data_9CLJ
# 
_entry.id   9CLJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9CLJ         pdb_00009clj 10.2210/pdb9clj/pdb 
WWPDB D_1000285822 ?            ?                   
EMDB  EMD-45676    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'EM metadata'     1 0 2025-03-05 ? 
3 FSC               1 0 2025-03-05 ? 
4 'Half map'        1 0 2025-03-05 1 
5 'Half map'        1 0 2025-03-05 2 
6 Image             1 0 2025-03-05 ? 
7 'Primary map'     1 0 2025-03-05 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 'Primary map'     repository 'Initial release' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CLJ 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'HIV-2 CA T=1 Icosahedron; assembled via lipid templating' 
_pdbx_database_related.db_id          EMD-45676 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yong.xiong@yale.edu 
_pdbx_contact_author.name_first         Yong 
_pdbx_contact_author.name_last          Xiong 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9625-9313 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Cook, M.'     1 0000-0002-8641-820X 
'Freniere, C.' 2 0000-0003-2846-669X 
'Xiong, Y.'    3 0000-0001-9625-9313 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Cell Rep' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2211-1247 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            44 
_citation.language                  ? 
_citation.page_first                115245 
_citation.page_last                 115245 
_citation.title                     
'Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.celrep.2025.115245 
_citation.pdbx_database_id_PubMed   39864060 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cook, M.'     1 ? 
primary 'Freniere, C.' 2 ? 
primary 'Wu, C.'       3 ? 
primary 'Lozano, F.'   4 ? 
primary 'Xiong, Y.'    5 ? 
# 
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 'Capsid protein p24'        26809.490 1   ? ? ? 
;Full length HIV-2 GL-AN capsid protein with a C-terminal Gly-Ser-Ser linker to a hexahistidine tag following proteolytic processing of N-terminal Met.
;
2 non-polymer syn 'INOSITOL HEXAKISPHOSPHATE' 660.035   2   ? ? ? ? 
3 water       nat water                       18.015    130 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        CA 
# 
_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       
;PVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINDEAADW
DAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEP
FQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLMGSSHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINDEAADW
DAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEP
FQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLMGSSHHHHHH
;
_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 'INOSITOL HEXAKISPHOSPHATE' IHP 
3 water                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   VAL n 
1 3   GLN n 
1 4   GLN n 
1 5   THR n 
1 6   GLY n 
1 7   GLY n 
1 8   GLY n 
1 9   ASN n 
1 10  TYR n 
1 11  ILE n 
1 12  HIS n 
1 13  VAL n 
1 14  PRO n 
1 15  LEU n 
1 16  SER n 
1 17  PRO n 
1 18  ARG n 
1 19  THR n 
1 20  LEU n 
1 21  ASN n 
1 22  ALA n 
1 23  TRP n 
1 24  VAL n 
1 25  LYS n 
1 26  LEU n 
1 27  VAL n 
1 28  GLU n 
1 29  ASP n 
1 30  LYS n 
1 31  LYS n 
1 32  PHE n 
1 33  GLY n 
1 34  ALA n 
1 35  GLU n 
1 36  VAL n 
1 37  VAL n 
1 38  PRO n 
1 39  GLY n 
1 40  PHE n 
1 41  GLN n 
1 42  ALA n 
1 43  LEU n 
1 44  SER n 
1 45  GLU n 
1 46  GLY n 
1 47  CYS n 
1 48  THR n 
1 49  PRO n 
1 50  TYR n 
1 51  ASP n 
1 52  ILE n 
1 53  ASN n 
1 54  GLN n 
1 55  MET n 
1 56  LEU n 
1 57  ASN n 
1 58  CYS n 
1 59  VAL n 
1 60  GLY n 
1 61  ASP n 
1 62  HIS n 
1 63  GLN n 
1 64  ALA n 
1 65  ALA n 
1 66  MET n 
1 67  GLN n 
1 68  ILE n 
1 69  ILE n 
1 70  ARG n 
1 71  GLU n 
1 72  ILE n 
1 73  ILE n 
1 74  ASN n 
1 75  ASP n 
1 76  GLU n 
1 77  ALA n 
1 78  ALA n 
1 79  ASP n 
1 80  TRP n 
1 81  ASP n 
1 82  ALA n 
1 83  GLN n 
1 84  HIS n 
1 85  PRO n 
1 86  ILE n 
1 87  PRO n 
1 88  GLY n 
1 89  PRO n 
1 90  LEU n 
1 91  PRO n 
1 92  ALA n 
1 93  GLY n 
1 94  GLN n 
1 95  LEU n 
1 96  ARG n 
1 97  ASP n 
1 98  PRO n 
1 99  ARG n 
1 100 GLY n 
1 101 SER n 
1 102 ASP n 
1 103 ILE n 
1 104 ALA n 
1 105 GLY n 
1 106 THR n 
1 107 THR n 
1 108 SER n 
1 109 THR n 
1 110 VAL n 
1 111 GLU n 
1 112 GLU n 
1 113 GLN n 
1 114 ILE n 
1 115 GLN n 
1 116 TRP n 
1 117 MET n 
1 118 TYR n 
1 119 ARG n 
1 120 PRO n 
1 121 GLN n 
1 122 ASN n 
1 123 PRO n 
1 124 VAL n 
1 125 PRO n 
1 126 VAL n 
1 127 GLY n 
1 128 ASN n 
1 129 ILE n 
1 130 TYR n 
1 131 ARG n 
1 132 ARG n 
1 133 TRP n 
1 134 ILE n 
1 135 GLN n 
1 136 ILE n 
1 137 GLY n 
1 138 LEU n 
1 139 GLN n 
1 140 LYS n 
1 141 CYS n 
1 142 VAL n 
1 143 ARG n 
1 144 MET n 
1 145 TYR n 
1 146 ASN n 
1 147 PRO n 
1 148 THR n 
1 149 ASN n 
1 150 ILE n 
1 151 LEU n 
1 152 ASP n 
1 153 VAL n 
1 154 LYS n 
1 155 GLN n 
1 156 GLY n 
1 157 PRO n 
1 158 LYS n 
1 159 GLU n 
1 160 PRO n 
1 161 PHE n 
1 162 GLN n 
1 163 SER n 
1 164 TYR n 
1 165 VAL n 
1 166 ASP n 
1 167 ARG n 
1 168 PHE n 
1 169 TYR n 
1 170 LYS n 
1 171 SER n 
1 172 LEU n 
1 173 ARG n 
1 174 ALA n 
1 175 GLU n 
1 176 GLN n 
1 177 THR n 
1 178 ASP n 
1 179 PRO n 
1 180 ALA n 
1 181 VAL n 
1 182 LYS n 
1 183 ASN n 
1 184 TRP n 
1 185 MET n 
1 186 THR n 
1 187 GLN n 
1 188 THR n 
1 189 LEU n 
1 190 LEU n 
1 191 ILE n 
1 192 GLN n 
1 193 ASN n 
1 194 ALA n 
1 195 ASN n 
1 196 PRO n 
1 197 ASP n 
1 198 CYS n 
1 199 LYS n 
1 200 LEU n 
1 201 VAL n 
1 202 LEU n 
1 203 LYS n 
1 204 GLY n 
1 205 LEU n 
1 206 GLY n 
1 207 MET n 
1 208 ASN n 
1 209 PRO n 
1 210 THR n 
1 211 LEU n 
1 212 GLU n 
1 213 GLU n 
1 214 MET n 
1 215 LEU n 
1 216 THR n 
1 217 ALA n 
1 218 CYS n 
1 219 GLN n 
1 220 GLY n 
1 221 VAL n 
1 222 GLY n 
1 223 GLY n 
1 224 PRO n 
1 225 GLY n 
1 226 GLN n 
1 227 LYS n 
1 228 ALA n 
1 229 ARG n 
1 230 LEU n 
1 231 MET n 
1 232 GLY n 
1 233 SER n 
1 234 SER n 
1 235 HIS n 
1 236 HIS n 
1 237 HIS n 
1 238 HIS n 
1 239 HIS n 
1 240 HIS 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                   240 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 gag-pol 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    GL-AN 
_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      'Human immunodeficiency virus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     11709 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                     ?                                                                      
'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                    ?                                                                      
'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ?                                                                      
'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ?                                                                      
'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                    ?                                                                      
'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ?                                                                      
'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ?                                                                      
'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                     ?                                                                      
'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                   ?                                                                      
'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                       ?                                                                      
'H2 O'           18.015  
IHP non-polymer         . 'INOSITOL HEXAKISPHOSPHATE' 'MYO-INOSITOL HEXAKISPHOSPHATE; INOSITOL 1,2,3,4,5,6-HEXAKISPHOSPHATE' 
'C6 H18 O24 P6'  660.035 
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   PRO 1   1   1   PRO PRO A . n 
A 1 2   VAL 2   2   2   VAL VAL A . n 
A 1 3   GLN 3   3   3   GLN GLN A . n 
A 1 4   GLN 4   4   4   GLN GLN A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   ASN 9   9   9   ASN ASN A . n 
A 1 10  TYR 10  10  10  TYR TYR A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ASN 21  21  21  ASN ASN A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  TRP 23  23  23  TRP TRP A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  LYS 25  25  25  LYS LYS A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  CYS 47  47  47  CYS CYS A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  TYR 50  50  50  TYR TYR A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  MET 55  55  55  MET MET A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  CYS 58  58  58  CYS CYS A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  HIS 62  62  62  HIS HIS A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  MET 66  66  66  MET MET A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  TRP 80  80  80  TRP TRP A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  HIS 84  84  84  HIS HIS A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  ILE 86  86  86  ILE ILE A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 GLN 113 113 113 GLN GLN A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 GLN 115 115 115 GLN GLN A . n 
A 1 116 TRP 116 116 116 TRP TRP A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 GLN 121 121 121 GLN GLN A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 ILE 129 129 129 ILE ILE A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 TRP 133 133 133 TRP TRP A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 GLN 139 139 139 GLN GLN A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 CYS 141 141 141 CYS CYS A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 MET 144 144 144 MET MET A . n 
A 1 145 TYR 145 145 145 TYR TYR A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 PRO 147 147 147 PRO PRO A . n 
A 1 148 THR 148 148 148 THR THR A . n 
A 1 149 ASN 149 149 149 ASN ASN A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ASP 152 152 152 ASP ASP A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 GLN 162 162 162 GLN GLN A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 ASP 166 166 166 ASP ASP A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ARG 173 173 173 ARG ARG A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 GLU 175 175 175 GLU GLU A . n 
A 1 176 GLN 176 176 176 GLN GLN A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 ASP 178 178 178 ASP ASP A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 LYS 182 182 182 LYS LYS A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 TRP 184 184 184 TRP TRP A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 THR 186 186 186 THR THR A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 THR 188 188 188 THR THR A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 ASN 195 195 195 ASN ASN A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 CYS 198 198 198 CYS CYS A . n 
A 1 199 LYS 199 199 199 LYS LYS A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 GLY 206 206 206 GLY GLY A . n 
A 1 207 MET 207 207 207 MET MET A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 MET 214 214 214 MET MET A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 CYS 218 218 218 CYS CYS A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 GLY 223 223 ?   ?   ?   A . n 
A 1 224 PRO 224 224 ?   ?   ?   A . n 
A 1 225 GLY 225 225 ?   ?   ?   A . n 
A 1 226 GLN 226 226 ?   ?   ?   A . n 
A 1 227 LYS 227 227 ?   ?   ?   A . n 
A 1 228 ALA 228 228 ?   ?   ?   A . n 
A 1 229 ARG 229 229 ?   ?   ?   A . n 
A 1 230 LEU 230 230 ?   ?   ?   A . n 
A 1 231 MET 231 231 ?   ?   ?   A . n 
A 1 232 GLY 232 232 ?   ?   ?   A . n 
A 1 233 SER 233 233 ?   ?   ?   A . n 
A 1 234 SER 234 234 ?   ?   ?   A . n 
A 1 235 HIS 235 235 ?   ?   ?   A . n 
A 1 236 HIS 236 236 ?   ?   ?   A . n 
A 1 237 HIS 237 237 ?   ?   ?   A . n 
A 1 238 HIS 238 238 ?   ?   ?   A . n 
A 1 239 HIS 239 239 ?   ?   ?   A . n 
A 1 240 HIS 240 240 ?   ?   ?   A . n 
# 
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 IHP 1   301 301 IHP IHP A . 
C 2 IHP 1   302 302 IHP IHP A . 
D 3 HOH 1   401 401 HOH HOH A . 
D 3 HOH 2   402 402 HOH HOH A . 
D 3 HOH 3   403 403 HOH HOH A . 
D 3 HOH 4   404 404 HOH HOH A . 
D 3 HOH 5   405 405 HOH HOH A . 
D 3 HOH 6   406 406 HOH HOH A . 
D 3 HOH 7   407 407 HOH HOH A . 
D 3 HOH 8   408 408 HOH HOH A . 
D 3 HOH 9   409 409 HOH HOH A . 
D 3 HOH 10  410 410 HOH HOH A . 
D 3 HOH 11  411 411 HOH HOH A . 
D 3 HOH 12  412 412 HOH HOH A . 
D 3 HOH 13  413 413 HOH HOH A . 
D 3 HOH 14  414 414 HOH HOH A . 
D 3 HOH 15  415 415 HOH HOH A . 
D 3 HOH 16  416 416 HOH HOH A . 
D 3 HOH 17  417 417 HOH HOH A . 
D 3 HOH 18  418 418 HOH HOH A . 
D 3 HOH 19  419 419 HOH HOH A . 
D 3 HOH 20  420 420 HOH HOH A . 
D 3 HOH 21  421 421 HOH HOH A . 
D 3 HOH 22  422 422 HOH HOH A . 
D 3 HOH 23  423 423 HOH HOH A . 
D 3 HOH 24  424 424 HOH HOH A . 
D 3 HOH 25  425 425 HOH HOH A . 
D 3 HOH 26  426 426 HOH HOH A . 
D 3 HOH 27  427 427 HOH HOH A . 
D 3 HOH 28  428 428 HOH HOH A . 
D 3 HOH 29  429 429 HOH HOH A . 
D 3 HOH 30  430 430 HOH HOH A . 
D 3 HOH 31  431 431 HOH HOH A . 
D 3 HOH 32  432 432 HOH HOH A . 
D 3 HOH 33  433 433 HOH HOH A . 
D 3 HOH 34  434 434 HOH HOH A . 
D 3 HOH 35  435 435 HOH HOH A . 
D 3 HOH 36  436 436 HOH HOH A . 
D 3 HOH 37  437 437 HOH HOH A . 
D 3 HOH 38  438 438 HOH HOH A . 
D 3 HOH 39  439 439 HOH HOH A . 
D 3 HOH 40  440 440 HOH HOH A . 
D 3 HOH 41  441 441 HOH HOH A . 
D 3 HOH 42  442 442 HOH HOH A . 
D 3 HOH 43  443 443 HOH HOH A . 
D 3 HOH 44  444 444 HOH HOH A . 
D 3 HOH 45  445 445 HOH HOH A . 
D 3 HOH 46  446 446 HOH HOH A . 
D 3 HOH 47  447 447 HOH HOH A . 
D 3 HOH 48  448 448 HOH HOH A . 
D 3 HOH 49  449 449 HOH HOH A . 
D 3 HOH 50  450 450 HOH HOH A . 
D 3 HOH 51  451 451 HOH HOH A . 
D 3 HOH 52  452 452 HOH HOH A . 
D 3 HOH 53  453 453 HOH HOH A . 
D 3 HOH 54  454 454 HOH HOH A . 
D 3 HOH 55  455 455 HOH HOH A . 
D 3 HOH 56  456 456 HOH HOH A . 
D 3 HOH 57  457 457 HOH HOH A . 
D 3 HOH 58  458 458 HOH HOH A . 
D 3 HOH 59  459 459 HOH HOH A . 
D 3 HOH 60  460 460 HOH HOH A . 
D 3 HOH 61  461 461 HOH HOH A . 
D 3 HOH 62  462 462 HOH HOH A . 
D 3 HOH 63  463 463 HOH HOH A . 
D 3 HOH 64  464 464 HOH HOH A . 
D 3 HOH 65  465 465 HOH HOH A . 
D 3 HOH 66  466 466 HOH HOH A . 
D 3 HOH 67  467 467 HOH HOH A . 
D 3 HOH 68  468 468 HOH HOH A . 
D 3 HOH 69  469 469 HOH HOH A . 
D 3 HOH 70  470 470 HOH HOH A . 
D 3 HOH 71  471 471 HOH HOH A . 
D 3 HOH 72  472 472 HOH HOH A . 
D 3 HOH 73  473 473 HOH HOH A . 
D 3 HOH 74  474 474 HOH HOH A . 
D 3 HOH 75  475 475 HOH HOH A . 
D 3 HOH 76  476 476 HOH HOH A . 
D 3 HOH 77  477 477 HOH HOH A . 
D 3 HOH 78  478 478 HOH HOH A . 
D 3 HOH 79  479 479 HOH HOH A . 
D 3 HOH 80  480 480 HOH HOH A . 
D 3 HOH 81  481 481 HOH HOH A . 
D 3 HOH 82  482 482 HOH HOH A . 
D 3 HOH 83  483 483 HOH HOH A . 
D 3 HOH 84  484 484 HOH HOH A . 
D 3 HOH 85  485 485 HOH HOH A . 
D 3 HOH 86  486 486 HOH HOH A . 
D 3 HOH 87  487 487 HOH HOH A . 
D 3 HOH 88  488 488 HOH HOH A . 
D 3 HOH 89  489 489 HOH HOH A . 
D 3 HOH 90  490 490 HOH HOH A . 
D 3 HOH 91  491 491 HOH HOH A . 
D 3 HOH 92  492 492 HOH HOH A . 
D 3 HOH 93  493 493 HOH HOH A . 
D 3 HOH 94  494 494 HOH HOH A . 
D 3 HOH 95  495 495 HOH HOH A . 
D 3 HOH 96  496 496 HOH HOH A . 
D 3 HOH 97  497 497 HOH HOH A . 
D 3 HOH 98  498 498 HOH HOH A . 
D 3 HOH 99  499 499 HOH HOH A . 
D 3 HOH 100 500 500 HOH HOH A . 
D 3 HOH 101 501 501 HOH HOH A . 
D 3 HOH 102 502 502 HOH HOH A . 
D 3 HOH 103 503 503 HOH HOH A . 
D 3 HOH 104 504 504 HOH HOH A . 
D 3 HOH 105 505 505 HOH HOH A . 
D 3 HOH 106 506 506 HOH HOH A . 
D 3 HOH 107 507 507 HOH HOH A . 
D 3 HOH 108 508 508 HOH HOH A . 
D 3 HOH 109 509 509 HOH HOH A . 
D 3 HOH 110 510 510 HOH HOH A . 
D 3 HOH 111 511 511 HOH HOH A . 
D 3 HOH 112 512 512 HOH HOH A . 
D 3 HOH 113 513 513 HOH HOH A . 
D 3 HOH 114 514 514 HOH HOH A . 
D 3 HOH 115 515 515 HOH HOH A . 
D 3 HOH 116 516 516 HOH HOH A . 
D 3 HOH 117 517 517 HOH HOH A . 
D 3 HOH 118 518 518 HOH HOH A . 
D 3 HOH 119 519 519 HOH HOH A . 
D 3 HOH 120 520 520 HOH HOH A . 
D 3 HOH 121 521 521 HOH HOH A . 
D 3 HOH 122 522 522 HOH HOH A . 
D 3 HOH 123 523 523 HOH HOH A . 
D 3 HOH 124 524 524 HOH HOH A . 
D 3 HOH 125 525 525 HOH HOH A . 
D 3 HOH 126 526 526 HOH HOH A . 
D 3 HOH 127 527 527 HOH HOH A . 
D 3 HOH 128 528 528 HOH HOH A . 
D 3 HOH 129 529 529 HOH HOH A . 
D 3 HOH 130 530 530 HOH HOH A . 
# 
_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                   9CLJ 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9CLJ 
_struct.title                        'HIV-2 CA T=1 Icosahedron; assembled via lipid templating' 
_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        9CLJ 
_struct_keywords.text            'HIV-2, Capsid, IP6, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POL_HV2G1 
_struct_ref.pdbx_db_accession          P18042 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINDEAADW
DAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEP
FQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLM
;
_struct_ref.pdbx_align_begin           136 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9CLJ 
_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                 231 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P18042 
_struct_ref_seq.db_align_beg                  136 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  366 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       231 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CLJ GLY A 232 ? UNP P18042 ? ? 'expression tag' 232 1 
1 9CLJ SER A 233 ? UNP P18042 ? ? 'expression tag' 233 2 
1 9CLJ SER A 234 ? UNP P18042 ? ? 'expression tag' 234 3 
1 9CLJ HIS A 235 ? UNP P18042 ? ? 'expression tag' 235 4 
1 9CLJ HIS A 236 ? UNP P18042 ? ? 'expression tag' 236 5 
1 9CLJ HIS A 237 ? UNP P18042 ? ? 'expression tag' 237 6 
1 9CLJ HIS A 238 ? UNP P18042 ? ? 'expression tag' 238 7 
1 9CLJ HIS A 239 ? UNP P18042 ? ? 'expression tag' 239 8 
1 9CLJ HIS A 240 ? UNP P18042 ? ? 'expression tag' 240 9 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 'complete icosahedral assembly'                ? 60-meric   60 
2 'icosahedral asymmetric unit'                  ? monomeric  1  
3 'icosahedral pentamer'                         ? pentameric 5  
4 'icosahedral 23 hexamer'                       ? hexameric  6  
5 'icosahedral asymmetric unit, std point frame' ? monomeric  1  
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 '(1-60)'           A,B,C,D 
2 1                  A,B,C,D 
3 '(1-5)'            A,B,C,D 
4 '(1,2,6,10,23,24)' A,B,C,D 
5 P                  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   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                
'Assembly of HIV-2 CA, templated on functionalized micelles, consisting of a T=1 icosahedral array of 12 pentamers.' 
# 
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] 
P  'transform to point frame' ?     ?     0.00000386  1.00000000  0.00000000  -179.42467 -0.00000009 0.00000000  -1.00000000 
179.42400  -1.00000000 0.00000386  0.00000009  179.42327  
1  'identity operation'       1_555 x,y,z 1.00000000  0.00000000  0.00000000  0.00000    0.00000000  1.00000000  0.00000000  
0.00000    0.00000000  0.00000000  1.00000000  0.00000    
2  'point symmetry operation' ?     ?     0.80901705  0.49999800  0.30902009  -110.89032 -0.50000186 0.30901699  0.80901585  
68.53440   0.30901384  -0.80901823 0.49999994  179.42478  
3  'point symmetry operation' ?     ?     0.50000015  0.30901190  0.80901885  -110.88957 -0.30902200 -0.80901699 0.49999690  
290.31554  0.80901499  -0.50000315 -0.30901714 179.42494  
4  'point symmetry operation' ?     ?     0.50000015  -0.30902200 0.80901499  0.00123    0.30901190  -0.80901699 -0.50000315 
358.84944  0.80901885  0.49999691  -0.30901714 0.00026    
5  'point symmetry operation' ?     ?     0.80901705  -0.50000186 0.30901384  68.53475   0.49999800  0.30901699  -0.80901823 
179.42456  0.30902009  0.80901585  0.49999994  -110.89045 
6  'point symmetry operation' ?     ?     1.00000000  -0.00000772 -0.00000018 0.00142    -0.00000772 -1.00000000 0.00000000  
358.84934  -0.00000018 0.00000000  -1.00000000 358.84800  
7  'point symmetry operation' ?     ?     0.80902085  0.49999576  0.30901375  -110.88947 0.49999561  -0.30902085 -0.80901823 
290.31580  -0.30901399 0.80901814  -0.50000000 179.42324  
8  'point symmetry operation' ?     ?     0.50000239  0.30901823  0.80901505  -110.89042 0.30901814  0.80901461  -0.50000315 
68.53465   -0.80901508 0.50000309  0.30901699  179.42308  
9  'point symmetry operation' ?     ?     0.49999761  -0.30901585 0.80901891  -0.00013   -0.30901576 0.80901938  0.49999690  
-0.00010   -0.80901894 -0.49999685 0.30901699  358.84774  
10 'point symmetry operation' ?     ?     0.80901313  -0.50000439 0.30902000  68.53480   -0.50000424 -0.30901313 0.80901585  
179.42425  -0.30902023 -0.80901576 -0.50000000 469.73844  
11 'point symmetry operation' ?     ?     -1.00000000 0.00000000  0.00000018  358.84793  0.00000000  -1.00000000 0.00000000  
358.84795  0.00000018  0.00000000  1.00000000  -0.00003   
12 'point symmetry operation' ?     ?     -0.80901699 -0.49999814 -0.30902000 469.73828  0.50000186  -0.30901699 -0.80901585 
290.31356  0.30901399  -0.80901814 0.50000000  179.42473  
13 'point symmetry operation' ?     ?     -0.50000000 -0.30901199 -0.80901891 469.73752  0.30902200  0.80901699  -0.49999690 
68.53241   0.80901508  -0.50000309 -0.30901699 179.42488  
14 'point symmetry operation' ?     ?     -0.50000000 0.30902209  -0.80901505 358.84670  -0.30901190 0.80901699  0.50000315  
-0.00148   0.80901894  0.49999685  -0.30901699 0.00022    
15 'point symmetry operation' ?     ?     -0.80901699 0.50000200  -0.30901375 290.31316  -0.49999800 -0.30901699 0.80901823  
179.42339  0.30902023  0.80901576  0.50000000  -110.89047 
16 'point symmetry operation' ?     ?     -1.00000000 0.00000772  0.00000000  358.84657  0.00000772  1.00000000  0.00000000  
-0.00139   0.00000000  0.00000000  -1.00000000 358.84797  
17 'point symmetry operation' ?     ?     -0.80902091 -0.49999561 -0.30901384 469.73743  -0.49999561 0.30902085  0.80901823  
68.53215   -0.30901384 0.80901823  -0.49999994 179.42319  
18 'point symmetry operation' ?     ?     -0.50000253 -0.30901814 -0.80901499 469.73838  -0.30901814 -0.80901461 0.50000315  
290.31330  -0.80901499 0.50000315  0.30901714  179.42303  
19 'point symmetry operation' ?     ?     -0.49999776 0.30901576  -0.80901885 358.84812  0.30901576  -0.80901938 -0.49999690 
358.84805  -0.80901885 -0.49999691 0.30901714  358.84771  
20 'point symmetry operation' ?     ?     -0.80901319 0.50000424  -0.30902009 290.31321  0.50000424  0.30901313  -0.80901585 
179.42371  -0.30902009 -0.80901585 -0.49999994 469.73842  
21 'point symmetry operation' ?     ?     -0.00000377 -0.00000009 1.00000000  0.00069    -1.00000000 0.00000386  -0.00000377 
358.84794  -0.00000386 -1.00000000 -0.00000009 358.84867  
22 'point symmetry operation' ?     ?     0.30901084  -0.80902014 0.49999871  179.42588  -0.80902014 -0.49999375 -0.30901885 
469.73785  0.49999871  -0.30901885 -0.80901708 290.31469  
23 'point symmetry operation' ?     ?     0.80901313  -0.50000424 -0.30902023 179.42601  -0.50000439 -0.30901313 -0.80901576 
469.73795  0.30902000  0.80901585  -0.50000000 68.53354   
24 'point symmetry operation' ?     ?     0.80901694  0.49999814  -0.30902014 0.00091    -0.50000200 0.30901699  -0.80901576 
358.84810  -0.30901390 0.80901814  0.50000006  -0.00077   
25 'point symmetry operation' ?     ?     0.30901699  0.80901770  0.49999885  -110.89004 -0.80901628 0.50000000  -0.30901885 
290.31430  -0.50000115 -0.30901514 0.80901699  179.42385  
26 'point symmetry operation' ?     ?     -0.00000395 0.00000009  -1.00000000 358.84866  -1.00000000 0.00000386  0.00000395  
358.84655  0.00000386  1.00000000  0.00000009  -0.00070   
27 'point symmetry operation' ?     ?     -0.30901708 0.80901628  -0.50000109 179.42432  -0.80901776 -0.50000000 -0.30901499 
469.73785  -0.49999871 0.30901885  0.80901708  68.53328   
28 'point symmetry operation' ?     ?     -0.80901699 0.50000186  0.30901399  179.42418  -0.49999814 -0.30901699 -0.80901814 
469.73795  -0.30902000 -0.80901585 0.50000000  290.31443  
29 'point symmetry operation' ?     ?     -0.80902080 -0.49999576 0.30901390  358.84843  -0.49999576 0.30902085  -0.80901814 
358.84671  0.30901390  -0.80901814 -0.50000006 358.84874  
30 'point symmetry operation' ?     ?     -0.30902324 -0.80901384 -0.50000124 469.73885  -0.80901390 0.50000625  -0.30901499 
290.31206  0.50000115  0.30901514  -0.80901699 179.42412  
31 'point symmetry operation' ?     ?     0.00000395  0.00000009  1.00000000  -0.00073   1.00000000  -0.00000386 -0.00000395 
0.00140    0.00000386  1.00000000  -0.00000009 -0.00067   
32 'point symmetry operation' ?     ?     0.30901699  -0.80901623 0.50000124  179.42362  0.80901776  0.50000000  0.30901499  
-110.88990 -0.49999876 0.30901900  0.80901699  68.53328   
33 'point symmetry operation' ?     ?     0.80901694  -0.50000200 -0.30901390 179.42379  0.49999814  0.30901699  0.80901814  
-110.89000 -0.30902014 -0.80901576 0.50000006  290.31443  
34 'point symmetry operation' ?     ?     0.80902085  0.49999561  -0.30901399 -0.00044   0.49999576  -0.30902085 0.80901814  
0.00124    0.30901375  -0.80901823 -0.50000000 358.84877  
35 'point symmetry operation' ?     ?     0.30902333  0.80901390  0.50000109  -110.89090 0.80901390  -0.50000625 0.30901499  
68.53589   0.50000109  0.30901499  -0.80901708 179.42417  
36 'point symmetry operation' ?     ?     0.00000377  -0.00000009 -1.00000000 358.84730  1.00000000  -0.00000386 0.00000377  
0.00001    -0.00000386 -1.00000000 0.00000009  358.84864  
37 'point symmetry operation' ?     ?     -0.30901075 0.80902009  -0.49999885 179.42210  0.80902014  0.49999375  0.30901885  
-110.88990 0.49999876  -0.30901900 -0.80901699 290.31469  
38 'point symmetry operation' ?     ?     -0.80901308 0.50000439  0.30902014  179.42192  0.50000439  0.30901313  0.80901576  
-110.89000 0.30902014  0.80901576  -0.50000006 68.53354   
39 'point symmetry operation' ?     ?     -0.80901699 -0.49999800 0.30902023  358.84701  0.50000200  -0.30901699 0.80901576  
-0.00014   -0.30901375 0.80901823  0.50000000  -0.00080   
40 'point symmetry operation' ?     ?     -0.30901708 -0.80901776 -0.49999871 469.73800  0.80901628  -0.50000000 0.30901885  
68.53365   -0.50000109 -0.30901499 0.80901708  179.42380  
41 'point symmetry operation' ?     ?     -0.00000377 -1.00000000 -0.00000386 358.84933  -0.00000009 0.00000386  -1.00000000 
358.84728  1.00000000  -0.00000377 -0.00000009 0.00070    
42 'point symmetry operation' ?     ?     0.49999761  -0.30901576 -0.80901894 290.31466  -0.30901585 0.80901938  -0.49999685 
179.42278  0.80901891  0.49999691  0.30901699  -110.88990 
43 'point symmetry operation' ?     ?     0.30901699  0.80901776  -0.49999876 68.53351   -0.80901623 0.50000000  0.30901900  
179.42348  0.50000124  0.30901499  0.80901699  -110.88998 
44 'point symmetry operation' ?     ?     -0.30901690 0.80901623  0.50000129  -0.00011   -0.80901770 -0.50000000 0.30901514  
358.84841  0.49999891  -0.30901900 0.80901690  0.00057    
45 'point symmetry operation' ?     ?     -0.50000224 -0.30901823 0.80901514  179.42493  -0.30901823 -0.80901461 -0.50000309 
469.73842  0.80901514  -0.50000309 0.30901685  68.53478   
46 'point symmetry operation' ?     ?     0.00000395  1.00000000  0.00000386  -0.00140   0.00000009  -0.00000386 1.00000000  
0.00067    1.00000000  -0.00000395 -0.00000009 0.00073    
47 'point symmetry operation' ?     ?     -0.49999747 0.30901585  0.80901900  68.53325   0.30901585  -0.80901938 0.49999685  
179.42517  0.80901900  0.49999685  0.30901685  -110.88988 
48 'point symmetry operation' ?     ?     -0.30901690 -0.80901770 0.49999891  290.31440  0.80901623  -0.50000000 -0.30901900 
179.42447  0.50000129  0.30901514  0.80901690  -110.89000 
49 'point symmetry operation' ?     ?     0.30901699  -0.80901628 -0.50000115 358.84804  0.80901770  0.50000000  -0.30901514 
-0.00046   0.49999885  -0.30901885 0.80901699  0.00054    
50 'point symmetry operation' ?     ?     0.50000239  0.30901814  -0.80901508 179.42301  0.30901823  0.80901461  0.50000309  
-110.89047 0.80901505  -0.50000315 0.30901699  68.53478   
51 'point symmetry operation' ?     ?     0.00000377  1.00000000  -0.00000386 0.00002    -0.00000009 -0.00000386 -1.00000000 
358.84867  -1.00000000 0.00000377  0.00000009  358.84727  
52 'point symmetry operation' ?     ?     -0.50000000 0.30902200  0.80901508  68.53330   -0.30901199 0.80901699  -0.50000309 
179.42364  -0.80901891 -0.49999691 -0.30901699 469.73787  
53 'point symmetry operation' ?     ?     -0.30902324 -0.80901390 0.50000115  290.31445  -0.80901384 0.50000625  0.30901514  
179.42262  -0.50000124 -0.30901499 -0.80901699 469.73795  
54 'point symmetry operation' ?     ?     0.30901066  -0.80902009 -0.49999891 358.84946  -0.80902009 -0.49999375 0.30901900  
358.84703  -0.49999891 0.30901900  -0.80901690 358.84740  
55 'point symmetry operation' ?     ?     0.49999985  0.30901199  -0.80901900 179.42527  -0.30902209 -0.80901699 -0.49999685 
469.73842  -0.80901514 0.50000309  -0.30901685 290.31319  
56 'point symmetry operation' ?     ?     -0.00000395 -1.00000000 0.00000386  358.84797  0.00000009  0.00000386  1.00000000  
-0.00072   -1.00000000 0.00000395  0.00000009  358.84724  
57 'point symmetry operation' ?     ?     0.49999985  -0.30902209 -0.80901514 290.31471  0.30901199  -0.80901699 0.50000309  
179.42432  -0.80901900 -0.49999685 -0.30901685 469.73785  
58 'point symmetry operation' ?     ?     0.30902315  0.80901384  -0.50000129 68.53356   0.80901384  -0.50000625 -0.30901514 
179.42533  -0.50000129 -0.30901514 -0.80901690 469.73797  
59 'point symmetry operation' ?     ?     -0.30901075 0.80902014  0.49999876  -0.00147   0.80902009  0.49999375  -0.30901900 
0.00093    -0.49999885 0.30901885  -0.80901699 358.84743  
60 'point symmetry operation' ?     ?     -0.50000000 -0.30901190 0.80901894  179.42271  0.30902209  0.80901699  0.49999685  
-110.89047 -0.80901505 0.50000315  -0.30901699 290.31319  
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 16  ? LYS A 30  ? SER A 16  LYS A 30  1 ? 15 
HELX_P HELX_P2  AA2 GLU A 35  ? SER A 44  ? GLU A 35  SER A 44  1 ? 10 
HELX_P HELX_P3  AA3 THR A 48  ? VAL A 59  ? THR A 48  VAL A 59  1 ? 12 
HELX_P HELX_P4  AA4 HIS A 62  ? HIS A 84  ? HIS A 62  HIS A 84  1 ? 23 
HELX_P HELX_P5  AA5 ARG A 99  ? GLY A 105 ? ARG A 99  GLY A 105 1 ? 7  
HELX_P HELX_P6  AA6 THR A 109 ? TYR A 118 ? THR A 109 TYR A 118 1 ? 10 
HELX_P HELX_P7  AA7 PRO A 125 ? ASN A 146 ? PRO A 125 ASN A 146 1 ? 22 
HELX_P HELX_P8  AA8 PRO A 160 ? GLU A 175 ? PRO A 160 GLU A 175 1 ? 16 
HELX_P HELX_P9  AA9 ASP A 178 ? THR A 188 ? ASP A 178 THR A 188 1 ? 11 
HELX_P HELX_P10 AB1 THR A 188 ? ASN A 193 ? THR A 188 ASN A 193 1 ? 6  
HELX_P HELX_P11 AB2 ASN A 195 ? GLY A 206 ? ASN A 195 GLY A 206 1 ? 12 
HELX_P HELX_P12 AB3 THR A 210 ? GLN A 219 ? THR A 210 GLN A 219 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 2  ? GLN A 4  ? VAL A 2  GLN A 4  
AA1 2 TYR A 10 ? HIS A 12 ? TYR A 10 HIS A 12 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   GLN 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    3 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    GLN 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     3 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   ILE 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    11 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    ILE 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     11 
# 
_pdbx_entry_details.entry_id                   9CLJ 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLN A 121 ? ? -96.46  -77.89 
2 1 ASN A 122 ? ? -119.54 72.67  
3 1 ASN A 193 ? ? -105.06 40.81  
# 
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 18  ? ? 0.101 'SIDE CHAIN' 
2 1 ARG A 132 ? ? 0.087 'SIDE CHAIN' 
3 1 ARG A 167 ? ? 0.097 'SIDE CHAIN' 
# 
_pdbx_point_symmetry.entry_id             9CLJ 
_pdbx_point_symmetry.Schoenflies_symbol   I 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9CLJ 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   'Cross-correlation coefficient' 
_em_3d_fitting.details           
;An HIV-1 CA chain from pentamers (PDB: 8CKW) was initially fit into the density by rigid body fitting. It was then mutated to match the HIV-2 sequence, with unmodeled residues being replaced before flexible fitting and refinement into the map volume.
;
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'FLEXIBLE FIT' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  8CKW 
_em_3d_fitting_list.pdb_chain_id                  A 
_em_3d_fitting_list.pdb_chain_residue_range       1-221 
_em_3d_fitting_list.details                       
'Due to structural similarities expected between HIV-2 and HIV-1, an HIV-1 model was used for initial fitting.' 
_em_3d_fitting_list.chain_id                      A 
_em_3d_fitting_list.chain_residue_range           1-221 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                8CKW 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9CLJ 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  1.98 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               74821 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       'The mixed buffer of storage buffer for the protein and lipid components with IP6 supplemented.' 
_em_buffer.pH            7 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'HIV-2 capsid protein assembled into a lattice via lipid templating.' 
_em_entity_assembly.details              
;C-terminally hexahistidine tagged HIV-2 CA associated with a micelle decorated with NiNTA headgroups which results in the assembly of an icosahedral lattice of CA.
;
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9CLJ 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             800 
_em_imaging.nominal_defocus_max             2000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           81000 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             'COMA FREE' 
_em_imaging.c2_aperture_diameter            30 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   200 
_em_sample_support.grid_type        'Quantifoil R2/1' 
_em_sample_support.details          '15 mA discharge current.' 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9CLJ 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   298 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               
'Grids were dual-side blotted with blot force 0 for 5.5 sec before plunge freezing in liquid ethane.' 
