1 
ATOM   2087 C CB  . ARG A 1 268 ? 39.170 26.620 80.045 1.00 37.28  ? 276 ARG A CB  1 
ATOM   2088 C CG  . ARG A 1 268 ? 39.309 27.943 80.778 1.00 37.52  ? 276 ARG A CG  1 
ATOM   2089 C CD  . ARG A 1 268 ? 39.987 28.996 79.927 1.00 39.12  ? 276 ARG A CD  1 
ATOM   2090 N NE  . ARG A 1 268 ? 41.389 28.702 79.620 1.00 39.10  ? 276 ARG A NE  1 
ATOM   2091 C CZ  . ARG A 1 268 ? 42.396 28.880 80.460 1.00 43.72  ? 276 ARG A CZ  1 
ATOM   2092 N NH1 . ARG A 1 268 ? 42.180 29.397 81.653 1.00 41.62  ? 276 ARG A NH1 1 
ATOM   2093 N NH2 . ARG A 1 268 ? 43.618 28.541 80.101 1.00 43.24  ? 276 ARG A NH2 1 
ATOM   2094 N N   . ALA A 1 269 ? 36.425 24.925 80.344 1.00 37.04  ? 277 ALA A N   1 
ATOM   2095 C CA  . ALA A 1 269 ? 34.990 24.888 80.581 1.00 36.48  ? 277 ALA A CA  1 
ATOM   2096 C C   . ALA A 1 269 ? 34.651 23.937 81.726 1.00 37.08  ? 277 ALA A C   1 
ATOM   2097 O O   . ALA A 1 269 ? 33.867 24.282 82.606 1.00 34.43  ? 277 ALA A O   1 
ATOM   2098 C CB  . ALA A 1 269 ? 34.243 24.482 79.317 1.00 35.88  ? 277 ALA A CB  1 
ATOM   2099 N N   . LYS A 1 270 ? 35.259 22.746 81.714 1.00 36.61  ? 278 LYS A N   1 
ATOM   2100 C CA  . LYS A 1 270 ? 35.058 21.779 82.783 1.00 39.62  ? 278 LYS A CA  1 
ATOM   2101 C C   . LYS A 1 270 ? 35.529 22.319 84.132 1.00 38.19  ? 278 LYS A C   1 
ATOM   2102 O O   . LYS A 1 270 ? 34.841 22.175 85.138 1.00 36.17  ? 278 LYS A O   1 
ATOM   2103 C CB  . LYS A 1 270 ? 35.789 20.466 82.472 1.00 44.76  ? 278 LYS A CB  1 
ATOM   2104 C CG  . LYS A 1 270 ? 35.453 19.361 83.459 1.00 47.29  ? 278 LYS A CG  1 
ATOM   2105 C CD  . LYS A 1 270 ? 35.882 18.001 82.987 1.00 52.02  ? 278 LYS A CD  1 
ATOM   2106 C CE  . LYS A 1 270 ? 35.328 16.911 83.876 1.00 59.20  ? 278 LYS A CE  1 
ATOM   2107 N NZ  . LYS A 1 270 ? 35.692 15.560 83.375 1.00 62.07  ? 278 LYS A NZ  1 
ATOM   2108 N N   . GLU A 1 271 ? 36.715 22.931 84.133 1.00 40.15  ? 279 GLU A N   1 
ATOM   2109 C CA  . GLU A 1 271 ? 37.295 23.539 85.318 1.00 43.70  ? 279 GLU A CA  1 
ATOM   2110 C C   . GLU A 1 271 ? 36.378 24.623 85.879 1.00 45.03  ? 279 GLU A C   1 
ATOM   2111 O O   . GLU A 1 271 ? 36.186 24.729 87.089 1.00 44.98  ? 279 GLU A O   1 
ATOM   2112 C CB  . GLU A 1 271 ? 38.659 24.127 84.938 1.00 50.11  ? 279 GLU A CB  1 
ATOM   2113 C CG  . GLU A 1 271 ? 39.412 24.811 86.057 1.00 59.97  ? 279 GLU A CG  1 
ATOM   2114 C CD  . GLU A 1 271 ? 40.601 25.588 85.532 1.00 67.88  ? 279 GLU A CD  1 
ATOM   2115 O OE1 . GLU A 1 271 ? 41.526 24.946 84.982 1.00 69.29  ? 279 GLU A OE1 1 
ATOM   2116 O OE2 . GLU A 1 271 ? 40.588 26.837 85.629 1.00 68.24  ? 279 GLU A OE2 1 
ATOM   2117 N N   . TYR A 1 272 ? 35.825 25.437 84.976 1.00 42.29  ? 280 TYR A N   1 
ATOM   2118 C CA  . TYR A 1 272 ? 34.872 26.467 85.346 1.00 38.43  ? 280 TYR A CA  1 
ATOM   2119 C C   . TYR A 1 272 ? 33.691 25.856 86.089 1.00 37.32  ? 280 TYR A C   1 
ATOM   2120 O O   . TYR A 1 272 ? 33.378 26.277 87.197 1.00 39.48  ? 280 TYR A O   1 
ATOM   2121 C CB  . TYR A 1 272 ? 34.432 27.216 84.083 1.00 40.26  ? 280 TYR A CB  1 
ATOM   2122 C CG  . TYR A 1 272 ? 33.256 28.150 84.238 1.00 38.67  ? 280 TYR A CG  1 
ATOM   2123 C CD1 . TYR A 1 272 ? 33.434 29.461 84.654 1.00 37.18  ? 280 TYR A CD1 1 
ATOM   2124 C CD2 . TYR A 1 272 ? 31.964 27.725 83.956 1.00 37.87  ? 280 TYR A CD2 1 
ATOM   2125 C CE1 . TYR A 1 272 ? 32.354 30.334 84.770 1.00 38.70  ? 280 TYR A CE1 1 
ATOM   2126 C CE2 . TYR A 1 272 ? 30.876 28.581 84.091 1.00 37.01  ? 280 TYR A CE2 1 
ATOM   2127 C CZ  . TYR A 1 272 ? 31.075 29.889 84.484 1.00 37.54  ? 280 TYR A CZ  1 
ATOM   2128 O OH  . TYR A 1 272 ? 29.997 30.739 84.608 1.00 38.77  ? 280 TYR A OH  1 
ATOM   2129 N N   . ALA A 1 273 ? 33.065 24.848 85.474 1.00 37.09  ? 281 ALA A N   1 
ATOM   2130 C CA  . ALA A 1 273 ? 31.886 24.210 86.036 1.00 41.17  ? 281 ALA A CA  1 
ATOM   2131 C C   . ALA A 1 273 ? 32.156 23.578 87.399 1.00 44.79  ? 281 ALA A C   1 
ATOM   2132 O O   . ALA A 1 273 ? 31.361 23.729 88.320 1.00 45.72  ? 281 ALA A O   1 
ATOM   2133 C CB  . ALA A 1 273 ? 31.335 23.159 85.077 1.00 37.54  ? 281 ALA A CB  1 
ATOM   2134 N N   . TYR A 1 274 ? 33.275 22.860 87.522 1.00 51.22  ? 282 TYR A N   1 
ATOM   2135 C CA  . TYR A 1 274 ? 33.538 22.116 88.741 1.00 54.13  ? 282 TYR A CA  1 
ATOM   2136 C C   . TYR A 1 274 ? 33.981 23.026 89.884 1.00 52.05  ? 282 TYR A C   1 
ATOM   2137 O O   . TYR A 1 274 ? 33.700 22.720 91.036 1.00 53.85  ? 282 TYR A O   1 
ATOM   2138 C CB  . TYR A 1 274 ? 34.514 20.950 88.478 1.00 57.92  ? 282 TYR A CB  1 
ATOM   2139 C CG  . TYR A 1 274 ? 33.784 19.745 87.913 1.00 63.48  ? 282 TYR A CG  1 
ATOM   2140 C CD1 . TYR A 1 274 ? 33.329 19.735 86.600 1.00 64.97  ? 282 TYR A CD1 1 
ATOM   2141 C CD2 . TYR A 1 274 ? 33.486 18.647 88.711 1.00 67.04  ? 282 TYR A CD2 1 
ATOM   2142 C CE1 . TYR A 1 274 ? 32.635 18.646 86.081 1.00 64.80  ? 282 TYR A CE1 1 
ATOM   2143 C CE2 . TYR A 1 274 ? 32.792 17.551 88.203 1.00 69.29  ? 282 TYR A CE2 1 
ATOM   2144 C CZ  . TYR A 1 274 ? 32.367 17.556 86.886 1.00 69.04  ? 282 TYR A CZ  1 
ATOM   2145 O OH  . TYR A 1 274 ? 31.681 16.488 86.363 1.00 67.67  ? 282 TYR A OH  1 
ATOM   2146 N N   . LYS A 1 275 ? 34.625 24.158 89.572 1.00 50.29  ? 283 LYS A N   1 
ATOM   2147 C CA  . LYS A 1 275 ? 34.889 25.169 90.585 1.00 53.14  ? 283 LYS A CA  1 
ATOM   2148 C C   . LYS A 1 275 ? 33.599 25.770 91.143 1.00 52.49  ? 283 LYS A C   1 
ATOM   2149 O O   . LYS A 1 275 ? 33.506 26.017 92.343 1.00 55.77  ? 283 LYS A O   1 
