data_9CNU
# 
_entry.id   9CNU 
# 
_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   9CNU         pdb_00009cnu 10.2210/pdb9cnu/pdb 
WWPDB D_1000285880 ?            ?                   
EMDB  EMD-45760    ?            ?                   
# 
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                        9CNU 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-15 
_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 hexamer bound with Nup153 peptide; assembled with liposome templating' 
_pdbx_database_related.db_id          EMD-45760 
_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 ? ?                                    ? 
;HIV-2 GL-AN capsid protein with C-terminal Gly-Ser-Ser linker followed by a hexahistidine tag after proteolytic processing of the N-terminal Met.
;
2 polymer     syn 'Nuclear pore complex protein Nup153' 2897.363  1 ? 'Delta(1-1410) and Delta(1426-1463)' ? 
'Peptide of Nup153, residues 1411-1425 and 1464-1475' 
3 non-polymer syn 'INOSITOL HEXAKISPHOSPHATE'           660.035   2 ? ?                                    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 CA                                       
2 '153 kDa nucleoporin,Nucleoporin Nup153' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;PVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINDEAADW
DAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEP
FQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLMGSSHHHHHH
;
;PVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINDEAADW
DAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEP
FQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLMGSSHHHHHH
;
A ? 
2 'polypeptide(L)' no no PSGVFTFGANSSTPAGRKIKTAVRRRK PSGVFTFGANSSTPAGRKIKTAVRRRK B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        'INOSITOL HEXAKISPHOSPHATE' 
_pdbx_entity_nonpoly.comp_id     IHP 
# 
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 
2 1   PRO n 
2 2   SER n 
2 3   GLY n 
2 4   VAL n 
2 5   PHE n 
2 6   THR n 
2 7   PHE n 
2 8   GLY n 
2 9   ALA n 
2 10  ASN n 
2 11  SER n 
2 12  SER n 
2 13  THR n 
2 14  PRO n 
2 15  ALA n 
2 16  GLY n 
2 17  ARG n 
2 18  LYS n 
2 19  ILE n 
2 20  LYS n 
2 21  THR n 
2 22  ALA n 
2 23  VAL n 
2 24  ARG n 
2 25  ARG n 
2 26  ARG n 
2 27  LYS 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_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1  15 'Homo sapiens' human 9606 'Sequence derived from Nup153 in humans.' 
2 2 sample 16 27 'Homo sapiens' human 9606 'Sequence derived from Nup153 in humans.' 
# 
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 
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 ?   ?   ?   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 
B 2 1   PRO 1   1   ?   ?   ?   B . n 
B 2 2   SER 2   2   2   SER SER B . n 
B 2 3   GLY 3   3   3   GLY GLY B . n 
B 2 4   VAL 4   4   4   VAL VAL B . n 
B 2 5   PHE 5   5   5   PHE PHE B . n 
B 2 6   THR 6   6   6   THR THR B . n 
B 2 7   PHE 7   7   7   PHE PHE B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   ALA 9   9   9   ALA ALA B . n 
B 2 10  ASN 10  10  ?   ?   ?   B . n 
B 2 11  SER 11  11  ?   ?   ?   B . n 
B 2 12  SER 12  12  ?   ?   ?   B . n 
B 2 13  THR 13  13  ?   ?   ?   B . n 
B 2 14  PRO 14  14  ?   ?   ?   B . n 
B 2 15  ALA 15  15  ?   ?   ?   B . n 
B 2 16  GLY 16  16  ?   ?   ?   B . n 
B 2 17  ARG 17  17  ?   ?   ?   B . n 
B 2 18  LYS 18  18  ?   ?   ?   B . n 
B 2 19  ILE 19  19  ?   ?   ?   B . n 
B 2 20  LYS 20  20  ?   ?   ?   B . n 
B 2 21  THR 21  21  ?   ?   ?   B . n 
B 2 22  ALA 22  22  ?   ?   ?   B . n 
B 2 23  VAL 23  23  ?   ?   ?   B . n 
B 2 24  ARG 24  24  ?   ?   ?   B . n 
B 2 25  ARG 25  25  ?   ?   ?   B . n 
B 2 26  ARG 26  26  ?   ?   ?   B . n 
B 2 27  LYS 27  27  ?   ?   ?   B . 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 
C 3 IHP 1 301 301 IHP IHP A . 
D 3 IHP 1 302 302 IHP IHP 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                   9CNU 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9CNU 
_struct.title                        'HIV-2 CA hexamer bound with Nup153 peptide; assembled with liposome 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        9CNU 
_struct_keywords.text            'HIV-2, Capsid, IP6, Nup153, 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 3 ? 