# 
_em_experiment.entry_id                9CLJ 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              9CLJ 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        I 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 223 ? A GLY 223 
2  1 Y 1 A PRO 224 ? A PRO 224 
3  1 Y 1 A GLY 225 ? A GLY 225 
4  1 Y 1 A GLN 226 ? A GLN 226 
5  1 Y 1 A LYS 227 ? A LYS 227 
6  1 Y 1 A ALA 228 ? A ALA 228 
7  1 Y 1 A ARG 229 ? A ARG 229 
8  1 Y 1 A LEU 230 ? A LEU 230 
9  1 Y 1 A MET 231 ? A MET 231 
10 1 Y 1 A GLY 232 ? A GLY 232 
11 1 Y 1 A SER 233 ? A SER 233 
12 1 Y 1 A SER 234 ? A SER 234 
13 1 Y 1 A HIS 235 ? A HIS 235 
14 1 Y 1 A HIS 236 ? A HIS 236 
15 1 Y 1 A HIS 237 ? A HIS 237 
16 1 Y 1 A HIS 238 ? A HIS 238 
17 1 Y 1 A HIS 239 ? A HIS 239 
18 1 Y 1 A HIS 240 ? A HIS 240 
# 
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 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
IHP C1   C N N 161 
IHP C2   C N N 162 
IHP C3   C N N 163 
IHP C4   C N N 164 
IHP C5   C N N 165 
IHP C6   C N N 166 
IHP O11  O N N 167 
IHP P1   P N N 168 
IHP O21  O N N 169 
IHP O31  O N N 170 
IHP O41  O N N 171 
IHP O12  O N N 172 
IHP P2   P N N 173 
IHP O22  O N N 174 
IHP O32  O N N 175 
IHP O42  O N N 176 
IHP O13  O N N 177 
IHP P3   P N N 178 
IHP O23  O N N 179 
IHP O33  O N N 180 
IHP O43  O N N 181 
IHP O14  O N N 182 
IHP P4   P N N 183 
IHP O24  O N N 184 
IHP O34  O N N 185 
IHP O44  O N N 186 
IHP O15  O N N 187 
IHP P5   P N N 188 
IHP O25  O N N 189 
IHP O35  O N N 190 
IHP O45  O N N 191 
IHP O16  O N N 192 
IHP P6   P N N 193 
IHP O26  O N N 194 
IHP O36  O N N 195 
IHP O46  O N N 196 
IHP H1   H N N 197 
IHP H2   H N N 198 
IHP H3   H N N 199 
IHP H4   H N N 200 
IHP H5   H N N 201 
IHP H6   H N N 202 
IHP H31  H N N 203 
IHP H41  H N N 204 
IHP H32  H N N 205 
IHP H42  H N N 206 
IHP H33  H N N 207 
IHP H43  H N N 208 
IHP H34  H N N 209 
IHP H44  H N N 210 
IHP H35  H N N 211 
IHP H45  H N N 212 
IHP H36  H N N 213 
IHP H46  H N N 214 
ILE N    N N N 215 
ILE CA   C N S 216 
ILE C    C N N 217 
ILE O    O N N 218 
ILE CB   C N S 219 
ILE CG1  C N N 220 
ILE CG2  C N N 221 
ILE CD1  C N N 222 
ILE OXT  O N N 223 
ILE H    H N N 224 
ILE H2   H N N 225 
ILE HA   H N N 226 
ILE HB   H N N 227 
ILE HG12 H N N 228 
ILE HG13 H N N 229 
ILE HG21 H N N 230 
ILE HG22 H N N 231 
ILE HG23 H N N 232 
ILE HD11 H N N 233 
ILE HD12 H N N 234 
ILE HD13 H N N 235 
ILE HXT  H N N 236 
LEU N    N N N 237 
LEU CA   C N S 238 
LEU C    C N N 239 
LEU O    O N N 240 
LEU CB   C N N 241 
LEU CG   C N N 242 
LEU CD1  C N N 243 
LEU CD2  C N N 244 
LEU OXT  O N N 245 
LEU H    H N N 246 
LEU H2   H N N 247 
LEU HA   H N N 248 
LEU HB2  H N N 249 
LEU HB3  H N N 250 
LEU HG   H N N 251 
LEU HD11 H N N 252 
LEU HD12 H N N 253 
LEU HD13 H N N 254 
LEU HD21 H N N 255 
LEU HD22 H N N 256 
LEU HD23 H N N 257 
LEU HXT  H N N 258 
LYS N    N N N 259 
LYS CA   C N S 260 
LYS C    C N N 261 
LYS O    O N N 262 
LYS CB   C N N 263 
LYS CG   C N N 264 
LYS CD   C N N 265 
LYS CE   C N N 266 
LYS NZ   N N N 267 
LYS OXT  O N N 268 
LYS H    H N N 269 
LYS H2   H N N 270 
LYS HA   H N N 271 
LYS HB2  H N N 272 
LYS HB3  H N N 273 
LYS HG2  H N N 274 
LYS HG3  H N N 275 
LYS HD2  H N N 276 
LYS HD3  H N N 277 
LYS HE2  H N N 278 
LYS HE3  H N N 279 
LYS HZ1  H N N 280 
LYS HZ2  H N N 281 
LYS HZ3  H N N 282 
LYS HXT  H N N 283 
MET N    N N N 284 
MET CA   C N S 285 
MET C    C N N 286 
MET O    O N N 287 
MET CB   C N N 288 
MET CG   C N N 289 
MET SD   S N N 290 
MET CE   C N N 291 
MET OXT  O N N 292 
MET H    H N N 293 
MET H2   H N N 294 
MET HA   H N N 295 
MET HB2  H N N 296 
MET HB3  H N N 297 
MET HG2  H N N 298 
MET HG3  H N N 299 
MET HE1  H N N 300 
MET HE2  H N N 301 
MET HE3  H N N 302 
MET HXT  H N N 303 
PHE N    N N N 304 
PHE CA   C N S 305 
PHE C    C N N 306 
PHE O    O N N 307 
PHE CB   C N N 308 
PHE CG   C Y N 309 
PHE CD1  C Y N 310 
PHE CD2  C Y N 311 
PHE CE1  C Y N 312 
PHE CE2  C Y N 313 
PHE CZ   C Y N 314 
PHE OXT  O N N 315 
PHE H    H N N 316 
PHE H2   H N N 317 
PHE HA   H N N 318 
PHE HB2  H N N 319 
PHE HB3  H N N 320 
PHE HD1  H N N 321 
PHE HD2  H N N 322 
PHE HE1  H N N 323 
PHE HE2  H N N 324 
PHE HZ   H N N 325 
PHE HXT  H N N 326 
PRO N    N N N 327 
PRO CA   C N S 328 
PRO C    C N N 329 
PRO O    O N N 330 
PRO CB   C N N 331 
PRO CG   C N N 332 
PRO CD   C N N 333 
PRO OXT  O N N 334 
PRO H    H N N 335 
PRO HA   H N N 336 
PRO HB2  H N N 337 
PRO HB3  H N N 338 
PRO HG2  H N N 339 
PRO HG3  H N N 340 
PRO HD2  H N N 341 
PRO HD3  H N N 342 
PRO HXT  H N N 343 
SER N    N N N 344 
SER CA   C N S 345 
SER C    C N N 346 
SER O    O N N 347 
SER CB   C N N 348 
SER OG   O N N 349 
SER OXT  O N N 350 
SER H    H N N 351 
SER H2   H N N 352 
SER HA   H N N 353 
SER HB2  H N N 354 
SER HB3  H N N 355 
SER HG   H N N 356 
SER HXT  H N N 357 
THR N    N N N 358 
THR CA   C N S 359 
THR C    C N N 360 
THR O    O N N 361 
THR CB   C N R 362 
THR OG1  O N N 363 
THR CG2  C N N 364 
THR OXT  O N N 365 
THR H    H N N 366 
THR H2   H N N 367 
THR HA   H N N 368 
THR HB   H N N 369 
THR HG1  H N N 370 
THR HG21 H N N 371 
THR HG22 H N N 372 
THR HG23 H N N 373 
THR HXT  H N N 374 
TRP N    N N N 375 
TRP CA   C N S 376 
TRP C    C N N 377 
TRP O    O N N 378 
TRP CB   C N N 379 
TRP CG   C Y N 380 
TRP CD1  C Y N 381 
TRP CD2  C Y N 382 
TRP NE1  N Y N 383 
TRP CE2  C Y N 384 
TRP CE3  C Y N 385 
TRP CZ2  C Y N 386 
TRP CZ3  C Y N 387 
TRP CH2  C Y N 388 
TRP OXT  O N N 389 
TRP H    H N N 390 
TRP H2   H N N 391 
TRP HA   H N N 392 
TRP HB2  H N N 393 
TRP HB3  H N N 394 
TRP HD1  H N N 395 
TRP HE1  H N N 396 
TRP HE3  H N N 397 
TRP HZ2  H N N 398 
TRP HZ3  H N N 399 
TRP HH2  H N N 400 
TRP HXT  H N N 401 
TYR N    N N N 402 
TYR CA   C N S 403 
TYR C    C N N 404 
TYR O    O N N 405 
TYR CB   C N N 406 
TYR CG   C Y N 407 
TYR CD1  C Y N 408 
TYR CD2  C Y N 409 
TYR CE1  C Y N 410 
TYR CE2  C Y N 411 
TYR CZ   C Y N 412 
TYR OH   O N N 413 
TYR OXT  O N N 414 
TYR H    H N N 415 
TYR H2   H N N 416 
TYR HA   H N N 417 
TYR HB2  H N N 418 
TYR HB3  H N N 419 
TYR HD1  H N N 420 
TYR HD2  H N N 421 
TYR HE1  H N N 422 
TYR HE2  H N N 423 
TYR HH   H N N 424 
TYR HXT  H N N 425 
VAL N    N N N 426 
VAL CA   C N S 427 
VAL C    C N N 428 
VAL O    O N N 429 
VAL CB   C N N 430 
VAL CG1  C N N 431 
VAL CG2  C N N 432 
VAL OXT  O N N 433 
VAL H    H N N 434 
VAL H2   H N N 435 
VAL HA   H N N 436 
VAL HB   H N N 437 
VAL HG11 H N N 438 
VAL HG12 H N N 439 
VAL HG13 H N N 440 
VAL HG21 H N N 441 
VAL HG22 H N N 442 
VAL HG23 H N N 443 
VAL HXT  H N N 444 
# 
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 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
IHP C1  C2   sing N N 152 
IHP C1  C6   sing N N 153 
IHP C1  O11  sing N N 154 
IHP C1  H1   sing N N 155 
IHP C2  C3   sing N N 156 
IHP C2  O12  sing N N 157 
IHP C2  H2   sing N N 158 
IHP C3  C4   sing N N 159 
IHP C3  O13  sing N N 160 
IHP C3  H3   sing N N 161 
IHP C4  C5   sing N N 162 
IHP C4  O14  sing N N 163 
IHP C4  H4   sing N N 164 
IHP C5  C6   sing N N 165 
IHP C5  O15  sing N N 166 
IHP C5  H5   sing N N 167 
IHP C6  O16  sing N N 168 
IHP C6  H6   sing N N 169 
IHP O11 P1   sing N N 170 
IHP P1  O21  doub N N 171 
IHP P1  O31  sing N N 172 
IHP P1  O41  sing N N 173 
IHP O31 H31  sing N N 174 
IHP O41 H41  sing N N 175 
IHP O12 P2   sing N N 176 
IHP P2  O22  doub N N 177 
IHP P2  O32  sing N N 178 
IHP P2  O42  sing N N 179 
IHP O32 H32  sing N N 180 
IHP O42 H42  sing N N 181 
IHP O13 P3   sing N N 182 
IHP P3  O23  doub N N 183 
IHP P3  O33  sing N N 184 
IHP P3  O43  sing N N 185 
IHP O33 H33  sing N N 186 
IHP O43 H43  sing N N 187 
IHP O14 P4   sing N N 188 
IHP P4  O24  doub N N 189 
IHP P4  O34  sing N N 190 
IHP P4  O44  sing N N 191 
IHP O34 H34  sing N N 192 
IHP O44 H44  sing N N 193 
IHP O15 P5   sing N N 194 
IHP P5  O25  doub N N 195 
IHP P5  O35  sing N N 196 
IHP P5  O45  sing N N 197 
IHP O35 H35  sing N N 198 
IHP O45 H45  sing N N 199 
IHP O16 P6   sing N N 200 
IHP P6  O26  doub N N 201 
IHP P6  O36  sing N N 202 
IHP P6  O46  sing N N 203 
IHP O36 H36  sing N N 204 
IHP O46 H46  sing N N 205 
ILE N   CA   sing N N 206 
ILE N   H    sing N N 207 
ILE N   H2   sing N N 208 
ILE CA  C    sing N N 209 
ILE CA  CB   sing N N 210 
ILE CA  HA   sing N N 211 
ILE C   O    doub N N 212 
ILE C   OXT  sing N N 213 
ILE CB  CG1  sing N N 214 
ILE CB  CG2  sing N N 215 
ILE CB  HB   sing N N 216 
ILE CG1 CD1  sing N N 217 
ILE CG1 HG12 sing N N 218 
ILE CG1 HG13 sing N N 219 
ILE CG2 HG21 sing N N 220 
ILE CG2 HG22 sing N N 221 
ILE CG2 HG23 sing N N 222 
ILE CD1 HD11 sing N N 223 
ILE CD1 HD12 sing N N 224 
ILE CD1 HD13 sing N N 225 
ILE OXT HXT  sing N N 226 
LEU N   CA   sing N N 227 
LEU N   H    sing N N 228 
LEU N   H2   sing N N 229 
LEU CA  C    sing N N 230 
LEU CA  CB   sing N N 231 
LEU CA  HA   sing N N 232 
LEU C   O    doub N N 233 
LEU C   OXT  sing N N 234 
LEU CB  CG   sing N N 235 
LEU CB  HB2  sing N N 236 
LEU CB  HB3  sing N N 237 
LEU CG  CD1  sing N N 238 
LEU CG  CD2  sing N N 239 
LEU CG  HG   sing N N 240 
LEU CD1 HD11 sing N N 241 
LEU CD1 HD12 sing N N 242 
LEU CD1 HD13 sing N N 243 
LEU CD2 HD21 sing N N 244 
LEU CD2 HD22 sing N N 245 
LEU CD2 HD23 sing N N 246 
LEU OXT HXT  sing N N 247 
LYS N   CA   sing N N 248 
LYS N   H    sing N N 249 
LYS N   H2   sing N N 250 
LYS CA  C    sing N N 251 
LYS CA  CB   sing N N 252 
LYS CA  HA   sing N N 253 
LYS C   O    doub N N 254 
LYS C   OXT  sing N N 255 
LYS CB  CG   sing N N 256 
LYS CB  HB2  sing N N 257 
LYS CB  HB3  sing N N 258 
LYS CG  CD   sing N N 259 
LYS CG  HG2  sing N N 260 
LYS CG  HG3  sing N N 261 
LYS CD  CE   sing N N 262 
LYS CD  HD2  sing N N 263 
LYS CD  HD3  sing N N 264 
LYS CE  NZ   sing N N 265 
LYS CE  HE2  sing N N 266 
LYS CE  HE3  sing N N 267 
LYS NZ  HZ1  sing N N 268 
LYS NZ  HZ2  sing N N 269 
LYS NZ  HZ3  sing N N 270 
LYS OXT HXT  sing N N 271 
MET N   CA   sing N N 272 
MET N   H    sing N N 273 
MET N   H2   sing N N 274 
MET CA  C    sing N N 275 
MET CA  CB   sing N N 276 
MET CA  HA   sing N N 277 
MET C   O    doub N N 278 
MET C   OXT  sing N N 279 
MET CB  CG   sing N N 280 
MET CB  HB2  sing N N 281 
MET CB  HB3  sing N N 282 
MET CG  SD   sing N N 283 
MET CG  HG2  sing N N 284 
MET CG  HG3  sing N N 285 
MET SD  CE   sing N N 286 
MET CE  HE1  sing N N 287 
MET CE  HE2  sing N N 288 
MET CE  HE3  sing N N 289 
MET OXT HXT  sing N N 290 
PHE N   CA   sing N N 291 
PHE N   H    sing N N 292 
PHE N   H2   sing N N 293 
PHE CA  C    sing N N 294 
PHE CA  CB   sing N N 295 
PHE CA  HA   sing N N 296 
PHE C   O    doub N N 297 
PHE C   OXT  sing N N 298 
PHE CB  CG   sing N N 299 
PHE CB  HB2  sing N N 300 
PHE CB  HB3  sing N N 301 
PHE CG  CD1  doub Y N 302 
PHE CG  CD2  sing Y N 303 
PHE CD1 CE1  sing Y N 304 
PHE CD1 HD1  sing N N 305 
PHE CD2 CE2  doub Y N 306 
PHE CD2 HD2  sing N N 307 
PHE CE1 CZ   doub Y N 308 
PHE CE1 HE1  sing N N 309 
PHE CE2 CZ   sing Y N 310 
PHE CE2 HE2  sing N N 311 
PHE CZ  HZ   sing N N 312 
PHE OXT HXT  sing N N 313 
PRO N   CA   sing N N 314 
PRO N   CD   sing N N 315 
PRO N   H    sing N N 316 
PRO CA  C    sing N N 317 
PRO CA  CB   sing N N 318 
PRO CA  HA   sing N N 319 
PRO C   O    doub N N 320 
PRO C   OXT  sing N N 321 
PRO CB  CG   sing N N 322 
PRO CB  HB2  sing N N 323 
PRO CB  HB3  sing N N 324 
PRO CG  CD   sing N N 325 
PRO CG  HG2  sing N N 326 
PRO CG  HG3  sing N N 327 
PRO CD  HD2  sing N N 328 
PRO CD  HD3  sing N N 329 
PRO OXT HXT  sing N N 330 
SER N   CA   sing N N 331 
SER N   H    sing N N 332 
SER N   H2   sing N N 333 
SER CA  C    sing N N 334 
SER CA  CB   sing N N 335 
SER CA  HA   sing N N 336 
SER C   O    doub N N 337 
SER C   OXT  sing N N 338 
SER CB  OG   sing N N 339 
SER CB  HB2  sing N N 340 
SER CB  HB3  sing N N 341 
SER OG  HG   sing N N 342 
SER OXT HXT  sing N N 343 
THR N   CA   sing N N 344 
THR N   H    sing N N 345 
THR N   H2   sing N N 346 
THR CA  C    sing N N 347 
THR CA  CB   sing N N 348 
THR CA  HA   sing N N 349 
THR C   O    doub N N 350 
THR C   OXT  sing N N 351 
THR CB  OG1  sing N N 352 
THR CB  CG2  sing N N 353 
THR CB  HB   sing N N 354 
THR OG1 HG1  sing N N 355 
THR CG2 HG21 sing N N 356 
THR CG2 HG22 sing N N 357 
THR CG2 HG23 sing N N 358 
THR OXT HXT  sing N N 359 
TRP N   CA   sing N N 360 
TRP N   H    sing N N 361 
TRP N   H2   sing N N 362 
TRP CA  C    sing N N 363 
TRP CA  CB   sing N N 364 
TRP CA  HA   sing N N 365 
TRP C   O    doub N N 366 
TRP C   OXT  sing N N 367 
TRP CB  CG   sing N N 368 
TRP CB  HB2  sing N N 369 
TRP CB  HB3  sing N N 370 
TRP CG  CD1  doub Y N 371 
TRP CG  CD2  sing Y N 372 
TRP CD1 NE1  sing Y N 373 
TRP CD1 HD1  sing N N 374 
TRP CD2 CE2  doub Y N 375 
TRP CD2 CE3  sing Y N 376 
TRP NE1 CE2  sing Y N 377 
TRP NE1 HE1  sing N N 378 
TRP CE2 CZ2  sing Y N 379 
TRP CE3 CZ3  doub Y N 380 
TRP CE3 HE3  sing N N 381 
TRP CZ2 CH2  doub Y N 382 
TRP CZ2 HZ2  sing N N 383 
TRP CZ3 CH2  sing Y N 384 
TRP CZ3 HZ3  sing N N 385 
TRP CH2 HH2  sing N N 386 
TRP OXT HXT  sing N N 387 
TYR N   CA   sing N N 388 
TYR N   H    sing N N 389 
TYR N   H2   sing N N 390 
TYR CA  C    sing N N 391 
TYR CA  CB   sing N N 392 
TYR CA  HA   sing N N 393 
TYR C   O    doub N N 394 
TYR C   OXT  sing N N 395 
TYR CB  CG   sing N N 396 
TYR CB  HB2  sing N N 397 
TYR CB  HB3  sing N N 398 
TYR CG  CD1  doub Y N 399 
TYR CG  CD2  sing Y N 400 
TYR CD1 CE1  sing Y N 401 
TYR CD1 HD1  sing N N 402 
TYR CD2 CE2  doub Y N 403 
TYR CD2 HD2  sing N N 404 
TYR CE1 CZ   doub Y N 405 
TYR CE1 HE1  sing N N 406 
TYR CE2 CZ   sing Y N 407 
TYR CE2 HE2  sing N N 408 
TYR CZ  OH   sing N N 409 
TYR OH  HH   sing N N 410 
TYR OXT HXT  sing N N 411 
VAL N   CA   sing N N 412 
VAL N   H    sing N N 413 
VAL N   H2   sing N N 414 
VAL CA  C    sing N N 415 
VAL CA  CB   sing N N 416 
VAL CA  HA   sing N N 417 
VAL C   O    doub N N 418 
VAL C   OXT  sing N N 419 
VAL CB  CG1  sing N N 420 
VAL CB  CG2  sing N N 421 
VAL CB  HB   sing N N 422 
VAL CG1 HG11 sing N N 423 
VAL CG1 HG12 sing N N 424 
VAL CG1 HG13 sing N N 425 
VAL CG2 HG21 sing N N 426 
VAL CG2 HG22 sing N N 427 
VAL CG2 HG23 sing N N 428 
VAL OXT HXT  sing N N 429 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-07-11 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9CLJ 
_em_admin.last_update        2025-03-05 
_em_admin.map_release_date   2025-03-05 
_em_admin.title              'HIV-2 CA T=1 Icosahedron; assembled via lipid templating' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 20  mM ?    1 HEPES             
1 250 mM NaCl 2 'Sodium chloride' 
1 0.1 mM ?    3 TCEP              
1 4   mM ?    4 IP6               
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                KILODALTONS/NANOMETER 
_em_entity_assembly_molwt.value                26.9 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          11709 
_em_entity_assembly_naturalsource.organism             'Human immunodeficiency virus 2' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               GL-AN 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          469008 
_em_entity_assembly_recombinant.organism             'Escherichia coli BL21(DE3)' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    15 
_em_imaging_optics.energyfilter_name          'GIF Quantum LS' 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   690629 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ?                                             1  1 ? ? cryoSPARC ? 
'IMAGE ACQUISITION'        'Collected at Brookhaven National Laboratory' 2  ? ? 1 EPU       ? 
MASKING                    ?                                             3  ? ? ? ?         ? 
'CTF CORRECTION'           ?                                             4  1 ? ? cryoSPARC ? 
'LAYERLINE INDEXING'       ?                                             5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'     ?                                             6  ? ? ? ?         ? 
'MODEL FITTING'            ?                                             7  ? 1 ? Coot      ? 
OTHER                      ?                                             8  ? ? ? ?         ? 
'MODEL REFINEMENT'         ?                                             9  ? 1 ? Coot      ? 
'INITIAL EULER ASSIGNMENT' ?                                             10 1 ? ? cryoSPARC ? 
'FINAL EULER ASSIGNMENT'   ?                                             11 1 ? ? cryoSPARC ? 
CLASSIFICATION             ?                                             12 1 ? ? cryoSPARC ? 
RECONSTRUCTION             ?                                             13 1 ? ? cryoSPARC ? 
# 
_em_specimen.concentration           10.7 
_em_specimen.details                 
;Sample was prepared with 400 uM HIV-2 CA-6xHis protein, 5.9 mM lipid mix (described in publication), and 4 mM IP6.

Sample was well-distributed on the grid, mostly monodisperse. Perhaps slightly more particles on carbon versus in the hole.
;
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' T32GM008283 1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' U54AI170791 2 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' P50AI150481 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8CKW 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CLJ 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . PRO A 1 1   ? 94.559  170.673 140.501 1.00 30.00 ? 1   PRO A N   1 
ATOM   2    C CA  . PRO A 1 1   ? 93.751  171.868 140.787 1.00 30.00 ? 1   PRO A CA  1 
ATOM   3    C C   . PRO A 1 1   ? 92.411  171.782 140.058 1.00 30.00 ? 1   PRO A C   1 
ATOM   4    O O   . PRO A 1 1   ? 92.180  170.815 139.354 1.00 30.00 ? 1   PRO A O   1 
ATOM   5    C CB  . PRO A 1 1   ? 94.656  172.998 140.296 1.00 30.00 ? 1   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 1   ? 96.022  172.534 140.727 1.00 30.00 ? 1   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 1   ? 95.982  171.030 140.549 1.00 30.00 ? 1   PRO A CD  1 
ATOM   8    N N   . VAL A 1 2   ? 91.570  172.787 140.263 1.00 30.00 ? 2   VAL A N   1 
ATOM   9    C CA  . VAL A 1 2   ? 90.204  172.744 139.669 1.00 30.00 ? 2   VAL A CA  1 
ATOM   10   C C   . VAL A 1 2   ? 89.921  174.001 138.846 1.00 30.00 ? 2   VAL A C   1 
ATOM   11   O O   . VAL A 1 2   ? 90.162  175.106 139.346 1.00 30.00 ? 2   VAL A O   1 
ATOM   12   C CB  . VAL A 1 2   ? 89.123  172.530 140.747 1.00 30.00 ? 2   VAL A CB  1 
ATOM   13   C CG1 . VAL A 1 2   ? 87.726  172.579 140.154 1.00 30.00 ? 2   VAL A CG1 1 
ATOM   14   C CG2 . VAL A 1 2   ? 89.343  171.234 141.509 1.00 30.00 ? 2   VAL A CG2 1 
ATOM   15   N N   . GLN A 1 3   ? 89.407  173.816 137.642 1.00 30.00 ? 3   GLN A N   1 
ATOM   16   C CA  . GLN A 1 3   ? 89.040  174.910 136.723 1.00 30.00 ? 3   GLN A CA  1 
ATOM   17   C C   . GLN A 1 3   ? 87.534  174.765 136.525 1.00 30.00 ? 3   GLN A C   1 
ATOM   18   O O   . GLN A 1 3   ? 87.070  173.631 136.520 1.00 30.00 ? 3   GLN A O   1 
ATOM   19   C CB  . GLN A 1 3   ? 89.820  174.776 135.421 1.00 30.00 ? 3   GLN A CB  1 
ATOM   20   C CG  . GLN A 1 3   ? 89.561  173.481 134.668 1.00 30.00 ? 3   GLN A CG  1 
ATOM   21   C CD  . GLN A 1 3   ? 90.289  173.447 133.348 1.00 30.00 ? 3   GLN A CD  1 
ATOM   22   O OE1 . GLN A 1 3   ? 91.123  172.580 133.097 1.00 30.00 ? 3   GLN A OE1 1 
ATOM   23   N NE2 . GLN A 1 3   ? 89.965  174.395 132.486 1.00 30.00 ? 3   GLN A NE2 1 
ATOM   24   N N   . GLN A 1 4   ? 86.801  175.861 136.401 1.00 30.00 ? 4   GLN A N   1 
ATOM   25   C CA  . GLN A 1 4   ? 85.347  175.800 136.124 1.00 30.00 ? 4   GLN A CA  1 
ATOM   26   C C   . GLN A 1 4   ? 85.152  175.815 134.610 1.00 30.00 ? 4   GLN A C   1 
ATOM   27   O O   . GLN A 1 4   ? 85.919  176.518 133.935 1.00 30.00 ? 4   GLN A O   1 
ATOM   28   C CB  . GLN A 1 4   ? 84.613  176.953 136.795 1.00 30.00 ? 4   GLN A CB  1 
ATOM   29   C CG  . GLN A 1 4   ? 83.100  176.808 136.713 1.00 30.00 ? 4   GLN A CG  1 
ATOM   30   C CD  . GLN A 1 4   ? 82.370  177.932 137.402 1.00 30.00 ? 4   GLN A CD  1 
ATOM   31   O OE1 . GLN A 1 4   ? 82.974  178.851 137.949 1.00 30.00 ? 4   GLN A OE1 1 
ATOM   32   N NE2 . GLN A 1 4   ? 81.050  177.863 137.379 1.00 30.00 ? 4   GLN A NE2 1 
ATOM   33   N N   . THR A 1 5   ? 84.179  175.061 134.099 1.00 30.00 ? 5   THR A N   1 
ATOM   34   C CA  . THR A 1 5   ? 83.908  174.958 132.643 1.00 30.00 ? 5   THR A CA  1 
ATOM   35   C C   . THR A 1 5   ? 82.438  175.292 132.379 1.00 30.00 ? 5   THR A C   1 
ATOM   36   O O   . THR A 1 5   ? 81.668  175.312 133.359 1.00 30.00 ? 5   THR A O   1 
ATOM   37   C CB  . THR A 1 5   ? 84.301  173.564 132.150 1.00 30.00 ? 5   THR A CB  1 
ATOM   38   O OG1 . THR A 1 5   ? 83.568  172.622 132.928 1.00 30.00 ? 5   THR A OG1 1 
ATOM   39   C CG2 . THR A 1 5   ? 85.781  173.284 132.278 1.00 30.00 ? 5   THR A CG2 1 
ATOM   40   N N   . GLY A 1 6   ? 82.055  175.540 131.121 1.00 30.00 ? 6   GLY A N   1 
ATOM   41   C CA  . GLY A 1 6   ? 80.676  175.914 130.751 1.00 30.00 ? 6   GLY A CA  1 
ATOM   42   C C   . GLY A 1 6   ? 79.670  174.908 131.274 1.00 30.00 ? 6   GLY A C   1 
ATOM   43   O O   . GLY A 1 6   ? 79.982  173.701 131.232 1.00 30.00 ? 6   GLY A O   1 
ATOM   44   N N   . GLY A 1 7   ? 78.512  175.374 131.752 1.00 30.00 ? 7   GLY A N   1 
ATOM   45   C CA  . GLY A 1 7   ? 77.471  174.506 132.337 1.00 30.00 ? 7   GLY A CA  1 
ATOM   46   C C   . GLY A 1 7   ? 77.457  174.615 133.850 1.00 30.00 ? 7   GLY A C   1 
ATOM   47   O O   . GLY A 1 7   ? 76.519  174.067 134.461 1.00 30.00 ? 7   GLY A O   1 
ATOM   48   N N   . GLY A 1 8   ? 78.452  175.284 134.441 1.00 30.00 ? 8   GLY A N   1 
ATOM   49   C CA  . GLY A 1 8   ? 78.520  175.496 135.900 1.00 30.00 ? 8   GLY A CA  1 
ATOM   50   C C   . GLY A 1 8   ? 79.231  174.354 136.601 1.00 30.00 ? 8   GLY A C   1 
ATOM   51   O O   . GLY A 1 8   ? 79.280  174.383 137.846 1.00 30.00 ? 8   GLY A O   1 
ATOM   52   N N   . ASN A 1 9   ? 79.774  173.394 135.847 1.00 30.00 ? 9   ASN A N   1 
ATOM   53   C CA  . ASN A 1 9   ? 80.454  172.202 136.422 1.00 30.00 ? 9   ASN A CA  1 
ATOM   54   C C   . ASN A 1 9   ? 81.953  172.476 136.512 1.00 30.00 ? 9   ASN A C   1 
ATOM   55   O O   . ASN A 1 9   ? 82.407  173.435 135.859 1.00 30.00 ? 9   ASN A O   1 
ATOM   56   C CB  . ASN A 1 9   ? 80.173  170.930 135.621 1.00 30.00 ? 9   ASN A CB  1 
ATOM   57   C CG  . ASN A 1 9   ? 80.752  170.946 134.224 1.00 30.00 ? 9   ASN A CG  1 
ATOM   58   O OD1 . ASN A 1 9   ? 81.966  170.877 134.048 1.00 30.00 ? 9   ASN A OD1 1 
ATOM   59   N ND2 . ASN A 1 9   ? 79.887  170.959 133.224 1.00 30.00 ? 9   ASN A ND2 1 
ATOM   60   N N   . TYR A 1 10  ? 82.696  171.666 137.264 1.00 30.00 ? 10  TYR A N   1 
ATOM   61   C CA  . TYR A 1 10  ? 84.153  171.860 137.460 1.00 30.00 ? 10  TYR A CA  1 
ATOM   62   C C   . TYR A 1 10  ? 84.904  170.610 137.005 1.00 30.00 ? 10  TYR A C   1 
ATOM   63   O O   . TYR A 1 10  ? 84.294  169.522 137.021 1.00 30.00 ? 10  TYR A O   1 
ATOM   64   C CB  . TYR A 1 10  ? 84.449  172.167 138.926 1.00 30.00 ? 10  TYR A CB  1 
ATOM   65   C CG  . TYR A 1 10  ? 83.838  173.435 139.464 1.00 30.00 ? 10  TYR A CG  1 
ATOM   66   C CD1 . TYR A 1 10  ? 82.467  173.596 139.554 1.00 30.00 ? 10  TYR A CD1 1 
ATOM   67   C CD2 . TYR A 1 10  ? 84.641  174.486 139.867 1.00 30.00 ? 10  TYR A CD2 1 
ATOM   68   C CE1 . TYR A 1 10  ? 81.908  174.760 140.051 1.00 30.00 ? 10  TYR A CE1 1 
ATOM   69   C CE2 . TYR A 1 10  ? 84.100  175.660 140.360 1.00 30.00 ? 10  TYR A CE2 1 
ATOM   70   C CZ  . TYR A 1 10  ? 82.728  175.797 140.454 1.00 30.00 ? 10  TYR A CZ  1 
ATOM   71   O OH  . TYR A 1 10  ? 82.187  176.956 140.943 1.00 30.00 ? 10  TYR A OH  1 
ATOM   72   N N   . ILE A 1 11  ? 86.172  170.756 136.616 1.00 30.00 ? 11  ILE A N   1 
ATOM   73   C CA  . ILE A 1 11  ? 87.018  169.618 136.149 1.00 30.00 ? 11  ILE A CA  1 
ATOM   74   C C   . ILE A 1 11  ? 88.368  169.687 136.861 1.00 30.00 ? 11  ILE A C   1 
ATOM   75   O O   . ILE A 1 11  ? 88.591  170.671 137.581 1.00 30.00 ? 11  ILE A O   1 
ATOM   76   C CB  . ILE A 1 11  ? 87.170  169.621 134.616 1.00 30.00 ? 11  ILE A CB  1 
ATOM   77   C CG1 . ILE A 1 11  ? 87.927  170.845 134.103 1.00 30.00 ? 11  ILE A CG1 1 
ATOM   78   C CG2 . ILE A 1 11  ? 85.804  169.492 133.959 1.00 30.00 ? 11  ILE A CG2 1 
ATOM   79   C CD1 . ILE A 1 11  ? 88.207  170.808 132.622 1.00 30.00 ? 11  ILE A CD1 1 
ATOM   80   N N   . HIS A 1 12  ? 89.222  168.680 136.668 1.00 30.00 ? 12  HIS A N   1 
ATOM   81   C CA  . HIS A 1 12  ? 90.517  168.638 137.397 1.00 30.00 ? 12  HIS A CA  1 
ATOM   82   C C   . HIS A 1 12  ? 91.672  168.887 136.423 1.00 30.00 ? 12  HIS A C   1 
ATOM   83   O O   . HIS A 1 12  ? 91.758  168.186 135.392 1.00 30.00 ? 12  HIS A O   1 
ATOM   84   C CB  . HIS A 1 12  ? 90.678  167.293 138.112 1.00 30.00 ? 12  HIS A CB  1 
ATOM   85   C CG  . HIS A 1 12  ? 92.056  167.055 138.626 1.00 30.00 ? 12  HIS A CG  1 
ATOM   86   N ND1 . HIS A 1 12  ? 92.579  167.763 139.684 1.00 30.00 ? 12  HIS A ND1 1 
ATOM   87   C CD2 . HIS A 1 12  ? 93.014  166.205 138.237 1.00 30.00 ? 12  HIS A CD2 1 
ATOM   88   C CE1 . HIS A 1 12  ? 93.811  167.345 139.918 1.00 30.00 ? 12  HIS A CE1 1 
ATOM   89   N NE2 . HIS A 1 12  ? 94.097  166.400 139.052 1.00 30.00 ? 12  HIS A NE2 1 
ATOM   90   N N   . VAL A 1 13  ? 92.537  169.853 136.742 1.00 30.00 ? 13  VAL A N   1 
ATOM   91   C CA  . VAL A 1 13  ? 93.735  170.111 135.889 1.00 30.00 ? 13  VAL A CA  1 
ATOM   92   C C   . VAL A 1 13  ? 94.969  169.631 136.657 1.00 30.00 ? 13  VAL A C   1 
ATOM   93   O O   . VAL A 1 13  ? 95.246  170.187 137.730 1.00 30.00 ? 13  VAL A O   1 
ATOM   94   C CB  . VAL A 1 13  ? 93.850  171.598 135.503 1.00 30.00 ? 13  VAL A CB  1 
ATOM   95   C CG1 . VAL A 1 13  ? 93.358  172.527 136.601 1.00 30.00 ? 13  VAL A CG1 1 
ATOM   96   C CG2 . VAL A 1 13  ? 95.251  171.974 135.047 1.00 30.00 ? 13  VAL A CG2 1 
ATOM   97   N N   . PRO A 1 14  ? 95.694  168.590 136.194 1.00 30.00 ? 14  PRO A N   1 
ATOM   98   C CA  . PRO A 1 14  ? 96.831  168.064 136.957 1.00 30.00 ? 14  PRO A CA  1 
ATOM   99   C C   . PRO A 1 14  ? 97.909  169.084 137.346 1.00 30.00 ? 14  PRO A C   1 
ATOM   100  O O   . PRO A 1 14  ? 98.292  169.876 136.501 1.00 30.00 ? 14  PRO A O   1 
ATOM   101  C CB  . PRO A 1 14  ? 97.453  167.050 135.990 1.00 30.00 ? 14  PRO A CB  1 
ATOM   102  C CG  . PRO A 1 14  ? 96.787  167.299 134.657 1.00 30.00 ? 14  PRO A CG  1 
ATOM   103  C CD  . PRO A 1 14  ? 95.408  167.799 135.007 1.00 30.00 ? 14  PRO A CD  1 
ATOM   104  N N   . LEU A 1 15  ? 98.335  169.086 138.617 1.00 30.00 ? 15  LEU A N   1 
ATOM   105  C CA  . LEU A 1 15  ? 99.418  169.976 139.124 1.00 30.00 ? 15  LEU A CA  1 
ATOM   106  C C   . LEU A 1 15  ? 100.561 170.004 138.102 1.00 30.00 ? 15  LEU A C   1 
ATOM   107  O O   . LEU A 1 15  ? 100.930 168.912 137.624 1.00 30.00 ? 15  LEU A O   1 
ATOM   108  C CB  . LEU A 1 15  ? 99.860  169.428 140.489 1.00 30.00 ? 15  LEU A CB  1 
ATOM   109  C CG  . LEU A 1 15  ? 100.456 170.425 141.474 1.00 30.00 ? 15  LEU A CG  1 
ATOM   110  C CD1 . LEU A 1 15  ? 99.460  171.514 141.819 1.00 30.00 ? 15  LEU A CD1 1 