ATOM   2150 C CB  . LYS A 1 275 ? 35.800 26.277 90.048 1.00 55.05  ? 283 LYS A CB  1 
ATOM   2151 C CG  . LYS A 1 275 ? 37.255 25.851 89.955 1.00 57.18  ? 283 LYS A CG  1 
ATOM   2152 C CD  . LYS A 1 275 ? 38.196 26.998 89.621 1.00 60.01  ? 283 LYS A CD  1 
ATOM   2153 C CE  . LYS A 1 275 ? 39.604 26.506 89.401 1.00 62.41  ? 283 LYS A CE  1 
ATOM   2154 N NZ  . LYS A 1 275 ? 40.503 27.592 88.943 1.00 66.10  ? 283 LYS A NZ  1 
ATOM   2155 N N   . LEU A 1 276 ? 32.605 25.993 90.275 1.00 50.89  ? 284 LEU A N   1 
ATOM   2156 C CA  . LEU A 1 276 ? 31.302 26.471 90.713 1.00 53.61  ? 284 LEU A CA  1 
ATOM   2157 C C   . LEU A 1 276 ? 30.551 25.425 91.536 1.00 56.96  ? 284 LEU A C   1 
ATOM   2158 O O   . LEU A 1 276 ? 30.010 25.746 92.591 1.00 59.99  ? 284 LEU A O   1 
ATOM   2159 C CB  . LEU A 1 276 ? 30.441 26.872 89.509 1.00 52.27  ? 284 LEU A CB  1 
ATOM   2160 C CG  . LEU A 1 276 ? 30.886 28.108 88.740 1.00 52.16  ? 284 LEU A CG  1 
ATOM   2161 C CD1 . LEU A 1 276 ? 30.007 28.329 87.531 1.00 52.51  ? 284 LEU A CD1 1 
ATOM   2162 C CD2 . LEU A 1 276 ? 30.866 29.342 89.614 1.00 53.68  ? 284 LEU A CD2 1 
ATOM   2163 N N   . LYS A 1 277 ? 30.498 24.185 91.031 1.00 61.77  ? 285 LYS A N   1 
ATOM   2164 C CA  . LYS A 1 277 ? 29.890 23.070 91.746 1.00 64.44  ? 285 LYS A CA  1 
ATOM   2165 C C   . LYS A 1 277 ? 30.291 23.038 93.221 1.00 71.04  ? 285 LYS A C   1 
ATOM   2166 O O   . LYS A 1 277 ? 29.432 23.002 94.101 1.00 72.26  ? 285 LYS A O   1 
ATOM   2167 C CB  . LYS A 1 277 ? 30.289 21.728 91.104 1.00 63.29  ? 285 LYS A CB  1 
ATOM   2168 C CG  . LYS A 1 277 ? 29.316 21.162 90.085 1.00 64.99  ? 285 LYS A CG  1 
ATOM   2169 C CD  . LYS A 1 277 ? 29.961 20.034 89.267 1.00 68.85  ? 285 LYS A CD  1 
ATOM   2170 C CE  . LYS A 1 277 ? 29.021 18.904 88.922 1.00 71.23  ? 285 LYS A CE  1 
ATOM   2171 N NZ  . LYS A 1 277 ? 27.835 19.368 88.175 1.00 70.49  ? 285 LYS A NZ  1 
ATOM   2172 N N   . LYS A 1 278 ? 31.607 23.052 93.467 1.00 72.67  ? 286 LYS A N   1 
ATOM   2173 C CA  . LYS A 1 278 ? 32.159 22.943 94.809 1.00 80.46  ? 286 LYS A CA  1 
ATOM   2174 C C   . LYS A 1 278 ? 31.792 24.114 95.718 1.00 79.44  ? 286 LYS A C   1 
ATOM   2175 O O   . LYS A 1 278 ? 31.694 23.940 96.930 1.00 81.37  ? 286 LYS A O   1 
ATOM   2176 C CB  . LYS A 1 278 ? 33.691 22.832 94.751 1.00 82.91  ? 286 LYS A CB  1 
ATOM   2177 C CG  . LYS A 1 278 ? 34.202 21.493 94.229 1.00 86.16  ? 286 LYS A CG  1 
ATOM   2178 C CD  . LYS A 1 278 ? 35.728 21.381 94.285 1.00 89.32  ? 286 LYS A CD  1 
ATOM   2179 C CE  . LYS A 1 278 ? 36.428 22.433 93.451 1.00 91.92  ? 286 LYS A CE  1 
ATOM   2180 N NZ  . LYS A 1 278 ? 37.893 22.199 93.380 1.00 92.95  ? 286 LYS A NZ  1 
ATOM   2181 N N   . MET A 1 279 ? 31.600 25.300 95.129 1.00 75.47  ? 287 MET A N   1 
ATOM   2182 C CA  . MET A 1 279 ? 31.308 26.499 95.899 1.00 76.31  ? 287 MET A CA  1 
ATOM   2183 C C   . MET A 1 279 ? 30.014 26.417 96.705 1.00 82.40  ? 287 MET A C   1 
ATOM   2184 O O   . MET A 1 279 ? 29.853 27.146 97.681 1.00 89.17  ? 287 MET A O   1 
ATOM   2185 C CB  . MET A 1 279 ? 31.219 27.707 94.983 1.00 73.76  ? 287 MET A CB  1 
ATOM   2186 C CG  . MET A 1 279 ? 32.534 28.303 94.707 1.00 74.77  ? 287 MET A CG  1 
ATOM   2187 S SD  . MET A 1 279 ? 32.374 29.690 93.600 1.00 72.97  ? 287 MET A SD  1 
ATOM   2188 C CE  . MET A 1 279 ? 34.083 29.848 93.035 1.00 68.68  ? 287 MET A CE  1 
ATOM   2189 N N   . GLY A 1 280 ? 29.087 25.552 96.277 1.00 78.53  ? 288 GLY A N   1 
ATOM   2190 C CA  . GLY A 1 280 ? 27.885 25.288 97.048 1.00 78.28  ? 288 GLY A CA  1 
ATOM   2191 C C   . GLY A 1 280 ? 26.848 26.397 96.905 1.00 80.29  ? 288 GLY A C   1 
ATOM   2192 O O   . GLY A 1 280 ? 27.195 27.570 96.769 1.00 78.24  ? 288 GLY A O   1 
ATOM   2193 N N   . GLY A 1 281 ? 25.570 26.000 96.942 1.00 78.44  ? 289 GLY A N   1 
ATOM   2194 C CA  . GLY A 1 281 ? 24.471 26.879 96.583 1.00 74.96  ? 289 GLY A CA  1 
ATOM   2195 C C   . GLY A 1 281 ? 24.317 27.062 95.072 1.00 73.07  ? 289 GLY A C   1 
ATOM   2196 O O   . GLY A 1 281 ? 23.377 27.712 94.620 1.00 71.23  ? 289 GLY A O   1 
ATOM   2197 N N   . LYS A 1 282 ? 25.236 26.467 94.298 1.00 71.34  ? 290 LYS A N   1 
ATOM   2198 C CA  . LYS A 1 282 ? 25.288 26.671 92.860 1.00 68.43  ? 290 LYS A CA  1 
ATOM   2199 C C   . LYS A 1 282 ? 24.915 25.396 92.111 1.00 64.33  ? 290 LYS A C   1 
ATOM   2200 O O   . LYS A 1 282 ? 25.610 24.389 92.222 1.00 67.05  ? 290 LYS A O   1 
ATOM   2201 C CB  . LYS A 1 282 ? 26.687 27.120 92.442 1.00 67.01  ? 290 LYS A CB  1 
ATOM   2202 C CG  . LYS A 1 282 ? 27.171 28.327 93.201 1.00 68.38  ? 290 LYS A CG  1 
ATOM   2203 C CD  . LYS A 1 282 ? 28.257 29.065 92.472 1.00 71.44  ? 290 LYS A CD  1 
ATOM   2204 C CE  . LYS A 1 282 ? 28.910 30.108 93.336 1.00 74.50  ? 290 LYS A CE  1 
ATOM   2205 N NZ  . LYS A 1 282 ? 27.926 31.047 93.931 1.00 73.70  ? 290 LYS A NZ  1 
ATOM   2206 N N   . ARG A 1 283 ? 23.813 25.457 91.354 1.00 59.34  ? 291 ARG A N   1 
ATOM   2207 C CA  . ARG A 1 283 ? 23.382 24.348 90.521 1.00 59.14  ? 291 ARG A CA  1 
ATOM   2208 C C   . ARG A 1 283 ? 24.038 24.521 89.150 1.00 57.18  ? 291 ARG A C   1 
ATOM   2209 O O   . ARG A 1 283 ? 23.699 25.429 88.396 1.00 56.17  ? 291 ARG A O   1 
ATOM   2210 C CB  . ARG A 1 283 ? 21.836 24.294 90.460 1.00 64.72  ? 291 ARG A CB  1 
ATOM   2211 C CG  . ARG A 1 283 ? 21.129 23.940 91.788 1.00 75.16  ? 291 ARG A CG  1 
ATOM   2212 C CD  . ARG A 1 283 ? 19.609 23.859 91.632 1.00 83.47  ? 291 ARG A CD  1 
ATOM   2213 N NE  . ARG A 1 283 ? 18.888 23.594 92.874 1.00 84.87  ? 291 ARG A NE  1 
ATOM   2214 C CZ  . ARG A 1 283 ? 17.566 23.595 93.003 1.00 80.39  ? 291 ARG A CZ  1 
ATOM   2215 N NH1 . ARG A 1 283 ? 16.782 24.148 92.094 1.00 81.36  ? 291 ARG A NH1 1 
ATOM   2216 N NH2 . ARG A 1 283 ? 17.019 23.035 94.078 1.00 79.42  ? 291 ARG A NH2 1 
ATOM   2217 N N   . VAL A 1 284 ? 25.010 23.655 88.854 1.00 51.03  ? 292 VAL A N   1 
ATOM   2218 C CA  . VAL A 1 284 ? 25.739 23.702 87.600 1.00 49.52  ? 292 VAL A CA  1 
ATOM   2219 C C   . VAL A 1 284 ? 25.767 22.308 86.990 1.00 48.11  ? 292 VAL A C   1 
ATOM   2220 O O   . VAL A 1 284 ? 26.292 21.383 87.601 1.00 51.99  ? 292 VAL A O   1 
ATOM   2221 C CB  . VAL A 1 284 ? 27.168 24.233 87.794 1.00 47.39  ? 292 VAL A CB  1 
ATOM   2222 C CG1 . VAL A 1 284 ? 27.941 24.223 86.476 1.00 50.71  ? 292 VAL A CG1 1 
ATOM   2223 C CG2 . VAL A 1 284 ? 27.154 25.620 88.412 1.00 49.85  ? 292 VAL A CG2 1 
ATOM   2224 N N   . ASP A 1 285 ? 25.197 22.165 85.790 1.00 44.30  ? 293 ASP A N   1 
ATOM   2225 C CA  . ASP A 1 285 ? 25.309 20.925 85.045 1.00 45.55  ? 293 ASP A CA  1 
ATOM   2226 C C   . ASP A 1 285 ? 26.403 21.106 83.996 1.00 46.34  ? 293 ASP A C   1 
ATOM   2227 O O   . ASP A 1 285 ? 26.478 22.141 83.336 1.00 43.30  ? 293 ASP A O   1 
ATOM   2228 C CB  . ASP A 1 285 ? 23.969 20.519 84.408 1.00 52.68  ? 293 ASP A CB  1 
ATOM   2229 C CG  . ASP A 1 285 ? 22.806 20.447 85.389 1.00 60.38  ? 293 ASP A CG  1 
ATOM   2230 O OD1 . ASP A 1 285 ? 23.016 19.978 86.521 1.00 65.16  ? 293 ASP A OD1 1 
ATOM   2231 O OD2 . ASP A 1 285 ? 21.680 20.844 85.010 1.00 68.05  ? 293 ASP A OD2 1 
ATOM   2232 N N   . TYR A 1 286 ? 27.272 20.097 83.892 1.00 42.32  ? 294 TYR A N   1 
ATOM   2233 C CA  . TYR A 1 286 ? 28.328 20.063 82.899 1.00 39.93  ? 294 TYR A CA  1 
ATOM   2234 C C   . TYR A 1 286 ? 28.040 18.876 81.991 1.00 39.52  ? 294 TYR A C   1 
ATOM   2235 O O   . TYR A 1 286 ? 27.863 17.766 82.480 1.00 38.92  ? 294 TYR A O   1 
ATOM   2236 C CB  . TYR A 1 286 ? 29.705 19.928 83.552 1.00 38.99  ? 294 TYR A CB  1 
ATOM   2237 C CG  . TYR A 1 286 ? 30.827 19.726 82.560 1.00 36.08  ? 294 TYR A CG  1 
ATOM   2238 C CD1 . TYR A 1 286 ? 31.362 20.796 81.857 1.00 34.46  ? 294 TYR A CD1 1 
ATOM   2239 C CD2 . TYR A 1 286 ? 31.334 18.461 82.304 1.00 35.73  ? 294 TYR A CD2 1 
ATOM   2240 C CE1 . TYR A 1 286 ? 32.394 20.613 80.939 1.00 35.08  ? 294 TYR A CE1 1 
ATOM   2241 C CE2 . TYR A 1 286 ? 32.353 18.261 81.381 1.00 37.58  ? 294 TYR A CE2 1 
ATOM   2242 C CZ  . TYR A 1 286 ? 32.890 19.340 80.704 1.00 36.71  ? 294 TYR A CZ  1 
ATOM   2243 O OH  . TYR A 1 286 ? 33.911 19.119 79.801 1.00 36.23  ? 294 TYR A OH  1 
ATOM   2244 N N   . ILE A 1 287 ? 27.983 19.127 80.676 1.00 40.33  ? 295 ILE A N   1 
ATOM   2245 C CA  . ILE A 1 287 ? 27.677 18.089 79.707 1.00 39.16  ? 295 ILE A CA  1 
ATOM   2246 C C   . ILE A 1 287 ? 28.696 18.135 78.574 1.00 41.37  ? 295 ILE A C   1 
ATOM   2247 O O   . ILE A 1 287 ? 28.898 19.171 77.936 1.00 40.66  ? 295 ILE A O   1 
ATOM   2248 C CB  . ILE A 1 287 ? 26.229 18.216 79.202 1.00 43.62  ? 295 ILE A CB  1 
ATOM   2249 C CG1 . ILE A 1 287 ? 25.241 18.229 80.391 1.00 49.12  ? 295 ILE A CG1 1 
ATOM   2250 C CG2 . ILE A 1 287 ? 25.883 17.109 78.209 1.00 44.42  ? 295 ILE A CG2 1 
ATOM   2251 C CD1 . ILE A 1 287 ? 23.822 18.288 79.997 1.00 50.93  ? 295 ILE A CD1 1 
ATOM   2252 N N   . GLU A 1 288 ? 29.324 16.980 78.340 1.00 40.09  ? 296 GLU A N   1 
ATOM   2253 C CA  . GLU A 1 288 ? 30.387 16.839 77.364 1.00 40.43  ? 296 GLU A CA  1 
ATOM   2254 C C   . GLU A 1 288 ? 29.956 15.859 76.280 1.00 39.00  ? 296 GLU A C   1 
ATOM   2255 O O   . GLU A 1 288 ? 29.665 14.705 76.579 1.00 39.94  ? 296 GLU A O   1 
ATOM   2256 C CB  . GLU A 1 288 ? 31.653 16.346 78.066 1.00 42.53  ? 296 GLU A CB  1 
ATOM   2257 C CG  . GLU A 1 288 ? 32.895 16.438 77.212 1.00 43.36  ? 296 GLU A CG  1 
ATOM   2258 C CD  . GLU A 1 288 ? 34.163 16.026 77.928 1.00 41.25  ? 296 GLU A CD  1 
ATOM   2259 O OE1 . GLU A 1 288 ? 34.424 16.551 79.032 1.00 39.52  ? 296 GLU A OE1 1 
ATOM   2260 O OE2 . GLU A 1 288 ? 34.908 15.189 77.373 1.00 44.21  ? 296 GLU A OE2 1 
ATOM   2261 N N   . PHE A 1 289 ? 29.906 16.332 75.028 1.00 34.85  ? 297 PHE A N   1 
ATOM   2262 C CA  . PHE A 1 289 ? 29.586 15.480 73.894 1.00 36.02  ? 297 PHE A CA  1 
ATOM   2263 C C   . PHE A 1 289 ? 30.858 14.882 73.296 1.00 38.16  ? 297 PHE A C   1 
ATOM   2264 O O   . PHE A 1 289 ? 31.617 15.571 72.622 1.00 33.53  ? 297 PHE A O   1 
ATOM   2265 C CB  . PHE A 1 289 ? 28.777 16.248 72.842 1.00 37.09  ? 297 PHE A CB  1 
ATOM   2266 C CG  . PHE A 1 289 ? 27.340 16.415 73.265 1.00 37.11  ? 297 PHE A CG  1 
ATOM   2267 C CD1 . PHE A 1 289 ? 26.983 17.363 74.208 1.00 37.76  ? 297 PHE A CD1 1 
ATOM   2268 C CD2 . PHE A 1 289 ? 26.354 15.582 72.765 1.00 36.96  ? 297 PHE A CD2 1 
ATOM   2269 C CE1 . PHE A 1 289 ? 25.657 17.501 74.610 1.00 37.14  ? 297 PHE A CE1 1 
ATOM   2270 C CE2 . PHE A 1 289 ? 25.034 15.721 73.172 1.00 36.00  ? 297 PHE A CE2 1 
ATOM   2271 C CZ  . PHE A 1 289 ? 24.695 16.674 74.094 1.00 35.99  ? 297 PHE A CZ  1 
ATOM   2272 N N   . GLU A 1 290 ? 31.071 13.586 73.560 1.00 44.23  ? 298 GLU A N   1 
ATOM   2273 C CA  . GLU A 1 290 ? 32.279 12.885 73.155 1.00 45.54  ? 298 GLU A CA  1 
ATOM   2274 C C   . GLU A 1 290 ? 32.581 13.085 71.673 1.00 40.01  ? 298 GLU A C   1 
ATOM   2275 O O   . GLU A 1 290 ? 31.689 12.981 70.836 1.00 37.72  ? 298 GLU A O   1 