ATOM   111  C CD2 . LEU A 1 15  ? 100.890 169.707 142.740 1.00 30.00 ? 15  LEU A CD2 1 
ATOM   112  N N   . SER A 1 16  ? 101.121 171.178 137.779 1.00 30.00 ? 16  SER A N   1 
ATOM   113  C CA  . SER A 1 16  ? 102.190 171.308 136.749 1.00 30.00 ? 16  SER A CA  1 
ATOM   114  C C   . SER A 1 16  ? 103.403 170.483 137.190 1.00 30.00 ? 16  SER A C   1 
ATOM   115  O O   . SER A 1 16  ? 103.674 170.428 138.405 1.00 30.00 ? 16  SER A O   1 
ATOM   116  C CB  . SER A 1 16  ? 102.577 172.752 136.464 1.00 30.00 ? 16  SER A CB  1 
ATOM   117  O OG  . SER A 1 16  ? 103.972 172.951 136.586 1.00 30.00 ? 16  SER A OG  1 
ATOM   118  N N   . PRO A 1 17  ? 104.138 169.833 136.262 1.00 30.00 ? 17  PRO A N   1 
ATOM   119  C CA  . PRO A 1 17  ? 105.342 169.084 136.619 1.00 30.00 ? 17  PRO A CA  1 
ATOM   120  C C   . PRO A 1 17  ? 106.363 169.953 137.361 1.00 30.00 ? 17  PRO A C   1 
ATOM   121  O O   . PRO A 1 17  ? 106.990 169.447 138.269 1.00 30.00 ? 17  PRO A O   1 
ATOM   122  C CB  . PRO A 1 17  ? 105.926 168.681 135.260 1.00 30.00 ? 17  PRO A CB  1 
ATOM   123  C CG  . PRO A 1 17  ? 104.730 168.605 134.352 1.00 30.00 ? 17  PRO A CG  1 
ATOM   124  C CD  . PRO A 1 17  ? 103.805 169.697 134.843 1.00 30.00 ? 17  PRO A CD  1 
ATOM   125  N N   . ARG A 1 18  ? 106.514 171.217 136.961 1.00 30.00 ? 18  ARG A N   1 
ATOM   126  C CA  . ARG A 1 18  ? 107.488 172.146 137.592 1.00 30.00 ? 18  ARG A CA  1 
ATOM   127  C C   . ARG A 1 18  ? 106.931 172.640 138.931 1.00 30.00 ? 18  ARG A C   1 
ATOM   128  O O   . ARG A 1 18  ? 107.741 173.105 139.736 1.00 30.00 ? 18  ARG A O   1 
ATOM   129  C CB  . ARG A 1 18  ? 107.834 173.278 136.622 1.00 30.00 ? 18  ARG A CB  1 
ATOM   130  C CG  . ARG A 1 18  ? 108.707 172.826 135.461 1.00 30.00 ? 18  ARG A CG  1 
ATOM   131  C CD  . ARG A 1 18  ? 108.982 173.866 134.398 1.00 30.00 ? 18  ARG A CD  1 
ATOM   132  N NE  . ARG A 1 18  ? 109.886 174.922 134.824 1.00 30.00 ? 18  ARG A NE  1 
ATOM   133  C CZ  . ARG A 1 18  ? 109.636 176.225 134.754 1.00 30.00 ? 18  ARG A CZ  1 
ATOM   134  N NH1 . ARG A 1 18  ? 108.766 176.693 133.880 1.00 30.00 ? 18  ARG A NH1 1 
ATOM   135  N NH2 . ARG A 1 18  ? 110.320 177.068 135.511 1.00 30.00 ? 18  ARG A NH2 1 
ATOM   136  N N   . THR A 1 19  ? 105.615 172.612 139.157 1.00 30.00 ? 19  THR A N   1 
ATOM   137  C CA  . THR A 1 19  ? 105.044 172.933 140.495 1.00 30.00 ? 19  THR A CA  1 
ATOM   138  C C   . THR A 1 19  ? 105.429 171.771 141.412 1.00 30.00 ? 19  THR A C   1 
ATOM   139  O O   . THR A 1 19  ? 105.794 172.040 142.573 1.00 30.00 ? 19  THR A O   1 
ATOM   140  C CB  . THR A 1 19  ? 103.529 173.172 140.453 1.00 30.00 ? 19  THR A CB  1 
ATOM   141  O OG1 . THR A 1 19  ? 103.289 174.318 139.639 1.00 30.00 ? 19  THR A OG1 1 
ATOM   142  C CG2 . THR A 1 19  ? 102.931 173.359 141.829 1.00 30.00 ? 19  THR A CG2 1 
ATOM   143  N N   . LEU A 1 20  ? 105.358 170.534 140.908 1.00 30.00 ? 20  LEU A N   1 
ATOM   144  C CA  . LEU A 1 20  ? 105.755 169.321 141.671 1.00 30.00 ? 20  LEU A CA  1 
ATOM   145  C C   . LEU A 1 20  ? 107.269 169.301 141.870 1.00 30.00 ? 20  LEU A C   1 
ATOM   146  O O   . LEU A 1 20  ? 107.689 168.845 142.935 1.00 30.00 ? 20  LEU A O   1 
ATOM   147  C CB  . LEU A 1 20  ? 105.349 168.068 140.895 1.00 30.00 ? 20  LEU A CB  1 
ATOM   148  C CG  . LEU A 1 20  ? 103.875 167.679 140.933 1.00 30.00 ? 20  LEU A CG  1 
ATOM   149  C CD1 . LEU A 1 20  ? 103.606 166.555 139.946 1.00 30.00 ? 20  LEU A CD1 1 
ATOM   150  C CD2 . LEU A 1 20  ? 103.464 167.259 142.335 1.00 30.00 ? 20  LEU A CD2 1 
ATOM   151  N N   . ASN A 1 21  ? 108.050 169.736 140.878 1.00 30.00 ? 21  ASN A N   1 
ATOM   152  C CA  . ASN A 1 21  ? 109.534 169.652 140.941 1.00 30.00 ? 21  ASN A CA  1 
ATOM   153  C C   . ASN A 1 21  ? 110.057 170.689 141.929 1.00 30.00 ? 21  ASN A C   1 
ATOM   154  O O   . ASN A 1 21  ? 111.101 170.426 142.496 1.00 30.00 ? 21  ASN A O   1 
ATOM   155  C CB  . ASN A 1 21  ? 110.188 169.858 139.580 1.00 30.00 ? 21  ASN A CB  1 
ATOM   156  C CG  . ASN A 1 21  ? 111.693 169.758 139.649 1.00 30.00 ? 21  ASN A CG  1 
ATOM   157  O OD1 . ASN A 1 21  ? 112.223 168.751 140.102 1.00 30.00 ? 21  ASN A OD1 1 
ATOM   158  N ND2 . ASN A 1 21  ? 112.383 170.811 139.253 1.00 30.00 ? 21  ASN A ND2 1 
ATOM   159  N N   . ALA A 1 22  ? 109.436 171.860 142.028 1.00 30.00 ? 22  ALA A N   1 
ATOM   160  C CA  . ALA A 1 22  ? 109.776 172.870 143.056 1.00 30.00 ? 22  ALA A CA  1 
ATOM   161  C C   . ALA A 1 22  ? 109.625 172.233 144.440 1.00 30.00 ? 22  ALA A C   1 
ATOM   162  O O   . ALA A 1 22  ? 110.571 172.329 145.245 1.00 30.00 ? 22  ALA A O   1 
ATOM   163  C CB  . ALA A 1 22  ? 108.888 174.080 142.909 1.00 30.00 ? 22  ALA A CB  1 
ATOM   164  N N   . TRP A 1 23  ? 108.475 171.604 144.696 1.00 30.00 ? 23  TRP A N   1 
ATOM   165  C CA  . TRP A 1 23  ? 108.240 170.920 145.995 1.00 30.00 ? 23  TRP A CA  1 
ATOM   166  C C   . TRP A 1 23  ? 109.394 169.954 146.284 1.00 30.00 ? 23  TRP A C   1 
ATOM   167  O O   . TRP A 1 23  ? 109.993 170.065 147.371 1.00 30.00 ? 23  TRP A O   1 
ATOM   168  C CB  . TRP A 1 23  ? 106.888 170.201 145.963 1.00 30.00 ? 23  TRP A CB  1 
ATOM   169  C CG  . TRP A 1 23  ? 106.642 169.281 147.115 1.00 30.00 ? 23  TRP A CG  1 
ATOM   170  C CD1 . TRP A 1 23  ? 106.348 167.951 147.049 1.00 30.00 ? 23  TRP A CD1 1 
ATOM   171  C CD2 . TRP A 1 23  ? 106.646 169.621 148.513 1.00 30.00 ? 23  TRP A CD2 1 
ATOM   172  N NE1 . TRP A 1 23  ? 106.169 167.442 148.305 1.00 30.00 ? 23  TRP A NE1 1 
ATOM   173  C CE2 . TRP A 1 23  ? 106.349 168.440 149.224 1.00 30.00 ? 23  TRP A CE2 1 
ATOM   174  C CE3 . TRP A 1 23  ? 106.870 170.801 149.231 1.00 30.00 ? 23  TRP A CE3 1 
ATOM   175  C CZ2 . TRP A 1 23  ? 106.273 168.406 150.614 1.00 30.00 ? 23  TRP A CZ2 1 
ATOM   176  C CZ3 . TRP A 1 23  ? 106.801 170.765 150.605 1.00 30.00 ? 23  TRP A CZ3 1 
ATOM   177  C CH2 . TRP A 1 23  ? 106.503 169.584 151.285 1.00 30.00 ? 23  TRP A CH2 1 
ATOM   178  N N   . VAL A 1 24  ? 109.684 169.046 145.348 1.00 30.00 ? 24  VAL A N   1 
ATOM   179  C CA  . VAL A 1 24  ? 110.816 168.086 145.516 1.00 30.00 ? 24  VAL A CA  1 
ATOM   180  C C   . VAL A 1 24  ? 112.067 168.870 145.925 1.00 30.00 ? 24  VAL A C   1 
ATOM   181  O O   . VAL A 1 24  ? 112.587 168.610 147.028 1.00 30.00 ? 24  VAL A O   1 
ATOM   182  C CB  . VAL A 1 24  ? 111.055 167.284 144.222 1.00 30.00 ? 24  VAL A CB  1 
ATOM   183  C CG1 . VAL A 1 24  ? 112.337 166.467 144.284 1.00 30.00 ? 24  VAL A CG1 1 
ATOM   184  C CG2 . VAL A 1 24  ? 109.866 166.404 143.876 1.00 30.00 ? 24  VAL A CG2 1 
ATOM   185  N N   . LYS A 1 25  ? 112.521 169.795 145.074 1.00 30.00 ? 25  LYS A N   1 
ATOM   186  C CA  . LYS A 1 25  ? 113.748 170.588 145.356 1.00 30.00 ? 25  LYS A CA  1 
ATOM   187  C C   . LYS A 1 25  ? 113.738 171.070 146.809 1.00 30.00 ? 25  LYS A C   1 
ATOM   188  O O   . LYS A 1 25  ? 114.706 170.775 147.535 1.00 30.00 ? 25  LYS A O   1 
ATOM   189  C CB  . LYS A 1 25  ? 113.820 171.786 144.405 1.00 30.00 ? 25  LYS A CB  1 
ATOM   190  C CG  . LYS A 1 25  ? 114.098 171.442 142.949 1.00 30.00 ? 25  LYS A CG  1 
ATOM   191  C CD  . LYS A 1 25  ? 113.484 172.418 141.973 1.00 30.00 ? 25  LYS A CD  1 
ATOM   192  C CE  . LYS A 1 25  ? 114.337 173.648 141.751 1.00 30.00 ? 25  LYS A CE  1 
ATOM   193  N NZ  . LYS A 1 25  ? 113.624 174.667 140.946 1.00 30.00 ? 25  LYS A NZ  1 
ATOM   194  N N   . LEU A 1 26  ? 112.691 171.796 147.206 1.00 30.00 ? 26  LEU A N   1 
ATOM   195  C CA  . LEU A 1 26  ? 112.604 172.358 148.581 1.00 30.00 ? 26  LEU A CA  1 
ATOM   196  C C   . LEU A 1 26  ? 112.870 171.264 149.622 1.00 30.00 ? 26  LEU A C   1 
ATOM   197  O O   . LEU A 1 26  ? 113.743 171.477 150.483 1.00 30.00 ? 26  LEU A O   1 
ATOM   198  C CB  . LEU A 1 26  ? 111.197 172.945 148.739 1.00 30.00 ? 26  LEU A CB  1 
ATOM   199  C CG  . LEU A 1 26  ? 110.849 173.507 150.115 1.00 30.00 ? 26  LEU A CG  1 
ATOM   200  C CD1 . LEU A 1 26  ? 111.512 174.857 150.326 1.00 30.00 ? 26  LEU A CD1 1 
ATOM   201  C CD2 . LEU A 1 26  ? 109.342 173.627 150.275 1.00 30.00 ? 26  LEU A CD2 1 
ATOM   202  N N   . VAL A 1 27  ? 112.170 170.132 149.531 1.00 30.00 ? 27  VAL A N   1 
ATOM   203  C CA  . VAL A 1 27  ? 112.276 169.047 150.548 1.00 30.00 ? 27  VAL A CA  1 
ATOM   204  C C   . VAL A 1 27  ? 113.687 168.452 150.504 1.00 30.00 ? 27  VAL A C   1 
ATOM   205  O O   . VAL A 1 27  ? 114.139 167.967 151.560 1.00 30.00 ? 27  VAL A O   1 
ATOM   206  C CB  . VAL A 1 27  ? 111.193 167.989 150.279 1.00 30.00 ? 27  VAL A CB  1 
ATOM   207  C CG1 . VAL A 1 27  ? 111.431 166.702 151.051 1.00 30.00 ? 27  VAL A CG1 1 
ATOM   208  C CG2 . VAL A 1 27  ? 109.798 168.526 150.553 1.00 30.00 ? 27  VAL A CG2 1 
ATOM   209  N N   . GLU A 1 28  ? 114.371 168.505 149.357 1.00 30.00 ? 28  GLU A N   1 
ATOM   210  C CA  . GLU A 1 28  ? 115.728 167.922 149.172 1.00 30.00 ? 28  GLU A CA  1 
ATOM   211  C C   . GLU A 1 28  ? 116.816 168.881 149.645 1.00 30.00 ? 28  GLU A C   1 
ATOM   212  O O   . GLU A 1 28  ? 117.945 168.402 149.865 1.00 30.00 ? 28  GLU A O   1 
ATOM   213  C CB  . GLU A 1 28  ? 115.978 167.657 147.690 1.00 30.00 ? 28  GLU A CB  1 
ATOM   214  C CG  . GLU A 1 28  ? 115.194 166.478 147.147 1.00 30.00 ? 28  GLU A CG  1 
ATOM   215  C CD  . GLU A 1 28  ? 115.731 165.108 147.520 1.00 30.00 ? 28  GLU A CD  1 
ATOM   216  O OE1 . GLU A 1 28  ? 116.796 165.036 148.157 1.00 30.00 ? 28  GLU A OE1 1 
ATOM   217  O OE2 . GLU A 1 28  ? 115.070 164.116 147.185 1.00 30.00 ? 28  GLU A OE2 1 
ATOM   218  N N   . ASP A 1 29  ? 116.508 170.170 149.789 1.00 30.00 ? 29  ASP A N   1 
ATOM   219  C CA  . ASP A 1 29  ? 117.524 171.200 150.127 1.00 30.00 ? 29  ASP A CA  1 
ATOM   220  C C   . ASP A 1 29  ? 117.309 171.729 151.545 1.00 30.00 ? 29  ASP A C   1 
ATOM   221  O O   . ASP A 1 29  ? 118.323 171.972 152.228 1.00 30.00 ? 29  ASP A O   1 
ATOM   222  C CB  . ASP A 1 29  ? 117.461 172.323 149.095 1.00 30.00 ? 29  ASP A CB  1 
ATOM   223  C CG  . ASP A 1 29  ? 118.264 173.560 149.450 1.00 30.00 ? 29  ASP A CG  1 
ATOM   224  O OD1 . ASP A 1 29  ? 119.489 173.434 149.641 1.00 30.00 ? 29  ASP A OD1 1 
ATOM   225  O OD2 . ASP A 1 29  ? 117.657 174.644 149.517 1.00 30.00 ? 29  ASP A OD2 1 
ATOM   226  N N   . LYS A 1 30  ? 116.060 171.911 151.981 1.00 30.00 ? 30  LYS A N   1 
ATOM   227  C CA  . LYS A 1 30  ? 115.756 172.489 153.316 1.00 30.00 ? 30  LYS A CA  1 
ATOM   228  C C   . LYS A 1 30  ? 115.619 171.359 154.333 1.00 30.00 ? 30  LYS A C   1 
ATOM   229  O O   . LYS A 1 30  ? 115.476 171.673 155.529 1.00 30.00 ? 30  LYS A O   1 
ATOM   230  C CB  . LYS A 1 30  ? 114.489 173.337 153.232 1.00 30.00 ? 30  LYS A CB  1 
ATOM   231  C CG  . LYS A 1 30  ? 114.519 174.436 152.183 1.00 30.00 ? 30  LYS A CG  1 
ATOM   232  C CD  . LYS A 1 30  ? 115.702 175.354 152.317 1.00 30.00 ? 30  LYS A CD  1 
ATOM   233  C CE  . LYS A 1 30  ? 115.662 176.500 151.334 1.00 30.00 ? 30  LYS A CE  1 
ATOM   234  N NZ  . LYS A 1 30  ? 116.860 177.359 151.467 1.00 30.00 ? 30  LYS A NZ  1 
ATOM   235  N N   . LYS A 1 31  ? 115.596 170.110 153.862 1.00 30.00 ? 31  LYS A N   1 
ATOM   236  C CA  . LYS A 1 31  ? 115.592 168.933 154.761 1.00 30.00 ? 31  LYS A CA  1 
ATOM   237  C C   . LYS A 1 31  ? 114.501 169.078 155.824 1.00 30.00 ? 31  LYS A C   1 
ATOM   238  O O   . LYS A 1 31  ? 114.832 168.987 157.023 1.00 30.00 ? 31  LYS A O   1 
ATOM   239  C CB  . LYS A 1 31  ? 116.983 168.839 155.386 1.00 30.00 ? 31  LYS A CB  1 
ATOM   240  C CG  . LYS A 1 31  ? 118.151 169.182 154.471 1.00 30.00 ? 31  LYS A CG  1 
ATOM   241  C CD  . LYS A 1 31  ? 118.153 168.443 153.157 1.00 30.00 ? 31  LYS A CD  1 
ATOM   242  C CE  . LYS A 1 31  ? 119.551 168.186 152.635 1.00 30.00 ? 31  LYS A CE  1 
ATOM   243  N NZ  . LYS A 1 31  ? 120.254 169.445 152.297 1.00 30.00 ? 31  LYS A NZ  1 
ATOM   244  N N   . PHE A 1 32  ? 113.249 169.289 155.416 1.00 30.00 ? 32  PHE A N   1 
ATOM   245  C CA  . PHE A 1 32  ? 112.104 169.426 156.354 1.00 30.00 ? 32  PHE A CA  1 
ATOM   246  C C   . PHE A 1 32  ? 112.424 170.537 157.355 1.00 30.00 ? 32  PHE A C   1 
ATOM   247  O O   . PHE A 1 32  ? 112.089 170.379 158.541 1.00 30.00 ? 32  PHE A O   1 
ATOM   248  C CB  . PHE A 1 32  ? 111.808 168.072 157.003 1.00 30.00 ? 32  PHE A CB  1 
ATOM   249  C CG  . PHE A 1 32  ? 111.196 167.105 156.032 1.00 30.00 ? 32  PHE A CG  1 
ATOM   250  C CD1 . PHE A 1 32  ? 109.888 167.266 155.615 1.00 30.00 ? 32  PHE A CD1 1 
ATOM   251  C CD2 . PHE A 1 32  ? 111.958 166.101 155.466 1.00 30.00 ? 32  PHE A CD2 1 
ATOM   252  C CE1 . PHE A 1 32  ? 109.335 166.401 154.687 1.00 30.00 ? 32  PHE A CE1 1 
ATOM   253  C CE2 . PHE A 1 32  ? 111.403 165.239 154.538 1.00 30.00 ? 32  PHE A CE2 1 
ATOM   254  C CZ  . PHE A 1 32  ? 110.095 165.389 154.152 1.00 30.00 ? 32  PHE A CZ  1 
ATOM   255  N N   . GLY A 1 33  ? 113.054 171.620 156.896 1.00 30.00 ? 33  GLY A N   1 
ATOM   256  C CA  . GLY A 1 33  ? 113.349 172.784 157.753 1.00 30.00 ? 33  GLY A CA  1 
ATOM   257  C C   . GLY A 1 33  ? 112.089 173.607 157.926 1.00 30.00 ? 33  GLY A C   1 
ATOM   258  O O   . GLY A 1 33  ? 111.145 173.369 157.165 1.00 30.00 ? 33  GLY A O   1 
ATOM   259  N N   . ALA A 1 34  ? 112.012 174.474 158.936 1.00 30.00 ? 34  ALA A N   1 
ATOM   260  C CA  . ALA A 1 34  ? 110.835 175.338 159.186 1.00 30.00 ? 34  ALA A CA  1 
ATOM   261  C C   . ALA A 1 34  ? 110.243 175.841 157.863 1.00 30.00 ? 34  ALA A C   1 
ATOM   262  O O   . ALA A 1 34  ? 109.013 175.759 157.725 1.00 30.00 ? 34  ALA A O   1 
ATOM   263  C CB  . ALA A 1 34  ? 111.242 176.478 160.078 1.00 30.00 ? 34  ALA A CB  1 
ATOM   264  N N   . GLU A 1 35  ? 111.070 176.308 156.923 1.00 30.00 ? 35  GLU A N   1 
ATOM   265  C CA  . GLU A 1 35  ? 110.622 176.900 155.625 1.00 30.00 ? 35  GLU A CA  1 
ATOM   266  C C   . GLU A 1 35  ? 109.765 175.936 154.796 1.00 30.00 ? 35  GLU A C   1 
ATOM   267  O O   . GLU A 1 35  ? 109.204 176.405 153.788 1.00 30.00 ? 35  GLU A O   1 
ATOM   268  C CB  . GLU A 1 35  ? 111.811 177.353 154.768 1.00 30.00 ? 35  GLU A CB  1 
ATOM   269  C CG  . GLU A 1 35  ? 112.941 176.344 154.618 1.00 30.00 ? 35  GLU A CG  1 
ATOM   270  C CD  . GLU A 1 35  ? 113.965 176.334 155.744 1.00 30.00 ? 35  GLU A CD  1 
ATOM   271  O OE1 . GLU A 1 35  ? 113.812 177.133 156.673 1.00 30.00 ? 35  GLU A OE1 1 
ATOM   272  O OE2 . GLU A 1 35  ? 114.898 175.517 155.703 1.00 30.00 ? 35  GLU A OE2 1 
ATOM   273  N N   A VAL A 1 36  ? 109.952 174.628 155.000 0.50 30.00 ? 36  VAL A N   1 
ATOM   274  N N   B VAL A 1 36  ? 109.962 174.629 154.985 0.50 30.00 ? 36  VAL A N   1 
ATOM   275  C CA  A VAL A 1 36  ? 109.197 173.611 154.206 0.50 30.00 ? 36  VAL A CA  1 
ATOM   276  C CA  B VAL A 1 36  ? 109.203 173.615 154.195 0.50 30.00 ? 36  VAL A CA  1 
ATOM   277  C C   A VAL A 1 36  ? 107.698 173.742 154.493 0.50 30.00 ? 36  VAL A C   1 
ATOM   278  C C   B VAL A 1 36  ? 107.706 173.744 154.496 0.50 30.00 ? 36  VAL A C   1 
ATOM   279  O O   A VAL A 1 36  ? 106.915 173.264 153.650 0.50 30.00 ? 36  VAL A O   1 
ATOM   280  O O   B VAL A 1 36  ? 106.913 173.581 153.570 0.50 30.00 ? 36  VAL A O   1 
ATOM   281  C CB  A VAL A 1 36  ? 109.699 172.182 154.498 0.50 30.00 ? 36  VAL A CB  1 
ATOM   282  C CB  B VAL A 1 36  ? 109.720 172.189 154.471 0.50 30.00 ? 36  VAL A CB  1 
ATOM   283  C CG1 A VAL A 1 36  ? 109.022 171.559 155.712 0.50 30.00 ? 36  VAL A CG1 1 
ATOM   284  C CG1 B VAL A 1 36  ? 108.873 171.129 153.784 0.50 30.00 ? 36  VAL A CG1 1 
ATOM   285  C CG2 A VAL A 1 36  ? 109.538 171.275 153.290 0.50 30.00 ? 36  VAL A CG2 1 
ATOM   286  C CG2 B VAL A 1 36  ? 111.179 172.043 154.067 0.50 30.00 ? 36  VAL A CG2 1 
ATOM   287  N N   . VAL A 1 37  ? 107.341 174.037 155.747 1.00 30.00 ? 37  VAL A N   1 
ATOM   288  C CA  . VAL A 1 37  ? 105.896 174.106 156.125 1.00 30.00 ? 37  VAL A CA  1 
ATOM   289  C C   . VAL A 1 37  ? 105.187 175.184 155.292 1.00 30.00 ? 37  VAL A C   1 
ATOM   290  O O   . VAL A 1 37  ? 104.172 174.842 154.647 1.00 30.00 ? 37  VAL A O   1 
ATOM   291  C CB  . VAL A 1 37  ? 105.736 174.355 157.637 1.00 30.00 ? 37  VAL A CB  1 
ATOM   292  C CG1 . VAL A 1 37  ? 104.283 174.583 158.016 1.00 30.00 ? 37  VAL A CG1 1 
ATOM   293  C CG2 . VAL A 1 37  ? 106.328 173.219 158.457 1.00 30.00 ? 37  VAL A CG2 1 
ATOM   294  N N   . PRO A 1 38  ? 105.673 176.445 155.220 1.00 30.00 ? 38  PRO A N   1 
ATOM   295  C CA  . PRO A 1 38  ? 105.066 177.460 154.352 1.00 30.00 ? 38  PRO A CA  1 
ATOM   296  C C   . PRO A 1 38  ? 105.234 177.109 152.870 1.00 30.00 ? 38  PRO A C   1 
ATOM   297  O O   . PRO A 1 38  ? 104.312 177.347 152.112 1.00 30.00 ? 38  PRO A O   1 
ATOM   298  C CB  . PRO A 1 38  ? 105.820 178.760 154.659 1.00 30.00 ? 38  PRO A CB  1 
ATOM   299  C CG  . PRO A 1 38  ? 107.092 178.328 155.338 1.00 30.00 ? 38  PRO A CG  1 
ATOM   300  C CD  . PRO A 1 38  ? 106.772 177.008 156.001 1.00 30.00 ? 38  PRO A CD  1 
ATOM   301  N N   . GLY A 1 39  ? 106.392 176.560 152.495 1.00 30.00 ? 39  GLY A N   1 
ATOM   302  C CA  . GLY A 1 39  ? 106.670 176.202 151.093 1.00 30.00 ? 39  GLY A CA  1 
ATOM   303  C C   . GLY A 1 39  ? 105.650 175.198 150.598 1.00 30.00 ? 39  GLY A C   1 
ATOM   304  O O   . GLY A 1 39  ? 105.196 175.352 149.452 1.00 30.00 ? 39  GLY A O   1 
ATOM   305  N N   . PHE A 1 40  ? 105.275 174.221 151.428 1.00 30.00 ? 40  PHE A N   1 
ATOM   306  C CA  . PHE A 1 40  ? 104.242 173.216 151.081 1.00 30.00 ? 40  PHE A CA  1 
ATOM   307  C C   . PHE A 1 40  ? 102.907 173.919 150.866 1.00 30.00 ? 40  PHE A C   1 
ATOM   308  O O   . PHE A 1 40  ? 102.279 173.647 149.836 1.00 30.00 ? 40  PHE A O   1 
ATOM   309  C CB  . PHE A 1 40  ? 104.027 172.212 152.212 1.00 30.00 ? 40  PHE A CB  1 
ATOM   310  C CG  . PHE A 1 40  ? 102.748 171.424 152.092 1.00 30.00 ? 40  PHE A CG  1 
ATOM   311  C CD1 . PHE A 1 40  ? 102.562 170.528 151.053 1.00 30.00 ? 40  PHE A CD1 1 
ATOM   312  C CD2 . PHE A 1 40  ? 101.714 171.613 152.992 1.00 30.00 ? 40  PHE A CD2 1 
ATOM   313  C CE1 . PHE A 1 40  ? 101.379 169.817 150.935 1.00 30.00 ? 40  PHE A CE1 1 
ATOM   314  C CE2 . PHE A 1 40  ? 100.530 170.903 152.871 1.00 30.00 ? 40  PHE A CE2 1 
ATOM   315  C CZ  . PHE A 1 40  ? 100.365 170.006 151.843 1.00 30.00 ? 40  PHE A CZ  1 
ATOM   316  N N   . GLN A 1 41  ? 102.532 174.829 151.768 1.00 30.00 ? 41  GLN A N   1 
ATOM   317  C CA  . GLN A 1 41  ? 101.217 175.522 151.724 1.00 30.00 ? 41  GLN A CA  1 
ATOM   318  C C   . GLN A 1 41  ? 101.066 176.327 150.434 1.00 30.00 ? 41  GLN A C   1 
ATOM   319  O O   . GLN A 1 41  ? 99.973  176.267 149.838 1.00 30.00 ? 41  GLN A O   1 
ATOM   320  C CB  . GLN A 1 41  ? 101.109 176.467 152.918 1.00 30.00 ? 41  GLN A CB  1 
ATOM   321  C CG  . GLN A 1 41  ? 99.713  177.031 153.122 1.00 30.00 ? 41  GLN A CG  1 
ATOM   322  C CD  . GLN A 1 41  ? 99.657  178.079 154.205 1.00 30.00 ? 41  GLN A CD  1 
ATOM   323  O OE1 . GLN A 1 41  ? 100.663 178.426 154.818 1.00 30.00 ? 41  GLN A OE1 1 
ATOM   324  N NE2 . GLN A 1 41  ? 98.466  178.599 154.443 1.00 30.00 ? 41  GLN A NE2 1 
ATOM   325  N N   . ALA A 1 42  ? 102.105 177.049 150.015 1.00 30.00 ? 42  ALA A N   1 
ATOM   326  C CA  . ALA A 1 42  ? 102.052 177.920 148.819 1.00 30.00 ? 42  ALA A CA  1 
ATOM   327  C C   . ALA A 1 42  ? 101.972 177.060 147.559 1.00 30.00 ? 42  ALA A C   1 
ATOM   328  O O   . ALA A 1 42  ? 101.253 177.466 146.625 1.00 30.00 ? 42  ALA A O   1 
ATOM   329  C CB  . ALA A 1 42  ? 103.272 178.795 148.795 1.00 30.00 ? 42  ALA A CB  1 
ATOM   330  N N   . LEU A 1 43  ? 102.662 175.920 147.531 1.00 30.00 ? 43  LEU A N   1 
ATOM   331  C CA  . LEU A 1 43  ? 102.712 175.011 146.357 1.00 30.00 ? 43  LEU A CA  1 
ATOM   332  C C   . LEU A 1 43  ? 101.543 174.020 146.367 1.00 30.00 ? 43  LEU A C   1 
ATOM   333  O O   . LEU A 1 43  ? 101.446 173.245 145.394 1.00 30.00 ? 43  LEU A O   1 
ATOM   334  C CB  . LEU A 1 43  ? 104.044 174.269 146.440 1.00 30.00 ? 43  LEU A CB  1 
ATOM   335  C CG  . LEU A 1 43  ? 105.308 175.077 146.153 1.00 30.00 ? 43  LEU A CG  1 
ATOM   336  C CD1 . LEU A 1 43  ? 106.545 174.225 146.377 1.00 30.00 ? 43  LEU A CD1 1 
ATOM   337  C CD2 . LEU A 1 43  ? 105.298 175.620 144.736 1.00 30.00 ? 43  LEU A CD2 1 
ATOM   338  N N   . SER A 1 44  ? 100.697 174.028 147.402 1.00 30.00 ? 44  SER A N   1 
ATOM   339  C CA  . SER A 1 44  ? 99.527  173.117 147.529 1.00 30.00 ? 44  SER A CA  1 
ATOM   340  C C   . SER A 1 44  ? 98.233  173.932 147.542 1.00 30.00 ? 44  SER A C   1 
ATOM   341  O O   . SER A 1 44  ? 97.173  173.338 147.800 1.00 30.00 ? 44  SER A O   1 
ATOM   342  C CB  . SER A 1 44  ? 99.640  172.284 148.766 1.00 30.00 ? 44  SER A CB  1 
ATOM   343  O OG  . SER A 1 44  ? 99.774  173.091 149.917 1.00 30.00 ? 44  SER A OG  1 
ATOM   344  N N   . GLU A 1 45  ? 98.306  175.233 147.268 1.00 30.00 ? 45  GLU A N   1 
ATOM   345  C CA  . GLU A 1 45  ? 97.135  176.145 147.308 1.00 30.00 ? 45  GLU A CA  1 
ATOM   346  C C   . GLU A 1 45  ? 96.193  175.799 146.154 1.00 30.00 ? 45  GLU A C   1 
ATOM   347  O O   . GLU A 1 45  ? 96.700  175.462 145.067 1.00 30.00 ? 45  GLU A O   1 
ATOM   348  C CB  . GLU A 1 45  ? 97.602  177.596 147.217 1.00 30.00 ? 45  GLU A CB  1 
ATOM   349  C CG  . GLU A 1 45  ? 96.479  178.617 147.261 1.00 30.00 ? 45  GLU A CG  1 
ATOM   350  C CD  . GLU A 1 45  ? 95.739  178.728 148.583 1.00 30.00 ? 45  GLU A CD  1 
ATOM   351  O OE1 . GLU A 1 45  ? 96.114  178.025 149.537 1.00 30.00 ? 45  GLU A OE1 1 
ATOM   352  O OE2 . GLU A 1 45  ? 94.776  179.514 148.647 1.00 30.00 ? 45  GLU A OE2 1 
ATOM   353  N N   . GLY A 1 46  ? 94.889  175.701 146.425 1.00 30.00 ? 46  GLY A N   1 
ATOM   354  C CA  . GLY A 1 46  ? 93.894  175.326 145.403 1.00 30.00 ? 46  GLY A CA  1 
ATOM   355  C C   . GLY A 1 46  ? 94.101  173.910 144.891 1.00 30.00 ? 46  GLY A C   1 
ATOM   356  O O   . GLY A 1 46  ? 93.725  173.664 143.737 1.00 30.00 ? 46  GLY A O   1 
ATOM   357  N N   . CYS A 1 47  ? 94.647  172.995 145.702 1.00 30.00 ? 47  CYS A N   1 
ATOM   358  C CA  . CYS A 1 47  ? 94.856  171.572 145.310 1.00 30.00 ? 47  CYS A CA  1 
ATOM   359  C C   . CYS A 1 47  ? 93.761  170.677 145.877 1.00 30.00 ? 47  CYS A C   1 
ATOM   360  O O   . CYS A 1 47  ? 93.298  170.959 146.999 1.00 30.00 ? 47  CYS A O   1 
ATOM   361  C CB  . CYS A 1 47  ? 96.141  170.953 145.847 1.00 30.00 ? 47  CYS A CB  1 
ATOM   362  S SG  . CYS A 1 47  ? 97.629  171.363 144.903 1.00 30.00 ? 47  CYS A SG  1 
ATOM   363  N N   . THR A 1 48  ? 93.381  169.632 145.145 1.00 30.00 ? 48  THR A N   1 
ATOM   364  C CA  . THR A 1 48  ? 92.431  168.616 145.654 1.00 30.00 ? 48  THR A CA  1 
ATOM   365  C C   . THR A 1 48  ? 93.267  167.688 146.535 1.00 30.00 ? 48  THR A C   1 
ATOM   366  O O   . THR A 1 48  ? 94.505  167.788 146.463 1.00 30.00 ? 48  THR A O   1 
ATOM   367  C CB  . THR A 1 48  ? 91.746  167.865 144.508 1.00 30.00 ? 48  THR A CB  1 
ATOM   368  O OG1 . THR A 1 48  ? 92.763  167.148 143.813 1.00 30.00 ? 48  THR A OG1 1 
ATOM   369  C CG2 . THR A 1 48  ? 91.005  168.775 143.554 1.00 30.00 ? 48  THR A CG2 1 
ATOM   370  N N   . PRO A 1 49  ? 92.681  166.828 147.389 1.00 30.00 ? 49  PRO A N   1 
ATOM   371  C CA  . PRO A 1 49  ? 93.480  165.871 148.153 1.00 30.00 ? 49  PRO A CA  1 
ATOM   372  C C   . PRO A 1 49  ? 94.318  164.984 147.227 1.00 30.00 ? 49  PRO A C   1 
ATOM   373  O O   . PRO A 1 49  ? 95.427  164.684 147.598 1.00 30.00 ? 49  PRO A O   1 
ATOM   374  C CB  . PRO A 1 49  ? 92.421  165.030 148.866 1.00 30.00 ? 49  PRO A CB  1 
ATOM   375  C CG  . PRO A 1 49  ? 91.238  165.961 148.999 1.00 30.00 ? 49  PRO A CG  1 
ATOM   376  C CD  . PRO A 1 49  ? 91.267  166.813 147.751 1.00 30.00 ? 49  PRO A CD  1 
ATOM   377  N N   . TYR A 1 50  ? 93.767  164.556 146.090 1.00 30.00 ? 50  TYR A N   1 
ATOM   378  C CA  . TYR A 1 50  ? 94.477  163.736 145.074 1.00 30.00 ? 50  TYR A CA  1 
ATOM   379  C C   . TYR A 1 50  ? 95.849  164.327 144.741 1.00 30.00 ? 50  TYR A C   1 
ATOM   380  O O   . TYR A 1 50  ? 96.815  163.547 144.662 1.00 30.00 ? 50  TYR A O   1 
ATOM   381  C CB  . TYR A 1 50  ? 93.627  163.686 143.806 1.00 30.00 ? 50  TYR A CB  1 
ATOM   382  C CG  . TYR A 1 50  ? 94.268  163.010 142.626 1.00 30.00 ? 50  TYR A CG  1 
ATOM   383  C CD1 . TYR A 1 50  ? 94.564  161.659 142.643 1.00 30.00 ? 50  TYR A CD1 1 
ATOM   384  C CD2 . TYR A 1 50  ? 94.626  163.741 141.510 1.00 30.00 ? 50  TYR A CD2 1 
ATOM   385  C CE1 . TYR A 1 50  ? 95.162  161.042 141.559 1.00 30.00 ? 50  TYR A CE1 1 
ATOM   386  C CE2 . TYR A 1 50  ? 95.233  163.143 140.421 1.00 30.00 ? 50  TYR A CE2 1 
ATOM   387  C CZ  . TYR A 1 50  ? 95.501  161.788 140.445 1.00 30.00 ? 50  TYR A CZ  1 
ATOM   388  O OH  . TYR A 1 50  ? 96.102  161.192 139.366 1.00 30.00 ? 50  TYR A OH  1 
ATOM   389  N N   . ASP A 1 51  ? 95.933  165.639 144.500 1.00 30.00 ? 51  ASP A N   1 
ATOM   390  C CA  . ASP A 1 51  ? 97.200  166.316 144.115 1.00 30.00 ? 51  ASP A CA  1 
ATOM   391  C C   . ASP A 1 51  ? 98.173  166.320 145.287 1.00 30.00 ? 51  ASP A C   1 
ATOM   392  O O   . ASP A 1 51  ? 99.384  166.157 145.051 1.00 30.00 ? 51  ASP A O   1 
ATOM   393  C CB  . ASP A 1 51  ? 96.960  167.771 143.731 1.00 30.00 ? 51  ASP A CB  1 
ATOM   394  C CG  . ASP A 1 51  ? 96.031  167.929 142.551 1.00 30.00 ? 51  ASP A CG  1 
ATOM   395  O OD1 . ASP A 1 51  ? 96.374  167.447 141.460 1.00 30.00 ? 51  ASP A OD1 1 
ATOM   396  O OD2 . ASP A 1 51  ? 94.974  168.509 142.750 1.00 30.00 ? 51  ASP A OD2 1 
ATOM   397  N N   . ILE A 1 52  ? 97.665  166.538 146.496 1.00 30.00 ? 52  ILE A N   1 
ATOM   398  C CA  . ILE A 1 52  ? 98.512  166.614 147.717 1.00 30.00 ? 52  ILE A CA  1 
ATOM   399  C C   . ILE A 1 52  ? 99.190  165.253 147.911 1.00 30.00 ? 52  ILE A C   1 
ATOM   400  O O   . ILE A 1 52  ? 100.374 165.247 148.288 1.00 30.00 ? 52  ILE A O   1 
ATOM   401  C CB  . ILE A 1 52  ? 97.650  167.055 148.915 1.00 30.00 ? 52  ILE A CB  1 
ATOM   402  C CG1 . ILE A 1 52  ? 97.060  168.454 148.714 1.00 30.00 ? 52  ILE A CG1 1 
ATOM   403  C CG2 . ILE A 1 52  ? 98.449  166.970 150.198 1.00 30.00 ? 52  ILE A CG2 1 
ATOM   404  C CD1 . ILE A 1 52  ? 95.816  168.716 149.528 1.00 30.00 ? 52  ILE A CD1 1 
ATOM   405  N N   . ASN A 1 53  ? 98.483  164.156 147.602 1.00 30.00 ? 53  ASN A N   1 
ATOM   406  C CA  . ASN A 1 53  ? 99.043  162.780 147.690 1.00 30.00 ? 53  ASN A CA  1 
ATOM   407  C C   . ASN A 1 53  ? 100.235 162.668 146.738 1.00 30.00 ? 53  ASN A C   1 
ATOM   408  O O   . ASN A 1 53  ? 101.251 162.111 147.160 1.00 30.00 ? 53  ASN A O   1 
ATOM   409  C CB  . ASN A 1 53  ? 98.013  161.693 147.364 1.00 30.00 ? 53  ASN A CB  1 
ATOM   410  C CG  . ASN A 1 53  ? 96.917  161.591 148.399 1.00 30.00 ? 53  ASN A CG  1 
ATOM   411  O OD1 . ASN A 1 53  ? 97.203  161.412 149.573 1.00 30.00 ? 53  ASN A OD1 1 
ATOM   412  N ND2 . ASN A 1 53  ? 95.669  161.714 147.984 1.00 30.00 ? 53  ASN A ND2 1 
ATOM   413  N N   . GLN A 1 54  ? 100.115 163.177 145.509 1.00 30.00 ? 54  GLN A N   1 
ATOM   414  C CA  . GLN A 1 54  ? 101.200 163.107 144.494 1.00 30.00 ? 54  GLN A CA  1 
ATOM   415  C C   . GLN A 1 54  ? 102.424 163.877 144.978 1.00 30.00 ? 54  GLN A C   1 
ATOM   416  O O   . GLN A 1 54  ? 103.545 163.377 144.791 1.00 30.00 ? 54  GLN A O   1 
ATOM   417  C CB  . GLN A 1 54  ? 100.769 163.747 143.182 1.00 30.00 ? 54  GLN A CB  1 
ATOM   418  C CG  . GLN A 1 54  ? 99.671  162.984 142.468 1.00 30.00 ? 54  GLN A CG  1 
ATOM   419  C CD  . GLN A 1 54  ? 99.222  163.699 141.222 1.00 30.00 ? 54  GLN A CD  1 
ATOM   420  O OE1 . GLN A 1 54  ? 98.051  164.038 141.079 1.00 30.00 ? 54  GLN A OE1 1 
ATOM   421  N NE2 . GLN A 1 54  ? 100.149 163.920 140.304 1.00 30.00 ? 54  GLN A NE2 1 
ATOM   422  N N   . MET A 1 55  ? 102.213 165.056 145.558 1.00 30.00 ? 55  MET A N   1 
ATOM   423  C CA  . MET A 1 55  ? 103.326 165.887 146.073 1.00 30.00 ? 55  MET A CA  1 
ATOM   424  C C   . MET A 1 55  ? 104.064 165.033 147.104 1.00 30.00 ? 55  MET A C   1 
ATOM   425  O O   . MET A 1 55  ? 105.294 164.906 146.983 1.00 30.00 ? 55  MET A O   1 
ATOM   426  C CB  . MET A 1 55  ? 102.775 167.150 146.733 1.00 30.00 ? 55  MET A CB  1 
ATOM   427  C CG  . MET A 1 55  ? 102.438 168.258 145.773 1.00 30.00 ? 55  MET A CG  1 
ATOM   428  S SD  . MET A 1 55  ? 101.660 169.634 146.650 1.00 30.00 ? 55  MET A SD  1 
ATOM   429  C CE  . MET A 1 55  ? 103.100 170.396 147.396 1.00 30.00 ? 55  MET A CE  1 
ATOM   430  N N   . LEU A 1 56  ? 103.328 164.384 148.009 1.00 30.00 ? 56  LEU A N   1 
ATOM   431  C CA  . LEU A 1 56  ? 103.911 163.493 149.046 1.00 30.00 ? 56  LEU A CA  1 
ATOM   432  C C   . LEU A 1 56  ? 104.582 162.300 148.369 1.00 30.00 ? 56  LEU A C   1 
ATOM   433  O O   . LEU A 1 56  ? 105.518 161.737 148.972 1.00 30.00 ? 56  LEU A O   1 
ATOM   434  C CB  . LEU A 1 56  ? 102.772 163.025 149.955 1.00 30.00 ? 56  LEU A CB  1 
ATOM   435  C CG  . LEU A 1 56  ? 102.144 164.092 150.852 1.00 30.00 ? 56  LEU A CG  1 
ATOM   436  C CD1 . LEU A 1 56  ? 101.028 163.498 151.690 1.00 30.00 ? 56  LEU A CD1 1 
ATOM   437  C CD2 . LEU A 1 56  ? 103.186 164.735 151.751 1.00 30.00 ? 56  LEU A CD2 1 
ATOM   438  N N   A ASN A 1 57  ? 103.959 161.782 147.305 0.60 30.00 ? 57  ASN A N   1 
ATOM   439  N N   B ASN A 1 57  ? 103.947 161.759 147.326 0.40 30.00 ? 57  ASN A N   1 
ATOM   440  C CA  A ASN A 1 57  ? 104.516 160.596 146.601 0.60 30.00 ? 57  ASN A CA  1 
ATOM   441  C CA  B ASN A 1 57  ? 104.511 160.595 146.592 0.40 30.00 ? 57  ASN A CA  1 
ATOM   442  C C   A ASN A 1 57  ? 105.817 160.976 145.889 0.60 30.00 ? 57  ASN A C   1 
ATOM   443  C C   B ASN A 1 57  ? 105.852 160.994 145.971 0.40 30.00 ? 57  ASN A C   1 
ATOM   444  O O   A ASN A 1 57  ? 106.752 160.153 145.936 0.60 30.00 ? 57  ASN A O   1 
ATOM   445  O O   B ASN A 1 57  ? 106.808 160.229 146.138 0.40 30.00 ? 57  ASN A O   1 
ATOM   446  C CB  A ASN A 1 57  ? 103.501 159.964 145.643 0.60 30.00 ? 57  ASN A CB  1 
ATOM   447  C CB  B ASN A 1 57  ? 103.520 160.074 145.546 0.40 30.00 ? 57  ASN A CB  1 
ATOM   448  C CG  A ASN A 1 57  ? 102.377 159.258 146.372 0.60 30.00 ? 57  ASN A CG  1 
ATOM   449  C CG  B ASN A 1 57  ? 103.924 158.750 144.933 0.40 30.00 ? 57  ASN A CG  1 
ATOM   450  O OD1 A ASN A 1 57  ? 102.624 158.403 147.218 0.60 30.00 ? 57  ASN A OD1 1 
ATOM   451  O OD1 B ASN A 1 57  ? 104.939 158.164 145.302 0.40 30.00 ? 57  ASN A OD1 1 
ATOM   452  N ND2 A ASN A 1 57  ? 101.142 159.631 146.086 0.60 30.00 ? 57  ASN A ND2 1 
ATOM   453  N ND2 B ASN A 1 57  ? 103.121 158.258 144.006 0.40 30.00 ? 57  ASN A ND2 1 
ATOM   454  N N   . CYS A 1 58  ? 105.980 162.260 145.563 1.00 30.00 ? 58  CYS A N   1 
ATOM   455  C CA  . CYS A 1 58  ? 107.236 162.733 144.917 1.00 30.00 ? 58  CYS A CA  1 
ATOM   456  C C   . CYS A 1 58  ? 108.360 162.853 145.958 1.00 30.00 ? 58  CYS A C   1 
ATOM   457  O O   . CYS A 1 58  ? 109.528 162.928 145.528 1.00 30.00 ? 58  CYS A O   1 
ATOM   458  C CB  . CYS A 1 58  ? 107.014 164.059 144.201 1.00 30.00 ? 58  CYS A CB  1 
ATOM   459  S SG  . CYS A 1 58  ? 106.224 163.873 142.584 1.00 30.00 ? 58  CYS A SG  1 
ATOM   460  N N   . VAL A 1 59  ? 108.039 162.877 147.258 1.00 30.00 ? 59  VAL A N   1 
ATOM   461  C CA  . VAL A 1 59  ? 109.047 163.023 148.357 1.00 30.00 ? 59  VAL A CA  1 
ATOM   462  C C   . VAL A 1 59  ? 108.939 161.835 149.323 1.00 30.00 ? 59  VAL A C   1 
ATOM   463  O O   . VAL A 1 59  ? 109.277 162.021 150.510 1.00 30.00 ? 59  VAL A O   1 
ATOM   464  C CB  . VAL A 1 59  ? 108.877 164.374 149.083 1.00 30.00 ? 59  VAL A CB  1 
ATOM   465  C CG1 . VAL A 1 59  ? 109.104 165.541 148.136 1.00 30.00 ? 59  VAL A CG1 1 
ATOM   466  C CG2 . VAL A 1 59  ? 107.524 164.503 149.768 1.00 30.00 ? 59  VAL A CG2 1 
ATOM   467  N N   . GLY A 1 60  ? 108.518 160.656 148.853 1.00 30.00 ? 60  GLY A N   1 
ATOM   468  C CA  . GLY A 1 60  ? 108.353 159.445 149.683 1.00 30.00 ? 60  GLY A CA  1 
ATOM   469  C C   . GLY A 1 60  ? 109.679 158.911 150.196 1.00 30.00 ? 60  GLY A C   1 
ATOM   470  O O   . GLY A 1 60  ? 109.698 158.416 151.339 1.00 30.00 ? 60  GLY A O   1 
ATOM   471  N N   . ASP A 1 61  ? 110.752 159.009 149.405 1.00 30.00 ? 61  ASP A N   1 
ATOM   472  C CA  . ASP A 1 61  ? 112.091 158.474 149.778 1.00 30.00 ? 61  ASP A CA  1 
ATOM   473  C C   . ASP A 1 61  ? 112.466 158.944 151.183 1.00 30.00 ? 61  ASP A C   1 
ATOM   474  O O   . ASP A 1 61  ? 113.162 158.175 151.870 1.00 30.00 ? 61  ASP A O   1 
ATOM   475  C CB  . ASP A 1 61  ? 113.167 158.896 148.781 1.00 30.00 ? 61  ASP A CB  1 
ATOM   476  C CG  . ASP A 1 61  ? 113.153 158.134 147.467 1.00 30.00 ? 61  ASP A CG  1 
ATOM   477  O OD1 . ASP A 1 61  ? 112.307 157.234 147.316 1.00 30.00 ? 61  ASP A OD1 1 
ATOM   478  O OD2 . ASP A 1 61  ? 113.995 158.449 146.604 1.00 30.00 ? 61  ASP A OD2 1 
ATOM   479  N N   . HIS A 1 62  ? 112.067 160.154 151.586 1.00 30.00 ? 62  HIS A N   1 
ATOM   480  C CA  . HIS A 1 62  ? 112.288 160.644 152.975 1.00 30.00 ? 62  HIS A CA  1 
ATOM   481  C C   . HIS A 1 62  ? 111.298 159.845 153.823 1.00 30.00 ? 62  HIS A C   1 
ATOM   482  O O   . HIS A 1 62  ? 110.316 160.440 154.315 1.00 30.00 ? 62  HIS A O   1 
ATOM   483  C CB  . HIS A 1 62  ? 112.131 162.166 153.016 1.00 30.00 ? 62  HIS A CB  1 
ATOM   484  C CG  . HIS A 1 62  ? 113.050 162.907 152.115 1.00 30.00 ? 62  HIS A CG  1 
ATOM   485  N ND1 . HIS A 1 62  ? 112.674 163.310 150.855 1.00 30.00 ? 62  HIS A ND1 1 
ATOM   486  C CD2 . HIS A 1 62  ? 114.314 163.292 152.264 1.00 30.00 ? 62  HIS A CD2 1 
ATOM   487  C CE1 . HIS A 1 62  ? 113.688 163.930 150.280 1.00 30.00 ? 62  HIS A CE1 1 
ATOM   488  N NE2 . HIS A 1 62  ? 114.692 163.935 151.121 1.00 30.00 ? 62  HIS A NE2 1 
ATOM   489  N N   . GLN A 1 63  ? 111.555 158.551 154.022 1.00 30.00 ? 63  GLN A N   1 
ATOM   490  C CA  . GLN A 1 63  ? 110.596 157.618 154.675 1.00 30.00 ? 63  GLN A CA  1 
ATOM   491  C C   . GLN A 1 63  ? 110.314 157.992 156.135 1.00 30.00 ? 63  GLN A C   1 
ATOM   492  O O   . GLN A 1 63  ? 109.148 157.882 156.534 1.00 30.00 ? 63  GLN A O   1 
ATOM   493  C CB  . GLN A 1 63  ? 111.109 156.183 154.508 1.00 30.00 ? 63  GLN A CB  1 
ATOM   494  C CG  . GLN A 1 63  ? 112.168 155.718 155.504 1.00 30.00 ? 63  GLN A CG  1 
ATOM   495  C CD  . GLN A 1 63  ? 113.586 156.100 155.154 1.00 30.00 ? 63  GLN A CD  1 
ATOM   496  O OE1 . GLN A 1 63  ? 113.848 156.833 154.206 1.00 30.00 ? 63  GLN A OE1 1 
ATOM   497  N NE2 . GLN A 1 63  ? 114.525 155.602 155.939 1.00 30.00 ? 63  GLN A NE2 1 
ATOM   498  N N   . ALA A 1 64  ? 111.314 158.386 156.916 1.00 30.00 ? 64  ALA A N   1 
ATOM   499  C CA  . ALA A 1 64  ? 111.125 158.684 158.351 1.00 30.00 ? 64  ALA A CA  1 
ATOM   500  C C   . ALA A 1 64  ? 110.100 159.808 158.503 1.00 30.00 ? 64  ALA A C   1 
ATOM   501  O O   . ALA A 1 64  ? 109.121 159.616 159.255 1.00 30.00 ? 64  ALA A O   1 
ATOM   502  C CB  . ALA A 1 64  ? 112.446 159.056 158.943 1.00 30.00 ? 64  ALA A CB  1 
ATOM   503  N N   . ALA A 1 65  ? 110.299 160.929 157.810 1.00 30.00 ? 65  ALA A N   1 
ATOM   504  C CA  . ALA A 1 65  ? 109.390 162.094 157.861 1.00 30.00 ? 65  ALA A CA  1 
ATOM   505  C C   . ALA A 1 65  ? 108.012 161.710 157.322 1.00 30.00 ? 65  ALA A C   1 
ATOM   506  O O   . ALA A 1 65  ? 107.010 162.173 157.895 1.00 30.00 ? 65  ALA A O   1 
ATOM   507  C CB  . ALA A 1 65  ? 109.985 163.202 157.046 1.00 30.00 ? 65  ALA A CB  1 
ATOM   508  N N   . MET A 1 66  ? 107.964 160.914 156.253 1.00 30.00 ? 66  MET A N   1 
ATOM   509  C CA  . MET A 1 66  ? 106.686 160.497 155.620 1.00 30.00 ? 66  MET A CA  1 
ATOM   510  C C   . MET A 1 66  ? 105.898 159.643 156.611 1.00 30.00 ? 66  MET A C   1 
ATOM   511  O O   . MET A 1 66  ? 104.668 159.758 156.624 1.00 30.00 ? 66  MET A O   1 
ATOM   512  C CB  . MET A 1 66  ? 106.912 159.681 154.346 1.00 30.00 ? 66  MET A CB  1 
ATOM   513  C CG  . MET A 1 66  ? 107.199 160.500 153.099 1.00 30.00 ? 66  MET A CG  1 
ATOM   514  S SD  . MET A 1 66  ? 106.211 162.003 152.919 1.00 30.00 ? 66  MET A SD  1 
ATOM   515  C CE  . MET A 1 66  ? 107.419 163.220 153.438 1.00 30.00 ? 66  MET A CE  1 
ATOM   516  N N   . GLN A 1 67  ? 106.584 158.834 157.413 1.00 30.00 ? 67  GLN A N   1 
ATOM   517  C CA  . GLN A 1 67  ? 105.921 157.985 158.431 1.00 30.00 ? 67  GLN A CA  1 
ATOM   518  C C   . GLN A 1 67  ? 105.288 158.892 159.487 1.00 30.00 ? 67  GLN A C   1 
ATOM   519  O O   . GLN A 1 67  ? 104.217 158.526 159.991 1.00 30.00 ? 67  GLN A O   1 
ATOM   520  C CB  . GLN A 1 67  ? 106.930 157.032 159.062 1.00 30.00 ? 67  GLN A CB  1 
ATOM   521  C CG  . GLN A 1 67  ? 106.290 156.053 160.032 1.00 30.00 ? 67  GLN A CG  1 
ATOM   522  C CD  . GLN A 1 67  ? 105.241 155.208 159.355 1.00 30.00 ? 67  GLN A CD  1 
ATOM   523  O OE1 . GLN A 1 67  ? 105.548 154.334 158.549 1.00 30.00 ? 67  GLN A OE1 1 
ATOM   524  N NE2 . GLN A 1 67  ? 103.985 155.471 159.674 1.00 30.00 ? 67  GLN A NE2 1 
ATOM   525  N N   . ILE A 1 68  ? 105.930 160.016 159.817 1.00 30.00 ? 68  ILE A N   1 
ATOM   526  C CA  . ILE A 1 68  ? 105.417 160.984 160.832 1.00 30.00 ? 68  ILE A CA  1 
ATOM   527  C C   . ILE A 1 68  ? 104.220 161.740 160.250 1.00 30.00 ? 68  ILE A C   1 
ATOM   528  O O   . ILE A 1 68  ? 103.250 161.940 160.992 1.00 30.00 ? 68  ILE A O   1 
ATOM   529  C CB  . ILE A 1 68  ? 106.541 161.938 161.274 1.00 30.00 ? 68  ILE A CB  1 
ATOM   530  C CG1 . ILE A 1 68  ? 107.528 161.224 162.195 1.00 30.00 ? 68  ILE A CG1 1 
ATOM   531  C CG2 . ILE A 1 68  ? 105.984 163.197 161.915 1.00 30.00 ? 68  ILE A CG2 1 
ATOM   532  C CD1 . ILE A 1 68  ? 108.919 161.764 162.115 1.00 30.00 ? 68  ILE A CD1 1 
ATOM   533  N N   . ILE A 1 69  ? 104.291 162.157 158.985 1.00 30.00 ? 69  ILE A N   1 
ATOM   534  C CA  . ILE A 1 69  ? 103.183 162.889 158.303 1.00 30.00 ? 69  ILE A CA  1 
ATOM   535  C C   . ILE A 1 69  ? 102.007 161.925 158.156 1.00 30.00 ? 69  ILE A C   1 
ATOM   536  O O   . ILE A 1 69  ? 100.865 162.399 158.219 1.00 30.00 ? 69  ILE A O   1 
ATOM   537  C CB  . ILE A 1 69  ? 103.658 163.431 156.941 1.00 30.00 ? 69  ILE A CB  1 
ATOM   538  C CG1 . ILE A 1 69  ? 104.670 164.565 157.123 1.00 30.00 ? 69  ILE A CG1 1 
ATOM   539  C CG2 . ILE A 1 69  ? 102.483 163.857 156.076 1.00 30.00 ? 69  ILE A CG2 1 
ATOM   540  C CD1 . ILE A 1 69  ? 105.679 164.662 156.014 1.00 30.00 ? 69  ILE A CD1 1 
ATOM   541  N N   . ARG A 1 70  ? 102.279 160.631 157.998 1.00 30.00 ? 70  ARG A N   1 
ATOM   542  C CA  . ARG A 1 70  ? 101.244 159.577 157.786 1.00 30.00 ? 70  ARG A CA  1 
ATOM   543  C C   . ARG A 1 70  ? 100.550 159.196 159.098 1.00 30.00 ? 70  ARG A C   1 
ATOM   544  O O   . ARG A 1 70  ? 99.360  158.906 159.047 1.00 30.00 ? 70  ARG A O   1 
ATOM   545  C CB  . ARG A 1 70  ? 101.888 158.334 157.171 1.00 30.00 ? 70  ARG A CB  1 
ATOM   546  C CG  . ARG A 1 70  ? 100.981 157.118 157.056 1.00 30.00 ? 70  ARG A CG  1 
ATOM   547  C CD  . ARG A 1 70  ? 99.751  157.332 156.197 1.00 30.00 ? 70  ARG A CD  1 
ATOM   548  N NE  . ARG A 1 70  ? 100.072 157.876 154.884 1.00 30.00 ? 70  ARG A NE  1 
ATOM   549  C CZ  . ARG A 1 70  ? 99.414  158.859 154.280 1.00 30.00 ? 70  ARG A CZ  1 
ATOM   550  N NH1 . ARG A 1 70  ? 98.446  159.507 154.902 1.00 30.00 ? 70  ARG A NH1 1 
ATOM   551  N NH2 . ARG A 1 70  ? 99.720  159.189 153.038 1.00 30.00 ? 70  ARG A NH2 1 
ATOM   552  N N   . GLU A 1 71  ? 101.244 159.243 160.228 1.00 30.00 ? 71  GLU A N   1 
ATOM   553  C CA  . GLU A 1 71  ? 100.629 158.913 161.537 1.00 30.00 ? 71  GLU A CA  1 
ATOM   554  C C   . GLU A 1 71  ? 99.766  160.098 161.980 1.00 30.00 ? 71  GLU A C   1 
ATOM   555  O O   . GLU A 1 71  ? 98.730  159.850 162.622 1.00 30.00 ? 71  GLU A O   1 
ATOM   556  C CB  . GLU A 1 71  ? 101.735 158.575 162.525 1.00 30.00 ? 71  GLU A CB  1 
ATOM   557  C CG  . GLU A 1 71  ? 102.320 157.196 162.309 1.00 30.00 ? 71  GLU A CG  1 
ATOM   558  C CD  . GLU A 1 71  ? 103.704 156.973 162.893 1.00 30.00 ? 71  GLU A CD  1 
ATOM   559  O OE1 . GLU A 1 71  ? 104.251 157.908 163.509 1.00 30.00 ? 71  GLU A OE1 1 
ATOM   560  O OE2 . GLU A 1 71  ? 104.237 155.857 162.724 1.00 30.00 ? 71  GLU A OE2 1 
ATOM   561  N N   . ILE A 1 72  ? 100.158 161.327 161.634 1.00 30.00 ? 72  ILE A N   1 
ATOM   562  C CA  . ILE A 1 72  ? 99.385  162.559 161.978 1.00 30.00 ? 72  ILE A CA  1 
ATOM   563  C C   . ILE A 1 72  ? 98.106  162.600 161.136 1.00 30.00 ? 72  ILE A C   1 
ATOM   564  O O   . ILE A 1 72  ? 97.076  163.023 161.680 1.00 30.00 ? 72  ILE A O   1 
ATOM   565  C CB  . ILE A 1 72  ? 100.253 163.815 161.763 1.00 30.00 ? 72  ILE A CB  1 
ATOM   566  C CG1 . ILE A 1 72  ? 101.411 163.890 162.761 1.00 30.00 ? 72  ILE A CG1 1 
ATOM   567  C CG2 . ILE A 1 72  ? 99.406  165.077 161.781 1.00 30.00 ? 72  ILE A CG2 1 
ATOM   568  C CD1 . ILE A 1 72  ? 101.006 164.265 164.158 1.00 30.00 ? 72  ILE A CD1 1 
ATOM   569  N N   . ILE A 1 73  ? 98.164  162.187 159.866 1.00 30.00 ? 73  ILE A N   1 
ATOM   570  C CA  . ILE A 1 73  ? 96.997  162.212 158.933 1.00 30.00 ? 73  ILE A CA  1 
ATOM   571  C C   . ILE A 1 73  ? 95.920  161.250 159.436 1.00 30.00 ? 73  ILE A C   1 
ATOM   572  O O   . ILE A 1 73  ? 94.751  161.647 159.407 1.00 30.00 ? 73  ILE A O   1 
ATOM   573  C CB  . ILE A 1 73  ? 97.461  161.825 157.515 1.00 30.00 ? 73  ILE A CB  1 
ATOM   574  C CG1 . ILE A 1 73  ? 98.177  162.984 156.820 1.00 30.00 ? 73  ILE A CG1 1 
ATOM   575  C CG2 . ILE A 1 73  ? 96.306  161.310 156.672 1.00 30.00 ? 73  ILE A CG2 1 
ATOM   576  C CD1 . ILE A 1 73  ? 99.041  162.558 155.662 1.00 30.00 ? 73  ILE A CD1 1 
ATOM   577  N N   . ASN A 1 74  ? 96.287  160.029 159.819 1.00 30.00 ? 74  ASN A N   1 
ATOM   578  C CA  . ASN A 1 74  ? 95.371  158.955 160.284 1.00 30.00 ? 74  ASN A CA  1 
ATOM   579  C C   . ASN A 1 74  ? 94.619  159.386 161.544 1.00 30.00 ? 74  ASN A C   1 
ATOM   580  O O   . ASN A 1 74  ? 93.474  158.937 161.701 1.00 30.00 ? 74  ASN A O   1 
ATOM   581  C CB  . ASN A 1 74  ? 96.163  157.686 160.592 1.00 30.00 ? 74  ASN A CB  1 
ATOM   582  C CG  . ASN A 1 74  ? 96.711  157.002 159.358 1.00 30.00 ? 74  ASN A CG  1 
ATOM   583  O OD1 . ASN A 1 74  ? 96.423  157.404 158.234 1.00 30.00 ? 74  ASN A OD1 1 
ATOM   584  N ND2 . ASN A 1 74  ? 97.502  155.963 159.560 1.00 30.00 ? 74  ASN A ND2 1 
ATOM   585  N N   . ASP A 1 75  ? 95.271  160.177 162.400 1.00 30.00 ? 75  ASP A N   1 
ATOM   586  C CA  . ASP A 1 75  ? 94.704  160.624 163.694 1.00 30.00 ? 75  ASP A CA  1 
ATOM   587  C C   . ASP A 1 75  ? 93.760  161.798 163.464 1.00 30.00 ? 75  ASP A C   1 
ATOM   588  O O   . ASP A 1 75  ? 92.757  161.879 164.182 1.00 30.00 ? 75  ASP A O   1 
ATOM   589  C CB  . ASP A 1 75  ? 95.828  161.069 164.621 1.00 30.00 ? 75  ASP A CB  1 
ATOM   590  C CG  . ASP A 1 75  ? 96.853  159.994 164.925 1.00 30.00 ? 75  ASP A CG  1 
ATOM   591  O OD1 . ASP A 1 75  ? 96.662  158.853 164.463 1.00 30.00 ? 75  ASP A OD1 1 
ATOM   592  O OD2 . ASP A 1 75  ? 97.845  160.312 165.608 1.00 30.00 ? 75  ASP A OD2 1 
ATOM   593  N N   . GLU A 1 76  ? 94.094  162.683 162.527 1.00 30.00 ? 76  GLU A N   1 
ATOM   594  C CA  . GLU A 1 76  ? 93.258  163.865 162.200 1.00 30.00 ? 76  GLU A CA  1 
ATOM   595  C C   . GLU A 1 76  ? 92.046  163.379 161.400 1.00 30.00 ? 76  GLU A C   1 
ATOM   596  O O   . GLU A 1 76  ? 91.044  164.118 161.361 1.00 30.00 ? 76  GLU A O   1 
ATOM   597  C CB  . GLU A 1 76  ? 94.113  164.878 161.443 1.00 30.00 ? 76  GLU A CB  1 
ATOM   598  C CG  . GLU A 1 76  ? 95.203  165.522 162.274 1.00 30.00 ? 76  GLU A CG  1 
ATOM   599  C CD  . GLU A 1 76  ? 94.727  166.613 163.215 1.00 30.00 ? 76  GLU A CD  1 
ATOM   600  O OE1 . GLU A 1 76  ? 94.061  167.551 162.742 1.00 30.00 ? 76  GLU A OE1 1 
ATOM   601  O OE2 . GLU A 1 76  ? 95.052  166.538 164.412 1.00 30.00 ? 76  GLU A OE2 1 
ATOM   602  N N   . ALA A 1 77  ? 92.122  162.186 160.800 1.00 30.00 ? 77  ALA A N   1 
ATOM   603  C CA  . ALA A 1 77  ? 91.018  161.571 160.024 1.00 30.00 ? 77  ALA A CA  1 
ATOM   604  C C   . ALA A 1 77  ? 90.101  160.803 160.970 1.00 30.00 ? 77  ALA A C   1 
ATOM   605  O O   . ALA A 1 77  ? 88.899  160.759 160.685 1.00 30.00 ? 77  ALA A O   1 
ATOM   606  C CB  . ALA A 1 77  ? 91.598  160.632 159.014 1.00 30.00 ? 77  ALA A CB  1 
ATOM   607  N N   . ALA A 1 78  ? 90.658  160.153 161.990 1.00 30.00 ? 78  ALA A N   1 
ATOM   608  C CA  . ALA A 1 78  ? 89.910  159.406 163.025 1.00 30.00 ? 78  ALA A CA  1 
ATOM   609  C C   . ALA A 1 78  ? 89.068  160.406 163.811 1.00 30.00 ? 78  ALA A C   1 
ATOM   610  O O   . ALA A 1 78  ? 87.905  160.085 164.127 1.00 30.00 ? 78  ALA A O   1 
ATOM   611  C CB  . ALA A 1 78  ? 90.876  158.690 163.925 1.00 30.00 ? 78  ALA A CB  1 
ATOM   612  N N   . ASP A 1 79  ? 89.635  161.577 164.099 1.00 30.00 ? 79  ASP A N   1 
ATOM   613  C CA  . ASP A 1 79  ? 88.932  162.646 164.848 1.00 30.00 ? 79  ASP A CA  1 
ATOM   614  C C   . ASP A 1 79  ? 87.808  163.181 163.964 1.00 30.00 ? 79  ASP A C   1 
ATOM   615  O O   . ASP A 1 79  ? 86.790  163.607 164.525 1.00 30.00 ? 79  ASP A O   1 
ATOM   616  C CB  . ASP A 1 79  ? 89.913  163.741 165.261 1.00 30.00 ? 79  ASP A CB  1 
ATOM   617  C CG  . ASP A 1 79  ? 91.047  163.260 166.147 1.00 30.00 ? 79  ASP A CG  1 
ATOM   618  O OD1 . ASP A 1 79  ? 91.081  162.053 166.454 1.00 30.00 ? 79  ASP A OD1 1 
ATOM   619  O OD2 . ASP A 1 79  ? 91.886  164.099 166.522 1.00 30.00 ? 79  ASP A OD2 1 
ATOM   620  N N   . TRP A 1 80  ? 87.992  163.176 162.641 1.00 30.00 ? 80  TRP A N   1 
ATOM   621  C CA  . TRP A 1 80  ? 86.952  163.617 161.674 1.00 30.00 ? 80  TRP A CA  1 
ATOM   622  C C   . TRP A 1 80  ? 85.874  162.538 161.565 1.00 30.00 ? 80  TRP A C   1 
ATOM   623  O O   . TRP A 1 80  ? 84.718  162.897 161.305 1.00 30.00 ? 80  TRP A O   1 
ATOM   624  C CB  . TRP A 1 80  ? 87.572  163.915 160.306 1.00 30.00 ? 80  TRP A CB  1 
ATOM   625  C CG  . TRP A 1 80  ? 86.567  164.397 159.310 1.00 30.00 ? 80  TRP A CG  1 
ATOM   626  C CD1 . TRP A 1 80  ? 85.699  163.638 158.583 1.00 30.00 ? 80  TRP A CD1 1 
ATOM   627  C CD2 . TRP A 1 80  ? 86.272  165.765 158.985 1.00 30.00 ? 80  TRP A CD2 1 
ATOM   628  N NE1 . TRP A 1 80  ? 84.908  164.437 157.805 1.00 30.00 ? 80  TRP A NE1 1 
ATOM   629  C CE2 . TRP A 1 80  ? 85.231  165.747 158.035 1.00 30.00 ? 80  TRP A CE2 1 
ATOM   630  C CE3 . TRP A 1 80  ? 86.797  166.996 159.387 1.00 30.00 ? 80  TRP A CE3 1 
ATOM   631  C CZ2 . TRP A 1 80  ? 84.714  166.913 157.475 1.00 30.00 ? 80  TRP A CZ2 1 
ATOM   632  C CZ3 . TRP A 1 80  ? 86.279  168.148 158.841 1.00 30.00 ? 80  TRP A CZ3 1 
ATOM   633  C CH2 . TRP A 1 80  ? 85.253  168.105 157.898 1.00 30.00 ? 80  TRP A CH2 1 
ATOM   634  N N   . ASP A 1 81  ? 86.234  161.270 161.767 1.00 30.00 ? 81  ASP A N   1 
ATOM   635  C CA  . ASP A 1 81  ? 85.289  160.130 161.641 1.00 30.00 ? 81  ASP A CA  1 
ATOM   636  C C   . ASP A 1 81  ? 84.551  159.937 162.968 1.00 30.00 ? 81  ASP A C   1 
ATOM   637  O O   . ASP A 1 81  ? 83.654  159.071 163.006 1.00 30.00 ? 81  ASP A O   1 
ATOM   638  C CB  . ASP A 1 81  ? 86.039  158.874 161.189 1.00 30.00 ? 81  ASP A CB  1 
ATOM   639  C CG  . ASP A 1 81  ? 86.318  158.824 159.699 1.00 30.00 ? 81  ASP A CG  1 
ATOM   640  O OD1 . ASP A 1 81  ? 85.782  159.682 158.981 1.00 30.00 ? 81  ASP A OD1 1 
ATOM   641  O OD2 . ASP A 1 81  ? 87.082  157.938 159.272 1.00 30.00 ? 81  ASP A OD2 1 
ATOM   642  N N   . ALA A 1 82  ? 84.886  160.724 163.997 1.00 30.00 ? 82  ALA A N   1 
ATOM   643  C CA  . ALA A 1 82  ? 84.255  160.651 165.335 1.00 30.00 ? 82  ALA A CA  1 
ATOM   644  C C   . ALA A 1 82  ? 83.363  161.869 165.562 1.00 30.00 ? 82  ALA A C   1 
ATOM   645  O O   . ALA A 1 82  ? 82.343  161.718 166.263 1.00 30.00 ? 82  ALA A O   1 
ATOM   646  C CB  . ALA A 1 82  ? 85.333  160.605 166.380 1.00 30.00 ? 82  ALA A CB  1 
ATOM   647  N N   . GLN A 1 83  ? 83.780  163.045 165.075 1.00 30.00 ? 83  GLN A N   1 
ATOM   648  C CA  . GLN A 1 83  ? 83.066  164.330 165.308 1.00 30.00 ? 83  GLN A CA  1 
ATOM   649  C C   . GLN A 1 83  ? 82.234  164.681 164.078 1.00 30.00 ? 83  GLN A C   1 
ATOM   650  O O   . GLN A 1 83  ? 81.376  165.578 164.198 1.00 30.00 ? 83  GLN A O   1 
ATOM   651  C CB  . GLN A 1 83  ? 84.091  165.425 165.590 1.00 30.00 ? 83  GLN A CB  1 
ATOM   652  C CG  . GLN A 1 83  ? 85.033  165.088 166.736 1.00 30.00 ? 83  GLN A CG  1 
ATOM   653  C CD  . GLN A 1 83  ? 86.250  165.978 166.766 1.00 30.00 ? 83  GLN A CD  1 
ATOM   654  O OE1 . GLN A 1 83  ? 86.381  166.919 165.986 1.00 30.00 ? 83  GLN A OE1 1 
ATOM   655  N NE2 . GLN A 1 83  ? 87.156  165.683 167.682 1.00 30.00 ? 83  GLN A NE2 1 
ATOM   656  N N   . HIS A 1 84  ? 82.485  164.022 162.947 1.00 30.00 ? 84  HIS A N   1 
ATOM   657  C CA  . HIS A 1 84  ? 81.679  164.205 161.711 1.00 30.00 ? 84  HIS A CA  1 
ATOM   658  C C   . HIS A 1 84  ? 81.254  162.793 161.313 1.00 30.00 ? 84  HIS A C   1 
ATOM   659  O O   . HIS A 1 84  ? 81.701  162.300 160.260 1.00 30.00 ? 84  HIS A O   1 
ATOM   660  C CB  . HIS A 1 84  ? 82.472  164.954 160.632 1.00 30.00 ? 84  HIS A CB  1 
ATOM   661  C CG  . HIS A 1 84  ? 83.289  166.098 161.129 1.00 30.00 ? 84  HIS A CG  1 
ATOM   662  N ND1 . HIS A 1 84  ? 84.344  165.970 162.005 1.00 30.00 ? 84  HIS A ND1 1 
ATOM   663  C CD2 . HIS A 1 84  ? 83.211  167.400 160.835 1.00 30.00 ? 84  HIS A CD2 1 
ATOM   664  C CE1 . HIS A 1 84  ? 84.867  167.163 162.239 1.00 30.00 ? 84  HIS A CE1 1 
ATOM   665  N NE2 . HIS A 1 84  ? 84.194  168.047 161.538 1.00 30.00 ? 84  HIS A NE2 1 
ATOM   666  N N   . PRO A 1 85  ? 80.395  162.112 162.106 1.00 30.00 ? 85  PRO A N   1 
ATOM   667  C CA  . PRO A 1 85  ? 80.033  160.718 161.847 1.00 30.00 ? 85  PRO A CA  1 
ATOM   668  C C   . PRO A 1 85  ? 79.120  160.586 160.627 1.00 30.00 ? 85  PRO A C   1 
ATOM   669  O O   . PRO A 1 85  ? 78.496  161.569 160.269 1.00 30.00 ? 85  PRO A O   1 
ATOM   670  C CB  . PRO A 1 85  ? 79.251  160.274 163.094 1.00 30.00 ? 85  PRO A CB  1 
ATOM   671  C CG  . PRO A 1 85  ? 79.457  161.388 164.095 1.00 30.00 ? 85  PRO A CG  1 
ATOM   672  C CD  . PRO A 1 85  ? 79.646  162.627 163.251 1.00 30.00 ? 85  PRO A CD  1 
ATOM   673  N N   . ILE A 1 86  ? 79.055  159.404 160.010 1.00 30.00 ? 86  ILE A N   1 
ATOM   674  C CA  . ILE A 1 86  ? 78.088  159.173 158.901 1.00 30.00 ? 86  ILE A CA  1 
ATOM   675  C C   . ILE A 1 86  ? 76.745  159.728 159.387 1.00 30.00 ? 86  ILE A C   1 
ATOM   676  O O   . ILE A 1 86  ? 76.321  159.347 160.496 1.00 30.00 ? 86  ILE A O   1 
ATOM   677  C CB  . ILE A 1 86  ? 77.993  157.685 158.507 1.00 30.00 ? 86  ILE A CB  1 
ATOM   678  C CG1 . ILE A 1 86  ? 77.017  157.489 157.345 1.00 30.00 ? 86  ILE A CG1 1 
ATOM   679  C CG2 . ILE A 1 86  ? 77.628  156.810 159.697 1.00 30.00 ? 86  ILE A CG2 1 
ATOM   680  C CD1 . ILE A 1 86  ? 77.016  156.095 156.770 1.00 30.00 ? 86  ILE A CD1 1 
ATOM   681  N N   . PRO A 1 87  ? 76.062  160.620 158.641 1.00 30.00 ? 87  PRO A N   1 
ATOM   682  C CA  . PRO A 1 87  ? 74.823  161.220 159.128 1.00 30.00 ? 87  PRO A CA  1 
ATOM   683  C C   . PRO A 1 87  ? 73.796  160.108 159.351 1.00 30.00 ? 87  PRO A C   1 
ATOM   684  O O   . PRO A 1 87  ? 73.055  160.193 160.311 1.00 30.00 ? 87  PRO A O   1 
ATOM   685  C CB  . PRO A 1 87  ? 74.393  162.175 158.006 1.00 30.00 ? 87  PRO A CB  1 
ATOM   686  C CG  . PRO A 1 87  ? 75.100  161.645 156.776 1.00 30.00 ? 87  PRO A CG  1 
ATOM   687  C CD  . PRO A 1 87  ? 76.403  161.075 157.292 1.00 30.00 ? 87  PRO A CD  1 
ATOM   688  N N   . GLY A 1 88  ? 73.781  159.104 158.474 1.00 30.00 ? 88  GLY A N   1 
ATOM   689  C CA  . GLY A 1 88  ? 72.828  157.983 158.551 1.00 30.00 ? 88  GLY A CA  1 
ATOM   690  C C   . GLY A 1 88  ? 72.756  157.292 157.205 1.00 30.00 ? 88  GLY A C   1 
ATOM   691  O O   . GLY A 1 88  ? 73.682  157.496 156.395 1.00 30.00 ? 88  GLY A O   1 
ATOM   692  N N   . PRO A 1 89  ? 71.712  156.488 156.882 1.00 30.00 ? 89  PRO A N   1 
ATOM   693  C CA  . PRO A 1 89  ? 71.591  155.891 155.544 1.00 30.00 ? 89  PRO A CA  1 
ATOM   694  C C   . PRO A 1 89  ? 71.534  156.962 154.445 1.00 30.00 ? 89  PRO A C   1 
ATOM   695  O O   . PRO A 1 89  ? 70.556  157.685 154.389 1.00 30.00 ? 89  PRO A O   1 
ATOM   696  C CB  . PRO A 1 89  ? 70.256  155.134 155.587 1.00 30.00 ? 89  PRO A CB  1 
ATOM   697  C CG  . PRO A 1 89  ? 70.039  154.855 157.054 1.00 30.00 ? 89  PRO A CG  1 
ATOM   698  C CD  . PRO A 1 89  ? 70.598  156.075 157.752 1.00 30.00 ? 89  PRO A CD  1 
ATOM   699  N N   . LEU A 1 90  ? 72.572  157.033 153.607 1.00 30.00 ? 90  LEU A N   1 
ATOM   700  C CA  . LEU A 1 90  ? 72.608  158.030 152.502 1.00 30.00 ? 90  LEU A CA  1 
ATOM   701  C C   . LEU A 1 90  ? 71.576  157.655 151.433 1.00 30.00 ? 90  LEU A C   1 
ATOM   702  O O   . LEU A 1 90  ? 71.489  156.459 151.092 1.00 30.00 ? 90  LEU A O   1 
ATOM   703  C CB  . LEU A 1 90  ? 74.017  158.054 151.904 1.00 30.00 ? 90  LEU A CB  1 
ATOM   704  C CG  . LEU A 1 90  ? 74.179  158.913 150.651 1.00 30.00 ? 90  LEU A CG  1 
ATOM   705  C CD1 . LEU A 1 90  ? 74.569  160.337 151.012 1.00 30.00 ? 90  LEU A CD1 1 
ATOM   706  C CD2 . LEU A 1 90  ? 75.191  158.298 149.699 1.00 30.00 ? 90  LEU A CD2 1 
ATOM   707  N N   . PRO A 1 91  ? 70.801  158.617 150.887 1.00 30.00 ? 91  PRO A N   1 
ATOM   708  C CA  . PRO A 1 91  ? 69.854  158.333 149.801 1.00 30.00 ? 91  PRO A CA  1 
ATOM   709  C C   . PRO A 1 91  ? 70.570  157.930 148.503 1.00 30.00 ? 91  PRO A C   1 
ATOM   710  O O   . PRO A 1 91  ? 71.671  158.399 148.276 1.00 30.00 ? 91  PRO A O   1 
ATOM   711  C CB  . PRO A 1 91  ? 69.135  159.673 149.582 1.00 30.00 ? 91  PRO A CB  1 
ATOM   712  C CG  . PRO A 1 91  ? 69.365  160.437 150.867 1.00 30.00 ? 91  PRO A CG  1 
ATOM   713  C CD  . PRO A 1 91  ? 70.744  160.012 151.322 1.00 30.00 ? 91  PRO A CD  1 
ATOM   714  N N   . ALA A 1 92  ? 69.931  157.084 147.689 1.00 30.00 ? 92  ALA A N   1 
ATOM   715  C CA  . ALA A 1 92  ? 70.540  156.622 146.418 1.00 30.00 ? 92  ALA A CA  1 
ATOM   716  C C   . ALA A 1 92  ? 70.615  157.780 145.417 1.00 30.00 ? 92  ALA A C   1 
ATOM   717  O O   . ALA A 1 92  ? 69.772  158.695 145.505 1.00 30.00 ? 92  ALA A O   1 
ATOM   718  C CB  . ALA A 1 92  ? 69.752  155.462 145.863 1.00 30.00 ? 92  ALA A CB  1 
ATOM   719  N N   . GLY A 1 93  ? 71.590  157.736 144.503 1.00 30.00 ? 93  GLY A N   1 
ATOM   720  C CA  . GLY A 1 93  ? 71.755  158.811 143.505 1.00 30.00 ? 93  GLY A CA  1 
ATOM   721  C C   . GLY A 1 93  ? 72.418  160.035 144.111 1.00 30.00 ? 93  GLY A C   1 
ATOM   722  O O   . GLY A 1 93  ? 72.366  161.107 143.476 1.00 30.00 ? 93  GLY A O   1 
ATOM   723  N N   . GLN A 1 94  ? 73.018  159.885 145.295 1.00 30.00 ? 94  GLN A N   1 
ATOM   724  C CA  . GLN A 1 94  ? 73.660  161.031 145.990 1.00 30.00 ? 94  GLN A CA  1 
ATOM   725  C C   . GLN A 1 94  ? 75.087  160.650 146.395 1.00 30.00 ? 94  GLN A C   1 