ATOM   2276 C CB  . GLU A 1 290 ? 32.152 11.376 73.422 1.00 52.44  ? 298 GLU A CB  1 
ATOM   2277 C CG  . GLU A 1 290 ? 31.964 10.986 74.877 1.00 61.78  ? 298 GLU A CG  1 
ATOM   2278 C CD  . GLU A 1 290 ? 31.648 9.512  75.057 1.00 70.59  ? 298 GLU A CD  1 
ATOM   2279 O OE1 . GLU A 1 290 ? 32.514 8.672  74.719 1.00 65.28  ? 298 GLU A OE1 1 
ATOM   2280 O OE2 . GLU A 1 290 ? 30.524 9.195  75.512 1.00 78.48  ? 298 GLU A OE2 1 
ATOM   2281 N N   . ASN A 1 291 ? 33.849 13.380 71.375 1.00 39.36  ? 299 ASN A N   1 
ATOM   2282 C CA  . ASN A 1 291 ? 34.367 13.386 70.017 1.00 40.98  ? 299 ASN A CA  1 
ATOM   2283 C C   . ASN A 1 291 ? 33.906 14.576 69.179 1.00 38.95  ? 299 ASN A C   1 
ATOM   2284 O O   . ASN A 1 291 ? 34.140 14.591 67.978 1.00 42.18  ? 299 ASN A O   1 
ATOM   2285 C CB  . ASN A 1 291 ? 34.001 12.074 69.277 1.00 44.46  ? 299 ASN A CB  1 
ATOM   2286 C CG  . ASN A 1 291 ? 34.260 10.830 70.107 1.00 50.47  ? 299 ASN A CG  1 
ATOM   2287 O OD1 . ASN A 1 291 ? 33.370 9.985  70.331 1.00 51.91  ? 299 ASN A OD1 1 
ATOM   2288 N ND2 . ASN A 1 291 ? 35.482 10.702 70.599 1.00 48.73  ? 299 ASN A ND2 1 
ATOM   2289 N N   . LYS A 1 292 ? 33.272 15.574 69.805 1.00 36.43  ? 300 LYS A N   1 
ATOM   2290 C CA  . LYS A 1 292 ? 32.749 16.711 69.064 1.00 34.47  ? 300 LYS A CA  1 
ATOM   2291 C C   . LYS A 1 292 ? 33.672 17.912 69.229 1.00 32.01  ? 300 LYS A C   1 
ATOM   2292 O O   . LYS A 1 292 ? 34.288 18.090 70.277 1.00 35.41  ? 300 LYS A O   1 
ATOM   2293 C CB  . LYS A 1 292 ? 31.326 17.070 69.511 1.00 33.67  ? 300 LYS A CB  1 
ATOM   2294 C CG  . LYS A 1 292 ? 30.323 15.941 69.342 1.00 38.05  ? 300 LYS A CG  1 
ATOM   2295 C CD  . LYS A 1 292 ? 30.135 15.525 67.895 1.00 41.78  ? 300 LYS A CD  1 
ATOM   2296 C CE  . LYS A 1 292 ? 29.253 14.319 67.753 1.00 47.01  ? 300 LYS A CE  1 
ATOM   2297 N NZ  . LYS A 1 292 ? 29.147 13.891 66.341 1.00 49.03  ? 300 LYS A NZ  1 
ATOM   2298 N N   . GLU A 1 293 ? 33.763 18.706 68.163 1.00 32.99  ? 301 GLU A N   1 
ATOM   2299 C CA  . GLU A 1 293 ? 34.527 19.941 68.152 1.00 34.92  ? 301 GLU A CA  1 
ATOM   2300 C C   . GLU A 1 293 ? 33.607 21.133 68.411 1.00 33.60  ? 301 GLU A C   1 
ATOM   2301 O O   . GLU A 1 293 ? 32.401 20.968 68.593 1.00 29.19  ? 301 GLU A O   1 
ATOM   2302 C CB  . GLU A 1 293 ? 35.269 20.067 66.817 1.00 37.66  ? 301 GLU A CB  1 
ATOM   2303 C CG  . GLU A 1 293 ? 36.441 19.097 66.715 1.00 41.65  ? 301 GLU A CG  1 
ATOM   2304 C CD  . GLU A 1 293 ? 37.208 19.153 65.408 1.00 44.23  ? 301 GLU A CD  1 
ATOM   2305 O OE1 . GLU A 1 293 ? 36.708 19.777 64.446 1.00 47.58  ? 301 GLU A OE1 1 
ATOM   2306 O OE2 . GLU A 1 293 ? 38.323 18.590 65.352 1.00 49.95  ? 301 GLU A OE2 1 
ATOM   2307 N N   . HIS A 1 294 ? 34.207 22.327 68.457 1.00 33.49  ? 302 HIS A N   1 
ATOM   2308 C CA  . HIS A 1 294 ? 33.499 23.539 68.828 1.00 33.00  ? 302 HIS A CA  1 
ATOM   2309 C C   . HIS A 1 294 ? 32.314 23.818 67.908 1.00 30.80  ? 302 HIS A C   1 
ATOM   2310 O O   . HIS A 1 294 ? 32.428 23.723 66.689 1.00 28.22  ? 302 HIS A O   1 
ATOM   2311 C CB  . HIS A 1 294 ? 34.460 24.730 68.807 1.00 33.23  ? 302 HIS A CB  1 
ATOM   2312 C CG  . HIS A 1 294 ? 33.886 25.998 69.365 1.00 36.14  ? 302 HIS A CG  1 
ATOM   2313 N ND1 . HIS A 1 294 ? 33.431 27.010 68.530 1.00 40.69  ? 302 HIS A ND1 1 
ATOM   2314 C CD2 . HIS A 1 294 ? 33.690 26.374 70.647 1.00 36.14  ? 302 HIS A CD2 1 
ATOM   2315 C CE1 . HIS A 1 294 ? 32.996 27.974 69.329 1.00 40.73  ? 302 HIS A CE1 1 
ATOM   2316 N NE2 . HIS A 1 294 ? 33.136 27.632 70.615 1.00 39.59  ? 302 HIS A NE2 1 
ATOM   2317 N N   . GLY A 1 295 ? 31.175 24.176 68.507 1.00 31.92  ? 303 GLY A N   1 
ATOM   2318 C CA  . GLY A 1 295 ? 30.011 24.588 67.739 1.00 32.03  ? 303 GLY A CA  1 
ATOM   2319 C C   . GLY A 1 295 ? 29.321 23.473 66.954 1.00 33.06  ? 303 GLY A C   1 
ATOM   2320 O O   . GLY A 1 295 ? 28.583 23.745 66.012 1.00 34.43  ? 303 GLY A O   1 
ATOM   2321 N N   . PHE A 1 296 ? 29.535 22.217 67.365 1.00 32.33  ? 304 PHE A N   1 
ATOM   2322 C CA  . PHE A 1 296 ? 28.907 21.085 66.698 1.00 32.05  ? 304 PHE A CA  1 
ATOM   2323 C C   . PHE A 1 296 ? 27.389 21.243 66.597 1.00 30.28  ? 304 PHE A C   1 
ATOM   2324 O O   . PHE A 1 296 ? 26.794 20.844 65.600 1.00 33.62  ? 304 PHE A O   1 
ATOM   2325 C CB  . PHE A 1 296 ? 29.288 19.765 67.419 1.00 32.13  ? 304 PHE A CB  1 
ATOM   2326 C CG  . PHE A 1 296 ? 28.733 19.615 68.810 1.00 28.57  ? 304 PHE A CG  1 
ATOM   2327 C CD1 . PHE A 1 296 ? 27.487 19.052 69.019 1.00 31.00  ? 304 PHE A CD1 1 
ATOM   2328 C CD2 . PHE A 1 296 ? 29.441 20.064 69.907 1.00 27.84  ? 304 PHE A CD2 1 
ATOM   2329 C CE1 . PHE A 1 296 ? 26.965 18.936 70.311 1.00 29.68  ? 304 PHE A CE1 1 
ATOM   2330 C CE2 . PHE A 1 296 ? 28.918 19.952 71.189 1.00 28.89  ? 304 PHE A CE2 1 
ATOM   2331 C CZ  . PHE A 1 296 ? 27.684 19.388 71.385 1.00 29.01  ? 304 PHE A CZ  1 
ATOM   2332 N N   . TYR A 1 297 ? 26.783 21.847 67.627 1.00 30.90  ? 305 TYR A N   1 
ATOM   2333 C CA  . TYR A 1 297 ? 25.335 22.011 67.730 1.00 29.90  ? 305 TYR A CA  1 
ATOM   2334 C C   . TYR A 1 297 ? 24.737 22.933 66.670 1.00 30.66  ? 305 TYR A C   1 
ATOM   2335 O O   . TYR A 1 297 ? 23.564 22.796 66.344 1.00 31.78  ? 305 TYR A O   1 
ATOM   2336 C CB  . TYR A 1 297 ? 24.932 22.523 69.151 1.00 30.14  ? 305 TYR A CB  1 
ATOM   2337 C CG  . TYR A 1 297 ? 25.892 23.555 69.701 1.00 30.58  ? 305 TYR A CG  1 
ATOM   2338 C CD1 . TYR A 1 297 ? 25.806 24.890 69.324 1.00 31.78  ? 305 TYR A CD1 1 
ATOM   2339 C CD2 . TYR A 1 297 ? 26.940 23.182 70.530 1.00 32.73  ? 305 TYR A CD2 1 
ATOM   2340 C CE1 . TYR A 1 297 ? 26.719 25.832 69.792 1.00 32.51  ? 305 TYR A CE1 1 
ATOM   2341 C CE2 . TYR A 1 297 ? 27.860 24.111 70.998 1.00 33.62  ? 305 TYR A CE2 1 
ATOM   2342 C CZ  . TYR A 1 297 ? 27.755 25.433 70.620 1.00 34.71  ? 305 TYR A CZ  1 
ATOM   2343 O OH  . TYR A 1 297 ? 28.691 26.325 71.098 1.00 39.94  ? 305 TYR A OH  1 
ATOM   2344 N N   . SER A 1 298 ? 25.528 23.887 66.159 1.00 31.35  ? 306 SER A N   1 
ATOM   2345 C CA  . SER A 1 298 ? 25.073 24.790 65.108 1.00 32.40  ? 306 SER A CA  1 
ATOM   2346 C C   . SER A 1 298 ? 25.725 24.534 63.753 1.00 33.71  ? 306 SER A C   1 
ATOM   2347 O O   . SER A 1 298 ? 25.148 24.887 62.727 1.00 32.74  ? 306 SER A O   1 
ATOM   2348 C CB  . SER A 1 298 ? 25.306 26.248 65.496 1.00 31.68  ? 306 SER A CB  1 
ATOM   2349 O OG  . SER A 1 298 ? 26.642 26.467 65.914 1.00 35.56  ? 306 SER A OG  1 
ATOM   2350 N N   . ASN A 1 299 ? 26.926 23.935 63.757 1.00 32.22  ? 307 ASN A N   1 
ATOM   2351 C CA  . ASN A 1 299 ? 27.620 23.588 62.523 1.00 34.82  ? 307 ASN A CA  1 
ATOM   2352 C C   . ASN A 1 299 ? 27.000 22.396 61.801 1.00 34.33  ? 307 ASN A C   1 
ATOM   2353 O O   . ASN A 1 299 ? 27.078 22.313 60.584 1.00 38.69  ? 307 ASN A O   1 
ATOM   2354 C CB  . ASN A 1 299 ? 29.098 23.276 62.802 1.00 37.86  ? 307 ASN A CB  1 
ATOM   2355 C CG  . ASN A 1 299 ? 29.901 24.498 63.146 1.00 38.58  ? 307 ASN A CG  1 
ATOM   2356 O OD1 . ASN A 1 299 ? 29.580 25.601 62.717 1.00 39.64  ? 307 ASN A OD1 1 
ATOM   2357 N ND2 . ASN A 1 299 ? 30.979 24.326 63.902 1.00 36.78  ? 307 ASN A ND2 1 
ATOM   2358 N N   . TYR A 1 300 ? 26.388 21.483 62.561 1.00 35.76  ? 308 TYR A N   1 
ATOM   2359 C CA  . TYR A 1 300 ? 25.747 20.308 61.999 1.00 35.76  ? 308 TYR A CA  1 
ATOM   2360 C C   . TYR A 1 300 ? 24.315 20.198 62.511 1.00 36.97  ? 308 TYR A C   1 
ATOM   2361 O O   . TYR A 1 300 ? 24.026 19.347 63.348 1.00 36.91  ? 308 TYR A O   1 
ATOM   2362 C CB  . TYR A 1 300 ? 26.548 19.055 62.368 1.00 37.20  ? 308 TYR A CB  1 
ATOM   2363 C CG  . TYR A 1 300 ? 28.000 19.124 61.966 1.00 36.60  ? 308 TYR A CG  1 
ATOM   2364 C CD1 . TYR A 1 300 ? 28.390 18.914 60.650 1.00 39.28  ? 308 TYR A CD1 1 
ATOM   2365 C CD2 . TYR A 1 300 ? 28.984 19.430 62.895 1.00 36.85  ? 308 TYR A CD2 1 
ATOM   2366 C CE1 . TYR A 1 300 ? 29.732 18.974 60.278 1.00 38.19  ? 308 TYR A CE1 1 
ATOM   2367 C CE2 . TYR A 1 300 ? 30.322 19.509 62.531 1.00 36.72  ? 308 TYR A CE2 1 
ATOM   2368 C CZ  . TYR A 1 300 ? 30.694 19.267 61.227 1.00 37.01  ? 308 TYR A CZ  1 
ATOM   2369 O OH  . TYR A 1 300 ? 32.016 19.349 60.885 1.00 40.81  ? 308 TYR A OH  1 
ATOM   2370 N N   . PRO A 1 301 ? 23.374 21.036 62.015 1.00 42.91  ? 309 PRO A N   1 
ATOM   2371 C CA  . PRO A 1 301 ? 22.011 21.059 62.541 1.00 46.78  ? 309 PRO A CA  1 
ATOM   2372 C C   . PRO A 1 301 ? 21.270 19.721 62.456 1.00 49.83  ? 309 PRO A C   1 
ATOM   2373 O O   . PRO A 1 301 ? 20.494 19.400 63.351 1.00 51.44  ? 309 PRO A O   1 
ATOM   2374 C CB  . PRO A 1 301 ? 21.313 22.126 61.686 1.00 46.31  ? 309 PRO A CB  1 
ATOM   2375 C CG  . PRO A 1 301 ? 22.434 22.945 61.080 1.00 48.49  ? 309 PRO A CG  1 
ATOM   2376 C CD  . PRO A 1 301 ? 23.577 21.987 60.909 1.00 44.78  ? 309 PRO A CD  1 
ATOM   2377 N N   . SER A 1 302 ? 21.503 18.954 61.380 1.00 50.53  ? 310 SER A N   1 
ATOM   2378 C CA  . SER A 1 302 ? 20.852 17.660 61.194 1.00 55.12  ? 310 SER A CA  1 
ATOM   2379 C C   . SER A 1 302 ? 21.367 16.553 62.109 1.00 49.17  ? 310 SER A C   1 
ATOM   2380 O O   . SER A 1 302 ? 20.740 15.502 62.217 1.00 54.08  ? 310 SER A O   1 
ATOM   2381 C CB  . SER A 1 302 ? 21.012 17.164 59.756 1.00 57.65  ? 310 SER A CB  1 
ATOM   2382 O OG  . SER A 1 302 ? 20.331 18.005 58.844 1.00 66.72  ? 310 SER A OG  1 
ATOM   2383 N N   . SER A 1 303 ? 22.526 16.778 62.734 1.00 44.41  ? 311 SER A N   1 
ATOM   2384 C CA  . SER A 1 303 ? 23.188 15.733 63.492 1.00 43.99  ? 311 SER A CA  1 
ATOM   2385 C C   . SER A 1 303 ? 22.405 15.371 64.750 1.00 43.85  ? 311 SER A C   1 
ATOM   2386 O O   . SER A 1 303 ? 21.640 16.180 65.281 1.00 41.00  ? 311 SER A O   1 
ATOM   2387 C CB  . SER A 1 303 ? 24.607 16.150 63.864 1.00 43.37  ? 311 SER A CB  1 
ATOM   2388 O OG  . SER A 1 303 ? 24.602 17.263 64.743 1.00 41.93  ? 311 SER A OG  1 
ATOM   2389 N N   . GLU A 1 304 ? 22.629 14.139 65.216 1.00 43.12  ? 312 GLU A N   1 
ATOM   2390 C CA  . GLU A 1 304 ? 22.004 13.644 66.428 1.00 43.52  ? 312 GLU A CA  1 
ATOM   2391 C C   . GLU A 1 304 ? 22.410 14.501 67.627 1.00 39.64  ? 312 GLU A C   1 
ATOM   2392 O O   . GLU A 1 304 ? 21.564 14.863 68.437 1.00 37.78  ? 312 GLU A O   1 
ATOM   2393 C CB  . GLU A 1 304 ? 22.365 12.157 66.634 1.00 45.72  ? 312 GLU A CB  1 
ATOM   2394 C CG  . GLU A 1 304 ? 21.743 11.522 67.864 1.00 51.60  ? 312 GLU A CG  1 
ATOM   2395 C CD  . GLU A 1 304 ? 20.223 11.504 67.917 1.00 60.15  ? 312 GLU A CD  1 
ATOM   2396 O OE1 . GLU A 1 304 ? 19.578 11.705 66.861 1.00 65.23  ? 312 GLU A OE1 1 
ATOM   2397 O OE2 . GLU A 1 304 ? 19.675 11.303 69.028 1.00 68.34  ? 312 GLU A OE2 1 
ATOM   2398 N N   . ALA A 1 305 ? 23.704 14.824 67.723 1.00 35.69  ? 313 ALA A N   1 
ATOM   2399 C CA  . ALA A 1 305 ? 24.237 15.610 68.824 1.00 35.22  ? 313 ALA A CA  1 
ATOM   2400 C C   . ALA A 1 305 ? 23.589 16.993 68.941 1.00 32.12  ? 313 ALA A C   1 
ATOM   2401 O O   . ALA A 1 305 ? 23.312 17.446 70.050 1.00 31.46  ? 313 ALA A O   1 
ATOM   2402 C CB  . ALA A 1 305 ? 25.745 15.755 68.674 1.00 32.89  ? 313 ALA A CB  1 