ATOM   726  O O   . GLN A 1 94  ? 75.307  159.471 146.728 1.00 30.00 ? 94  GLN A O   1 
ATOM   727  C CB  . GLN A 1 94  ? 72.839  161.426 147.217 1.00 30.00 ? 94  GLN A CB  1 
ATOM   728  C CG  . GLN A 1 94  ? 73.477  162.523 148.055 1.00 30.00 ? 94  GLN A CG  1 
ATOM   729  C CD  . GLN A 1 94  ? 72.571  162.978 149.171 1.00 30.00 ? 94  GLN A CD  1 
ATOM   730  O OE1 . GLN A 1 94  ? 71.442  162.513 149.307 1.00 30.00 ? 94  GLN A OE1 1 
ATOM   731  N NE2 . GLN A 1 94  ? 73.060  163.906 149.977 1.00 30.00 ? 94  GLN A NE2 1 
ATOM   732  N N   . LEU A 1 95  ? 76.017  161.610 146.355 1.00 30.00 ? 95  LEU A N   1 
ATOM   733  C CA  . LEU A 1 95  ? 77.410  161.343 146.801 1.00 30.00 ? 95  LEU A CA  1 
ATOM   734  C C   . LEU A 1 95  ? 77.426  161.215 148.327 1.00 30.00 ? 95  LEU A C   1 
ATOM   735  O O   . LEU A 1 95  ? 76.798  162.060 148.994 1.00 30.00 ? 95  LEU A O   1 
ATOM   736  C CB  . LEU A 1 95  ? 78.311  162.494 146.345 1.00 30.00 ? 95  LEU A CB  1 
ATOM   737  C CG  . LEU A 1 95  ? 79.748  162.449 146.861 1.00 30.00 ? 95  LEU A CG  1 
ATOM   738  C CD1 . LEU A 1 95  ? 80.473  161.220 146.339 1.00 30.00 ? 95  LEU A CD1 1 
ATOM   739  C CD2 . LEU A 1 95  ? 80.499  163.712 146.475 1.00 30.00 ? 95  LEU A CD2 1 
ATOM   740  N N   . ARG A 1 96  ? 78.122  160.203 148.852 1.00 30.00 ? 96  ARG A N   1 
ATOM   741  C CA  . ARG A 1 96  ? 78.240  160.041 150.323 1.00 30.00 ? 96  ARG A CA  1 
ATOM   742  C C   . ARG A 1 96  ? 78.941  161.282 150.862 1.00 30.00 ? 96  ARG A C   1 
ATOM   743  O O   . ARG A 1 96  ? 79.710  161.850 150.104 1.00 30.00 ? 96  ARG A O   1 
ATOM   744  C CB  . ARG A 1 96  ? 79.075  158.814 150.694 1.00 30.00 ? 96  ARG A CB  1 
ATOM   745  C CG  . ARG A 1 96  ? 80.564  158.944 150.399 1.00 30.00 ? 96  ARG A CG  1 
ATOM   746  C CD  . ARG A 1 96  ? 81.338  157.721 150.844 1.00 30.00 ? 96  ARG A CD  1 
ATOM   747  N NE  . ARG A 1 96  ? 82.747  157.775 150.479 1.00 30.00 ? 96  ARG A NE  1 
ATOM   748  C CZ  . ARG A 1 96  ? 83.217  157.779 149.237 1.00 30.00 ? 96  ARG A CZ  1 
ATOM   749  N NH1 . ARG A 1 96  ? 82.415  157.544 148.213 1.00 30.00 ? 96  ARG A NH1 1 
ATOM   750  N NH2 . ARG A 1 96  ? 84.505  157.986 149.023 1.00 30.00 ? 96  ARG A NH2 1 
ATOM   751  N N   . ASP A 1 97  ? 78.745  161.649 152.128 1.00 30.00 ? 97  ASP A N   1 
ATOM   752  C CA  . ASP A 1 97  ? 79.494  162.782 152.730 1.00 30.00 ? 97  ASP A CA  1 
ATOM   753  C C   . ASP A 1 97  ? 80.933  162.329 152.976 1.00 30.00 ? 97  ASP A C   1 
ATOM   754  O O   . ASP A 1 97  ? 81.153  161.110 153.121 1.00 30.00 ? 97  ASP A O   1 
ATOM   755  C CB  . ASP A 1 97  ? 78.858  163.270 154.027 1.00 30.00 ? 97  ASP A CB  1 
ATOM   756  C CG  . ASP A 1 97  ? 77.676  164.193 153.794 1.00 30.00 ? 97  ASP A CG  1 
ATOM   757  O OD1 . ASP A 1 97  ? 76.785  163.809 153.015 1.00 30.00 ? 97  ASP A OD1 1 
ATOM   758  O OD2 . ASP A 1 97  ? 77.653  165.283 154.400 1.00 30.00 ? 97  ASP A OD2 1 
ATOM   759  N N   . PRO A 1 98  ? 81.917  163.249 153.038 1.00 30.00 ? 98  PRO A N   1 
ATOM   760  C CA  . PRO A 1 98  ? 83.317  162.855 153.187 1.00 30.00 ? 98  PRO A CA  1 
ATOM   761  C C   . PRO A 1 98  ? 83.665  162.318 154.580 1.00 30.00 ? 98  PRO A C   1 
ATOM   762  O O   . PRO A 1 98  ? 83.118  162.834 155.534 1.00 30.00 ? 98  PRO A O   1 
ATOM   763  C CB  . PRO A 1 98  ? 84.104  164.151 152.937 1.00 30.00 ? 98  PRO A CB  1 
ATOM   764  C CG  . PRO A 1 98  ? 83.124  165.259 153.259 1.00 30.00 ? 98  PRO A CG  1 
ATOM   765  C CD  . PRO A 1 98  ? 81.749  164.700 152.958 1.00 30.00 ? 98  PRO A CD  1 
ATOM   766  N N   . ARG A 1 99  ? 84.508  161.288 154.662 1.00 30.00 ? 99  ARG A N   1 
ATOM   767  C CA  . ARG A 1 99  ? 85.023  160.731 155.940 1.00 30.00 ? 99  ARG A CA  1 
ATOM   768  C C   . ARG A 1 99  ? 86.489  161.162 156.009 1.00 30.00 ? 99  ARG A C   1 
ATOM   769  O O   . ARG A 1 99  ? 86.945  161.685 155.005 1.00 30.00 ? 99  ARG A O   1 
ATOM   770  C CB  . ARG A 1 99  ? 84.854  159.212 155.940 1.00 30.00 ? 99  ARG A CB  1 
ATOM   771  C CG  . ARG A 1 99  ? 83.420  158.771 155.684 1.00 30.00 ? 99  ARG A CG  1 
ATOM   772  C CD  . ARG A 1 99  ? 82.919  157.739 156.674 1.00 30.00 ? 99  ARG A CD  1 
ATOM   773  N NE  . ARG A 1 99  ? 83.115  158.103 158.072 1.00 30.00 ? 99  ARG A NE  1 
ATOM   774  C CZ  . ARG A 1 99  ? 82.542  159.127 158.698 1.00 30.00 ? 99  ARG A CZ  1 
ATOM   775  N NH1 . ARG A 1 99  ? 81.840  160.031 158.039 1.00 30.00 ? 99  ARG A NH1 1 
ATOM   776  N NH2 . ARG A 1 99  ? 82.672  159.237 160.007 1.00 30.00 ? 99  ARG A NH2 1 
ATOM   777  N N   . GLY A 1 100 ? 87.165  161.062 157.151 1.00 30.00 ? 100 GLY A N   1 
ATOM   778  C CA  . GLY A 1 100 ? 88.602  161.382 157.259 1.00 30.00 ? 100 GLY A CA  1 
ATOM   779  C C   . GLY A 1 100 ? 89.405  160.833 156.088 1.00 30.00 ? 100 GLY A C   1 
ATOM   780  O O   . GLY A 1 100 ? 90.287  161.567 155.609 1.00 30.00 ? 100 GLY A O   1 
ATOM   781  N N   . SER A 1 101 ? 89.145  159.598 155.640 1.00 30.00 ? 101 SER A N   1 
ATOM   782  C CA  . SER A 1 101 ? 89.864  158.926 154.525 1.00 30.00 ? 101 SER A CA  1 
ATOM   783  C C   . SER A 1 101 ? 89.539  159.614 153.196 1.00 30.00 ? 101 SER A C   1 
ATOM   784  O O   . SER A 1 101 ? 90.436  159.659 152.350 1.00 30.00 ? 101 SER A O   1 
ATOM   785  C CB  . SER A 1 101 ? 89.545  157.459 154.464 1.00 30.00 ? 101 SER A CB  1 
ATOM   786  O OG  . SER A 1 101 ? 88.143  157.241 154.532 1.00 30.00 ? 101 SER A OG  1 
ATOM   787  N N   . ASP A 1 102 ? 88.297  160.064 152.989 1.00 30.00 ? 102 ASP A N   1 
ATOM   788  C CA  . ASP A 1 102 ? 87.899  160.798 151.756 1.00 30.00 ? 102 ASP A CA  1 
ATOM   789  C C   . ASP A 1 102 ? 88.629  162.143 151.721 1.00 30.00 ? 102 ASP A C   1 
ATOM   790  O O   . ASP A 1 102 ? 89.079  162.546 150.636 1.00 30.00 ? 102 ASP A O   1 
ATOM   791  C CB  . ASP A 1 102 ? 86.387  161.018 151.677 1.00 30.00 ? 102 ASP A CB  1 
ATOM   792  C CG  . ASP A 1 102 ? 85.556  159.747 151.646 1.00 30.00 ? 102 ASP A CG  1 
ATOM   793  O OD1 . ASP A 1 102 ? 86.145  158.663 151.540 1.00 30.00 ? 102 ASP A OD1 1 
ATOM   794  O OD2 . ASP A 1 102 ? 84.322  159.855 151.754 1.00 30.00 ? 102 ASP A OD2 1 
ATOM   795  N N   . ILE A 1 103 ? 88.738  162.827 152.861 1.00 30.00 ? 103 ILE A N   1 
ATOM   796  C CA  . ILE A 1 103 ? 89.451  164.134 152.947 1.00 30.00 ? 103 ILE A CA  1 
ATOM   797  C C   . ILE A 1 103 ? 90.884  163.919 152.470 1.00 30.00 ? 103 ILE A C   1 
ATOM   798  O O   . ILE A 1 103 ? 91.414  164.819 151.800 1.00 30.00 ? 103 ILE A O   1 
ATOM   799  C CB  . ILE A 1 103 ? 89.408  164.691 154.379 1.00 30.00 ? 103 ILE A CB  1 
ATOM   800  C CG1 . ILE A 1 103 ? 88.022  165.257 154.696 1.00 30.00 ? 103 ILE A CG1 1 
ATOM   801  C CG2 . ILE A 1 103 ? 90.507  165.722 154.606 1.00 30.00 ? 103 ILE A CG2 1 
ATOM   802  C CD1 . ILE A 1 103 ? 87.810  165.582 156.146 1.00 30.00 ? 103 ILE A CD1 1 
ATOM   803  N N   . ALA A 1 104 ? 91.490  162.782 152.816 1.00 30.00 ? 104 ALA A N   1 
ATOM   804  C CA  . ALA A 1 104 ? 92.872  162.452 152.411 1.00 30.00 ? 104 ALA A CA  1 
ATOM   805  C C   . ALA A 1 104 ? 92.907  162.200 150.904 1.00 30.00 ? 104 ALA A C   1 
ATOM   806  O O   . ALA A 1 104 ? 93.871  162.663 150.285 1.00 30.00 ? 104 ALA A O   1 
ATOM   807  C CB  . ALA A 1 104 ? 93.349  161.254 153.178 1.00 30.00 ? 104 ALA A CB  1 
ATOM   808  N N   . GLY A 1 105 ? 91.900  161.516 150.348 1.00 30.00 ? 105 GLY A N   1 
ATOM   809  C CA  . GLY A 1 105 ? 91.821  161.184 148.909 1.00 30.00 ? 105 GLY A CA  1 
ATOM   810  C C   . GLY A 1 105 ? 92.122  159.714 148.676 1.00 30.00 ? 105 GLY A C   1 
ATOM   811  O O   . GLY A 1 105 ? 91.959  159.259 147.532 1.00 30.00 ? 105 GLY A O   1 
ATOM   812  N N   . THR A 1 106 ? 92.510  158.978 149.715 1.00 30.00 ? 106 THR A N   1 
ATOM   813  C CA  . THR A 1 106 ? 92.901  157.544 149.648 1.00 30.00 ? 106 THR A CA  1 
ATOM   814  C C   . THR A 1 106 ? 91.704  156.674 149.255 1.00 30.00 ? 106 THR A C   1 
ATOM   815  O O   . THR A 1 106 ? 91.910  155.764 148.427 1.00 30.00 ? 106 THR A O   1 
ATOM   816  C CB  . THR A 1 106 ? 93.487  157.051 150.978 1.00 30.00 ? 106 THR A CB  1 
ATOM   817  O OG1 . THR A 1 106 ? 93.700  155.646 150.852 1.00 30.00 ? 106 THR A OG1 1 
ATOM   818  C CG2 . THR A 1 106 ? 92.610  157.312 152.183 1.00 30.00 ? 106 THR A CG2 1 
ATOM   819  N N   . THR A 1 107 ? 90.516  156.928 149.815 1.00 30.00 ? 107 THR A N   1 
ATOM   820  C CA  . THR A 1 107 ? 89.327  156.087 149.513 1.00 30.00 ? 107 THR A CA  1 
ATOM   821  C C   . THR A 1 107 ? 88.336  156.876 148.658 1.00 30.00 ? 107 THR A C   1 
ATOM   822  O O   . THR A 1 107 ? 87.136  156.538 148.693 1.00 30.00 ? 107 THR A O   1 
ATOM   823  C CB  . THR A 1 107 ? 88.588  155.639 150.779 1.00 30.00 ? 107 THR A CB  1 
ATOM   824  O OG1 . THR A 1 107 ? 88.074  156.801 151.431 1.00 30.00 ? 107 THR A OG1 1 
ATOM   825  C CG2 . THR A 1 107 ? 89.462  154.851 151.728 1.00 30.00 ? 107 THR A CG2 1 
ATOM   826  N N   . SER A 1 108 ? 88.811  157.888 147.929 1.00 30.00 ? 108 SER A N   1 
ATOM   827  C CA  . SER A 1 108 ? 87.855  158.743 147.182 1.00 30.00 ? 108 SER A CA  1 
ATOM   828  C C   . SER A 1 108 ? 88.448  159.207 145.849 1.00 30.00 ? 108 SER A C   1 
ATOM   829  O O   . SER A 1 108 ? 89.673  159.420 145.789 1.00 30.00 ? 108 SER A O   1 
ATOM   830  C CB  . SER A 1 108 ? 87.464  159.909 148.034 1.00 30.00 ? 108 SER A CB  1 
ATOM   831  O OG  . SER A 1 108 ? 88.582  160.750 148.280 1.00 30.00 ? 108 SER A OG  1 
ATOM   832  N N   . THR A 1 109 ? 87.600  159.370 144.829 1.00 30.00 ? 109 THR A N   1 
ATOM   833  C CA  . THR A 1 109 ? 88.070  159.875 143.511 1.00 30.00 ? 109 THR A CA  1 
ATOM   834  C C   . THR A 1 109 ? 88.238  161.396 143.584 1.00 30.00 ? 109 THR A C   1 
ATOM   835  O O   . THR A 1 109 ? 87.581  162.017 144.441 1.00 30.00 ? 109 THR A O   1 
ATOM   836  C CB  . THR A 1 109 ? 87.097  159.489 142.391 1.00 30.00 ? 109 THR A CB  1 
ATOM   837  O OG1 . THR A 1 109 ? 85.886  160.214 142.589 1.00 30.00 ? 109 THR A OG1 1 
ATOM   838  C CG2 . THR A 1 109 ? 86.831  158.001 142.326 1.00 30.00 ? 109 THR A CG2 1 
ATOM   839  N N   . VAL A 1 110 ? 89.061  161.967 142.700 1.00 30.00 ? 110 VAL A N   1 
ATOM   840  C CA  . VAL A 1 110 ? 89.272  163.447 142.676 1.00 30.00 ? 110 VAL A CA  1 
ATOM   841  C C   . VAL A 1 110 ? 87.929  164.127 142.380 1.00 30.00 ? 110 VAL A C   1 
ATOM   842  O O   . VAL A 1 110 ? 87.674  165.199 142.956 1.00 30.00 ? 110 VAL A O   1 
ATOM   843  C CB  . VAL A 1 110 ? 90.369  163.854 141.671 1.00 30.00 ? 110 VAL A CB  1 
ATOM   844  C CG1 . VAL A 1 110 ? 90.167  163.232 140.298 1.00 30.00 ? 110 VAL A CG1 1 
ATOM   845  C CG2 . VAL A 1 110 ? 90.534  165.360 141.571 1.00 30.00 ? 110 VAL A CG2 1 
ATOM   846  N N   . GLU A 1 111 ? 87.101  163.516 141.527 1.00 30.00 ? 111 GLU A N   1 
ATOM   847  C CA  . GLU A 1 111 ? 85.779  164.099 141.176 1.00 30.00 ? 111 GLU A CA  1 
ATOM   848  C C   . GLU A 1 111 ? 84.929  164.234 142.441 1.00 30.00 ? 111 GLU A C   1 
ATOM   849  O O   . GLU A 1 111 ? 84.306  165.296 142.619 1.00 30.00 ? 111 GLU A O   1 
ATOM   850  C CB  . GLU A 1 111 ? 85.035  163.204 140.186 1.00 30.00 ? 111 GLU A CB  1 
ATOM   851  C CG  . GLU A 1 111 ? 85.706  163.080 138.829 1.00 30.00 ? 111 GLU A CG  1 
ATOM   852  C CD  . GLU A 1 111 ? 86.964  162.231 138.766 1.00 30.00 ? 111 GLU A CD  1 
ATOM   853  O OE1 . GLU A 1 111 ? 87.354  161.667 139.809 1.00 30.00 ? 111 GLU A OE1 1 
ATOM   854  O OE2 . GLU A 1 111 ? 87.559  162.145 137.674 1.00 30.00 ? 111 GLU A OE2 1 
ATOM   855  N N   . GLU A 1 112 ? 84.921  163.201 143.286 1.00 30.00 ? 112 GLU A N   1 
ATOM   856  C CA  . GLU A 1 112 ? 84.163  163.265 144.562 1.00 30.00 ? 112 GLU A CA  1 
ATOM   857  C C   . GLU A 1 112 ? 84.729  164.411 145.397 1.00 30.00 ? 112 GLU A C   1 
ATOM   858  O O   . GLU A 1 112 ? 83.931  165.194 145.947 1.00 30.00 ? 112 GLU A O   1 
ATOM   859  C CB  . GLU A 1 112 ? 84.339  161.955 145.324 1.00 30.00 ? 112 GLU A CB  1 
ATOM   860  C CG  . GLU A 1 112 ? 83.696  160.758 144.654 1.00 30.00 ? 112 GLU A CG  1 
ATOM   861  C CD  . GLU A 1 112 ? 84.091  159.426 145.267 1.00 30.00 ? 112 GLU A CD  1 
ATOM   862  O OE1 . GLU A 1 112 ? 83.854  159.235 146.470 1.00 30.00 ? 112 GLU A OE1 1 
ATOM   863  O OE2 . GLU A 1 112 ? 84.633  158.580 144.537 1.00 30.00 ? 112 GLU A OE2 1 
ATOM   864  N N   . GLN A 1 113 ? 86.058  164.507 145.464 1.00 30.00 ? 113 GLN A N   1 
ATOM   865  C CA  . GLN A 1 113 ? 86.721  165.600 146.220 1.00 30.00 ? 113 GLN A CA  1 
ATOM   866  C C   . GLN A 1 113 ? 86.253  166.938 145.640 1.00 30.00 ? 113 GLN A C   1 
ATOM   867  O O   . GLN A 1 113 ? 85.957  167.848 146.436 1.00 30.00 ? 113 GLN A O   1 
ATOM   868  C CB  . GLN A 1 113 ? 88.233  165.403 146.109 1.00 30.00 ? 113 GLN A CB  1 
ATOM   869  C CG  . GLN A 1 113 ? 88.695  164.028 146.570 1.00 30.00 ? 113 GLN A CG  1 
ATOM   870  C CD  . GLN A 1 113 ? 90.107  163.703 146.153 1.00 30.00 ? 113 GLN A CD  1 
ATOM   871  O OE1 . GLN A 1 113 ? 90.806  164.516 145.555 1.00 30.00 ? 113 GLN A OE1 1 
ATOM   872  N NE2 . GLN A 1 113 ? 90.542  162.496 146.466 1.00 30.00 ? 113 GLN A NE2 1 
ATOM   873  N N   . ILE A 1 114 ? 86.116  167.045 144.317 1.00 30.00 ? 114 ILE A N   1 
ATOM   874  C CA  . ILE A 1 114 ? 85.709  168.312 143.639 1.00 30.00 ? 114 ILE A CA  1 
ATOM   875  C C   . ILE A 1 114 ? 84.228  168.572 143.918 1.00 30.00 ? 114 ILE A C   1 
ATOM   876  O O   . ILE A 1 114 ? 83.881  169.741 144.174 1.00 30.00 ? 114 ILE A O   1 
ATOM   877  C CB  . ILE A 1 114 ? 86.005  168.220 142.130 1.00 30.00 ? 114 ILE A CB  1 
ATOM   878  C CG1 . ILE A 1 114 ? 87.511  168.215 141.863 1.00 30.00 ? 114 ILE A CG1 1 
ATOM   879  C CG2 . ILE A 1 114 ? 85.315  169.340 141.365 1.00 30.00 ? 114 ILE A CG2 1 
ATOM   880  C CD1 . ILE A 1 114 ? 87.889  167.890 140.444 1.00 30.00 ? 114 ILE A CD1 1 
ATOM   881  N N   . GLN A 1 115 ? 83.395  167.531 143.901 1.00 30.00 ? 115 GLN A N   1 
ATOM   882  C CA  . GLN A 1 115 ? 81.933  167.670 144.125 1.00 30.00 ? 115 GLN A CA  1 
ATOM   883  C C   . GLN A 1 115 ? 81.711  168.238 145.525 1.00 30.00 ? 115 GLN A C   1 
ATOM   884  O O   . GLN A 1 115 ? 80.867  169.137 145.653 1.00 30.00 ? 115 GLN A O   1 
ATOM   885  C CB  . GLN A 1 115 ? 81.239  166.320 143.954 1.00 30.00 ? 115 GLN A CB  1 
ATOM   886  C CG  . GLN A 1 115 ? 81.122  165.897 142.499 1.00 30.00 ? 115 GLN A CG  1 
ATOM   887  C CD  . GLN A 1 115 ? 80.541  164.517 142.324 1.00 30.00 ? 115 GLN A CD  1 
ATOM   888  O OE1 . GLN A 1 115 ? 80.176  163.842 143.283 1.00 30.00 ? 115 GLN A OE1 1 
ATOM   889  N NE2 . GLN A 1 115 ? 80.444  164.087 141.078 1.00 30.00 ? 115 GLN A NE2 1 
ATOM   890  N N   . TRP A 1 116 ? 82.467  167.767 146.520 1.00 30.00 ? 116 TRP A N   1 
ATOM   891  C CA  . TRP A 1 116 ? 82.376  168.277 147.911 1.00 30.00 ? 116 TRP A CA  1 
ATOM   892  C C   . TRP A 1 116 ? 82.945  169.691 147.959 1.00 30.00 ? 116 TRP A C   1 
ATOM   893  O O   . TRP A 1 116 ? 82.229  170.596 148.410 1.00 30.00 ? 116 TRP A O   1 
ATOM   894  C CB  . TRP A 1 116 ? 83.156  167.384 148.875 1.00 30.00 ? 116 TRP A CB  1 
ATOM   895  C CG  . TRP A 1 116 ? 82.584  166.020 149.083 1.00 30.00 ? 116 TRP A CG  1 
ATOM   896  C CD1 . TRP A 1 116 ? 81.300  165.724 149.420 1.00 30.00 ? 116 TRP A CD1 1 
ATOM   897  C CD2 . TRP A 1 116 ? 83.306  164.777 149.111 1.00 30.00 ? 116 TRP A CD2 1 
ATOM   898  N NE1 . TRP A 1 116 ? 81.155  164.377 149.584 1.00 30.00 ? 116 TRP A NE1 1 
ATOM   899  C CE2 . TRP A 1 116 ? 82.370  163.767 149.410 1.00 30.00 ? 116 TRP A CE2 1 
ATOM   900  C CE3 . TRP A 1 116 ? 84.638  164.419 148.891 1.00 30.00 ? 116 TRP A CE3 1 
ATOM   901  C CZ2 . TRP A 1 116 ? 82.730  162.423 149.486 1.00 30.00 ? 116 TRP A CZ2 1 
ATOM   902  C CZ3 . TRP A 1 116 ? 84.993  163.091 148.963 1.00 30.00 ? 116 TRP A CZ3 1 
ATOM   903  C CH2 . TRP A 1 116 ? 84.049  162.109 149.259 1.00 30.00 ? 116 TRP A CH2 1 
ATOM   904  N N   . MET A 1 117 ? 84.153  169.882 147.437 1.00 30.00 ? 117 MET A N   1 
ATOM   905  C CA  . MET A 1 117 ? 84.852  171.190 147.478 1.00 30.00 ? 117 MET A CA  1 
ATOM   906  C C   . MET A 1 117 ? 83.941  172.274 146.906 1.00 30.00 ? 117 MET A C   1 
ATOM   907  O O   . MET A 1 117 ? 84.030  173.417 147.395 1.00 30.00 ? 117 MET A O   1 
ATOM   908  C CB  . MET A 1 117 ? 86.138  171.096 146.656 1.00 30.00 ? 117 MET A CB  1 
ATOM   909  C CG  . MET A 1 117 ? 87.323  170.684 147.498 1.00 30.00 ? 117 MET A CG  1 
ATOM   910  S SD  . MET A 1 117 ? 88.741  170.161 146.519 1.00 30.00 ? 117 MET A SD  1 
ATOM   911  C CE  . MET A 1 117 ? 89.310  171.746 145.911 1.00 30.00 ? 117 MET A CE  1 
ATOM   912  N N   . TYR A 1 118 ? 83.087  171.927 145.940 1.00 30.00 ? 118 TYR A N   1 
ATOM   913  C CA  . TYR A 1 118 ? 82.188  172.890 145.257 1.00 30.00 ? 118 TYR A CA  1 
ATOM   914  C C   . TYR A 1 118 ? 80.744  172.393 145.325 1.00 30.00 ? 118 TYR A C   1 
ATOM   915  O O   . TYR A 1 118 ? 80.050  172.447 144.290 1.00 30.00 ? 118 TYR A O   1 
ATOM   916  C CB  . TYR A 1 118 ? 82.669  173.048 143.817 1.00 30.00 ? 118 TYR A CB  1 
ATOM   917  C CG  . TYR A 1 118 ? 84.081  173.558 143.706 1.00 30.00 ? 118 TYR A CG  1 
ATOM   918  C CD1 . TYR A 1 118 ? 84.408  174.844 144.093 1.00 30.00 ? 118 TYR A CD1 1 
ATOM   919  C CD2 . TYR A 1 118 ? 85.104  172.723 143.299 1.00 30.00 ? 118 TYR A CD2 1 
ATOM   920  C CE1 . TYR A 1 118 ? 85.709  175.311 144.014 1.00 30.00 ? 118 TYR A CE1 1 
ATOM   921  C CE2 . TYR A 1 118 ? 86.411  173.168 143.228 1.00 30.00 ? 118 TYR A CE2 1 
ATOM   922  C CZ  . TYR A 1 118 ? 86.715  174.468 143.581 1.00 30.00 ? 118 TYR A CZ  1 
ATOM   923  O OH  . TYR A 1 118 ? 88.015  174.899 143.504 1.00 30.00 ? 118 TYR A OH  1 
ATOM   924  N N   . ARG A 1 119 ? 80.296  171.934 146.495 1.00 30.00 ? 119 ARG A N   1 
ATOM   925  C CA  . ARG A 1 119 ? 78.886  171.501 146.665 1.00 30.00 ? 119 ARG A CA  1 
ATOM   926  C C   . ARG A 1 119 ? 78.042  172.775 146.684 1.00 30.00 ? 119 ARG A C   1 
ATOM   927  O O   . ARG A 1 119 ? 78.403  173.705 147.430 1.00 30.00 ? 119 ARG A O   1 
ATOM   928  C CB  . ARG A 1 119 ? 78.682  170.686 147.945 1.00 30.00 ? 119 ARG A CB  1 
ATOM   929  C CG  . ARG A 1 119 ? 77.397  169.877 147.980 1.00 30.00 ? 119 ARG A CG  1 
ATOM   930  C CD  . ARG A 1 119 ? 77.592  168.563 148.711 1.00 30.00 ? 119 ARG A CD  1 
ATOM   931  N NE  . ARG A 1 119 ? 77.962  168.732 150.110 1.00 30.00 ? 119 ARG A NE  1 
ATOM   932  C CZ  . ARG A 1 119 ? 78.214  167.742 150.960 1.00 30.00 ? 119 ARG A CZ  1 
ATOM   933  N NH1 . ARG A 1 119 ? 78.272  166.488 150.544 1.00 30.00 ? 119 ARG A NH1 1 
ATOM   934  N NH2 . ARG A 1 119 ? 78.424  168.011 152.236 1.00 30.00 ? 119 ARG A NH2 1 
ATOM   935  N N   . PRO A 1 120 ? 76.943  172.868 145.908 1.00 30.00 ? 120 PRO A N   1 
ATOM   936  C CA  . PRO A 1 120 ? 76.074  174.034 145.970 1.00 30.00 ? 120 PRO A CA  1 
ATOM   937  C C   . PRO A 1 120 ? 75.500  174.186 147.381 1.00 30.00 ? 120 PRO A C   1 
ATOM   938  O O   . PRO A 1 120 ? 75.243  175.309 147.769 1.00 30.00 ? 120 PRO A O   1 
ATOM   939  C CB  . PRO A 1 120 ? 74.936  173.714 144.983 1.00 30.00 ? 120 PRO A CB  1 
ATOM   940  C CG  . PRO A 1 120 ? 75.523  172.665 144.068 1.00 30.00 ? 120 PRO A CG  1 
ATOM   941  C CD  . PRO A 1 120 ? 76.472  171.877 144.943 1.00 30.00 ? 120 PRO A CD  1 
ATOM   942  N N   . GLN A 1 121 ? 75.368  173.096 148.135 1.00 30.00 ? 121 GLN A N   1 
ATOM   943  C CA  . GLN A 1 121 ? 74.675  173.136 149.449 1.00 30.00 ? 121 GLN A CA  1 
ATOM   944  C C   . GLN A 1 121 ? 75.642  173.287 150.622 1.00 30.00 ? 121 GLN A C   1 
ATOM   945  O O   . GLN A 1 121 ? 75.739  174.413 151.129 1.00 30.00 ? 121 GLN A O   1 
ATOM   946  C CB  . GLN A 1 121 ? 73.853  171.858 149.608 1.00 30.00 ? 121 GLN A CB  1 
ATOM   947  C CG  . GLN A 1 121 ? 72.740  171.748 148.580 1.00 30.00 ? 121 GLN A CG  1 
ATOM   948  C CD  . GLN A 1 121 ? 71.836  172.957 148.612 1.00 30.00 ? 121 GLN A CD  1 
ATOM   949  O OE1 . GLN A 1 121 ? 71.225  173.271 149.631 1.00 30.00 ? 121 GLN A OE1 1 
ATOM   950  N NE2 . GLN A 1 121 ? 71.765  173.665 147.497 1.00 30.00 ? 121 GLN A NE2 1 
ATOM   951  N N   . ASN A 1 122 ? 76.317  172.218 151.034 1.00 30.00 ? 122 ASN A N   1 
ATOM   952  C CA  . ASN A 1 122 ? 77.208  172.243 152.220 1.00 30.00 ? 122 ASN A CA  1 
ATOM   953  C C   . ASN A 1 122 ? 78.611  171.886 151.727 1.00 30.00 ? 122 ASN A C   1 
ATOM   954  O O   . ASN A 1 122 ? 79.060  170.764 151.989 1.00 30.00 ? 122 ASN A O   1 
ATOM   955  C CB  . ASN A 1 122 ? 76.692  171.286 153.290 1.00 30.00 ? 122 ASN A CB  1 
ATOM   956  C CG  . ASN A 1 122 ? 75.256  171.574 153.673 1.00 30.00 ? 122 ASN A CG  1 
ATOM   957  O OD1 . ASN A 1 122 ? 74.950  172.642 154.198 1.00 30.00 ? 122 ASN A OD1 1 
ATOM   958  N ND2 . ASN A 1 122 ? 74.371  170.623 153.423 1.00 30.00 ? 122 ASN A ND2 1 
ATOM   959  N N   . PRO A 1 123 ? 79.312  172.780 151.006 1.00 30.00 ? 123 PRO A N   1 
ATOM   960  C CA  . PRO A 1 123 ? 80.605  172.422 150.440 1.00 30.00 ? 123 PRO A CA  1 
ATOM   961  C C   . PRO A 1 123 ? 81.604  172.070 151.545 1.00 30.00 ? 123 PRO A C   1 
ATOM   962  O O   . PRO A 1 123 ? 81.708  172.843 152.482 1.00 30.00 ? 123 PRO A O   1 
ATOM   963  C CB  . PRO A 1 123 ? 81.034  173.688 149.688 1.00 30.00 ? 123 PRO A CB  1 
ATOM   964  C CG  . PRO A 1 123 ? 80.239  174.799 150.328 1.00 30.00 ? 123 PRO A CG  1 
ATOM   965  C CD  . PRO A 1 123 ? 78.928  174.159 150.727 1.00 30.00 ? 123 PRO A CD  1 
ATOM   966  N N   . VAL A 1 124 ? 82.306  170.943 151.416 1.00 30.00 ? 124 VAL A N   1 
ATOM   967  C CA  . VAL A 1 124 ? 83.357  170.537 152.393 1.00 30.00 ? 124 VAL A CA  1 
ATOM   968  C C   . VAL A 1 124 ? 84.700  170.818 151.721 1.00 30.00 ? 124 VAL A C   1 
ATOM   969  O O   . VAL A 1 124 ? 84.926  170.273 150.627 1.00 30.00 ? 124 VAL A O   1 
ATOM   970  C CB  . VAL A 1 124 ? 83.251  169.063 152.817 1.00 30.00 ? 124 VAL A CB  1 
ATOM   971  C CG1 . VAL A 1 124 ? 84.318  168.695 153.836 1.00 30.00 ? 124 VAL A CG1 1 
ATOM   972  C CG2 . VAL A 1 124 ? 81.869  168.723 153.349 1.00 30.00 ? 124 VAL A CG2 1 
ATOM   973  N N   . PRO A 1 125 ? 85.573  171.659 152.314 1.00 30.00 ? 125 PRO A N   1 
ATOM   974  C CA  . PRO A 1 125 ? 86.853  172.009 151.702 1.00 30.00 ? 125 PRO A CA  1 
ATOM   975  C C   . PRO A 1 125 ? 87.866  170.907 152.031 1.00 30.00 ? 125 PRO A C   1 
ATOM   976  O O   . PRO A 1 125 ? 88.741  171.144 152.841 1.00 30.00 ? 125 PRO A O   1 
ATOM   977  C CB  . PRO A 1 125 ? 87.100  173.367 152.362 1.00 30.00 ? 125 PRO A CB  1 
ATOM   978  C CG  . PRO A 1 125 ? 86.608  173.183 153.770 1.00 30.00 ? 125 PRO A CG  1 
ATOM   979  C CD  . PRO A 1 125 ? 85.397  172.291 153.624 1.00 30.00 ? 125 PRO A CD  1 
ATOM   980  N N   . VAL A 1 126 ? 87.756  169.755 151.371 1.00 30.00 ? 126 VAL A N   1 
ATOM   981  C CA  . VAL A 1 126 ? 88.600  168.559 151.659 1.00 30.00 ? 126 VAL A CA  1 
ATOM   982  C C   . VAL A 1 126 ? 90.079  168.872 151.400 1.00 30.00 ? 126 VAL A C   1 
ATOM   983  O O   . VAL A 1 126 ? 90.903  168.407 152.179 1.00 30.00 ? 126 VAL A O   1 
ATOM   984  C CB  . VAL A 1 126 ? 88.120  167.332 150.857 1.00 30.00 ? 126 VAL A CB  1 
ATOM   985  C CG1 . VAL A 1 126 ? 86.739  166.884 151.308 1.00 30.00 ? 126 VAL A CG1 1 
ATOM   986  C CG2 . VAL A 1 126 ? 88.134  167.547 149.353 1.00 30.00 ? 126 VAL A CG2 1 
ATOM   987  N N   . GLY A 1 127 ? 90.389  169.639 150.361 1.00 30.00 ? 127 GLY A N   1 
ATOM   988  C CA  . GLY A 1 127 ? 91.772  170.005 150.029 1.00 30.00 ? 127 GLY A CA  1 
ATOM   989  C C   . GLY A 1 127 ? 92.426  170.783 151.146 1.00 30.00 ? 127 GLY A C   1 
ATOM   990  O O   . GLY A 1 127 ? 93.504  170.386 151.547 1.00 30.00 ? 127 GLY A O   1 
ATOM   991  N N   . ASN A 1 128 ? 91.740  171.753 151.745 1.00 30.00 ? 128 ASN A N   1 
ATOM   992  C CA  . ASN A 1 128 ? 92.355  172.621 152.782 1.00 30.00 ? 128 ASN A CA  1 
ATOM   993  C C   . ASN A 1 128 ? 92.465  171.861 154.109 1.00 30.00 ? 128 ASN A C   1 
ATOM   994  O O   . ASN A 1 128 ? 93.478  172.054 154.803 1.00 30.00 ? 128 ASN A O   1 
ATOM   995  C CB  . ASN A 1 128 ? 91.562  173.915 152.936 1.00 30.00 ? 128 ASN A CB  1 
ATOM   996  C CG  . ASN A 1 128 ? 91.496  174.708 151.649 1.00 30.00 ? 128 ASN A CG  1 
ATOM   997  O OD1 . ASN A 1 128 ? 92.524  175.033 151.065 1.00 30.00 ? 128 ASN A OD1 1 
ATOM   998  N ND2 . ASN A 1 128 ? 90.295  174.985 151.173 1.00 30.00 ? 128 ASN A ND2 1 
ATOM   999  N N   . ILE A 1 129 ? 91.489  171.012 154.445 1.00 30.00 ? 129 ILE A N   1 
ATOM   1000 C CA  . ILE A 1 129 ? 91.509  170.205 155.703 1.00 30.00 ? 129 ILE A CA  1 
ATOM   1001 C C   . ILE A 1 129 ? 92.731  169.285 155.657 1.00 30.00 ? 129 ILE A C   1 
ATOM   1002 O O   . ILE A 1 129 ? 93.435  169.200 156.680 1.00 30.00 ? 129 ILE A O   1 
ATOM   1003 C CB  . ILE A 1 129 ? 90.197  169.409 155.866 1.00 30.00 ? 129 ILE A CB  1 
ATOM   1004 C CG1 . ILE A 1 129 ? 88.984  170.337 155.985 1.00 30.00 ? 129 ILE A CG1 1 
ATOM   1005 C CG2 . ILE A 1 129 ? 90.286  168.452 157.041 1.00 30.00 ? 129 ILE A CG2 1 
ATOM   1006 C CD1 . ILE A 1 129 ? 87.666  169.666 155.691 1.00 30.00 ? 129 ILE A CD1 1 
ATOM   1007 N N   . TYR A 1 130 ? 92.982  168.629 154.523 1.00 30.00 ? 130 TYR A N   1 
ATOM   1008 C CA  . TYR A 1 130 ? 94.110  167.675 154.356 1.00 30.00 ? 130 TYR A CA  1 
ATOM   1009 C C   . TYR A 1 130 ? 95.443  168.431 154.380 1.00 30.00 ? 130 TYR A C   1 
ATOM   1010 O O   . TYR A 1 130 ? 96.406  167.893 154.957 1.00 30.00 ? 130 TYR A O   1 
ATOM   1011 C CB  . TYR A 1 130 ? 93.872  166.864 153.081 1.00 30.00 ? 130 TYR A CB  1 
ATOM   1012 C CG  . TYR A 1 130 ? 94.856  165.761 152.807 1.00 30.00 ? 130 TYR A CG  1 
ATOM   1013 C CD1 . TYR A 1 130 ? 95.247  164.888 153.807 1.00 30.00 ? 130 TYR A CD1 1 
ATOM   1014 C CD2 . TYR A 1 130 ? 95.296  165.511 151.520 1.00 30.00 ? 130 TYR A CD2 1 
ATOM   1015 C CE1 . TYR A 1 130 ? 96.121  163.848 153.553 1.00 30.00 ? 130 TYR A CE1 1 
ATOM   1016 C CE2 . TYR A 1 130 ? 96.161  164.468 151.244 1.00 30.00 ? 130 TYR A CE2 1 
ATOM   1017 C CZ  . TYR A 1 130 ? 96.575  163.635 152.266 1.00 30.00 ? 130 TYR A CZ  1 
ATOM   1018 O OH  . TYR A 1 130 ? 97.431  162.603 152.009 1.00 30.00 ? 130 TYR A OH  1 
ATOM   1019 N N   . ARG A 1 131 ? 95.507  169.628 153.789 1.00 30.00 ? 131 ARG A N   1 
ATOM   1020 C CA  . ARG A 1 131 ? 96.732  170.472 153.816 1.00 30.00 ? 131 ARG A CA  1 
ATOM   1021 C C   . ARG A 1 131 ? 97.029  170.829 155.273 1.00 30.00 ? 131 ARG A C   1 
ATOM   1022 O O   . ARG A 1 131 ? 98.214  170.809 155.646 1.00 30.00 ? 131 ARG A O   1 
ATOM   1023 C CB  . ARG A 1 131 ? 96.543  171.730 152.966 1.00 30.00 ? 131 ARG A CB  1 
ATOM   1024 C CG  . ARG A 1 131 ? 96.529  171.454 151.472 1.00 30.00 ? 131 ARG A CG  1 
ATOM   1025 C CD  . ARG A 1 131 ? 96.012  172.610 150.646 1.00 30.00 ? 131 ARG A CD  1 
ATOM   1026 N NE  . ARG A 1 131 ? 96.899  173.762 150.707 1.00 30.00 ? 131 ARG A NE  1 
ATOM   1027 C CZ  . ARG A 1 131 ? 96.572  174.987 151.103 1.00 30.00 ? 131 ARG A CZ  1 
ATOM   1028 N NH1 . ARG A 1 131 ? 95.349  175.283 151.504 1.00 30.00 ? 131 ARG A NH1 1 
ATOM   1029 N NH2 . ARG A 1 131 ? 97.487  175.936 151.085 1.00 30.00 ? 131 ARG A NH2 1 
ATOM   1030 N N   . ARG A 1 132 ? 95.995  171.121 156.066 1.00 30.00 ? 132 ARG A N   1 
ATOM   1031 C CA  . ARG A 1 132 ? 96.149  171.465 157.504 1.00 30.00 ? 132 ARG A CA  1 
ATOM   1032 C C   . ARG A 1 132 ? 96.705  170.245 158.247 1.00 30.00 ? 132 ARG A C   1 
ATOM   1033 O O   . ARG A 1 132 ? 97.626  170.431 159.048 1.00 30.00 ? 132 ARG A O   1 