ATOM   2403 N N   . ALA A 1 306 ? 23.350 17.650 67.799 1.00 33.01  ? 314 ALA A N   1 
ATOM   2404 C CA  . ALA A 1 306 ? 22.696 18.951 67.774 1.00 32.76  ? 314 ALA A CA  1 
ATOM   2405 C C   . ALA A 1 306 ? 21.276 18.855 68.325 1.00 34.15  ? 314 ALA A C   1 
ATOM   2406 O O   . ALA A 1 306 ? 20.872 19.673 69.149 1.00 29.76  ? 314 ALA A O   1 
ATOM   2407 C CB  . ALA A 1 306 ? 22.683 19.517 66.369 1.00 33.29  ? 314 ALA A CB  1 
ATOM   2408 N N   . GLU A 1 307 ? 20.533 17.830 67.886 1.00 35.22  ? 315 GLU A N   1 
ATOM   2409 C CA  . GLU A 1 307 ? 19.180 17.608 68.365 1.00 35.25  ? 315 GLU A CA  1 
ATOM   2410 C C   . GLU A 1 307 ? 19.170 17.330 69.864 1.00 32.63  ? 315 GLU A C   1 
ATOM   2411 O O   . GLU A 1 307 ? 18.281 17.799 70.568 1.00 34.05  ? 315 GLU A O   1 
ATOM   2412 C CB  . GLU A 1 307 ? 18.502 16.467 67.594 1.00 42.19  ? 315 GLU A CB  1 
ATOM   2413 C CG  . GLU A 1 307 ? 18.304 16.812 66.127 1.00 52.28  ? 315 GLU A CG  1 
ATOM   2414 C CD  . GLU A 1 307 ? 17.485 18.060 65.849 1.00 63.08  ? 315 GLU A CD  1 
ATOM   2415 O OE1 . GLU A 1 307 ? 16.475 18.285 66.554 1.00 69.06  ? 315 GLU A OE1 1 
ATOM   2416 O OE2 . GLU A 1 307 ? 17.861 18.817 64.923 1.00 68.07  ? 315 GLU A OE2 1 
ATOM   2417 N N   . GLN A 1 308 ? 20.167 16.583 70.351 1.00 30.69  ? 316 GLN A N   1 
ATOM   2418 C CA  . GLN A 1 308 ? 20.256 16.271 71.770 1.00 32.39  ? 316 GLN A CA  1 
ATOM   2419 C C   . GLN A 1 308 ? 20.526 17.510 72.623 1.00 31.89  ? 316 GLN A C   1 
ATOM   2420 O O   . GLN A 1 308 ? 20.007 17.626 73.727 1.00 28.47  ? 316 GLN A O   1 
ATOM   2421 C CB  . GLN A 1 308 ? 21.344 15.219 72.027 1.00 33.82  ? 316 GLN A CB  1 
ATOM   2422 C CG  . GLN A 1 308 ? 20.944 13.837 71.495 1.00 36.24  ? 316 GLN A CG  1 
ATOM   2423 C CD  . GLN A 1 308 ? 21.950 12.762 71.826 1.00 37.61  ? 316 GLN A CD  1 
ATOM   2424 O OE1 . GLN A 1 308 ? 22.771 12.891 72.736 1.00 40.68  ? 316 GLN A OE1 1 
ATOM   2425 N NE2 . GLN A 1 308 ? 21.868 11.649 71.112 1.00 37.21  ? 316 GLN A NE2 1 
ATOM   2426 N N   . VAL A 1 309 ? 21.359 18.423 72.110 1.00 31.76  ? 317 VAL A N   1 
ATOM   2427 C CA  . VAL A 1 309 ? 21.612 19.683 72.794 1.00 32.55  ? 317 VAL A CA  1 
ATOM   2428 C C   . VAL A 1 309 ? 20.308 20.463 72.947 1.00 29.51  ? 317 VAL A C   1 
ATOM   2429 O O   . VAL A 1 309 ? 20.015 20.977 74.023 1.00 30.09  ? 317 VAL A O   1 
ATOM   2430 C CB  . VAL A 1 309 ? 22.699 20.500 72.067 1.00 31.28  ? 317 VAL A CB  1 
ATOM   2431 C CG1 . VAL A 1 309 ? 22.787 21.933 72.596 1.00 32.01  ? 317 VAL A CG1 1 
ATOM   2432 C CG2 . VAL A 1 309 ? 24.046 19.808 72.166 1.00 32.57  ? 317 VAL A CG2 1 
ATOM   2433 N N   . LEU A 1 310 ? 19.517 20.527 71.871 1.00 30.67  ? 318 LEU A N   1 
ATOM   2434 C CA  . LEU A 1 310 ? 18.241 21.227 71.922 1.00 31.70  ? 318 LEU A CA  1 
ATOM   2435 C C   . LEU A 1 310 ? 17.286 20.616 72.948 1.00 33.43  ? 318 LEU A C   1 
ATOM   2436 O O   . LEU A 1 310 ? 16.633 21.345 73.690 1.00 31.18  ? 318 LEU A O   1 
ATOM   2437 C CB  . LEU A 1 310 ? 17.607 21.230 70.553 1.00 33.45  ? 318 LEU A CB  1 
ATOM   2438 C CG  . LEU A 1 310 ? 18.322 22.109 69.539 1.00 40.78  ? 318 LEU A CG  1 
ATOM   2439 C CD1 . LEU A 1 310 ? 17.862 21.782 68.156 1.00 43.21  ? 318 LEU A CD1 1 
ATOM   2440 C CD2 . LEU A 1 310 ? 18.110 23.574 69.848 1.00 43.37  ? 318 LEU A CD2 1 
ATOM   2441 N N   . ARG A 1 311 ? 17.222 19.277 73.002 1.00 33.93  ? 319 ARG A N   1 
ATOM   2442 C CA  . ARG A 1 311 ? 16.395 18.600 73.991 1.00 36.68  ? 319 ARG A CA  1 
ATOM   2443 C C   . ARG A 1 311 ? 16.851 18.899 75.414 1.00 31.21  ? 319 ARG A C   1 
ATOM   2444 O O   . ARG A 1 311 ? 16.028 19.123 76.296 1.00 31.52  ? 319 ARG A O   1 
ATOM   2445 C CB  . ARG A 1 311 ? 16.370 17.066 73.772 1.00 44.84  ? 319 ARG A CB  1 
ATOM   2446 C CG  . ARG A 1 311 ? 15.364 16.641 72.700 1.00 54.90  ? 319 ARG A CG  1 
ATOM   2447 C CD  . ARG A 1 311 ? 14.530 15.452 73.131 1.00 66.38  ? 319 ARG A CD  1 
ATOM   2448 N NE  . ARG A 1 311 ? 14.010 15.617 74.487 1.00 70.72  ? 319 ARG A NE  1 
ATOM   2449 C CZ  . ARG A 1 311 ? 14.110 14.703 75.446 1.00 72.36  ? 319 ARG A CZ  1 
ATOM   2450 N NH1 . ARG A 1 311 ? 14.259 13.419 75.163 1.00 64.46  ? 319 ARG A NH1 1 
ATOM   2451 N NH2 . ARG A 1 311 ? 14.036 15.083 76.719 1.00 74.92  ? 319 ARG A NH2 1 
ATOM   2452 N N   . ILE A 1 312 ? 18.165 18.909 75.633 1.00 30.47  ? 320 ILE A N   1 
ATOM   2453 C CA  . ILE A 1 312 ? 18.706 19.196 76.951 1.00 32.76  ? 320 ILE A CA  1 
ATOM   2454 C C   . ILE A 1 312 ? 18.440 20.628 77.421 1.00 31.65  ? 320 ILE A C   1 
ATOM   2455 O O   . ILE A 1 312 ? 18.158 20.855 78.595 1.00 30.66  ? 320 ILE A O   1 
ATOM   2456 C CB  . ILE A 1 312 ? 20.200 18.881 76.950 1.00 33.24  ? 320 ILE A CB  1 
ATOM   2457 C CG1 . ILE A 1 312 ? 20.432 17.365 76.863 1.00 36.06  ? 320 ILE A CG1 1 
ATOM   2458 C CG2 . ILE A 1 312 ? 20.896 19.457 78.167 1.00 34.03  ? 320 ILE A CG2 1 
ATOM   2459 C CD1 . ILE A 1 312 ? 21.845 16.999 76.588 1.00 35.32  ? 320 ILE A CD1 1 
ATOM   2460 N N   . ILE A 1 313 ? 18.563 21.599 76.511 1.00 30.48  ? 321 ILE A N   1 
ATOM   2461 C CA  . ILE A 1 313 ? 18.242 22.980 76.840 1.00 30.12  ? 321 ILE A CA  1 
ATOM   2462 C C   . ILE A 1 313 ? 16.765 23.078 77.223 1.00 29.47  ? 321 ILE A C   1 
ATOM   2463 O O   . ILE A 1 313 ? 16.415 23.745 78.197 1.00 30.20  ? 321 ILE A O   1 
ATOM   2464 C CB  . ILE A 1 313 ? 18.605 23.948 75.688 1.00 30.68  ? 321 ILE A CB  1 
ATOM   2465 C CG1 . ILE A 1 313 ? 20.126 23.960 75.442 1.00 31.20  ? 321 ILE A CG1 1 
ATOM   2466 C CG2 . ILE A 1 313 ? 18.072 25.359 75.983 1.00 30.83  ? 321 ILE A CG2 1 
ATOM   2467 C CD1 . ILE A 1 313 ? 20.548 24.670 74.198 1.00 32.61  ? 321 ILE A CD1 1 
ATOM   2468 N N   . GLY A 1 314 ? 15.912 22.418 76.435 1.00 30.92  ? 322 GLY A N   1 
ATOM   2469 C CA  . GLY A 1 314 ? 14.481 22.379 76.692 1.00 33.37  ? 322 GLY A CA  1 
ATOM   2470 C C   . GLY A 1 314 ? 14.128 21.763 78.045 1.00 35.96  ? 322 GLY A C   1 
ATOM   2471 O O   . GLY A 1 314 ? 13.287 22.295 78.768 1.00 33.56  ? 322 GLY A O   1 
ATOM   2472 N N   . ASP A 1 315 ? 14.785 20.642 78.376 1.00 35.26  ? 323 ASP A N   1 
ATOM   2473 C CA  . ASP A 1 315 ? 14.594 19.982 79.658 1.00 36.46  ? 323 ASP A CA  1 
ATOM   2474 C C   . ASP A 1 315 ? 15.042 20.896 80.792 1.00 38.43  ? 323 ASP A C   1 
ATOM   2475 O O   . ASP A 1 315 ? 14.353 21.013 81.802 1.00 40.10  ? 323 ASP A O   1 
ATOM   2476 C CB  . ASP A 1 315 ? 15.373 18.656 79.716 1.00 39.63  ? 323 ASP A CB  1 
ATOM   2477 C CG  . ASP A 1 315 ? 14.846 17.562 78.797 1.00 42.17  ? 323 ASP A CG  1 
ATOM   2478 O OD1 . ASP A 1 315 ? 13.709 17.700 78.302 1.00 43.75  ? 323 ASP A OD1 1 
ATOM   2479 O OD2 . ASP A 1 315 ? 15.590 16.577 78.550 1.00 49.38  ? 323 ASP A OD2 1 
ATOM   2480 N N   . PHE A 1 316 ? 16.210 21.528 80.610 1.00 35.53  ? 324 PHE A N   1 
ATOM   2481 C CA  . PHE A 1 316 ? 16.734 22.496 81.558 1.00 34.35  ? 324 PHE A CA  1 
ATOM   2482 C C   . PHE A 1 316 ? 15.722 23.607 81.829 1.00 34.63  ? 324 PHE A C   1 
ATOM   2483 O O   . PHE A 1 316 ? 15.478 23.963 82.977 1.00 35.57  ? 324 PHE A O   1 
ATOM   2484 C CB  . PHE A 1 316 ? 18.037 23.063 81.001 1.00 34.07  ? 324 PHE A CB  1 
ATOM   2485 C CG  . PHE A 1 316 ? 18.717 24.119 81.826 1.00 34.12  ? 324 PHE A CG  1 
ATOM   2486 C CD1 . PHE A 1 316 ? 19.438 23.779 82.954 1.00 34.62  ? 324 PHE A CD1 1 
ATOM   2487 C CD2 . PHE A 1 316 ? 18.657 25.452 81.457 1.00 33.78  ? 324 PHE A CD2 1 
ATOM   2488 C CE1 . PHE A 1 316 ? 20.086 24.752 83.700 1.00 37.13  ? 324 PHE A CE1 1 
ATOM   2489 C CE2 . PHE A 1 316 ? 19.304 26.422 82.204 1.00 36.38  ? 324 PHE A CE2 1 
ATOM   2490 C CZ  . PHE A 1 316 ? 20.015 26.067 83.322 1.00 37.29  ? 324 PHE A CZ  1 
ATOM   2491 N N   . MET A 1 317 ? 15.117 24.127 80.756 1.00 34.09  ? 325 MET A N   1 
ATOM   2492 C CA  . MET A 1 317 ? 14.118 25.181 80.852 1.00 35.29  ? 325 MET A CA  1 
ATOM   2493 C C   . MET A 1 317 ? 12.862 24.695 81.578 1.00 38.92  ? 325 MET A C   1 
ATOM   2494 O O   . MET A 1 317 ? 12.355 25.372 82.471 1.00 35.07  ? 325 MET A O   1 
ATOM   2495 C CB  . MET A 1 317 ? 13.760 25.691 79.449 1.00 32.33  ? 325 MET A CB  1 
ATOM   2496 C CG  . MET A 1 317 ? 14.814 26.630 78.855 1.00 31.46  ? 325 MET A CG  1 
ATOM   2497 S SD  . MET A 1 317 ? 14.506 26.994 77.114 1.00 31.64  ? 325 MET A SD  1 
ATOM   2498 C CE  . MET A 1 317 ? 13.019 28.031 77.262 1.00 32.35  ? 325 MET A CE  1 
ATOM   2499 N N   . ASN A 1 318 ? 12.368 23.514 81.189 1.00 40.60  ? 326 ASN A N   1 
ATOM   2500 C CA  . ASN A 1 318 ? 11.212 22.910 81.836 1.00 46.28  ? 326 ASN A CA  1 
ATOM   2501 C C   . ASN A 1 318 ? 11.411 22.718 83.339 1.00 47.04  ? 326 ASN A C   1 
ATOM   2502 O O   . ASN A 1 318 ? 10.517 23.034 84.116 1.00 48.63  ? 326 ASN A O   1 
ATOM   2503 C CB  . ASN A 1 318 ? 10.860 21.572 81.185 1.00 47.65  ? 326 ASN A CB  1 
ATOM   2504 C CG  . ASN A 1 318 ? 10.290 21.723 79.798 1.00 52.89  ? 326 ASN A CG  1 
ATOM   2505 O OD1 . ASN A 1 318 ? 9.905  22.812 79.362 1.00 54.29  ? 326 ASN A OD1 1 
ATOM   2506 N ND2 . ASN A 1 318 ? 10.211 20.623 79.067 1.00 56.37  ? 326 ASN A ND2 1 
ATOM   2507 N N   . ASN A 1 319 ? 12.588 22.220 83.737 1.00 46.57  ? 327 ASN A N   1 
ATOM   2508 C CA  . ASN A 1 319 ? 12.889 21.970 85.138 1.00 46.39  ? 327 ASN A CA  1 
ATOM   2509 C C   . ASN A 1 319 ? 12.876 23.242 85.981 1.00 49.66  ? 327 ASN A C   1 
ATOM   2510 O O   . ASN A 1 319 ? 12.558 23.189 87.164 1.00 49.85  ? 327 ASN A O   1 
ATOM   2511 C CB  . ASN A 1 319 ? 14.249 21.270 85.292 1.00 48.12  ? 327 ASN A CB  1 
ATOM   2512 C CG  . ASN A 1 319 ? 14.246 19.825 84.837 1.00 53.78  ? 327 ASN A CG  1 
ATOM   2513 O OD1 . ASN A 1 319 ? 13.195 19.198 84.662 1.00 57.82  ? 327 ASN A OD1 1 
ATOM   2514 N ND2 . ASN A 1 319 ? 15.424 19.254 84.642 1.00 55.96  ? 327 ASN A ND2 1 
ATOM   2515 N N   . LEU A 1 320 ? 13.232 24.377 85.367 1.00 48.76  ? 328 LEU A N   1 
ATOM   2516 C CA  . LEU A 1 320 ? 13.347 25.637 86.082 1.00 44.42  ? 328 LEU A CA  1 
ATOM   2517 C C   . LEU A 1 320 ? 12.102 26.511 85.968 1.00 43.98  ? 328 LEU A C   1 
ATOM   2518 O O   . LEU A 1 320 ? 12.016 27.533 86.638 1.00 43.42  ? 328 LEU A O   1 
ATOM   2519 C CB  . LEU A 1 320 ? 14.559 26.408 85.551 1.00 42.66  ? 328 LEU A CB  1 
ATOM   2520 C CG  . LEU A 1 320 ? 15.899 25.773 85.842 1.00 43.88  ? 328 LEU A CG  1 
ATOM   2521 C CD1 . LEU A 1 320 ? 17.003 26.511 85.155 1.00 44.14  ? 328 LEU A CD1 1 
ATOM   2522 C CD2 . LEU A 1 320 ? 16.173 25.723 87.341 1.00 48.08  ? 328 LEU A CD2 1 
ATOM   2523 N N   . SER A 1 321 ? 11.145 26.095 85.132 1.00 47.68  ? 329 SER A N   1 
ATOM   2524 C CA  . SER A 1 321 ? 9.943  26.869 84.871 1.00 53.22  ? 329 SER A CA  1 
ATOM   2525 C C   . SER A 1 321 ? 8.745  26.460 85.762 1.00 55.91  ? 329 SER A C   1 
ATOM   2526 O O   . SER A 1 321 ? 8.761  25.414 86.404 1.00 51.68  ? 329 SER A O   1 
ATOM   2527 C CB  . SER A 1 321 ? 9.559  26.750 83.398 1.00 56.88  ? 329 SER A CB  1 
ATOM   2528 O OG  . SER A 1 321 ? 10.482 27.442 82.569 1.00 57.82  ? 329 SER A OG  1 