ATOM   1034 C CB  . ARG A 1 132 ? 94.801  171.928 158.063 1.00 30.00 ? 132 ARG A CB  1 
ATOM   1035 C CG  . ARG A 1 132 ? 94.838  172.461 159.486 1.00 30.00 ? 132 ARG A CG  1 
ATOM   1036 C CD  . ARG A 1 132 ? 93.448  172.898 159.901 1.00 30.00 ? 132 ARG A CD  1 
ATOM   1037 N NE  . ARG A 1 132 ? 92.896  173.863 158.958 1.00 30.00 ? 132 ARG A NE  1 
ATOM   1038 C CZ  . ARG A 1 132 ? 91.815  173.672 158.208 1.00 30.00 ? 132 ARG A CZ  1 
ATOM   1039 N NH1 . ARG A 1 132 ? 90.934  172.735 158.509 1.00 30.00 ? 132 ARG A NH1 1 
ATOM   1040 N NH2 . ARG A 1 132 ? 91.609  174.443 157.155 1.00 30.00 ? 132 ARG A NH2 1 
ATOM   1041 N N   . TRP A 1 133 ? 96.199  169.043 157.963 1.00 30.00 ? 133 TRP A N   1 
ATOM   1042 C CA  . TRP A 1 133 ? 96.664  167.790 158.618 1.00 30.00 ? 133 TRP A CA  1 
ATOM   1043 C C   . TRP A 1 133 ? 98.143  167.566 158.296 1.00 30.00 ? 133 TRP A C   1 
ATOM   1044 O O   . TRP A 1 133 ? 98.892  167.200 159.221 1.00 30.00 ? 133 TRP A O   1 
ATOM   1045 C CB  . TRP A 1 133 ? 95.827  166.599 158.146 1.00 30.00 ? 133 TRP A CB  1 
ATOM   1046 C CG  . TRP A 1 133 ? 94.380  166.634 158.526 1.00 30.00 ? 133 TRP A CG  1 
ATOM   1047 C CD1 . TRP A 1 133 ? 93.733  167.579 159.267 1.00 30.00 ? 133 TRP A CD1 1 
ATOM   1048 C CD2 . TRP A 1 133 ? 93.383  165.671 158.148 1.00 30.00 ? 133 TRP A CD2 1 
ATOM   1049 N NE1 . TRP A 1 133 ? 92.409  167.262 159.387 1.00 30.00 ? 133 TRP A NE1 1 
ATOM   1050 C CE2 . TRP A 1 133 ? 92.165  166.095 158.714 1.00 30.00 ? 133 TRP A CE2 1 
ATOM   1051 C CE3 . TRP A 1 133 ? 93.405  164.490 157.399 1.00 30.00 ? 133 TRP A CE3 1 
ATOM   1052 C CZ2 . TRP A 1 133 ? 90.980  165.384 158.545 1.00 30.00 ? 133 TRP A CZ2 1 
ATOM   1053 C CZ3 . TRP A 1 133 ? 92.234  163.785 157.237 1.00 30.00 ? 133 TRP A CZ3 1 
ATOM   1054 C CH2 . TRP A 1 133 ? 91.041  164.230 157.801 1.00 30.00 ? 133 TRP A CH2 1 
ATOM   1055 N N   . ILE A 1 134 ? 98.546  167.774 157.041 1.00 30.00 ? 134 ILE A N   1 
ATOM   1056 C CA  . ILE A 1 134 ? 99.953  167.571 156.579 1.00 30.00 ? 134 ILE A CA  1 
ATOM   1057 C C   . ILE A 1 134 ? 100.857 168.631 157.206 1.00 30.00 ? 134 ILE A C   1 
ATOM   1058 O O   . ILE A 1 134 ? 102.016 168.309 157.491 1.00 30.00 ? 134 ILE A O   1 
ATOM   1059 C CB  . ILE A 1 134 ? 99.993  167.589 155.041 1.00 30.00 ? 134 ILE A CB  1 
ATOM   1060 C CG1 . ILE A 1 134 ? 99.365  166.302 154.505 1.00 30.00 ? 134 ILE A CG1 1 
ATOM   1061 C CG2 . ILE A 1 134 ? 101.403 167.794 154.508 1.00 30.00 ? 134 ILE A CG2 1 
ATOM   1062 C CD1 . ILE A 1 134 ? 98.956  166.381 153.081 1.00 30.00 ? 134 ILE A CD1 1 
ATOM   1063 N N   . GLN A 1 135 ? 100.349 169.851 157.366 1.00 30.00 ? 135 GLN A N   1 
ATOM   1064 C CA  . GLN A 1 135 ? 101.136 170.931 158.021 1.00 30.00 ? 135 GLN A CA  1 
ATOM   1065 C C   . GLN A 1 135 ? 101.408 170.530 159.474 1.00 30.00 ? 135 GLN A C   1 
ATOM   1066 O O   . GLN A 1 135 ? 102.529 170.798 159.932 1.00 30.00 ? 135 GLN A O   1 
ATOM   1067 C CB  . GLN A 1 135 ? 100.422 172.264 157.820 1.00 30.00 ? 135 GLN A CB  1 
ATOM   1068 C CG  . GLN A 1 135 ? 100.673 172.788 156.411 1.00 30.00 ? 135 GLN A CG  1 
ATOM   1069 C CD  . GLN A 1 135 ? 99.940  174.050 156.034 1.00 30.00 ? 135 GLN A CD  1 
ATOM   1070 O OE1 . GLN A 1 135 ? 99.175  174.071 155.073 1.00 30.00 ? 135 GLN A OE1 1 
ATOM   1071 N NE2 . GLN A 1 135 ? 100.207 175.124 156.758 1.00 30.00 ? 135 GLN A NE2 1 
ATOM   1072 N N   . ILE A 1 136 ? 100.458 169.882 160.151 1.00 30.00 ? 136 ILE A N   1 
ATOM   1073 C CA  . ILE A 1 136 ? 100.744 169.382 161.529 1.00 30.00 ? 136 ILE A CA  1 
ATOM   1074 C C   . ILE A 1 136 ? 101.865 168.341 161.422 1.00 30.00 ? 136 ILE A C   1 
ATOM   1075 O O   . ILE A 1 136 ? 102.766 168.365 162.279 1.00 30.00 ? 136 ILE A O   1 
ATOM   1076 C CB  . ILE A 1 136 ? 99.468  168.825 162.196 1.00 30.00 ? 136 ILE A CB  1 
ATOM   1077 C CG1 . ILE A 1 136 ? 98.370  169.887 162.291 1.00 30.00 ? 136 ILE A CG1 1 
ATOM   1078 C CG2 . ILE A 1 136 ? 99.785  168.220 163.552 1.00 30.00 ? 136 ILE A CG2 1 
ATOM   1079 C CD1 . ILE A 1 136 ? 96.993  169.327 162.549 1.00 30.00 ? 136 ILE A CD1 1 
ATOM   1080 N N   . GLY A 1 137 ? 101.829 167.472 160.405 1.00 30.00 ? 137 GLY A N   1 
ATOM   1081 C CA  . GLY A 1 137 ? 102.859 166.433 160.196 1.00 30.00 ? 137 GLY A CA  1 
ATOM   1082 C C   . GLY A 1 137 ? 104.220 167.022 159.858 1.00 30.00 ? 137 GLY A C   1 
ATOM   1083 O O   . GLY A 1 137 ? 105.218 166.528 160.418 1.00 30.00 ? 137 GLY A O   1 
ATOM   1084 N N   . LEU A 1 138 ? 104.277 168.032 158.984 1.00 30.00 ? 138 LEU A N   1 
ATOM   1085 C CA  . LEU A 1 138 ? 105.548 168.687 158.567 1.00 30.00 ? 138 LEU A CA  1 
ATOM   1086 C C   . LEU A 1 138 ? 106.124 169.477 159.745 1.00 30.00 ? 138 LEU A C   1 
ATOM   1087 O O   . LEU A 1 138 ? 107.349 169.472 159.900 1.00 30.00 ? 138 LEU A O   1 
ATOM   1088 C CB  . LEU A 1 138 ? 105.284 169.619 157.381 1.00 30.00 ? 138 LEU A CB  1 
ATOM   1089 C CG  . LEU A 1 138 ? 105.036 168.958 156.029 1.00 30.00 ? 138 LEU A CG  1 
ATOM   1090 C CD1 . LEU A 1 138 ? 104.578 169.991 155.011 1.00 30.00 ? 138 LEU A CD1 1 
ATOM   1091 C CD2 . LEU A 1 138 ? 106.289 168.249 155.537 1.00 30.00 ? 138 LEU A CD2 1 
ATOM   1092 N N   . GLN A 1 139 ? 105.268 170.152 160.516 1.00 30.00 ? 139 GLN A N   1 
ATOM   1093 C CA  . GLN A 1 139 ? 105.726 170.939 161.694 1.00 30.00 ? 139 GLN A CA  1 
ATOM   1094 C C   . GLN A 1 139 ? 106.337 169.983 162.721 1.00 30.00 ? 139 GLN A C   1 
ATOM   1095 O O   . GLN A 1 139 ? 107.348 170.347 163.301 1.00 30.00 ? 139 GLN A O   1 
ATOM   1096 C CB  . GLN A 1 139 ? 104.599 171.768 162.309 1.00 30.00 ? 139 GLN A CB  1 
ATOM   1097 C CG  . GLN A 1 139 ? 105.043 172.624 163.483 1.00 30.00 ? 139 GLN A CG  1 
ATOM   1098 C CD  . GLN A 1 139 ? 106.220 173.513 163.161 1.00 30.00 ? 139 GLN A CD  1 
ATOM   1099 O OE1 . GLN A 1 139 ? 106.170 174.342 162.256 1.00 30.00 ? 139 GLN A OE1 1 
ATOM   1100 N NE2 . GLN A 1 139 ? 107.303 173.334 163.901 1.00 30.00 ? 139 GLN A NE2 1 
ATOM   1101 N N   . LYS A 1 140 ? 105.760 168.794 162.891 1.00 30.00 ? 140 LYS A N   1 
ATOM   1102 C CA  . LYS A 1 140 ? 106.398 167.800 163.793 1.00 30.00 ? 140 LYS A CA  1 
ATOM   1103 C C   . LYS A 1 140 ? 107.753 167.394 163.205 1.00 30.00 ? 140 LYS A C   1 
ATOM   1104 O O   . LYS A 1 140 ? 108.656 167.138 164.010 1.00 30.00 ? 140 LYS A O   1 
ATOM   1105 C CB  . LYS A 1 140 ? 105.484 166.594 164.000 1.00 30.00 ? 140 LYS A CB  1 
ATOM   1106 C CG  . LYS A 1 140 ? 106.044 165.501 164.894 1.00 30.00 ? 140 LYS A CG  1 
ATOM   1107 C CD  . LYS A 1 140 ? 105.033 164.431 165.209 1.00 30.00 ? 140 LYS A CD  1 
ATOM   1108 C CE  . LYS A 1 140 ? 105.620 163.293 166.014 1.00 30.00 ? 140 LYS A CE  1 
ATOM   1109 N NZ  . LYS A 1 140 ? 104.603 162.258 166.306 1.00 30.00 ? 140 LYS A NZ  1 
ATOM   1110 N N   . CYS A 1 141 ? 107.883 167.280 161.876 1.00 30.00 ? 141 CYS A N   1 
ATOM   1111 C CA  . CYS A 1 141 ? 109.170 166.951 161.197 1.00 30.00 ? 141 CYS A CA  1 
ATOM   1112 C C   . CYS A 1 141 ? 110.158 168.115 161.360 1.00 30.00 ? 141 CYS A C   1 
ATOM   1113 O O   . CYS A 1 141 ? 111.347 167.827 161.511 1.00 30.00 ? 141 CYS A O   1 
ATOM   1114 C CB  . CYS A 1 141 ? 108.994 166.631 159.714 1.00 30.00 ? 141 CYS A CB  1 
ATOM   1115 S SG  . CYS A 1 141 ? 108.028 165.139 159.404 1.00 30.00 ? 141 CYS A SG  1 
ATOM   1116 N N   . VAL A 1 142 ? 109.700 169.372 161.313 1.00 30.00 ? 142 VAL A N   1 
ATOM   1117 C CA  . VAL A 1 142 ? 110.577 170.569 161.501 1.00 30.00 ? 142 VAL A CA  1 
ATOM   1118 C C   . VAL A 1 142 ? 111.182 170.484 162.900 1.00 30.00 ? 142 VAL A C   1 
ATOM   1119 O O   . VAL A 1 142 ? 112.396 170.708 163.024 1.00 30.00 ? 142 VAL A O   1 
ATOM   1120 C CB  . VAL A 1 142 ? 109.825 171.902 161.309 1.00 30.00 ? 142 VAL A CB  1 
ATOM   1121 C CG1 . VAL A 1 142 ? 110.613 173.090 161.833 1.00 30.00 ? 142 VAL A CG1 1 
ATOM   1122 C CG2 . VAL A 1 142 ? 109.437 172.117 159.856 1.00 30.00 ? 142 VAL A CG2 1 
ATOM   1123 N N   . ARG A 1 143 ? 110.374 170.174 163.912 1.00 30.00 ? 143 ARG A N   1 
ATOM   1124 C CA  . ARG A 1 143 ? 110.835 170.087 165.323 1.00 30.00 ? 143 ARG A CA  1 
ATOM   1125 C C   . ARG A 1 143 ? 111.814 168.918 165.486 1.00 30.00 ? 143 ARG A C   1 
ATOM   1126 O O   . ARG A 1 143 ? 112.850 169.130 166.116 1.00 30.00 ? 143 ARG A O   1 
ATOM   1127 C CB  . ARG A 1 143 ? 109.644 169.939 166.271 1.00 30.00 ? 143 ARG A CB  1 
ATOM   1128 C CG  . ARG A 1 143 ? 110.050 169.844 167.735 1.00 30.00 ? 143 ARG A CG  1 
ATOM   1129 C CD  . ARG A 1 143 ? 108.869 169.886 168.681 1.00 30.00 ? 143 ARG A CD  1 
ATOM   1130 N NE  . ARG A 1 143 ? 107.919 168.801 168.475 1.00 30.00 ? 143 ARG A NE  1 
ATOM   1131 C CZ  . ARG A 1 143 ? 108.180 167.509 168.633 1.00 30.00 ? 143 ARG A CZ  1 
ATOM   1132 N NH1 . ARG A 1 143 ? 107.261 166.614 168.319 1.00 30.00 ? 143 ARG A NH1 1 
ATOM   1133 N NH2 . ARG A 1 143 ? 109.350 167.108 169.098 1.00 30.00 ? 143 ARG A NH2 1 
ATOM   1134 N N   . MET A 1 144 ? 111.529 167.757 164.893 1.00 30.00 ? 144 MET A N   1 
ATOM   1135 C CA  . MET A 1 144 ? 112.370 166.539 165.051 1.00 30.00 ? 144 MET A CA  1 
ATOM   1136 C C   . MET A 1 144 ? 113.749 166.771 164.431 1.00 30.00 ? 144 MET A C   1 
ATOM   1137 O O   . MET A 1 144 ? 114.733 166.290 165.027 1.00 30.00 ? 144 MET A O   1 
ATOM   1138 C CB  . MET A 1 144 ? 111.709 165.348 164.353 1.00 30.00 ? 144 MET A CB  1 
ATOM   1139 C CG  . MET A 1 144 ? 112.612 164.172 164.144 1.00 30.00 ? 144 MET A CG  1 
ATOM   1140 S SD  . MET A 1 144 ? 111.633 162.717 163.758 1.00 30.00 ? 144 MET A SD  1 
ATOM   1141 C CE  . MET A 1 144 ? 112.012 162.530 162.017 1.00 30.00 ? 144 MET A CE  1 
ATOM   1142 N N   . TYR A 1 145 ? 113.834 167.480 163.304 1.00 30.00 ? 145 TYR A N   1 
ATOM   1143 C CA  . TYR A 1 145 ? 115.100 167.689 162.552 1.00 30.00 ? 145 TYR A CA  1 
ATOM   1144 C C   . TYR A 1 145 ? 115.716 169.053 162.873 1.00 30.00 ? 145 TYR A C   1 
ATOM   1145 O O   . TYR A 1 145 ? 116.777 169.366 162.299 1.00 30.00 ? 145 TYR A O   1 
ATOM   1146 C CB  . TYR A 1 145 ? 114.830 167.570 161.053 1.00 30.00 ? 145 TYR A CB  1 
ATOM   1147 C CG  . TYR A 1 145 ? 114.546 166.169 160.586 1.00 30.00 ? 145 TYR A CG  1 
ATOM   1148 C CD1 . TYR A 1 145 ? 115.497 165.173 160.716 1.00 30.00 ? 145 TYR A CD1 1 
ATOM   1149 C CD2 . TYR A 1 145 ? 113.324 165.836 160.030 1.00 30.00 ? 145 TYR A CD2 1 
ATOM   1150 C CE1 . TYR A 1 145 ? 115.249 163.882 160.286 1.00 30.00 ? 145 TYR A CE1 1 
ATOM   1151 C CE2 . TYR A 1 145 ? 113.061 164.550 159.592 1.00 30.00 ? 145 TYR A CE2 1 
ATOM   1152 C CZ  . TYR A 1 145 ? 114.029 163.571 159.718 1.00 30.00 ? 145 TYR A CZ  1 
ATOM   1153 O OH  . TYR A 1 145 ? 113.771 162.291 159.307 1.00 30.00 ? 145 TYR A OH  1 
ATOM   1154 N N   . ASN A 1 146 ? 115.101 169.834 163.765 1.00 30.00 ? 146 ASN A N   1 
ATOM   1155 C CA  . ASN A 1 146 ? 115.638 171.162 164.157 1.00 30.00 ? 146 ASN A CA  1 
ATOM   1156 C C   . ASN A 1 146 ? 117.073 170.965 164.654 1.00 30.00 ? 146 ASN A C   1 
ATOM   1157 O O   . ASN A 1 146 ? 117.260 170.189 165.610 1.00 30.00 ? 146 ASN A O   1 
ATOM   1158 C CB  . ASN A 1 146 ? 114.758 171.842 165.203 1.00 30.00 ? 146 ASN A CB  1 
ATOM   1159 C CG  . ASN A 1 146 ? 115.409 173.049 165.840 1.00 30.00 ? 146 ASN A CG  1 
ATOM   1160 O OD1 . ASN A 1 146 ? 115.479 173.147 167.059 1.00 30.00 ? 146 ASN A OD1 1 
ATOM   1161 N ND2 . ASN A 1 146 ? 115.828 174.003 165.030 1.00 30.00 ? 146 ASN A ND2 1 
ATOM   1162 N N   . PRO A 1 147 ? 118.086 171.642 164.071 1.00 30.00 ? 147 PRO A N   1 
ATOM   1163 C CA  . PRO A 1 147 ? 119.484 171.417 164.458 1.00 30.00 ? 147 PRO A CA  1 
ATOM   1164 C C   . PRO A 1 147 ? 119.910 172.114 165.759 1.00 30.00 ? 147 PRO A C   1 
ATOM   1165 O O   . PRO A 1 147 ? 120.715 171.529 166.461 1.00 30.00 ? 147 PRO A O   1 
ATOM   1166 C CB  . PRO A 1 147 ? 120.248 172.002 163.260 1.00 30.00 ? 147 PRO A CB  1 
ATOM   1167 C CG  . PRO A 1 147 ? 119.366 173.106 162.754 1.00 30.00 ? 147 PRO A CG  1 
ATOM   1168 C CD  . PRO A 1 147 ? 117.963 172.582 162.953 1.00 30.00 ? 147 PRO A CD  1 
ATOM   1169 N N   . THR A 1 148 ? 119.387 173.310 166.056 1.00 30.00 ? 148 THR A N   1 
ATOM   1170 C CA  . THR A 1 148 ? 119.759 174.096 167.262 1.00 30.00 ? 148 THR A CA  1 
ATOM   1171 C C   . THR A 1 148 ? 118.522 174.394 168.106 1.00 30.00 ? 148 THR A C   1 
ATOM   1172 O O   . THR A 1 148 ? 117.539 174.905 167.539 1.00 30.00 ? 148 THR A O   1 
ATOM   1173 C CB  . THR A 1 148 ? 120.438 175.413 166.883 1.00 30.00 ? 148 THR A CB  1 
ATOM   1174 O OG1 . THR A 1 148 ? 121.535 175.111 166.022 1.00 30.00 ? 148 THR A OG1 1 
ATOM   1175 C CG2 . THR A 1 148 ? 120.929 176.192 168.083 1.00 30.00 ? 148 THR A CG2 1 
ATOM   1176 N N   . ASN A 1 149 ? 118.596 174.141 169.411 1.00 30.00 ? 149 ASN A N   1 
ATOM   1177 C CA  . ASN A 1 149 ? 117.468 174.398 170.339 1.00 30.00 ? 149 ASN A CA  1 
ATOM   1178 C C   . ASN A 1 149 ? 117.462 175.888 170.684 1.00 30.00 ? 149 ASN A C   1 
ATOM   1179 O O   . ASN A 1 149 ? 118.548 176.497 170.658 1.00 30.00 ? 149 ASN A O   1 
ATOM   1180 C CB  . ASN A 1 149 ? 117.569 173.521 171.585 1.00 30.00 ? 149 ASN A CB  1 
ATOM   1181 C CG  . ASN A 1 149 ? 116.395 173.686 172.523 1.00 30.00 ? 149 ASN A CG  1 
ATOM   1182 O OD1 . ASN A 1 149 ? 116.563 174.102 173.666 1.00 30.00 ? 149 ASN A OD1 1 
ATOM   1183 N ND2 . ASN A 1 149 ? 115.203 173.373 172.045 1.00 30.00 ? 149 ASN A ND2 1 
ATOM   1184 N N   . ILE A 1 150 ? 116.288 176.452 170.962 1.00 30.00 ? 150 ILE A N   1 
ATOM   1185 C CA  . ILE A 1 150 ? 116.144 177.890 171.321 1.00 30.00 ? 150 ILE A CA  1 
ATOM   1186 C C   . ILE A 1 150 ? 117.127 178.244 172.440 1.00 30.00 ? 150 ILE A C   1 
ATOM   1187 O O   . ILE A 1 150 ? 117.778 179.298 172.322 1.00 30.00 ? 150 ILE A O   1 
ATOM   1188 C CB  . ILE A 1 150 ? 114.685 178.178 171.724 1.00 30.00 ? 150 ILE A CB  1 
ATOM   1189 C CG1 . ILE A 1 150 ? 114.462 179.670 171.980 1.00 30.00 ? 150 ILE A CG1 1 
ATOM   1190 C CG2 . ILE A 1 150 ? 114.245 177.347 172.920 1.00 30.00 ? 150 ILE A CG2 1 
ATOM   1191 C CD1 . ILE A 1 150 ? 114.691 180.530 170.776 1.00 30.00 ? 150 ILE A CD1 1 
ATOM   1192 N N   . LEU A 1 151 ? 117.244 177.405 173.472 1.00 30.00 ? 151 LEU A N   1 
ATOM   1193 C CA  . LEU A 1 151 ? 118.103 177.688 174.654 1.00 30.00 ? 151 LEU A CA  1 
ATOM   1194 C C   . LEU A 1 151 ? 119.575 177.782 174.246 1.00 30.00 ? 151 LEU A C   1 
ATOM   1195 O O   . LEU A 1 151 ? 120.250 178.713 174.718 1.00 30.00 ? 151 LEU A O   1 
ATOM   1196 C CB  . LEU A 1 151 ? 117.911 176.558 175.669 1.00 30.00 ? 151 LEU A CB  1 
ATOM   1197 C CG  . LEU A 1 151 ? 116.522 176.429 176.293 1.00 30.00 ? 151 LEU A CG  1 
ATOM   1198 C CD1 . LEU A 1 151 ? 116.581 175.560 177.536 1.00 30.00 ? 151 LEU A CD1 1 
ATOM   1199 C CD2 . LEU A 1 151 ? 115.927 177.787 176.631 1.00 30.00 ? 151 LEU A CD2 1 
ATOM   1200 N N   . ASP A 1 152 ? 120.056 176.874 173.397 1.00 30.00 ? 152 ASP A N   1 
ATOM   1201 C CA  . ASP A 1 152 ? 121.491 176.820 173.009 1.00 30.00 ? 152 ASP A CA  1 
ATOM   1202 C C   . ASP A 1 152 ? 121.896 178.097 172.273 1.00 30.00 ? 152 ASP A C   1 
ATOM   1203 O O   . ASP A 1 152 ? 123.050 178.528 172.455 1.00 30.00 ? 152 ASP A O   1 
ATOM   1204 C CB  . ASP A 1 152 ? 121.777 175.587 172.157 1.00 30.00 ? 152 ASP A CB  1 
ATOM   1205 C CG  . ASP A 1 152 ? 121.835 174.311 172.979 1.00 30.00 ? 152 ASP A CG  1 
ATOM   1206 O OD1 . ASP A 1 152 ? 122.724 174.217 173.842 1.00 30.00 ? 152 ASP A OD1 1 
ATOM   1207 O OD2 . ASP A 1 152 ? 120.979 173.434 172.763 1.00 30.00 ? 152 ASP A OD2 1 
ATOM   1208 N N   . VAL A 1 153 ? 121.003 178.667 171.464 1.00 30.00 ? 153 VAL A N   1 
ATOM   1209 C CA  . VAL A 1 153 ? 121.325 179.877 170.655 1.00 30.00 ? 153 VAL A CA  1 
ATOM   1210 C C   . VAL A 1 153 ? 121.864 180.946 171.609 1.00 30.00 ? 153 VAL A C   1 
ATOM   1211 O O   . VAL A 1 153 ? 121.128 181.310 172.543 1.00 30.00 ? 153 VAL A O   1 
ATOM   1212 C CB  . VAL A 1 153 ? 120.087 180.376 169.892 1.00 30.00 ? 153 VAL A CB  1 
ATOM   1213 C CG1 . VAL A 1 153 ? 120.341 181.701 169.189 1.00 30.00 ? 153 VAL A CG1 1 
ATOM   1214 C CG2 . VAL A 1 153 ? 119.563 179.346 168.904 1.00 30.00 ? 153 VAL A CG2 1 
ATOM   1215 N N   . LYS A 1 154 ? 123.101 181.414 171.403 1.00 30.00 ? 154 LYS A N   1 
ATOM   1216 C CA  . LYS A 1 154 ? 123.736 182.458 172.254 1.00 30.00 ? 154 LYS A CA  1 
ATOM   1217 C C   . LYS A 1 154 ? 124.528 183.401 171.346 1.00 30.00 ? 154 LYS A C   1 
ATOM   1218 O O   . LYS A 1 154 ? 125.379 182.897 170.592 1.00 30.00 ? 154 LYS A O   1 
ATOM   1219 C CB  . LYS A 1 154 ? 124.607 181.797 173.329 1.00 30.00 ? 154 LYS A CB  1 
ATOM   1220 C CG  . LYS A 1 154 ? 123.814 181.109 174.431 1.00 30.00 ? 154 LYS A CG  1 
ATOM   1221 C CD  . LYS A 1 154 ? 124.646 180.295 175.382 1.00 30.00 ? 154 LYS A CD  1 
ATOM   1222 C CE  . LYS A 1 154 ? 123.799 179.560 176.399 1.00 30.00 ? 154 LYS A CE  1 
ATOM   1223 N NZ  . LYS A 1 154 ? 123.046 178.445 175.779 1.00 30.00 ? 154 LYS A NZ  1 
ATOM   1224 N N   . GLN A 1 155 ? 124.298 184.714 171.440 1.00 30.00 ? 155 GLN A N   1 
ATOM   1225 C CA  . GLN A 1 155 ? 124.946 185.711 170.546 1.00 30.00 ? 155 GLN A CA  1 
ATOM   1226 C C   . GLN A 1 155 ? 126.463 185.561 170.596 1.00 30.00 ? 155 GLN A C   1 
ATOM   1227 O O   . GLN A 1 155 ? 127.003 185.431 171.711 1.00 30.00 ? 155 GLN A O   1 
ATOM   1228 C CB  . GLN A 1 155 ? 124.597 187.131 170.985 1.00 30.00 ? 155 GLN A CB  1 
ATOM   1229 C CG  . GLN A 1 155 ? 125.138 188.226 170.080 1.00 30.00 ? 155 GLN A CG  1 
ATOM   1230 C CD  . GLN A 1 155 ? 124.746 189.606 170.550 1.00 30.00 ? 155 GLN A CD  1 
ATOM   1231 O OE1 . GLN A 1 155 ? 124.054 189.776 171.549 1.00 30.00 ? 155 GLN A OE1 1 
ATOM   1232 N NE2 . GLN A 1 155 ? 125.201 190.617 169.832 1.00 30.00 ? 155 GLN A NE2 1 
ATOM   1233 N N   . GLY A 1 156 ? 127.127 185.593 169.441 1.00 30.00 ? 156 GLY A N   1 
ATOM   1234 C CA  . GLY A 1 156 ? 128.598 185.551 169.388 1.00 30.00 ? 156 GLY A CA  1 
ATOM   1235 C C   . GLY A 1 156 ? 129.164 186.859 169.909 1.00 30.00 ? 156 GLY A C   1 
ATOM   1236 O O   . GLY A 1 156 ? 128.467 187.882 169.798 1.00 30.00 ? 156 GLY A O   1 
ATOM   1237 N N   . PRO A 1 157 ? 130.399 186.906 170.447 1.00 30.00 ? 157 PRO A N   1 
ATOM   1238 C CA  . PRO A 1 157 ? 130.921 188.136 171.035 1.00 30.00 ? 157 PRO A CA  1 
ATOM   1239 C C   . PRO A 1 157 ? 130.879 189.278 170.016 1.00 30.00 ? 157 PRO A C   1 
ATOM   1240 O O   . PRO A 1 157 ? 130.645 190.399 170.425 1.00 30.00 ? 157 PRO A O   1 
ATOM   1241 C CB  . PRO A 1 157 ? 132.375 187.791 171.374 1.00 30.00 ? 157 PRO A CB  1 
ATOM   1242 C CG  . PRO A 1 157 ? 132.372 186.290 171.535 1.00 30.00 ? 157 PRO A CG  1 
ATOM   1243 C CD  . PRO A 1 157 ? 131.340 185.793 170.547 1.00 30.00 ? 157 PRO A CD  1 
ATOM   1244 N N   . LYS A 1 158 ? 131.125 188.979 168.739 1.00 30.00 ? 158 LYS A N   1 
ATOM   1245 C CA  . LYS A 1 158 ? 131.135 189.996 167.656 1.00 30.00 ? 158 LYS A CA  1 
ATOM   1246 C C   . LYS A 1 158 ? 129.845 189.946 166.844 1.00 30.00 ? 158 LYS A C   1 
ATOM   1247 O O   . LYS A 1 158 ? 129.591 190.914 166.101 1.00 30.00 ? 158 LYS A O   1 
ATOM   1248 C CB  . LYS A 1 158 ? 132.271 189.717 166.676 1.00 30.00 ? 158 LYS A CB  1 
ATOM   1249 C CG  . LYS A 1 158 ? 133.565 189.216 167.293 1.00 30.00 ? 158 LYS A CG  1 
ATOM   1250 C CD  . LYS A 1 158 ? 134.115 190.112 168.371 1.00 30.00 ? 158 LYS A CD  1 
ATOM   1251 C CE  . LYS A 1 158 ? 135.568 189.811 168.667 1.00 30.00 ? 158 LYS A CE  1 
ATOM   1252 N NZ  . LYS A 1 158 ? 135.753 188.391 169.046 1.00 30.00 ? 158 LYS A NZ  1 
ATOM   1253 N N   . GLU A 1 159 ? 129.062 188.875 166.966 1.00 30.00 ? 159 GLU A N   1 
ATOM   1254 C CA  . GLU A 1 159 ? 127.852 188.703 166.125 1.00 30.00 ? 159 GLU A CA  1 
ATOM   1255 C C   . GLU A 1 159 ? 126.948 189.928 166.287 1.00 30.00 ? 159 GLU A C   1 
ATOM   1256 O O   . GLU A 1 159 ? 126.647 190.284 167.437 1.00 30.00 ? 159 GLU A O   1 
ATOM   1257 C CB  . GLU A 1 159 ? 127.105 187.427 166.506 1.00 30.00 ? 159 GLU A CB  1 
ATOM   1258 C CG  . GLU A 1 159 ? 125.866 187.223 165.678 1.00 30.00 ? 159 GLU A CG  1 
ATOM   1259 C CD  . GLU A 1 159 ? 125.206 185.892 165.942 1.00 30.00 ? 159 GLU A CD  1 
ATOM   1260 O OE1 . GLU A 1 159 ? 125.661 185.222 166.868 1.00 30.00 ? 159 GLU A OE1 1 
ATOM   1261 O OE2 . GLU A 1 159 ? 124.281 185.534 165.199 1.00 30.00 ? 159 GLU A OE2 1 
ATOM   1262 N N   . PRO A 1 160 ? 126.494 190.582 165.195 1.00 30.00 ? 160 PRO A N   1 
ATOM   1263 C CA  . PRO A 1 160 ? 125.545 191.696 165.302 1.00 30.00 ? 160 PRO A CA  1 
ATOM   1264 C C   . PRO A 1 160 ? 124.268 191.225 166.010 1.00 30.00 ? 160 PRO A C   1 
ATOM   1265 O O   . PRO A 1 160 ? 123.877 190.103 165.782 1.00 30.00 ? 160 PRO A O   1 
ATOM   1266 C CB  . PRO A 1 160 ? 125.277 192.084 163.840 1.00 30.00 ? 160 PRO A CB  1 
ATOM   1267 C CG  . PRO A 1 160 ? 126.505 191.622 163.099 1.00 30.00 ? 160 PRO A CG  1 
ATOM   1268 C CD  . PRO A 1 160 ? 126.942 190.368 163.820 1.00 30.00 ? 160 PRO A CD  1 
ATOM   1269 N N   . PHE A 1 161 ? 123.663 192.056 166.862 1.00 30.00 ? 161 PHE A N   1 
ATOM   1270 C CA  . PHE A 1 161 ? 122.467 191.666 167.652 1.00 30.00 ? 161 PHE A CA  1 
ATOM   1271 C C   . PHE A 1 161 ? 121.361 191.139 166.733 1.00 30.00 ? 161 PHE A C   1 
ATOM   1272 O O   . PHE A 1 161 ? 120.658 190.272 167.218 1.00 30.00 ? 161 PHE A O   1 
ATOM   1273 C CB  . PHE A 1 161 ? 121.913 192.833 168.472 1.00 30.00 ? 161 PHE A CB  1 
ATOM   1274 C CG  . PHE A 1 161 ? 120.701 192.486 169.296 1.00 30.00 ? 161 PHE A CG  1 
ATOM   1275 C CD1 . PHE A 1 161 ? 120.790 191.585 170.345 1.00 30.00 ? 161 PHE A CD1 1 
ATOM   1276 C CD2 . PHE A 1 161 ? 119.463 193.031 169.000 1.00 30.00 ? 161 PHE A CD2 1 
ATOM   1277 C CE1 . PHE A 1 161 ? 119.672 191.259 171.095 1.00 30.00 ? 161 PHE A CE1 1 
ATOM   1278 C CE2 . PHE A 1 161 ? 118.347 192.705 169.752 1.00 30.00 ? 161 PHE A CE2 1 
ATOM   1279 C CZ  . PHE A 1 161 ? 118.453 191.818 170.797 1.00 30.00 ? 161 PHE A CZ  1 
ATOM   1280 N N   . GLN A 1 162 ? 121.197 191.652 165.507 1.00 30.00 ? 162 GLN A N   1 
ATOM   1281 C CA  . GLN A 1 162 ? 120.083 191.269 164.590 1.00 30.00 ? 162 GLN A CA  1 
ATOM   1282 C C   . GLN A 1 162 ? 120.247 189.826 164.097 1.00 30.00 ? 162 GLN A C   1 
ATOM   1283 O O   . GLN A 1 162 ? 119.218 189.147 163.921 1.00 30.00 ? 162 GLN A O   1 
ATOM   1284 C CB  . GLN A 1 162 ? 119.959 192.288 163.449 1.00 30.00 ? 162 GLN A CB  1 
ATOM   1285 C CG  . GLN A 1 162 ? 121.094 192.365 162.437 1.00 30.00 ? 162 GLN A CG  1 
ATOM   1286 C CD  . GLN A 1 162 ? 121.042 191.282 161.386 1.00 30.00 ? 162 GLN A CD  1 
ATOM   1287 O OE1 . GLN A 1 162 ? 119.998 191.010 160.799 1.00 30.00 ? 162 GLN A OE1 1 
ATOM   1288 N NE2 . GLN A 1 162 ? 122.163 190.612 161.183 1.00 30.00 ? 162 GLN A NE2 1 
ATOM   1289 N N   . SER A 1 163 ? 121.484 189.397 163.817 1.00 30.00 ? 163 SER A N   1 
ATOM   1290 C CA  . SER A 1 163 ? 121.774 188.020 163.338 1.00 30.00 ? 163 SER A CA  1 
ATOM   1291 C C   . SER A 1 163 ? 121.508 187.057 164.491 1.00 30.00 ? 163 SER A C   1 
ATOM   1292 O O   . SER A 1 163 ? 120.952 185.975 164.232 1.00 30.00 ? 163 SER A O   1 
ATOM   1293 C CB  . SER A 1 163 ? 123.177 187.886 162.807 1.00 30.00 ? 163 SER A CB  1 
ATOM   1294 O OG  . SER A 1 163 ? 124.122 188.547 163.619 1.00 30.00 ? 163 SER A OG  1 
ATOM   1295 N N   . TYR A 1 164 ? 121.873 187.439 165.716 1.00 30.00 ? 164 TYR A N   1 
ATOM   1296 C CA  . TYR A 1 164 ? 121.569 186.628 166.918 1.00 30.00 ? 164 TYR A CA  1 
ATOM   1297 C C   . TYR A 1 164 ? 120.042 186.578 167.049 1.00 30.00 ? 164 TYR A C   1 
ATOM   1298 O O   . TYR A 1 164 ? 119.521 185.491 167.368 1.00 30.00 ? 164 TYR A O   1 
ATOM   1299 C CB  . TYR A 1 164 ? 122.270 187.216 168.145 1.00 30.00 ? 164 TYR A CB  1 
ATOM   1300 C CG  . TYR A 1 164 ? 121.627 186.792 169.436 1.00 30.00 ? 164 TYR A CG  1 
ATOM   1301 C CD1 . TYR A 1 164 ? 121.609 185.462 169.823 1.00 30.00 ? 164 TYR A CD1 1 
ATOM   1302 C CD2 . TYR A 1 164 ? 120.968 187.714 170.231 1.00 30.00 ? 164 TYR A CD2 1 
ATOM   1303 C CE1 . TYR A 1 164 ? 120.997 185.067 170.999 1.00 30.00 ? 164 TYR A CE1 1 
ATOM   1304 C CE2 . TYR A 1 164 ? 120.351 187.336 171.409 1.00 30.00 ? 164 TYR A CE2 1 
ATOM   1305 C CZ  . TYR A 1 164 ? 120.365 186.008 171.792 1.00 30.00 ? 164 TYR A CZ  1 
ATOM   1306 O OH  . TYR A 1 164 ? 119.746 185.646 172.953 1.00 30.00 ? 164 TYR A OH  1 
ATOM   1307 N N   . VAL A 1 165 ? 119.344 187.690 166.780 1.00 30.00 ? 165 VAL A N   1 
ATOM   1308 C CA  . VAL A 1 165 ? 117.848 187.747 166.801 1.00 30.00 ? 165 VAL A CA  1 
ATOM   1309 C C   . VAL A 1 165 ? 117.331 186.808 165.706 1.00 30.00 ? 165 VAL A C   1 
ATOM   1310 O O   . VAL A 1 165 ? 116.373 186.067 165.980 1.00 30.00 ? 165 VAL A O   1 
ATOM   1311 C CB  . VAL A 1 165 ? 117.322 189.192 166.622 1.00 30.00 ? 165 VAL A CB  1 
ATOM   1312 C CG1 . VAL A 1 165 ? 115.864 189.234 166.205 1.00 30.00 ? 165 VAL A CG1 1 
ATOM   1313 C CG2 . VAL A 1 165 ? 117.536 190.028 167.874 1.00 30.00 ? 165 VAL A CG2 1 
ATOM   1314 N N   . ASP A 1 166 ? 117.966 186.794 164.531 1.00 30.00 ? 166 ASP A N   1 
ATOM   1315 C CA  . ASP A 1 166 ? 117.525 185.971 163.369 1.00 30.00 ? 166 ASP A CA  1 
ATOM   1316 C C   . ASP A 1 166 ? 117.599 184.482 163.733 1.00 30.00 ? 166 ASP A C   1 
ATOM   1317 O O   . ASP A 1 166 ? 116.605 183.784 163.521 1.00 30.00 ? 166 ASP A O   1 
ATOM   1318 C CB  . ASP A 1 166 ? 118.379 186.282 162.141 1.00 30.00 ? 166 ASP A CB  1 
ATOM   1319 C CG  . ASP A 1 166 ? 117.805 185.755 160.840 1.00 30.00 ? 166 ASP A CG  1 
ATOM   1320 O OD1 . ASP A 1 166 ? 116.712 186.209 160.449 1.00 30.00 ? 166 ASP A OD1 1 
ATOM   1321 O OD2 . ASP A 1 166 ? 118.443 184.883 160.239 1.00 30.00 ? 166 ASP A OD2 1 
ATOM   1322 N N   . ARG A 1 167 ? 118.694 184.040 164.345 1.00 30.00 ? 167 ARG A N   1 
ATOM   1323 C CA  . ARG A 1 167 ? 118.857 182.620 164.746 1.00 30.00 ? 167 ARG A CA  1 
ATOM   1324 C C   . ARG A 1 167 ? 117.905 182.304 165.904 1.00 30.00 ? 167 ARG A C   1 
ATOM   1325 O O   . ARG A 1 167 ? 117.354 181.188 165.907 1.00 30.00 ? 167 ARG A O   1 
ATOM   1326 C CB  . ARG A 1 167 ? 120.305 182.346 165.144 1.00 30.00 ? 167 ARG A CB  1 
ATOM   1327 C CG  . ARG A 1 167 ? 121.323 182.582 164.041 1.00 30.00 ? 167 ARG A CG  1 
ATOM   1328 C CD  . ARG A 1 167 ? 122.723 182.157 164.428 1.00 30.00 ? 167 ARG A CD  1 
ATOM   1329 N NE  . ARG A 1 167 ? 123.206 182.803 165.641 1.00 30.00 ? 167 ARG A NE  1 
ATOM   1330 C CZ  . ARG A 1 167 ? 123.574 182.174 166.752 1.00 30.00 ? 167 ARG A CZ  1 
ATOM   1331 N NH1 . ARG A 1 167 ? 123.139 180.956 167.016 1.00 30.00 ? 167 ARG A NH1 1 
ATOM   1332 N NH2 . ARG A 1 167 ? 124.342 182.791 167.629 1.00 30.00 ? 167 ARG A NH2 1 
ATOM   1333 N N   . PHE A 1 168 ? 117.713 183.234 166.845 1.00 30.00 ? 168 PHE A N   1 
ATOM   1334 C CA  . PHE A 1 168 ? 116.859 183.010 168.042 1.00 30.00 ? 168 PHE A CA  1 
ATOM   1335 C C   . PHE A 1 168 ? 115.416 182.762 167.598 1.00 30.00 ? 168 PHE A C   1 
ATOM   1336 O O   . PHE A 1 168 ? 114.796 181.831 168.138 1.00 30.00 ? 168 PHE A O   1 
ATOM   1337 C CB  . PHE A 1 168 ? 116.949 184.188 169.019 1.00 30.00 ? 168 PHE A CB  1 
ATOM   1338 C CG  . PHE A 1 168 ? 116.113 184.035 170.257 1.00 30.00 ? 168 PHE A CG  1 
ATOM   1339 C CD1 . PHE A 1 168 ? 114.738 184.184 170.215 1.00 30.00 ? 168 PHE A CD1 1 
ATOM   1340 C CD2 . PHE A 1 168 ? 116.708 183.677 171.453 1.00 30.00 ? 168 PHE A CD2 1 
ATOM   1341 C CE1 . PHE A 1 168 ? 113.982 184.031 171.365 1.00 30.00 ? 168 PHE A CE1 1 
ATOM   1342 C CE2 . PHE A 1 168 ? 115.946 183.517 172.598 1.00 30.00 ? 168 PHE A CE2 1 
ATOM   1343 C CZ  . PHE A 1 168 ? 114.589 183.694 172.548 1.00 30.00 ? 168 PHE A CZ  1 
ATOM   1344 N N   . TYR A 1 169 ? 114.905 183.536 166.639 1.00 30.00 ? 169 TYR A N   1 
ATOM   1345 C CA  . TYR A 1 169 ? 113.492 183.424 166.192 1.00 30.00 ? 169 TYR A CA  1 
ATOM   1346 C C   . TYR A 1 169 ? 113.294 182.224 165.263 1.00 30.00 ? 169 TYR A C   1 
ATOM   1347 O O   . TYR A 1 169 ? 112.168 181.714 165.215 1.00 30.00 ? 169 TYR A O   1 
ATOM   1348 C CB  . TYR A 1 169 ? 113.021 184.704 165.504 1.00 30.00 ? 169 TYR A CB  1 
ATOM   1349 C CG  . TYR A 1 169 ? 112.527 185.747 166.468 1.00 30.00 ? 169 TYR A CG  1 
ATOM   1350 C CD1 . TYR A 1 169 ? 113.400 186.463 167.265 1.00 30.00 ? 169 TYR A CD1 1 
ATOM   1351 C CD2 . TYR A 1 169 ? 111.172 185.910 166.679 1.00 30.00 ? 169 TYR A CD2 1 
ATOM   1352 C CE1 . TYR A 1 169 ? 112.941 187.390 168.182 1.00 30.00 ? 169 TYR A CE1 1 
ATOM   1353 C CE2 . TYR A 1 169 ? 110.693 186.819 167.603 1.00 30.00 ? 169 TYR A CE2 1 
ATOM   1354 C CZ  . TYR A 1 169 ? 111.583 187.564 168.352 1.00 30.00 ? 169 TYR A CZ  1 
ATOM   1355 O OH  . TYR A 1 169 ? 111.116 188.467 169.262 1.00 30.00 ? 169 TYR A OH  1 
ATOM   1356 N N   . LYS A 1 170 ? 114.336 181.785 164.559 1.00 30.00 ? 170 LYS A N   1 
ATOM   1357 C CA  . LYS A 1 170 ? 114.232 180.653 163.603 1.00 30.00 ? 170 LYS A CA  1 
ATOM   1358 C C   . LYS A 1 170 ? 114.034 179.364 164.404 1.00 30.00 ? 170 LYS A C   1 
ATOM   1359 O O   . LYS A 1 170 ? 113.261 178.509 163.941 1.00 30.00 ? 170 LYS A O   1 
ATOM   1360 C CB  . LYS A 1 170 ? 115.495 180.613 162.742 1.00 30.00 ? 170 LYS A CB  1 
ATOM   1361 C CG  . LYS A 1 170 ? 115.547 179.488 161.716 1.00 30.00 ? 170 LYS A CG  1 
ATOM   1362 C CD  . LYS A 1 170 ? 114.381 179.506 160.753 1.00 30.00 ? 170 LYS A CD  1 
ATOM   1363 C CE  . LYS A 1 170 ? 114.388 178.366 159.756 1.00 30.00 ? 170 LYS A CE  1 
ATOM   1364 N NZ  . LYS A 1 170 ? 115.557 178.420 158.848 1.00 30.00 ? 170 LYS A NZ  1 
ATOM   1365 N N   . SER A 1 171 ? 114.702 179.222 165.547 1.00 30.00 ? 171 SER A N   1 
ATOM   1366 C CA  . SER A 1 171 ? 114.608 178.050 166.452 1.00 30.00 ? 171 SER A CA  1 
ATOM   1367 C C   . SER A 1 171 ? 113.257 178.076 167.167 1.00 30.00 ? 171 SER A C   1 
ATOM   1368 O O   . SER A 1 171 ? 112.672 176.994 167.361 1.00 30.00 ? 171 SER A O   1 
ATOM   1369 C CB  . SER A 1 171 ? 115.738 178.066 167.425 1.00 30.00 ? 171 SER A CB  1 
ATOM   1370 O OG  . SER A 1 171 ? 116.984 177.990 166.759 1.00 30.00 ? 171 SER A OG  1 
ATOM   1371 N N   . LEU A 1 172 ? 112.785 179.279 167.494 1.00 30.00 ? 172 LEU A N   1 
ATOM   1372 C CA  . LEU A 1 172 ? 111.470 179.474 168.146 1.00 30.00 ? 172 LEU A CA  1 
ATOM   1373 C C   . LEU A 1 172 ? 110.373 178.989 167.193 1.00 30.00 ? 172 LEU A C   1 
ATOM   1374 O O   . LEU A 1 172 ? 109.393 178.418 167.691 1.00 30.00 ? 172 LEU A O   1 
ATOM   1375 C CB  . LEU A 1 172 ? 111.350 180.965 168.470 1.00 30.00 ? 172 LEU A CB  1 
ATOM   1376 C CG  . LEU A 1 172 ? 110.234 181.344 169.436 1.00 30.00 ? 172 LEU A CG  1 
ATOM   1377 C CD1 . LEU A 1 172 ? 110.564 180.900 170.851 1.00 30.00 ? 172 LEU A CD1 1 
ATOM   1378 C CD2 . LEU A 1 172 ? 109.980 182.841 169.388 1.00 30.00 ? 172 LEU A CD2 1 
ATOM   1379 N N   . ARG A 1 173 ? 110.553 179.148 165.876 1.00 30.00 ? 173 ARG A N   1 
ATOM   1380 C CA  . ARG A 1 173 ? 109.566 178.672 164.867 1.00 30.00 ? 173 ARG A CA  1 
ATOM   1381 C C   . ARG A 1 173 ? 109.414 177.159 165.035 1.00 30.00 ? 173 ARG A C   1 
ATOM   1382 O O   . ARG A 1 173 ? 108.262 176.684 164.990 1.00 30.00 ? 173 ARG A O   1 
ATOM   1383 C CB  . ARG A 1 173 ? 109.996 179.004 163.432 1.00 30.00 ? 173 ARG A CB  1 
ATOM   1384 C CG  . ARG A 1 173 ? 109.838 180.461 163.037 1.00 30.00 ? 173 ARG A CG  1 
ATOM   1385 C CD  . ARG A 1 173 ? 110.377 180.717 161.644 1.00 30.00 ? 173 ARG A CD  1 
ATOM   1386 N NE  . ARG A 1 173 ? 109.661 179.988 160.607 1.00 30.00 ? 173 ARG A NE  1 
ATOM   1387 C CZ  . ARG A 1 173 ? 109.956 180.026 159.312 1.00 30.00 ? 173 ARG A CZ  1 
ATOM   1388 N NH1 . ARG A 1 173 ? 111.105 180.532 158.900 1.00 30.00 ? 173 ARG A NH1 1 
ATOM   1389 N NH2 . ARG A 1 173 ? 109.107 179.532 158.428 1.00 30.00 ? 173 ARG A NH2 1 
ATOM   1390 N N   . ALA A 1 174 ? 110.517 176.430 165.228 1.00 30.00 ? 174 ALA A N   1 
ATOM   1391 C CA  . ALA A 1 174 ? 110.505 174.961 165.433 1.00 30.00 ? 174 ALA A CA  1 
ATOM   1392 C C   . ALA A 1 174 ? 109.842 174.618 166.770 1.00 30.00 ? 174 ALA A C   1 
ATOM   1393 O O   . ALA A 1 174 ? 109.142 173.587 166.820 1.00 30.00 ? 174 ALA A O   1 
ATOM   1394 C CB  . ALA A 1 174 ? 111.910 174.420 165.367 1.00 30.00 ? 174 ALA A CB  1 
ATOM   1395 N N   . GLU A 1 175 ? 110.048 175.431 167.813 1.00 30.00 ? 175 GLU A N   1 
ATOM   1396 C CA  . GLU A 1 175 ? 109.509 175.142 169.170 1.00 30.00 ? 175 GLU A CA  1 
ATOM   1397 C C   . GLU A 1 175 ? 107.997 174.931 169.084 1.00 30.00 ? 175 GLU A C   1 
ATOM   1398 O O   . GLU A 1 175 ? 107.330 175.774 168.451 1.00 30.00 ? 175 GLU A O   1 
ATOM   1399 C CB  . GLU A 1 175 ? 109.795 176.277 170.158 1.00 30.00 ? 175 GLU A CB  1 
ATOM   1400 C CG  . GLU A 1 175 ? 111.233 176.341 170.624 1.00 30.00 ? 175 GLU A CG  1 
ATOM   1401 C CD  . GLU A 1 175 ? 111.586 175.312 171.683 1.00 30.00 ? 175 GLU A CD  1 
ATOM   1402 O OE1 . GLU A 1 175 ? 110.970 175.343 172.763 1.00 30.00 ? 175 GLU A OE1 1 
ATOM   1403 O OE2 . GLU A 1 175 ? 112.472 174.483 171.426 1.00 30.00 ? 175 GLU A OE2 1 
ATOM   1404 N N   . GLN A 1 176 ? 107.482 173.863 169.697 1.00 30.00 ? 176 GLN A N   1 
ATOM   1405 C CA  . GLN A 1 176 ? 106.024 173.564 169.740 1.00 30.00 ? 176 GLN A CA  1 
ATOM   1406 C C   . GLN A 1 176 ? 105.501 173.907 171.137 1.00 30.00 ? 176 GLN A C   1 
ATOM   1407 O O   . GLN A 1 176 ? 104.355 173.530 171.431 1.00 30.00 ? 176 GLN A O   1 
ATOM   1408 C CB  . GLN A 1 176 ? 105.752 172.100 169.374 1.00 30.00 ? 176 GLN A CB  1 
ATOM   1409 C CG  . GLN A 1 176 ? 106.324 171.073 170.341 1.00 30.00 ? 176 GLN A CG  1 
ATOM   1410 C CD  . GLN A 1 176 ? 105.508 170.878 171.594 1.00 30.00 ? 176 GLN A CD  1 
ATOM   1411 O OE1 . GLN A 1 176 ? 104.392 170.364 171.557 1.00 30.00 ? 176 GLN A OE1 1 
ATOM   1412 N NE2 . GLN A 1 176 ? 106.077 171.263 172.725 1.00 30.00 ? 176 GLN A NE2 1 
ATOM   1413 N N   . THR A 1 177 ? 106.287 174.607 171.960 1.00 30.00 ? 177 THR A N   1 
ATOM   1414 C CA  . THR A 1 177 ? 105.918 174.939 173.364 1.00 30.00 ? 177 THR A CA  1 
ATOM   1415 C C   . THR A 1 177 ? 104.720 175.894 173.413 1.00 30.00 ? 177 THR A C   1 
ATOM   1416 O O   . THR A 1 177 ? 104.431 176.513 172.369 1.00 30.00 ? 177 THR A O   1 
ATOM   1417 C CB  . THR A 1 177 ? 107.113 175.531 174.119 1.00 30.00 ? 177 THR A CB  1 
ATOM   1418 O OG1 . THR A 1 177 ? 107.554 176.684 173.402 1.00 30.00 ? 177 THR A OG1 1 
ATOM   1419 C CG2 . THR A 1 177 ? 108.256 174.554 174.271 1.00 30.00 ? 177 THR A CG2 1 
ATOM   1420 N N   . ASP A 1 178 ? 104.030 175.947 174.556 1.00 30.00 ? 178 ASP A N   1 
ATOM   1421 C CA  . ASP A 1 178 ? 102.846 176.817 174.767 1.00 30.00 ? 178 ASP A CA  1 
ATOM   1422 C C   . ASP A 1 178 ? 103.179 178.252 174.342 1.00 30.00 ? 178 ASP A C   1 
ATOM   1423 O O   . ASP A 1 178 ? 104.343 178.655 174.509 1.00 30.00 ? 178 ASP A O   1 
ATOM   1424 C CB  . ASP A 1 178 ? 102.429 176.726 176.234 1.00 30.00 ? 178 ASP A CB  1 
ATOM   1425 C CG  . ASP A 1 178 ? 101.085 177.352 176.553 1.00 30.00 ? 178 ASP A CG  1 
ATOM   1426 O OD1 . ASP A 1 178 ? 100.069 176.849 176.040 1.00 30.00 ? 178 ASP A OD1 1 
ATOM   1427 O OD2 . ASP A 1 178 ? 101.072 178.354 177.285 1.00 30.00 ? 178 ASP A OD2 1 
ATOM   1428 N N   . PRO A 1 179 ? 102.210 179.058 173.852 1.00 30.00 ? 179 PRO A N   1 
ATOM   1429 C CA  . PRO A 1 179 ? 102.484 180.417 173.368 1.00 30.00 ? 179 PRO A CA  1 
ATOM   1430 C C   . PRO A 1 179 ? 103.073 181.329 174.451 1.00 30.00 ? 179 PRO A C   1 
ATOM   1431 O O   . PRO A 1 179 ? 103.860 182.183 174.109 1.00 30.00 ? 179 PRO A O   1 
ATOM   1432 C CB  . PRO A 1 179 ? 101.103 180.944 172.963 1.00 30.00 ? 179 PRO A CB  1 
ATOM   1433 C CG  . PRO A 1 179 ? 100.316 179.701 172.662 1.00 30.00 ? 179 PRO A CG  1 
ATOM   1434 C CD  . PRO A 1 179 ? 100.791 178.727 173.713 1.00 30.00 ? 179 PRO A CD  1 
ATOM   1435 N N   . ALA A 1 180 ? 102.652 181.172 175.706 1.00 30.00 ? 180 ALA A N   1 
ATOM   1436 C CA  . ALA A 1 180 ? 103.171 181.972 176.838 1.00 30.00 ? 180 ALA A CA  1 
ATOM   1437 C C   . ALA A 1 180 ? 104.664 181.699 177.000 1.00 30.00 ? 180 ALA A C   1 
ATOM   1438 O O   . ALA A 1 180 ? 105.413 182.661 177.248 1.00 30.00 ? 180 ALA A O   1 
ATOM   1439 C CB  . ALA A 1 180 ? 102.435 181.609 178.088 1.00 30.00 ? 180 ALA A CB  1 
ATOM   1440 N N   . VAL A 1 181 ? 105.078 180.439 176.866 1.00 30.00 ? 181 VAL A N   1 
ATOM   1441 C CA  . VAL A 1 181 ? 106.515 180.054 176.953 1.00 30.00 ? 181 VAL A CA  1 
ATOM   1442 C C   . VAL A 1 181 ? 107.226 180.761 175.801 1.00 30.00 ? 181 VAL A C   1 
ATOM   1443 O O   . VAL A 1 181 ? 108.386 181.142 175.990 1.00 30.00 ? 181 VAL A O   1 
ATOM   1444 C CB  . VAL A 1 181 ? 106.700 178.528 176.889 1.00 30.00 ? 181 VAL A CB  1 
ATOM   1445 C CG1 . VAL A 1 181 ? 108.160 178.124 176.821 1.00 30.00 ? 181 VAL A CG1 1 
ATOM   1446 C CG2 . VAL A 1 181 ? 105.995 177.823 178.032 1.00 30.00 ? 181 VAL A CG2 1 
ATOM   1447 N N   . LYS A 1 182 ? 106.563 180.892 174.649 1.00 30.00 ? 182 LYS A N   1 
ATOM   1448 C CA  . LYS A 1 182 ? 107.135 181.583 173.460 1.00 30.00 ? 182 LYS A CA  1 
ATOM   1449 C C   . LYS A 1 182 ? 107.268 183.077 173.754 1.00 30.00 ? 182 LYS A C   1 
ATOM   1450 O O   . LYS A 1 182 ? 108.288 183.650 173.355 1.00 30.00 ? 182 LYS A O   1 
ATOM   1451 C CB  . LYS A 1 182 ? 106.295 181.287 172.218 1.00 30.00 ? 182 LYS A CB  1 
ATOM   1452 C CG  . LYS A 1 182 ? 106.161 179.802 171.908 1.00 30.00 ? 182 LYS A CG  1 
ATOM   1453 C CD  . LYS A 1 182 ? 105.821 179.473 170.477 1.00 30.00 ? 182 LYS A CD  1 
ATOM   1454 C CE  . LYS A 1 182 ? 106.963 179.755 169.526 1.00 30.00 ? 182 LYS A CE  1 
ATOM   1455 N NZ  . LYS A 1 182 ? 106.644 179.322 168.147 1.00 30.00 ? 182 LYS A NZ  1 
ATOM   1456 N N   . ASN A 1 183 ? 106.292 183.673 174.433 1.00 30.00 ? 183 ASN A N   1 
ATOM   1457 C CA  . ASN A 1 183 ? 106.309 185.117 174.780 1.00 30.00 ? 183 ASN A CA  1 
ATOM   1458 C C   . ASN A 1 183 ? 107.373 185.387 175.848 1.00 30.00 ? 183 ASN A C   1 
ATOM   1459 O O   . ASN A 1 183 ? 108.000 186.456 175.777 1.00 30.00 ? 183 ASN A O   1 
ATOM   1460 C CB  . ASN A 1 183 ? 104.933 185.579 175.249 1.00 30.00 ? 183 ASN A CB  1 
ATOM   1461 C CG  . ASN A 1 183 ? 103.840 185.493 174.202 1.00 30.00 ? 183 ASN A CG  1 
ATOM   1462 O OD1 . ASN A 1 183 ? 102.686 185.782 174.502 1.00 30.00 ? 183 ASN A OD1 1 
ATOM   1463 N ND2 . ASN A 1 183 ? 104.161 185.090 172.983 1.00 30.00 ? 183 ASN A ND2 1 
ATOM   1464 N N   . TRP A 1 184 ? 107.574 184.468 176.797 1.00 30.00 ? 184 TRP A N   1 
ATOM   1465 C CA  . TRP A 1 184 ? 108.538 184.650 177.916 1.00 30.00 ? 184 TRP A CA  1 
ATOM   1466 C C   . TRP A 1 184 ? 109.965 184.475 177.400 1.00 30.00 ? 184 TRP A C   1 
ATOM   1467 O O   . TRP A 1 184 ? 110.854 185.075 177.996 1.00 30.00 ? 184 TRP A O   1 
ATOM   1468 C CB  . TRP A 1 184 ? 108.245 183.655 179.040 1.00 30.00 ? 184 TRP A CB  1 
ATOM   1469 C CG  . TRP A 1 184 ? 109.403 183.502 179.971 1.00 30.00 ? 184 TRP A CG  1 
ATOM   1470 C CD1 . TRP A 1 184 ? 109.588 184.133 181.163 1.00 30.00 ? 184 TRP A CD1 1 
ATOM   1471 C CD2 . TRP A 1 184 ? 110.546 182.653 179.783 1.00 30.00 ? 184 TRP A CD2 1 
ATOM   1472 N NE1 . TRP A 1 184 ? 110.775 183.752 181.720 1.00 30.00 ? 184 TRP A NE1 1 
ATOM   1473 C CE2 . TRP A 1 184 ? 111.384 182.844 180.898 1.00 30.00 ? 184 TRP A CE2 1 
ATOM   1474 C CE3 . TRP A 1 184 ? 110.944 181.760 178.784 1.00 30.00 ? 184 TRP A CE3 1 
ATOM   1475 C CZ2 . TRP A 1 184 ? 112.594 182.173 181.040 1.00 30.00 ? 184 TRP A CZ2 1 
ATOM   1476 C CZ3 . TRP A 1 184 ? 112.141 181.099 178.923 1.00 30.00 ? 184 TRP A CZ3 1 
ATOM   1477 C CH2 . TRP A 1 184 ? 112.953 181.304 180.037 1.00 30.00 ? 184 TRP A CH2 1 
ATOM   1478 N N   . MET A 1 185 ? 110.178 183.618 176.410 1.00 30.00 ? 185 MET A N   1 
ATOM   1479 C CA  . MET A 1 185 ? 111.483 183.360 175.751 1.00 30.00 ? 185 MET A CA  1 
ATOM   1480 C C   . MET A 1 185 ? 111.903 184.606 174.977 1.00 30.00 ? 185 MET A C   1 
ATOM   1481 O O   . MET A 1 185 ? 113.056 185.044 175.146 1.00 30.00 ? 185 MET A O   1 
ATOM   1482 C CB  . MET A 1 185 ? 111.330 182.208 174.759 1.00 30.00 ? 185 MET A CB  1 
ATOM   1483 C CG  . MET A 1 185 ? 111.692 180.858 175.319 1.00 30.00 ? 185 MET A CG  1 
ATOM   1484 S SD  . MET A 1 185 ? 111.265 179.532 174.169 1.00 30.00 ? 185 MET A SD  1 
ATOM   1485 C CE  . MET A 1 185 ? 111.327 178.116 175.264 1.00 30.00 ? 185 MET A CE  1 
ATOM   1486 N N   . THR A 1 186 ? 110.985 185.196 174.216 1.00 30.00 ? 186 THR A N   1 
ATOM   1487 C CA  . THR A 1 186 ? 111.274 186.375 173.359 1.00 30.00 ? 186 THR A CA  1 
ATOM   1488 C C   . THR A 1 186 ? 111.528 187.614 174.216 1.00 30.00 ? 186 THR A C   1 
ATOM   1489 O O   . THR A 1 186 ? 112.247 188.490 173.733 1.00 30.00 ? 186 THR A O   1 
ATOM   1490 C CB  . THR A 1 186 ? 110.145 186.627 172.356 1.00 30.00 ? 186 THR A CB  1 
ATOM   1491 O OG1 . THR A 1 186 ? 108.909 186.631 173.063 1.00 30.00 ? 186 THR A OG1 1 
ATOM   1492 C CG2 . THR A 1 186 ? 110.097 185.590 171.257 1.00 30.00 ? 186 THR A CG2 1 
ATOM   1493 N N   . GLN A 1 187 ? 111.014 187.638 175.450 1.00 30.00 ? 187 GLN A N   1 
ATOM   1494 C CA  . GLN A 1 187 ? 111.100 188.818 176.348 1.00 30.00 ? 187 GLN A CA  1 
ATOM   1495 C C   . GLN A 1 187 ? 112.178 188.633 177.420 1.00 30.00 ? 187 GLN A C   1 
ATOM   1496 O O   . GLN A 1 187 ? 112.661 189.669 177.919 1.00 30.00 ? 187 GLN A O   1 
ATOM   1497 C CB  . GLN A 1 187 ? 109.728 189.006 176.995 1.00 30.00 ? 187 GLN A CB  1 
ATOM   1498 C CG  . GLN A 1 187 ? 108.656 189.458 176.015 1.00 30.00 ? 187 GLN A CG  1 
ATOM   1499 C CD  . GLN A 1 187 ? 107.268 189.470 176.606 1.00 30.00 ? 187 GLN A CD  1 
ATOM   1500 O OE1 . GLN A 1 187 ? 107.054 189.125 177.765 1.00 30.00 ? 187 GLN A OE1 1 
ATOM   1501 N NE2 . GLN A 1 187 ? 106.301 189.875 175.800 1.00 30.00 ? 187 GLN A NE2 1 
ATOM   1502 N N   . THR A 1 188 ? 112.549 187.395 177.765 1.00 30.00 ? 188 THR A N   1 
ATOM   1503 C CA  . THR A 1 188 ? 113.512 187.101 178.864 1.00 30.00 ? 188 THR A CA  1 
ATOM   1504 C C   . THR A 1 188 ? 114.747 186.365 178.327 1.00 30.00 ? 188 THR A C   1 
ATOM   1505 O O   . THR A 1 188 ? 115.859 186.885 178.537 1.00 30.00 ? 188 THR A O   1 
ATOM   1506 C CB  . THR A 1 188 ? 112.811 186.319 179.986 1.00 30.00 ? 188 THR A CB  1 
ATOM   1507 O OG1 . THR A 1 188 ? 111.573 186.967 180.269 1.00 30.00 ? 188 THR A OG1 1 
ATOM   1508 C CG2 . THR A 1 188 ? 113.655 186.221 181.236 1.00 30.00 ? 188 THR A CG2 1 
ATOM   1509 N N   . LEU A 1 189 ? 114.581 185.225 177.646 1.00 30.00 ? 189 LEU A N   1 
ATOM   1510 C CA  . LEU A 1 189 ? 115.719 184.393 177.159 1.00 30.00 ? 189 LEU A CA  1 
ATOM   1511 C C   . LEU A 1 189 ? 116.553 185.177 176.138 1.00 30.00 ? 189 LEU A C   1 
ATOM   1512 O O   . LEU A 1 189 ? 117.787 185.009 176.152 1.00 30.00 ? 189 LEU A O   1 
ATOM   1513 C CB  . LEU A 1 189 ? 115.165 183.096 176.554 1.00 30.00 ? 189 LEU A CB  1 
ATOM   1514 C CG  . LEU A 1 189 ? 116.193 182.065 176.101 1.00 30.00 ? 189 LEU A CG  1 
ATOM   1515 C CD1 . LEU A 1 189 ? 116.952 181.497 177.285 1.00 30.00 ? 189 LEU A CD1 1 
ATOM   1516 C CD2 . LEU A 1 189 ? 115.518 180.952 175.316 1.00 30.00 ? 189 LEU A CD2 1 
ATOM   1517 N N   . LEU A 1 190 ? 115.924 185.980 175.277 1.00 30.00 ? 190 LEU A N   1 
ATOM   1518 C CA  . LEU A 1 190 ? 116.628 186.749 174.212 1.00 30.00 ? 190 LEU A CA  1 
ATOM   1519 C C   . LEU A 1 190 ? 117.557 187.808 174.826 1.00 30.00 ? 190 LEU A C   1 
ATOM   1520 O O   . LEU A 1 190 ? 118.549 188.164 174.172 1.00 30.00 ? 190 LEU A O   1 
ATOM   1521 C CB  . LEU A 1 190 ? 115.590 187.388 173.286 1.00 30.00 ? 190 LEU A CB  1 
ATOM   1522 C CG  . LEU A 1 190 ? 116.163 188.179 172.107 1.00 30.00 ? 190 LEU A CG  1 
ATOM   1523 C CD1 . LEU A 1 190 ? 116.824 187.256 171.094 1.00 30.00 ? 190 LEU A CD1 1 
ATOM   1524 C CD2 . LEU A 1 190 ? 115.087 189.013 171.437 1.00 30.00 ? 190 LEU A CD2 1 
ATOM   1525 N N   . ILE A 1 191 ? 117.217 188.385 175.977 1.00 30.00 ? 191 ILE A N   1 
ATOM   1526 C CA  . ILE A 1 191 ? 118.127 189.346 176.672 1.00 30.00 ? 191 ILE A CA  1 
ATOM   1527 C C   . ILE A 1 191 ? 119.140 188.535 177.489 1.00 30.00 ? 191 ILE A C   1 
ATOM   1528 O O   . ILE A 1 191 ? 120.292 188.998 177.615 1.00 30.00 ? 191 ILE A O   1 
ATOM   1529 C CB  . ILE A 1 191 ? 117.322 190.351 177.518 1.00 30.00 ? 191 ILE A CB  1 
ATOM   1530 C CG1 . ILE A 1 191 ? 116.552 191.325 176.623 1.00 30.00 ? 191 ILE A CG1 1 
ATOM   1531 C CG2 . ILE A 1 191 ? 118.229 191.078 178.498 1.00 30.00 ? 191 ILE A CG2 1 
ATOM   1532 C CD1 . ILE A 1 191 ? 115.522 192.157 177.347 1.00 30.00 ? 191 ILE A CD1 1 
ATOM   1533 N N   . GLN A 1 192 ? 118.745 187.365 177.999 1.00 30.00 ? 192 GLN A N   1 
ATOM   1534 C CA  . GLN A 1 192 ? 119.615 186.487 178.827 1.00 30.00 ? 192 GLN A CA  1 
ATOM   1535 C C   . GLN A 1 192 ? 120.779 185.934 178.005 1.00 30.00 ? 192 GLN A C   1 
ATOM   1536 O O   . GLN A 1 192 ? 121.880 185.865 178.558 1.00 30.00 ? 192 GLN A O   1 
ATOM   1537 C CB  . GLN A 1 192 ? 118.782 185.331 179.389 1.00 30.00 ? 192 GLN A CB  1 
ATOM   1538 C CG  . GLN A 1 192 ? 119.563 184.320 180.214 1.00 30.00 ? 192 GLN A CG  1 
ATOM   1539 C CD  . GLN A 1 192 ? 120.286 184.943 181.381 1.00 30.00 ? 192 GLN A CD  1 
ATOM   1540 O OE1 . GLN A 1 192 ? 121.441 184.630 181.653 1.00 30.00 ? 192 GLN A OE1 1 
ATOM   1541 N NE2 . GLN A 1 192 ? 119.591 185.796 182.113 1.00 30.00 ? 192 GLN A NE2 1 
ATOM   1542 N N   . ASN A 1 193 ? 120.557 185.576 176.740 1.00 30.00 ? 193 ASN A N   1 
ATOM   1543 C CA  . ASN A 1 193 ? 121.590 184.900 175.910 1.00 30.00 ? 193 ASN A CA  1 
ATOM   1544 C C   . ASN A 1 193 ? 122.191 185.870 174.892 1.00 30.00 ? 193 ASN A C   1 
ATOM   1545 O O   . ASN A 1 193 ? 122.431 185.429 173.769 1.00 30.00 ? 193 ASN A O   1 
ATOM   1546 C CB  . ASN A 1 193 ? 121.000 183.655 175.243 1.00 30.00 ? 193 ASN A CB  1 
ATOM   1547 C CG  . ASN A 1 193 ? 120.734 182.538 176.229 1.00 30.00 ? 193 ASN A CG  1 
ATOM   1548 O OD1 . ASN A 1 193 ? 121.001 182.673 177.417 1.00 30.00 ? 193 ASN A OD1 1 
ATOM   1549 N ND2 . ASN A 1 193 ? 120.223 181.422 175.747 1.00 30.00 ? 193 ASN A ND2 1 
ATOM   1550 N N   . ALA A 1 194 ? 122.458 187.121 175.266 1.00 30.00 ? 194 ALA A N   1 
ATOM   1551 C CA  . ALA A 1 194 ? 123.117 188.105 174.378 1.00 30.00 ? 194 ALA A CA  1 
ATOM   1552 C C   . ALA A 1 194 ? 124.543 188.330 174.885 1.00 30.00 ? 194 ALA A C   1 
ATOM   1553 O O   . ALA A 1 194 ? 124.771 188.096 176.086 1.00 30.00 ? 194 ALA A O   1 
ATOM   1554 C CB  . ALA A 1 194 ? 122.320 189.376 174.349 1.00 30.00 ? 194 ALA A CB  1 
ATOM   1555 N N   . ASN A 1 195 ? 125.460 188.777 174.023 1.00 30.00 ? 195 ASN A N   1 
ATOM   1556 C CA  . ASN A 1 195 ? 126.887 188.961 174.401 1.00 30.00 ? 195 ASN A CA  1 
ATOM   1557 C C   . ASN A 1 195 ? 126.943 190.032 175.494 1.00 30.00 ? 195 ASN A C   1 
ATOM   1558 O O   . ASN A 1 195 ? 126.032 190.868 175.532 1.00 30.00 ? 195 ASN A O   1 
ATOM   1559 C CB  . ASN A 1 195 ? 127.770 189.244 173.180 1.00 30.00 ? 195 ASN A CB  1 
ATOM   1560 C CG  . ASN A 1 195 ? 127.441 190.522 172.443 1.00 30.00 ? 195 ASN A CG  1 
ATOM   1561 O OD1 . ASN A 1 195 ? 126.737 191.387 172.950 1.00 30.00 ? 195 ASN A OD1 1 
ATOM   1562 N ND2 . ASN A 1 195 ? 127.968 190.654 171.239 1.00 30.00 ? 195 ASN A ND2 1 
ATOM   1563 N N   . PRO A 1 196 ? 127.944 190.027 176.398 1.00 30.00 ? 196 PRO A N   1 
ATOM   1564 C CA  . PRO A 1 196 ? 127.970 190.954 177.542 1.00 30.00 ? 196 PRO A CA  1 
ATOM   1565 C C   . PRO A 1 196 ? 127.520 192.397 177.269 1.00 30.00 ? 196 PRO A C   1 
ATOM   1566 O O   . PRO A 1 196 ? 126.699 192.872 178.022 1.00 30.00 ? 196 PRO A O   1 
ATOM   1567 C CB  . PRO A 1 196 ? 129.460 190.953 177.908 1.00 30.00 ? 196 PRO A CB  1 
ATOM   1568 C CG  . PRO A 1 196 ? 129.894 189.541 177.607 1.00 30.00 ? 196 PRO A CG  1 
ATOM   1569 C CD  . PRO A 1 196 ? 129.132 189.170 176.354 1.00 30.00 ? 196 PRO A CD  1 
ATOM   1570 N N   . ASP A 1 197 ? 128.035 193.049 176.227 1.00 30.00 ? 197 ASP A N   1 
ATOM   1571 C CA  . ASP A 1 197 ? 127.689 194.482 176.019 1.00 30.00 ? 197 ASP A CA  1 
ATOM   1572 C C   . ASP A 1 197 ? 126.210 194.640 175.650 1.00 30.00 ? 197 ASP A C   1 
ATOM   1573 O O   . ASP A 1 197 ? 125.540 195.483 176.278 1.00 30.00 ? 197 ASP A O   1 
ATOM   1574 C CB  . ASP A 1 197 ? 128.575 195.132 174.961 1.00 30.00 ? 197 ASP A CB  1 
ATOM   1575 C CG  . ASP A 1 197 ? 129.825 195.777 175.537 1.00 30.00 ? 197 ASP A CG  1 
ATOM   1576 O OD1 . ASP A 1 197 ? 130.037 195.663 176.760 1.00 30.00 ? 197 ASP A OD1 1 
ATOM   1577 O OD2 . ASP A 1 197 ? 130.566 196.406 174.760 1.00 30.00 ? 197 ASP A OD2 1 
ATOM   1578 N N   . CYS A 1 198 ? 125.721 193.868 174.675 1.00 30.00 ? 198 CYS A N   1 
ATOM   1579 C CA  . CYS A 1 198 ? 124.315 194.056 174.227 1.00 30.00 ? 198 CYS A CA  1 
ATOM   1580 C C   . CYS A 1 198 ? 123.404 193.841 175.438 1.00 30.00 ? 198 CYS A C   1 
ATOM   1581 O O   . CYS A 1 198 ? 122.444 194.617 175.596 1.00 30.00 ? 198 CYS A O   1 
ATOM   1582 C CB  . CYS A 1 198 ? 123.952 193.094 173.100 1.00 30.00 ? 198 CYS A CB  1 
ATOM   1583 S SG  . CYS A 1 198 ? 124.718 193.531 171.516 1.00 30.00 ? 198 CYS A SG  1 
ATOM   1584 N N   . LYS A 1 199 ? 123.766 192.910 176.326 1.00 30.00 ? 199 LYS A N   1 
ATOM   1585 C CA  . LYS A 1 199 ? 122.983 192.614 177.554 1.00 30.00 ? 199 LYS A CA  1 
ATOM   1586 C C   . LYS A 1 199 ? 122.878 193.862 178.437 1.00 30.00 ? 199 LYS A C   1 
ATOM   1587 O O   . LYS A 1 199 ? 121.837 194.004 179.088 1.00 30.00 ? 199 LYS A O   1 
ATOM   1588 C CB  . LYS A 1 199 ? 123.645 191.479 178.336 1.00 30.00 ? 199 LYS A CB  1 
ATOM   1589 C CG  . LYS A 1 199 ? 122.728 190.768 179.316 1.00 30.00 ? 199 LYS A CG  1 
ATOM   1590 C CD  . LYS A 1 199 ? 123.103 189.329 179.563 1.00 30.00 ? 199 LYS A CD  1 
ATOM   1591 C CE  . LYS A 1 199 ? 122.143 188.655 180.516 1.00 30.00 ? 199 LYS A CE  1 
ATOM   1592 N NZ  . LYS A 1 199 ? 122.641 187.335 180.963 1.00 30.00 ? 199 LYS A NZ  1 
ATOM   1593 N N   . LEU A 1 200 ? 123.910 194.712 178.482 1.00 30.00 ? 200 LEU A N   1 
ATOM   1594 C CA  . LEU A 1 200 ? 123.921 195.941 179.325 1.00 30.00 ? 200 LEU A CA  1 
ATOM   1595 C C   . LEU A 1 200 ? 123.019 197.006 178.702 1.00 30.00 ? 200 LEU A C   1 
ATOM   1596 O O   . LEU A 1 200 ? 122.426 197.768 179.476 1.00 30.00 ? 200 LEU A O   1 
ATOM   1597 C CB  . LEU A 1 200 ? 125.343 196.501 179.433 1.00 30.00 ? 200 LEU A CB  1 
ATOM   1598 C CG  . LEU A 1 200 ? 126.373 195.620 180.136 1.00 30.00 ? 200 LEU A CG  1 
ATOM   1599 C CD1 . LEU A 1 200 ? 127.680 196.370 180.328 1.00 30.00 ? 200 LEU A CD1 1 
ATOM   1600 C CD2 . LEU A 1 200 ? 125.851 195.117 181.470 1.00 30.00 ? 200 LEU A CD2 1 
ATOM   1601 N N   . VAL A 1 201 ? 123.005 197.121 177.371 1.00 30.00 ? 201 VAL A N   1 
ATOM   1602 C CA  . VAL A 1 201 ? 122.180 198.131 176.642 1.00 30.00 ? 201 VAL A CA  1 
ATOM   1603 C C   . VAL A 1 201 ? 120.709 197.730 176.767 1.00 30.00 ? 201 VAL A C   1 
ATOM   1604 O O   . VAL A 1 201 ? 119.880 198.631 176.990 1.00 30.00 ? 201 VAL A O   1 
ATOM   1605 C CB  . VAL A 1 201 ? 122.604 198.258 175.165 1.00 30.00 ? 201 VAL A CB  1 
ATOM   1606 C CG1 . VAL A 1 201 ? 121.615 199.086 174.360 1.00 30.00 ? 201 VAL A CG1 1 
ATOM   1607 C CG2 . VAL A 1 201 ? 124.011 198.808 175.016 1.00 30.00 ? 201 VAL A CG2 1 
ATOM   1608 N N   . LEU A 1 202 ? 120.397 196.439 176.637 1.00 30.00 ? 202 LEU A N   1 
ATOM   1609 C CA  . LEU A 1 202 ? 119.004 195.923 176.720 1.00 30.00 ? 202 LEU A CA  1 
ATOM   1610 C C   . LEU A 1 202 ? 118.452 196.161 178.131 1.00 30.00 ? 202 LEU A C   1 
ATOM   1611 O O   . LEU A 1 202 ? 117.309 196.643 178.232 1.00 30.00 ? 202 LEU A O   1 
ATOM   1612 C CB  . LEU A 1 202 ? 119.031 194.439 176.339 1.00 30.00 ? 202 LEU A CB  1 
ATOM   1613 C CG  . LEU A 1 202 ? 119.441 194.155 174.890 1.00 30.00 ? 202 LEU A CG  1 
ATOM   1614 C CD1 . LEU A 1 202 ? 119.784 192.687 174.684 1.00 30.00 ? 202 LEU A CD1 1 
ATOM   1615 C CD2 . LEU A 1 202 ? 118.357 194.581 173.922 1.00 30.00 ? 202 LEU A CD2 1 
ATOM   1616 N N   . LYS A 1 203 ? 119.231 195.881 179.180 1.00 30.00 ? 203 LYS A N   1 
ATOM   1617 C CA  . LYS A 1 203 ? 118.822 196.146 180.589 1.00 30.00 ? 203 LYS A CA  1 
ATOM   1618 C C   . LYS A 1 203 ? 118.690 197.663 180.734 1.00 30.00 ? 203 LYS A C   1 
ATOM   1619 O O   . LYS A 1 203 ? 117.803 198.108 181.485 1.00 30.00 ? 203 LYS A O   1 
ATOM   1620 C CB  . LYS A 1 203 ? 119.823 195.504 181.548 1.00 30.00 ? 203 LYS A CB  1 
ATOM   1621 C CG  . LYS A 1 203 ? 119.838 193.982 181.512 1.00 30.00 ? 203 LYS A CG  1 
ATOM   1622 C CD  . LYS A 1 203 ? 121.072 193.371 182.124 1.00 30.00 ? 203 LYS A CD  1 
ATOM   1623 C CE  . LYS A 1 203 ? 121.006 191.860 182.191 1.00 30.00 ? 203 LYS A CE  1 
ATOM   1624 N NZ  . LYS A 1 203 ? 119.962 191.399 183.134 1.00 30.00 ? 203 LYS A NZ  1 
ATOM   1625 N N   . GLY A 1 204 ? 119.530 198.427 180.033 1.00 30.00 ? 204 GLY A N   1 
ATOM   1626 C CA  . GLY A 1 204 ? 119.478 199.901 180.049 1.00 30.00 ? 204 GLY A CA  1 
ATOM   1627 C C   . GLY A 1 204 ? 118.156 200.407 179.505 1.00 30.00 ? 204 GLY A C   1 
ATOM   1628 O O   . GLY A 1 204 ? 117.654 201.407 180.047 1.00 30.00 ? 204 GLY A O   1 
ATOM   1629 N N   . LEU A 1 205 ? 117.592 199.738 178.493 1.00 30.00 ? 205 LEU A N   1 
ATOM   1630 C CA  . LEU A 1 205 ? 116.316 200.161 177.856 1.00 30.00 ? 205 LEU A CA  1 
ATOM   1631 C C   . LEU A 1 205 ? 115.226 200.217 178.926 1.00 30.00 ? 205 LEU A C   1 
ATOM   1632 O O   . LEU A 1 205 ? 114.434 201.176 178.898 1.00 30.00 ? 205 LEU A O   1 
ATOM   1633 C CB  . LEU A 1 205 ? 115.930 199.168 176.755 1.00 30.00 ? 205 LEU A CB  1 
ATOM   1634 C CG  . LEU A 1 205 ? 116.793 199.199 175.498 1.00 30.00 ? 205 LEU A CG  1 
ATOM   1635 C CD1 . LEU A 1 205 ? 116.229 198.268 174.433 1.00 30.00 ? 205 LEU A CD1 1 
ATOM   1636 C CD2 . LEU A 1 205 ? 116.910 200.619 174.969 1.00 30.00 ? 205 LEU A CD2 1 
ATOM   1637 N N   . GLY A 1 206 ? 115.191 199.236 179.830 1.00 30.00 ? 206 GLY A N   1 
ATOM   1638 C CA  . GLY A 1 206 ? 114.194 199.194 180.917 1.00 30.00 ? 206 GLY A CA  1 
ATOM   1639 C C   . GLY A 1 206 ? 113.363 197.929 180.852 1.00 30.00 ? 206 GLY A C   1 
ATOM   1640 O O   . GLY A 1 206 ? 113.837 196.969 180.237 1.00 30.00 ? 206 GLY A O   1 
ATOM   1641 N N   . MET A 1 207 ? 112.159 197.916 181.427 1.00 30.00 ? 207 MET A N   1 
ATOM   1642 C CA  . MET A 1 207 ? 111.298 196.702 181.503 1.00 30.00 ? 207 MET A CA  1 
ATOM   1643 C C   . MET A 1 207 ? 110.425 196.553 180.248 1.00 30.00 ? 207 MET A C   1 
ATOM   1644 O O   . MET A 1 207 ? 109.860 197.554 179.822 1.00 30.00 ? 207 MET A O   1 
ATOM   1645 C CB  . MET A 1 207 ? 110.403 196.794 182.743 1.00 30.00 ? 207 MET A CB  1 
ATOM   1646 C CG  . MET A 1 207 ? 109.240 195.824 182.775 1.00 30.00 ? 207 MET A CG  1 
ATOM   1647 S SD  . MET A 1 207 ? 109.771 194.109 182.984 1.00 30.00 ? 207 MET A SD  1 
ATOM   1648 C CE  . MET A 1 207 ? 109.592 193.929 184.757 1.00 30.00 ? 207 MET A CE  1 