ATOM   2529 O OXT . SER A 1 321 ? 7.759  27.188 85.823 1.00 58.31  ? 329 SER A OXT 1 
HETATM 2530 C C1  . GOL B 2 .   ? 43.644 31.346 75.173 1.00 40.01  ? 401 GOL A C1  1 
HETATM 2531 O O1  . GOL B 2 .   ? 43.594 31.498 73.758 1.00 38.19  ? 401 GOL A O1  1 
HETATM 2532 C C2  . GOL B 2 .   ? 43.001 30.054 75.623 1.00 41.35  ? 401 GOL A C2  1 
HETATM 2533 O O2  . GOL B 2 .   ? 42.891 30.061 77.046 1.00 41.91  ? 401 GOL A O2  1 
HETATM 2534 C C3  . GOL B 2 .   ? 41.642 29.802 74.995 1.00 42.12  ? 401 GOL A C3  1 
HETATM 2535 O O3  . GOL B 2 .   ? 40.771 30.922 75.143 1.00 36.28  ? 401 GOL A O3  1 
HETATM 2536 C C1  . GOL C 2 .   ? 29.799 15.767 62.811 1.00 64.69  ? 402 GOL A C1  1 
HETATM 2537 O O1  . GOL C 2 .   ? 29.607 15.844 64.222 1.00 64.48  ? 402 GOL A O1  1 
HETATM 2538 C C2  . GOL C 2 .   ? 28.750 14.899 62.144 1.00 63.89  ? 402 GOL A C2  1 
HETATM 2539 O O2  . GOL C 2 .   ? 27.492 15.054 62.798 1.00 63.32  ? 402 GOL A O2  1 
HETATM 2540 C C3  . GOL C 2 .   ? 28.593 15.177 60.663 1.00 62.05  ? 402 GOL A C3  1 
HETATM 2541 O O3  . GOL C 2 .   ? 27.290 14.835 60.198 1.00 59.16  ? 402 GOL A O3  1 
HETATM 2542 O O   . HOH D 3 .   ? 19.755 41.182 90.259 1.00 39.50  ? 501 HOH A O   1 
HETATM 2543 O O   . HOH D 3 .   ? 0.561  44.047 66.969 1.00 36.53  ? 502 HOH A O   1 
HETATM 2544 O O   . HOH D 3 .   ? -1.059 36.188 68.510 1.00 47.00  ? 503 HOH A O   1 
HETATM 2545 O O   . HOH D 3 .   ? 20.137 35.916 86.718 1.00 38.89  ? 504 HOH A O   1 
HETATM 2546 O O   . HOH D 3 .   ? 27.567 42.228 64.005 1.00 19.72  ? 505 HOH A O   1 
HETATM 2547 O O   . HOH D 3 .   ? 40.500 33.964 56.187 1.00 39.02  ? 506 HOH A O   1 
HETATM 2548 O O   . HOH D 3 .   ? 23.988 11.312 74.349 1.00 38.22  ? 507 HOH A O   1 
HETATM 2549 O O   . HOH D 3 .   ? 25.419 49.945 73.365 1.00 44.25  ? 508 HOH A O   1 
HETATM 2550 O O   . HOH D 3 .   ? 30.487 40.573 84.685 1.00 37.00  ? 509 HOH A O   1 
HETATM 2551 O O   . HOH D 3 .   ? 46.347 36.330 73.360 1.00 34.65  ? 510 HOH A O   1 
HETATM 2552 O O   . HOH D 3 .   ? 30.980 24.090 71.323 1.00 30.26  ? 511 HOH A O   1 
HETATM 2553 O O   . HOH D 3 .   ? 43.721 12.062 56.842 1.00 47.55  ? 512 HOH A O   1 
HETATM 2554 O O   . HOH D 3 .   ? 45.795 29.548 77.509 1.00 39.97  ? 513 HOH A O   1 
HETATM 2555 O O   . HOH D 3 .   ? 27.717 42.505 81.734 1.00 35.30  ? 514 HOH A O   1 
HETATM 2556 O O   . HOH D 3 .   ? 23.058 34.846 88.338 1.00 39.22  ? 515 HOH A O   1 
HETATM 2557 O O   . HOH D 3 .   ? 19.063 36.486 58.008 1.00 35.55  ? 516 HOH A O   1 
HETATM 2558 O O   . HOH D 3 .   ? 46.804 23.394 70.551 1.00 37.67  ? 517 HOH A O   1 
HETATM 2559 O O   . HOH D 3 .   ? 23.101 45.826 64.779 1.00 32.01  ? 518 HOH A O   1 
HETATM 2560 O O   . HOH D 3 .   ? 3.409  41.374 68.963 1.00 42.78  ? 519 HOH A O   1 
HETATM 2561 O O   . HOH D 3 .   ? 29.344 11.864 62.146 1.00 39.79  ? 520 HOH A O   1 
HETATM 2562 O O   . HOH D 3 .   ? 28.458 28.264 66.770 1.00 50.23  ? 521 HOH A O   1 
HETATM 2563 O O   . HOH D 3 .   ? 20.033 35.284 64.896 1.00 32.57  ? 522 HOH A O   1 
HETATM 2564 O O   . HOH D 3 .   ? 33.816 15.602 61.520 1.00 50.18  ? 523 HOH A O   1 
HETATM 2565 O O   . HOH D 3 .   ? 39.366 18.386 74.289 1.00 36.59  ? 524 HOH A O   1 
HETATM 2566 O O   . HOH D 3 .   ? 24.651 48.970 78.867 1.00 33.48  ? 525 HOH A O   1 
HETATM 2567 O O   . HOH D 3 .   ? 39.559 30.243 83.138 1.00 44.19  ? 526 HOH A O   1 
HETATM 2568 O O   . HOH D 3 .   ? 27.370 41.258 66.641 1.00 25.53  ? 527 HOH A O   1 
HETATM 2569 O O   . HOH D 3 .   ? 36.817 24.154 65.280 1.00 32.57  ? 528 HOH A O   1 
HETATM 2570 O O   . HOH D 3 .   ? 37.141 24.793 71.525 1.00 36.52  ? 529 HOH A O   1 
HETATM 2571 O O   . HOH D 3 .   ? 48.463 37.744 76.908 1.00 50.78  ? 530 HOH A O   1 
HETATM 2572 O O   . HOH D 3 .   ? 23.277 37.053 69.040 1.00 26.80  ? 531 HOH A O   1 
HETATM 2573 O O   . HOH D 3 .   ? 31.864 37.624 68.365 1.00 26.91  ? 532 HOH A O   1 
HETATM 2574 O O   . HOH D 3 .   ? 40.544 24.549 77.724 1.00 40.06  ? 533 HOH A O   1 
HETATM 2575 O O   . HOH D 3 .   ? 13.625 49.429 65.248 1.00 41.25  ? 534 HOH A O   1 
HETATM 2576 O O   . HOH D 3 .   ? 16.245 40.795 86.995 1.00 37.73  ? 535 HOH A O   1 
HETATM 2577 O O   . HOH D 3 .   ? 44.617 29.412 83.186 1.00 42.28  ? 536 HOH A O   1 
HETATM 2578 O O   . HOH D 3 .   ? 38.213 27.931 83.917 1.00 42.97  ? 537 HOH A O   1 
HETATM 2579 O O   . HOH D 3 .   ? 36.044 27.342 78.278 1.00 34.94  ? 538 HOH A O   1 
HETATM 2580 O O   . HOH D 3 .   ? 23.934 18.746 59.779 1.00 41.31  ? 539 HOH A O   1 
HETATM 2581 O O   . HOH D 3 .   ? 30.722 46.284 65.742 1.00 37.94  ? 540 HOH A O   1 
HETATM 2582 O O   . HOH D 3 .   ? 33.560 44.080 72.672 1.00 31.57  ? 541 HOH A O   1 
HETATM 2583 O O   . HOH D 3 .   ? 17.164 38.138 86.694 1.00 41.70  ? 542 HOH A O   1 
HETATM 2584 O O   . HOH D 3 .   ? 26.458 32.059 57.994 1.00 41.29  ? 543 HOH A O   1 
HETATM 2585 O O   . HOH D 3 .   ? 32.074 18.096 65.726 1.00 34.70  ? 544 HOH A O   1 
HETATM 2586 O O   . HOH D 3 .   ? 36.351 45.588 64.267 1.00 44.17  ? 545 HOH A O   1 
HETATM 2587 O O   . HOH D 3 .   ? 32.833 42.805 83.505 1.00 59.55  ? 546 HOH A O   1 
HETATM 2588 O O   . HOH D 3 .   ? 30.188 42.690 83.148 1.00 44.87  ? 547 HOH A O   1 
HETATM 2589 O O   . HOH D 3 .   ? 35.547 17.457 61.188 1.00 55.74  ? 548 HOH A O   1 
HETATM 2590 O O   . HOH D 3 .   ? 37.655 5.134  61.267 1.00 53.11  ? 549 HOH A O   1 
HETATM 2591 O O   . HOH D 3 .   ? 31.921 44.698 83.073 1.00 70.73  ? 550 HOH A O   1 
# 