ATOM   1649 N N   . ASN A 1 208 ? 110.304 195.337 179.711 1.00 30.00 ? 208 ASN A N   1 
ATOM   1650 C CA  . ASN A 1 208 ? 109.468 195.017 178.516 1.00 30.00 ? 208 ASN A CA  1 
ATOM   1651 C C   . ASN A 1 208 ? 109.875 195.839 177.286 1.00 30.00 ? 208 ASN A C   1 
ATOM   1652 O O   . ASN A 1 208 ? 109.000 196.474 176.690 1.00 30.00 ? 208 ASN A O   1 
ATOM   1653 C CB  . ASN A 1 208 ? 107.976 195.156 178.838 1.00 30.00 ? 208 ASN A CB  1 
ATOM   1654 C CG  . ASN A 1 208 ? 107.510 194.136 179.856 1.00 30.00 ? 208 ASN A CG  1 
ATOM   1655 O OD1 . ASN A 1 208 ? 106.974 194.491 180.903 1.00 30.00 ? 208 ASN A OD1 1 
ATOM   1656 N ND2 . ASN A 1 208 ? 107.687 192.863 179.547 1.00 30.00 ? 208 ASN A ND2 1 
ATOM   1657 N N   . PRO A 1 209 ? 111.154 195.846 176.867 1.00 30.00 ? 209 PRO A N   1 
ATOM   1658 C CA  . PRO A 1 209 ? 111.535 196.530 175.636 1.00 30.00 ? 209 PRO A CA  1 
ATOM   1659 C C   . PRO A 1 209 ? 110.966 195.754 174.433 1.00 30.00 ? 209 PRO A C   1 
ATOM   1660 O O   . PRO A 1 209 ? 111.116 194.560 174.420 1.00 30.00 ? 209 PRO A O   1 
ATOM   1661 C CB  . PRO A 1 209 ? 113.064 196.504 175.688 1.00 30.00 ? 209 PRO A CB  1 
ATOM   1662 C CG  . PRO A 1 209 ? 113.393 195.273 176.490 1.00 30.00 ? 209 PRO A CG  1 
ATOM   1663 C CD  . PRO A 1 209 ? 112.281 195.172 177.508 1.00 30.00 ? 209 PRO A CD  1 
ATOM   1664 N N   . THR A 1 210 ? 110.333 196.412 173.464 1.00 30.00 ? 210 THR A N   1 
ATOM   1665 C CA  . THR A 1 210 ? 109.818 195.758 172.228 1.00 30.00 ? 210 THR A CA  1 
ATOM   1666 C C   . THR A 1 210 ? 111.014 195.340 171.366 1.00 30.00 ? 210 THR A C   1 
ATOM   1667 O O   . THR A 1 210 ? 112.103 195.871 171.599 1.00 30.00 ? 210 THR A O   1 
ATOM   1668 C CB  . THR A 1 210 ? 108.892 196.670 171.420 1.00 30.00 ? 210 THR A CB  1 
ATOM   1669 O OG1 . THR A 1 210 ? 109.694 197.701 170.847 1.00 30.00 ? 210 THR A OG1 1 
ATOM   1670 C CG2 . THR A 1 210 ? 107.773 197.266 172.243 1.00 30.00 ? 210 THR A CG2 1 
ATOM   1671 N N   . LEU A 1 211 ? 110.848 194.389 170.456 1.00 30.00 ? 211 LEU A N   1 
ATOM   1672 C CA  . LEU A 1 211 ? 111.949 193.905 169.586 1.00 30.00 ? 211 LEU A CA  1 
ATOM   1673 C C   . LEU A 1 211 ? 112.508 195.066 168.753 1.00 30.00 ? 211 LEU A C   1 
ATOM   1674 O O   . LEU A 1 211 ? 113.718 195.151 168.654 1.00 30.00 ? 211 LEU A O   1 
ATOM   1675 C CB  . LEU A 1 211 ? 111.450 192.779 168.681 1.00 30.00 ? 211 LEU A CB  1 
ATOM   1676 C CG  . LEU A 1 211 ? 112.508 192.168 167.763 1.00 30.00 ? 211 LEU A CG  1 
ATOM   1677 C CD1 . LEU A 1 211 ? 113.618 191.503 168.561 1.00 30.00 ? 211 LEU A CD1 1 
ATOM   1678 C CD2 . LEU A 1 211 ? 111.875 191.166 166.814 1.00 30.00 ? 211 LEU A CD2 1 
ATOM   1679 N N   . GLU A 1 212 ? 111.647 195.919 168.203 1.00 30.00 ? 212 GLU A N   1 
ATOM   1680 C CA  . GLU A 1 212 ? 112.082 197.093 167.399 1.00 30.00 ? 212 GLU A CA  1 
ATOM   1681 C C   . GLU A 1 212 ? 113.011 197.947 168.265 1.00 30.00 ? 212 GLU A C   1 
ATOM   1682 O O   . GLU A 1 212 ? 114.118 198.198 167.826 1.00 30.00 ? 212 GLU A O   1 
ATOM   1683 C CB  . GLU A 1 212 ? 110.893 197.939 166.957 1.00 30.00 ? 212 GLU A CB  1 
ATOM   1684 C CG  . GLU A 1 212 ? 111.299 199.179 166.177 1.00 30.00 ? 212 GLU A CG  1 
ATOM   1685 C CD  . GLU A 1 212 ? 110.175 200.146 165.846 1.00 30.00 ? 212 GLU A CD  1 
ATOM   1686 O OE1 . GLU A 1 212 ? 109.024 199.881 166.237 1.00 30.00 ? 212 GLU A OE1 1 
ATOM   1687 O OE2 . GLU A 1 212 ? 110.460 201.171 165.201 1.00 30.00 ? 212 GLU A OE2 1 
ATOM   1688 N N   . GLU A 1 213 ? 112.620 198.241 169.508 1.00 30.00 ? 213 GLU A N   1 
ATOM   1689 C CA  . GLU A 1 213 ? 113.423 199.084 170.441 1.00 30.00 ? 213 GLU A CA  1 
ATOM   1690 C C   . GLU A 1 213 ? 114.763 198.407 170.727 1.00 30.00 ? 213 GLU A C   1 
ATOM   1691 O O   . GLU A 1 213 ? 115.768 199.096 170.724 1.00 30.00 ? 213 GLU A O   1 
ATOM   1692 C CB  . GLU A 1 213 ? 112.636 199.365 171.720 1.00 30.00 ? 213 GLU A CB  1 
ATOM   1693 C CG  . GLU A 1 213 ? 111.443 200.273 171.501 1.00 30.00 ? 213 GLU A CG  1 
ATOM   1694 C CD  . GLU A 1 213 ? 110.504 200.425 172.686 1.00 30.00 ? 213 GLU A CD  1 
ATOM   1695 O OE1 . GLU A 1 213 ? 110.762 199.809 173.736 1.00 30.00 ? 213 GLU A OE1 1 
ATOM   1696 O OE2 . GLU A 1 213 ? 109.511 201.156 172.549 1.00 30.00 ? 213 GLU A OE2 1 
ATOM   1697 N N   . MET A 1 214 ? 114.779 197.092 170.890 1.00 30.00 ? 214 MET A N   1 
ATOM   1698 C CA  . MET A 1 214 ? 116.011 196.320 171.173 1.00 30.00 ? 214 MET A CA  1 
ATOM   1699 C C   . MET A 1 214 ? 116.933 196.300 169.948 1.00 30.00 ? 214 MET A C   1 
ATOM   1700 O O   . MET A 1 214 ? 118.118 196.472 170.139 1.00 30.00 ? 214 MET A O   1 
ATOM   1701 C CB  . MET A 1 214 ? 115.653 194.881 171.563 1.00 30.00 ? 214 MET A CB  1 
ATOM   1702 C CG  . MET A 1 214 ? 115.156 194.735 172.988 1.00 30.00 ? 214 MET A CG  1 
ATOM   1703 S SD  . MET A 1 214 ? 114.943 193.008 173.522 1.00 30.00 ? 214 MET A SD  1 
ATOM   1704 C CE  . MET A 1 214 ? 113.857 192.371 172.249 1.00 30.00 ? 214 MET A CE  1 
ATOM   1705 N N   . LEU A 1 215 ? 116.402 196.046 168.752 1.00 30.00 ? 215 LEU A N   1 
ATOM   1706 C CA  . LEU A 1 215 ? 117.191 196.037 167.492 1.00 30.00 ? 215 LEU A CA  1 
ATOM   1707 C C   . LEU A 1 215 ? 117.762 197.439 167.257 1.00 30.00 ? 215 LEU A C   1 
ATOM   1708 O O   . LEU A 1 215 ? 118.954 197.523 167.006 1.00 30.00 ? 215 LEU A O   1 
ATOM   1709 C CB  . LEU A 1 215 ? 116.272 195.595 166.352 1.00 30.00 ? 215 LEU A CB  1 
ATOM   1710 C CG  . LEU A 1 215 ? 115.991 194.094 166.294 1.00 30.00 ? 215 LEU A CG  1 
ATOM   1711 C CD1 . LEU A 1 215 ? 114.878 193.779 165.312 1.00 30.00 ? 215 LEU A CD1 1 
ATOM   1712 C CD2 . LEU A 1 215 ? 117.247 193.324 165.926 1.00 30.00 ? 215 LEU A CD2 1 
ATOM   1713 N N   . THR A 1 216 ? 116.961 198.484 167.428 1.00 30.00 ? 216 THR A N   1 
ATOM   1714 C CA  . THR A 1 216 ? 117.399 199.895 167.248 1.00 30.00 ? 216 THR A CA  1 
ATOM   1715 C C   . THR A 1 216 ? 118.514 200.210 168.248 1.00 30.00 ? 216 THR A C   1 
ATOM   1716 O O   . THR A 1 216 ? 119.524 200.759 167.825 1.00 30.00 ? 216 THR A O   1 
ATOM   1717 C CB  . THR A 1 216 ? 116.199 200.843 167.350 1.00 30.00 ? 216 THR A CB  1 
ATOM   1718 O OG1 . THR A 1 216 ? 115.196 200.445 166.418 1.00 30.00 ? 216 THR A OG1 1 
ATOM   1719 C CG2 . THR A 1 216 ? 116.575 202.285 167.092 1.00 30.00 ? 216 THR A CG2 1 
ATOM   1720 N N   . ALA A 1 217 ? 118.358 199.825 169.514 1.00 30.00 ? 217 ALA A N   1 
ATOM   1721 C CA  . ALA A 1 217 ? 119.376 200.122 170.551 1.00 30.00 ? 217 ALA A CA  1 
ATOM   1722 C C   . ALA A 1 217 ? 120.690 199.362 170.319 1.00 30.00 ? 217 ALA A C   1 
ATOM   1723 O O   . ALA A 1 217 ? 121.736 199.966 170.569 1.00 30.00 ? 217 ALA A O   1 
ATOM   1724 C CB  . ALA A 1 217 ? 118.828 199.869 171.937 1.00 30.00 ? 217 ALA A CB  1 
ATOM   1725 N N   . CYS A 1 218 ? 120.656 198.101 169.883 1.00 30.00 ? 218 CYS A N   1 
ATOM   1726 C CA  . CYS A 1 218 ? 121.919 197.313 169.775 1.00 30.00 ? 218 CYS A CA  1 
ATOM   1727 C C   . CYS A 1 218 ? 122.559 197.387 168.377 1.00 30.00 ? 218 CYS A C   1 
ATOM   1728 O O   . CYS A 1 218 ? 123.586 196.729 168.178 1.00 30.00 ? 218 CYS A O   1 
ATOM   1729 C CB  . CYS A 1 218 ? 121.683 195.859 170.171 1.00 30.00 ? 218 CYS A CB  1 
ATOM   1730 S SG  . CYS A 1 218 ? 121.247 195.687 171.920 1.00 30.00 ? 218 CYS A SG  1 
ATOM   1731 N N   . GLN A 1 219 ? 121.975 198.139 167.452 1.00 30.00 ? 219 GLN A N   1 
ATOM   1732 C CA  . GLN A 1 219 ? 122.586 198.309 166.104 1.00 30.00 ? 219 GLN A CA  1 
ATOM   1733 C C   . GLN A 1 219 ? 123.988 198.918 166.246 1.00 30.00 ? 219 GLN A C   1 
ATOM   1734 O O   . GLN A 1 219 ? 124.085 200.026 166.766 1.00 30.00 ? 219 GLN A O   1 
ATOM   1735 C CB  . GLN A 1 219 ? 121.685 199.170 165.221 1.00 30.00 ? 219 GLN A CB  1 
ATOM   1736 C CG  . GLN A 1 219 ? 122.113 199.176 163.762 1.00 30.00 ? 219 GLN A CG  1 
ATOM   1737 C CD  . GLN A 1 219 ? 121.074 199.804 162.868 1.00 30.00 ? 219 GLN A CD  1 
ATOM   1738 O OE1 . GLN A 1 219 ? 120.081 200.358 163.332 1.00 30.00 ? 219 GLN A OE1 1 
ATOM   1739 N NE2 . GLN A 1 219 ? 121.297 199.722 161.568 1.00 30.00 ? 219 GLN A NE2 1 
ATOM   1740 N N   . GLY A 1 220 ? 125.027 198.194 165.822 1.00 30.00 ? 220 GLY A N   1 
ATOM   1741 C CA  . GLY A 1 220 ? 126.409 198.702 165.888 1.00 30.00 ? 220 GLY A CA  1 
ATOM   1742 C C   . GLY A 1 220 ? 127.043 198.555 167.255 1.00 30.00 ? 220 GLY A C   1 
ATOM   1743 O O   . GLY A 1 220 ? 128.063 199.220 167.491 1.00 30.00 ? 220 GLY A O   1 
ATOM   1744 N N   . VAL A 1 221 ? 126.482 197.741 168.150 1.00 30.00 ? 221 VAL A N   1 
ATOM   1745 C CA  . VAL A 1 221 ? 127.095 197.482 169.488 1.00 30.00 ? 221 VAL A CA  1 
ATOM   1746 C C   . VAL A 1 221 ? 127.897 196.185 169.357 1.00 30.00 ? 221 VAL A C   1 
ATOM   1747 O O   . VAL A 1 221 ? 127.264 195.130 169.215 1.00 30.00 ? 221 VAL A O   1 
ATOM   1748 C CB  . VAL A 1 221 ? 126.047 197.420 170.620 1.00 30.00 ? 221 VAL A CB  1 
ATOM   1749 C CG1 . VAL A 1 221 ? 126.678 197.012 171.943 1.00 30.00 ? 221 VAL A CG1 1 
ATOM   1750 C CG2 . VAL A 1 221 ? 125.277 198.720 170.766 1.00 30.00 ? 221 VAL A CG2 1 
ATOM   1751 N N   . GLY A 1 222 ? 129.229 196.259 169.350 1.00 30.00 ? 222 GLY A N   1 
ATOM   1752 C CA  . GLY A 1 222 ? 130.118 195.092 169.173 1.00 30.00 ? 222 GLY A CA  1 
ATOM   1753 C C   . GLY A 1 222 ? 130.723 195.057 167.775 1.00 30.00 ? 222 GLY A C   1 
ATOM   1754 O O   . GLY A 1 222 ? 129.939 195.157 166.810 1.00 30.00 ? 222 GLY A O   1 
HETATM 1755 C C1  . IHP B 2 .   ? 104.525 178.547 132.295 0.17 20.00 ? 301 IHP A C1  1 
HETATM 1756 C C2  . IHP B 2 .   ? 103.386 178.301 133.283 0.17 20.00 ? 301 IHP A C2  1 
HETATM 1757 C C3  . IHP B 2 .   ? 102.945 179.526 134.071 0.17 20.00 ? 301 IHP A C3  1 
HETATM 1758 C C4  . IHP B 2 .   ? 102.797 180.748 133.188 0.17 20.00 ? 301 IHP A C4  1 
HETATM 1759 C C5  . IHP B 2 .   ? 104.163 181.008 132.600 0.17 20.00 ? 301 IHP A C5  1 
HETATM 1760 C C6  . IHP B 2 .   ? 104.488 179.908 131.607 0.17 20.00 ? 301 IHP A C6  1 
HETATM 1761 O O11 . IHP B 2 .   ? 104.435 177.567 131.306 0.17 20.00 ? 301 IHP A O11 1 
HETATM 1762 P P1  . IHP B 2 .   ? 105.667 176.482 131.189 0.17 20.00 ? 301 IHP A P1  1 
HETATM 1763 O O21 . IHP B 2 .   ? 106.508 176.833 129.988 0.17 20.00 ? 301 IHP A O21 1 
HETATM 1764 O O31 . IHP B 2 .   ? 106.518 176.542 132.432 0.17 20.00 ? 301 IHP A O31 1 
HETATM 1765 O O41 . IHP B 2 .   ? 105.096 175.094 131.045 0.17 20.00 ? 301 IHP A O41 1 
HETATM 1766 O O12 . IHP B 2 .   ? 103.903 177.433 134.235 0.17 20.00 ? 301 IHP A O12 1 
HETATM 1767 P P2  . IHP B 2 .   ? 103.215 175.960 134.446 0.17 20.00 ? 301 IHP A P2  1 
HETATM 1768 O O22 . IHP B 2 .   ? 102.281 175.662 133.300 0.17 20.00 ? 301 IHP A O22 1 
HETATM 1769 O O32 . IHP B 2 .   ? 104.314 174.931 134.482 0.17 20.00 ? 301 IHP A O32 1 
HETATM 1770 O O42 . IHP B 2 .   ? 102.451 175.983 135.745 0.17 20.00 ? 301 IHP A O42 1 
HETATM 1771 O O13 . IHP B 2 .   ? 101.702 179.277 134.644 0.17 20.00 ? 301 IHP A O13 1 
HETATM 1772 P P3  . IHP B 2 .   ? 101.536 179.763 136.202 0.17 20.00 ? 301 IHP A P3  1 
HETATM 1773 O O23 . IHP B 2 .   ? 101.885 181.226 136.323 0.17 20.00 ? 301 IHP A O23 1 
HETATM 1774 O O33 . IHP B 2 .   ? 100.110 179.535 136.632 0.17 20.00 ? 301 IHP A O33 1 
HETATM 1775 O O43 . IHP B 2 .   ? 102.479 178.953 137.055 0.17 20.00 ? 301 IHP A O43 1 
HETATM 1776 O O14 . IHP B 2 .   ? 101.860 180.530 132.175 0.17 20.00 ? 301 IHP A O14 1 
HETATM 1777 P P4  . IHP B 2 .   ? 100.599 181.584 132.106 0.17 20.00 ? 301 IHP A P4  1 
HETATM 1778 O O24 . IHP B 2 .   ? 101.081 182.899 131.541 0.17 20.00 ? 301 IHP A O24 1 
HETATM 1779 O O34 . IHP B 2 .   ? 99.512  181.021 131.223 0.17 20.00 ? 301 IHP A O34 1 
HETATM 1780 O O44 . IHP B 2 .   ? 100.060 181.796 133.499 0.17 20.00 ? 301 IHP A O44 1 
HETATM 1781 O O15 . IHP B 2 .   ? 104.093 182.247 131.976 0.17 20.00 ? 301 IHP A O15 1 
HETATM 1782 P P5  . IHP B 2 .   ? 104.483 183.550 132.891 0.17 20.00 ? 301 IHP A P5  1 
HETATM 1783 O O25 . IHP B 2 .   ? 103.318 183.896 133.784 0.17 20.00 ? 301 IHP A O25 1 
HETATM 1784 O O35 . IHP B 2 .   ? 105.689 183.207 133.731 0.17 20.00 ? 301 IHP A O35 1 
HETATM 1785 O O45 . IHP B 2 .   ? 104.804 184.701 131.972 0.17 20.00 ? 301 IHP A O45 1 
HETATM 1786 O O16 . IHP B 2 .   ? 105.772 180.119 131.118 0.17 20.00 ? 301 IHP A O16 1 
HETATM 1787 P P6  . IHP B 2 .   ? 106.020 181.028 129.771 0.17 20.00 ? 301 IHP A P6  1 
HETATM 1788 O O26 . IHP B 2 .   ? 106.847 180.223 128.801 0.17 20.00 ? 301 IHP A O26 1 
HETATM 1789 O O36 . IHP B 2 .   ? 106.749 182.281 130.182 0.17 20.00 ? 301 IHP A O36 1 
HETATM 1790 O O46 . IHP B 2 .   ? 104.703 181.402 129.137 0.17 20.00 ? 301 IHP A O46 1 
HETATM 1791 C C1  . IHP C 2 .   ? 112.144 178.653 138.621 0.17 20.00 ? 302 IHP A C1  1 
HETATM 1792 C C2  . IHP C 2 .   ? 113.348 178.202 137.783 0.17 20.00 ? 302 IHP A C2  1 
HETATM 1793 C C3  . IHP C 2 .   ? 113.874 179.288 136.850 0.17 20.00 ? 302 IHP A C3  1 
HETATM 1794 C C4  . IHP C 2 .   ? 114.144 180.541 137.650 0.17 20.00 ? 302 IHP A C4  1 
HETATM 1795 C C5  . IHP C 2 .   ? 112.771 181.055 138.005 0.17 20.00 ? 302 IHP A C5  1 
HETATM 1796 C C6  . IHP C 2 .   ? 112.132 180.128 139.030 0.17 20.00 ? 302 IHP A C6  1 
HETATM 1797 O O11 . IHP C 2 .   ? 112.210 177.954 139.823 0.17 20.00 ? 302 IHP A O11 1 
HETATM 1798 P P1  . IHP C 2 .   ? 110.984 176.936 140.224 0.17 20.00 ? 302 IHP A P1  1 
HETATM 1799 O O21 . IHP C 2 .   ? 109.709 177.719 140.413 0.17 20.00 ? 302 IHP A O21 1 
HETATM 1800 O O31 . IHP C 2 .   ? 110.791 175.965 139.087 0.17 20.00 ? 302 IHP A O31 1 
HETATM 1801 O O41 . IHP C 2 .   ? 111.350 176.214 141.495 0.17 20.00 ? 302 IHP A O41 1 
HETATM 1802 O O12 . IHP C 2 .   ? 112.954 177.124 136.987 0.17 20.00 ? 302 IHP A O12 1 
HETATM 1803 P P2  . IHP C 2 .   ? 113.746 175.695 137.169 0.17 20.00 ? 302 IHP A P2  1 
HETATM 1804 O O22 . IHP C 2 .   ? 114.874 175.587 136.179 0.17 20.00 ? 302 IHP A O22 1 
HETATM 1805 O O32 . IHP C 2 .   ? 114.311 175.634 138.563 0.17 20.00 ? 302 IHP A O32 1 
HETATM 1806 O O42 . IHP C 2 .   ? 112.759 174.575 136.970 0.17 20.00 ? 302 IHP A O42 1 
HETATM 1807 O O13 . IHP C 2 .   ? 115.079 178.909 136.257 0.17 20.00 ? 302 IHP A O13 1 
HETATM 1808 P P3  . IHP C 2 .   ? 115.351 179.529 134.759 0.17 20.00 ? 302 IHP A P3  1 
HETATM 1809 O O23 . IHP C 2 .   ? 115.927 180.918 134.852 0.17 20.00 ? 302 IHP A O23 1 
HETATM 1810 O O33 . IHP C 2 .   ? 116.317 178.645 134.012 0.17 20.00 ? 302 IHP A O33 1 
HETATM 1811 O O43 . IHP C 2 .   ? 114.023 179.577 134.049 0.17 20.00 ? 302 IHP A O43 1 
HETATM 1812 O O14 . IHP C 2 .   ? 114.886 180.254 138.801 0.17 20.00 ? 302 IHP A O14 1 
HETATM 1813 P P4  . IHP C 2 .   ? 116.486 180.655 138.815 0.17 20.00 ? 302 IHP A P4  1 
HETATM 1814 O O24 . IHP C 2 .   ? 116.809 181.534 137.629 0.17 20.00 ? 302 IHP A O24 1 
HETATM 1815 O O34 . IHP C 2 .   ? 116.805 181.413 140.078 0.17 20.00 ? 302 IHP A O34 1 
HETATM 1816 O O44 . IHP C 2 .   ? 117.315 179.395 138.734 0.17 20.00 ? 302 IHP A O44 1 
HETATM 1817 O O15 . IHP C 2 .   ? 112.937 182.333 138.537 0.17 20.00 ? 302 IHP A O15 1 
HETATM 1818 P P5  . IHP C 2 .   ? 113.029 183.575 137.467 0.17 20.00 ? 302 IHP A P5  1 
HETATM 1819 O O25 . IHP C 2 .   ? 114.447 184.076 137.393 0.17 20.00 ? 302 IHP A O25 1 
HETATM 1820 O O35 . IHP C 2 .   ? 112.579 183.083 136.113 0.17 20.00 ? 302 IHP A O35 1 
HETATM 1821 O O45 . IHP C 2 .   ? 112.112 184.690 137.919 0.17 20.00 ? 302 IHP A O45 1 
HETATM 1822 O O16 . IHP C 2 .   ? 110.800 180.513 139.174 0.17 20.00 ? 302 IHP A O16 1 
HETATM 1823 P P6  . IHP C 2 .   ? 110.359 181.376 140.506 0.17 20.00 ? 302 IHP A P6  1 
HETATM 1824 O O26 . IHP C 2 .   ? 109.195 180.689 141.175 0.17 20.00 ? 302 IHP A O26 1 
HETATM 1825 O O36 . IHP C 2 .   ? 109.952 182.755 140.056 0.17 20.00 ? 302 IHP A O36 1 
HETATM 1826 O O46 . IHP C 2 .   ? 111.502 181.484 141.483 0.17 20.00 ? 302 IHP A O46 1 
HETATM 1827 O O   . HOH D 3 .   ? 110.343 173.562 139.512 1.00 30.00 ? 401 HOH A O   1 
HETATM 1828 O O   . HOH D 3 .   ? 115.351 195.149 179.376 1.00 30.00 ? 402 HOH A O   1 
HETATM 1829 O O   . HOH D 3 .   ? 97.774  166.326 139.675 1.00 30.00 ? 403 HOH A O   1 
HETATM 1830 O O   . HOH D 3 .   ? 118.647 181.608 173.668 1.00 30.00 ? 404 HOH A O   1 
HETATM 1831 O O   . HOH D 3 .   ? 117.098 167.574 165.571 1.00 30.00 ? 405 HOH A O   1 
HETATM 1832 O O   . HOH D 3 .   ? 91.793  174.550 142.194 1.00 30.00 ? 406 HOH A O   1 
HETATM 1833 O O   . HOH D 3 .   ? 114.607 168.071 141.085 1.00 30.00 ? 407 HOH A O   1 
HETATM 1834 O O   . HOH D 3 .   ? 92.728  160.495 145.295 1.00 30.00 ? 408 HOH A O   1 
HETATM 1835 O O   . HOH D 3 .   ? 117.437 190.219 162.234 1.00 30.00 ? 409 HOH A O   1 
HETATM 1836 O O   . HOH D 3 .   ? 96.866  175.089 155.978 1.00 30.00 ? 410 HOH A O   1 
HETATM 1837 O O   . HOH D 3 .   ? 119.370 182.423 160.776 1.00 30.00 ? 411 HOH A O   1 
HETATM 1838 O O   . HOH D 3 .   ? 121.031 180.853 179.406 1.00 30.00 ? 412 HOH A O   1 
HETATM 1839 O O   . HOH D 3 .   ? 114.122 171.661 161.174 1.00 30.00 ? 413 HOH A O   1 
HETATM 1840 O O   . HOH D 3 .   ? 116.385 196.322 182.943 1.00 30.00 ? 414 HOH A O   1 
HETATM 1841 O O   . HOH D 3 .   ? 102.981 169.392 164.775 1.00 30.00 ? 415 HOH A O   1 
HETATM 1842 O O   . HOH D 3 .   ? 114.414 203.222 177.115 1.00 30.00 ? 416 HOH A O   1 
HETATM 1843 O O   . HOH D 3 .   ? 116.518 203.760 179.265 1.00 30.00 ? 417 HOH A O   1 
HETATM 1844 O O   . HOH D 3 .   ? 120.109 202.186 165.360 1.00 30.00 ? 418 HOH A O   1 
HETATM 1845 O O   . HOH D 3 .   ? 109.761 183.006 165.273 1.00 30.00 ? 419 HOH A O   1 
HETATM 1846 O O   . HOH D 3 .   ? 117.979 198.639 163.727 1.00 30.00 ? 420 HOH A O   1 
HETATM 1847 O O   . HOH D 3 .   ? 106.025 186.738 178.677 1.00 30.00 ? 421 HOH A O   1 
HETATM 1848 O O   . HOH D 3 .   ? 125.231 194.493 167.457 1.00 30.00 ? 422 HOH A O   1 
HETATM 1849 O O   . HOH D 3 .   ? 114.250 175.973 163.468 1.00 30.00 ? 423 HOH A O   1 
HETATM 1850 O O   . HOH D 3 .   ? 124.583 185.849 177.948 1.00 30.00 ? 424 HOH A O   1 
HETATM 1851 O O   . HOH D 3 .   ? 100.481 159.744 143.397 1.00 30.00 ? 425 HOH A O   1 
HETATM 1852 O O   . HOH D 3 .   ? 111.749 190.069 171.437 1.00 30.00 ? 426 HOH A O   1 
HETATM 1853 O O   . HOH D 3 .   ? 94.337  174.692 154.651 1.00 30.00 ? 427 HOH A O   1 
HETATM 1854 O O   . HOH D 3 .   ? 123.766 182.872 177.677 1.00 30.00 ? 428 HOH A O   1 
HETATM 1855 O O   . HOH D 3 .   ? 108.397 189.061 169.022 1.00 30.00 ? 429 HOH A O   1 
HETATM 1856 O O   . HOH D 3 .   ? 103.922 155.371 156.509 1.00 30.00 ? 430 HOH A O   1 
HETATM 1857 O O   . HOH D 3 .   ? 114.550 184.454 161.725 1.00 30.00 ? 431 HOH A O   1 
HETATM 1858 O O   . HOH D 3 .   ? 126.757 192.183 180.752 1.00 30.00 ? 432 HOH A O   1 
HETATM 1859 O O   . HOH D 3 .   ? 116.231 188.459 180.852 1.00 30.00 ? 433 HOH A O   1 
HETATM 1860 O O   . HOH D 3 .   ? 105.651 172.464 134.148 1.00 30.00 ? 434 HOH A O   1 
HETATM 1861 O O   . HOH D 3 .   ? 126.801 187.961 178.053 1.00 30.00 ? 435 HOH A O   1 
HETATM 1862 O O   . HOH D 3 .   ? 128.173 192.232 168.896 1.00 30.00 ? 436 HOH A O   1 
HETATM 1863 O O   . HOH D 3 .   ? 108.855 187.738 180.029 1.00 30.00 ? 437 HOH A O   1 
HETATM 1864 O O   . HOH D 3 .   ? 125.993 185.641 174.354 1.00 30.00 ? 438 HOH A O   1 
HETATM 1865 O O   . HOH D 3 .   ? 113.852 173.883 174.491 1.00 30.00 ? 439 HOH A O   1 
HETATM 1866 O O   . HOH D 3 .   ? 95.430  159.735 145.959 1.00 30.00 ? 440 HOH A O   1 
HETATM 1867 O O   . HOH D 3 .   ? 107.551 156.641 151.909 1.00 30.00 ? 441 HOH A O   1 
HETATM 1868 O O   . HOH D 3 .   ? 110.480 192.646 180.636 1.00 30.00 ? 442 HOH A O   1 
HETATM 1869 O O   . HOH D 3 .   ? 112.234 163.847 147.327 1.00 30.00 ? 443 HOH A O   1 
HETATM 1870 O O   . HOH D 3 .   ? 102.490 177.415 156.768 1.00 30.00 ? 444 HOH A O   1 
HETATM 1871 O O   . HOH D 3 .   ? 114.050 175.180 169.087 1.00 30.00 ? 445 HOH A O   1 
HETATM 1872 O O   . HOH D 3 .   ? 119.560 179.243 177.479 1.00 30.00 ? 446 HOH A O   1 
HETATM 1873 O O   . HOH D 3 .   ? 107.740 189.219 172.707 1.00 30.00 ? 447 HOH A O   1 
HETATM 1874 O O   . HOH D 3 .   ? 93.324  176.577 148.787 1.00 30.00 ? 448 HOH A O   1 
HETATM 1875 O O   . HOH D 3 .   ? 103.569 160.954 163.667 1.00 30.00 ? 449 HOH A O   1 
HETATM 1876 O O   . HOH D 3 .   ? 115.553 201.907 171.277 1.00 30.00 ? 450 HOH A O   1 
HETATM 1877 O O   . HOH D 3 .   ? 108.834 195.376 167.982 1.00 30.00 ? 451 HOH A O   1 
HETATM 1878 O O   . HOH D 3 .   ? 116.060 160.746 158.465 1.00 30.00 ? 452 HOH A O   1 
HETATM 1879 O O   . HOH D 3 .   ? 107.672 176.808 160.066 1.00 30.00 ? 453 HOH A O   1 
HETATM 1880 O O   . HOH D 3 .   ? 114.479 155.882 150.689 1.00 30.00 ? 454 HOH A O   1 
HETATM 1881 O O   . HOH D 3 .   ? 121.101 172.324 170.085 1.00 30.00 ? 455 HOH A O   1 
HETATM 1882 O O   . HOH D 3 .   ? 119.179 188.628 181.607 1.00 30.00 ? 456 HOH A O   1 
HETATM 1883 O O   . HOH D 3 .   ? 98.964  174.057 143.884 1.00 30.00 ? 457 HOH A O   1 
HETATM 1884 O O   . HOH D 3 .   ? 118.049 165.492 150.751 1.00 30.00 ? 458 HOH A O   1 
HETATM 1885 O O   . HOH D 3 .   ? 112.954 161.761 156.550 1.00 30.00 ? 459 HOH A O   1 
HETATM 1886 O O   . HOH D 3 .   ? 103.984 161.726 142.415 1.00 30.00 ? 460 HOH A O   1 
HETATM 1887 O O   . HOH D 3 .   ? 111.334 175.155 145.244 1.00 30.00 ? 461 HOH A O   1 
HETATM 1888 O O   . HOH D 3 .   ? 119.015 178.870 164.829 1.00 30.00 ? 462 HOH A O   1 
HETATM 1889 O O   . HOH D 3 .   ? 105.640 169.687 166.845 1.00 30.00 ? 463 HOH A O   1 
HETATM 1890 O O   . HOH D 3 .   ? 104.320 184.452 179.311 1.00 30.00 ? 464 HOH A O   1 
HETATM 1891 O O   . HOH D 3 .   ? 108.237 193.031 170.379 1.00 30.00 ? 465 HOH A O   1 
HETATM 1892 O O   . HOH D 3 .   ? 96.870  159.603 152.410 1.00 30.00 ? 466 HOH A O   1 
HETATM 1893 O O   . HOH D 3 .   ? 117.452 176.451 164.286 1.00 30.00 ? 467 HOH A O   1 
HETATM 1894 O O   . HOH D 3 .   ? 121.797 185.164 161.523 1.00 30.00 ? 468 HOH A O   1 
HETATM 1895 O O   . HOH D 3 .   ? 97.406  160.839 143.648 1.00 30.00 ? 469 HOH A O   1 
HETATM 1896 O O   . HOH D 3 .   ? 121.813 178.801 165.491 1.00 30.00 ? 470 HOH A O   1 
HETATM 1897 O O   . HOH D 3 .   ? 118.991 200.850 160.104 1.00 30.00 ? 471 HOH A O   1 
HETATM 1898 O O   . HOH D 3 .   ? 112.055 199.575 178.181 1.00 30.00 ? 472 HOH A O   1 
HETATM 1899 O O   . HOH D 3 .   ? 108.455 199.989 169.391 1.00 30.00 ? 473 HOH A O   1 
HETATM 1900 O O   . HOH D 3 .   ? 107.563 181.413 166.219 1.00 30.00 ? 474 HOH A O   1 
HETATM 1901 O O   . HOH D 3 .   ? 107.320 155.849 155.324 1.00 30.00 ? 475 HOH A O   1 
HETATM 1902 O O   . HOH D 3 .   ? 120.332 195.611 165.158 1.00 30.00 ? 476 HOH A O   1 
HETATM 1903 O O   . HOH D 3 .   ? 109.265 172.303 171.537 1.00 30.00 ? 477 HOH A O   1 
HETATM 1904 O O   . HOH D 3 .   ? 92.240  173.466 148.277 1.00 30.00 ? 478 HOH A O   1 
HETATM 1905 O O   . HOH D 3 .   ? 111.021 160.362 146.732 1.00 30.00 ? 479 HOH A O   1 
HETATM 1906 O O   . HOH D 3 .   ? 107.517 194.681 174.775 1.00 30.00 ? 480 HOH A O   1 
HETATM 1907 O O   . HOH D 3 .   ? 107.243 197.786 167.471 1.00 30.00 ? 481 HOH A O   1 
HETATM 1908 O O   . HOH D 3 .   ? 117.212 170.919 145.858 1.00 30.00 ? 482 HOH A O   1 
HETATM 1909 O O   . HOH D 3 .   ? 89.637  172.435 149.430 1.00 30.00 ? 483 HOH A O   1 
HETATM 1910 O O   . HOH D 3 .   ? 110.141 158.286 161.797 1.00 30.00 ? 484 HOH A O   1 
HETATM 1911 O O   . HOH D 3 .   ? 115.905 166.227 157.747 1.00 30.00 ? 485 HOH A O   1 
HETATM 1912 O O   . HOH D 3 .   ? 131.512 193.828 178.702 1.00 30.00 ? 486 HOH A O   1 
HETATM 1913 O O   . HOH D 3 .   ? 90.915  160.047 141.214 1.00 30.00 ? 487 HOH A O   1 
HETATM 1914 O O   . HOH D 3 .   ? 117.455 173.800 156.497 1.00 30.00 ? 488 HOH A O   1 
HETATM 1915 O O   . HOH D 3 .   ? 93.098  170.271 161.687 1.00 30.00 ? 489 HOH A O   1 
HETATM 1916 O O   . HOH D 3 .   ? 116.803 170.803 159.581 1.00 30.00 ? 490 HOH A O   1 
HETATM 1917 O O   . HOH D 3 .   ? 106.766 185.259 171.216 1.00 30.00 ? 491 HOH A O   1 
HETATM 1918 O O   . HOH D 3 .   ? 129.385 185.794 173.657 1.00 30.00 ? 492 HOH A O   1 
HETATM 1919 O O   . HOH D 3 .   ? 113.852 190.210 180.737 1.00 30.00 ? 493 HOH A O   1 
HETATM 1920 O O   . HOH D 3 .   ? 122.960 194.467 165.032 1.00 30.00 ? 494 HOH A O   1 
HETATM 1921 O O   . HOH D 3 .   ? 112.438 166.758 169.015 1.00 30.00 ? 495 HOH A O   1 
HETATM 1922 O O   . HOH D 3 .   ? 124.710 179.545 169.464 1.00 30.00 ? 496 HOH A O   1 
HETATM 1923 O O   . HOH D 3 .   ? 110.536 192.242 176.463 1.00 30.00 ? 497 HOH A O   1 
HETATM 1924 O O   . HOH D 3 .   ? 114.532 203.182 181.323 1.00 30.00 ? 498 HOH A O   1 
HETATM 1925 O O   . HOH D 3 .   ? 107.893 179.415 135.235 1.00 30.00 ? 499 HOH A O   1 
HETATM 1926 O O   . HOH D 3 .   ? 122.819 200.938 179.396 1.00 30.00 ? 500 HOH A O   1 
HETATM 1927 O O   . HOH D 3 .   ? 131.148 186.160 167.229 1.00 30.00 ? 501 HOH A O   1 
HETATM 1928 O O   . HOH D 3 .   ? 98.403  172.865 137.886 1.00 30.00 ? 502 HOH A O   1 
HETATM 1929 O O   . HOH D 3 .   ? 100.412 159.671 149.224 1.00 30.00 ? 503 HOH A O   1 
HETATM 1930 O O   . HOH D 3 .   ? 104.712 173.715 176.785 1.00 30.00 ? 504 HOH A O   1 
HETATM 1931 O O   . HOH D 3 .   ? 89.009  175.838 154.025 1.00 30.00 ? 505 HOH A O   1 
HETATM 1932 O O   . HOH D 3 .   ? 130.432 192.005 174.301 1.00 30.00 ? 506 HOH A O   1 
HETATM 1933 O O   . HOH D 3 .   ? 112.701 182.587 160.908 1.00 30.00 ? 507 HOH A O   1 
HETATM 1934 O O   . HOH D 3 .   ? 114.647 174.596 161.063 1.00 30.00 ? 508 HOH A O   1 
HETATM 1935 O O   . HOH D 3 .   ? 97.902  158.102 149.309 1.00 30.00 ? 509 HOH A O   1 
HETATM 1936 O O   . HOH D 3 .   ? 114.494 159.503 156.218 1.00 30.00 ? 510 HOH A O   1 
HETATM 1937 O O   . HOH D 3 .   ? 115.643 170.323 140.113 1.00 30.00 ? 511 HOH A O   1 
HETATM 1938 O O   . HOH D 3 .   ? 102.523 159.235 151.028 1.00 30.00 ? 512 HOH A O   1 
HETATM 1939 O O   . HOH D 3 .   ? 120.985 187.415 159.537 1.00 30.00 ? 513 HOH A O   1 
HETATM 1940 O O   . HOH D 3 .   ? 110.203 154.474 157.657 1.00 30.00 ? 514 HOH A O   1 
HETATM 1941 O O   . HOH D 3 .   ? 113.359 192.972 179.546 1.00 30.00 ? 515 HOH A O   1 
HETATM 1942 O O   . HOH D 3 .   ? 109.706 191.519 172.678 1.00 30.00 ? 516 HOH A O   1 
HETATM 1943 O O   . HOH D 3 .   ? 112.454 202.295 168.705 1.00 30.00 ? 517 HOH A O   1 
HETATM 1944 O O   . HOH D 3 .   ? 110.196 184.179 162.582 1.00 30.00 ? 518 HOH A O   1 
HETATM 1945 O O   . HOH D 3 .   ? 116.610 165.531 154.395 1.00 30.00 ? 519 HOH A O   1 
HETATM 1946 O O   . HOH D 3 .   ? 114.725 163.562 155.392 1.00 30.00 ? 520 HOH A O   1 
HETATM 1947 O O   . HOH D 3 .   ? 117.457 163.088 157.264 1.00 30.00 ? 521 HOH A O   1 
HETATM 1948 O O   . HOH D 3 .   ? 101.119 171.643 164.613 1.00 30.00 ? 522 HOH A O   1 
HETATM 1949 O O   . HOH D 3 .   ? 109.679 155.226 160.415 1.00 30.00 ? 523 HOH A O   1 
HETATM 1950 O O   . HOH D 3 .   ? 101.508 167.322 166.589 1.00 30.00 ? 524 HOH A O   1 
HETATM 1951 O O   . HOH D 3 .   ? 126.664 183.402 175.970 1.00 30.00 ? 525 HOH A O   1 
HETATM 1952 O O   . HOH D 3 .   ? 115.631 166.591 143.183 1.00 30.00 ? 526 HOH A O   1 
HETATM 1953 O O   . HOH D 3 .   ? 119.349 179.695 161.845 1.00 30.00 ? 527 HOH A O   1 
HETATM 1954 O O   . HOH D 3 .   ? 117.307 168.864 143.836 1.00 30.00 ? 528 HOH A O   1 
HETATM 1955 O O   . HOH D 3 .   ? 117.496 172.790 143.883 1.00 30.00 ? 529 HOH A O   1 
HETATM 1956 O O   . HOH D 3 .   ? 117.664 170.933 141.736 1.00 30.00 ? 530 HOH A O   1 
# 