D N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POL_HV2G1   P18042 ? 1 
;PVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINDEAADW
DAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEP
FQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLM
;
136  
2 UNP NU153_HUMAN P49790 ? 2 PSGVFTFGANSSTPA 1411 
3 UNP NU153_HUMAN P49790 ? 2 GRKIKTAVRRRK 1464 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CNU A 1  ? 231 ? P18042 136  ? 366  ? 1  231 
2 2 9CNU B 1  ? 15  ? P49790 1411 ? 1425 ? 1  15  
3 3 9CNU B 16 ? 27  ? P49790 1464 ? 1475 ? 16 27  
# 
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 9CNU GLY A 232 ? UNP P18042 ? ? 'expression tag' 232 1 
1 9CNU SER A 233 ? UNP P18042 ? ? 'expression tag' 233 2 
1 9CNU SER A 234 ? UNP P18042 ? ? 'expression tag' 234 3 
1 9CNU HIS A 235 ? UNP P18042 ? ? 'expression tag' 235 4 
1 9CNU HIS A 236 ? UNP P18042 ? ? 'expression tag' 236 5 
1 9CNU HIS A 237 ? UNP P18042 ? ? 'expression tag' 237 6 
1 9CNU HIS A 238 ? UNP P18042 ? ? 'expression tag' 238 7 
1 9CNU HIS A 239 ? UNP P18042 ? ? 'expression tag' 239 8 
1 9CNU 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 point assembly' ? dodecameric 12 
2 'point asymmetric unit'   ? dimeric     2  
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 '(1-6)' A,B,C,D 
2 1       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                
;A hexameric lattice of HIV-2 CA is apparent from 2D classes and is consistent with HIV-1 CA behavior. CPSF6 should be able to bind at 6 positions in a CA hexamer.
;
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'       1_555 x,y,z 1.00000000  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' ?     ?     0.50000000  0.86600000  0.00000000 -35.18240 -0.86600000 0.50000000  0.00000000 131.30220 
0.00000000 0.00000000 1.00000000 0.00000 
3 'point symmetry operation' ?     ?     -0.50000000 0.86600000  0.00000000 60.93740  -0.86600000 -0.50000000 0.00000000 227.42230 
0.00000000 0.00000000 1.00000000 0.00000 
4 'point symmetry operation' ?     ?     -1.00000000 0.00000000  0.00000000 192.23970 0.00000000  -1.00000000 0.00000000 192.24020 
0.00000000 0.00000000 1.00000000 0.00000 
5 'point symmetry operation' ?     ?     -0.50000000 -0.86600000 0.00000000 227.42250 0.86600000  -0.50000000 0.00000000 60.93810  
0.00000000 0.00000000 1.00000000 0.00000 
6 'point symmetry operation' ?     ?     0.50000000  -0.86600000 0.00000000 131.30290 0.86600000  0.50000000  0.00000000 -35.18220 
0.00000000 0.00000000 1.00000000 0.00000 
# 
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 ARG A 18  ? LYS A 30  ? ARG A 18  LYS A 30  1 ? 13 
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 VAL A 110 ? TYR A 118 ? VAL A 110 TYR A 118 1 ? 9  
HELX_P HELX_P7  AA7 PRO A 125 ? ASN A 146 ? PRO A 125 ASN A 146 1 ? 22 
HELX_P HELX_P8  AA8 ASN A 149 ? VAL A 153 ? ASN A 149 VAL A 153 5 ? 5  
HELX_P HELX_P9  AA9 PRO A 160 ? GLN A 176 ? PRO A 160 GLN A 176 1 ? 17 
HELX_P HELX_P10 AB1 ASP A 178 ? ASN A 193 ? ASP A 178 ASN A 193 1 ? 16 
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 ? CYS A 218 ? THR A 210 CYS A 218 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            198 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           A 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            218 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             198 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             218 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.032 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       198 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      218 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        198 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       218 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
_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 ? THR A 5  ? VAL A 2 THR A 5  
AA1 2 ASN A 9 ? HIS A 12 ? ASN A 9 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                   9CNU 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ILE A 86  ? ? 41.17   71.77   
2 1 PRO A 87  ? ? -60.69  -178.15 
3 1 THR A 106 ? ? -102.14 -72.80  
4 1 THR A 148 ? ? -127.97 -163.96 
5 1 THR A 188 ? ? -125.70 -59.41  
6 1 ASN A 195 ? ? -49.46  157.04  
# 
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  ? ? 0.089 'SIDE CHAIN' 
2 1 ARG A 119 ? ? 0.102 'SIDE CHAIN' 
3 1 ARG A 131 ? ? 0.113 'SIDE CHAIN' 
4 1 ARG A 132 ? ? 0.117 'SIDE CHAIN' 
5 1 ARG A 167 ? ? 0.104 'SIDE CHAIN' 
6 1 ARG A 173 ? ? 0.157 'SIDE CHAIN' 
# 
_pdbx_point_symmetry.entry_id             9CNU 
_pdbx_point_symmetry.Schoenflies_symbol   C 
_pdbx_point_symmetry.circular_symmetry    1 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9CNU 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   'Cross-correlation coefficient' 
_em_3d_fitting.details           
;The HIV-2 CA pentamer chain derived from micelle-templated icosahedra described in this publication was used as an initial model for fitting. Flexible fitting was used to move the CTD into its proper location. The peptide was modeled by backbone tracing.
;
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      OTHER 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  . 
_em_3d_fitting_list.pdb_chain_id                  . 
_em_3d_fitting_list.pdb_chain_residue_range       . 
_em_3d_fitting_list.details                       'NTDs matched well, but the CTD had to be realigned.' 
_em_3d_fitting_list.chain_id                      A 
_em_3d_fitting_list.chain_residue_range           1-223 
_em_3d_fitting_list.source_name                   Other 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                9CLJ 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9CNU 
_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                  2.99 
_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               1494376 
_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 
# 
loop_
_em_entity_assembly.id 
_em_entity_assembly.parent_id 
_em_entity_assembly.source 
_em_entity_assembly.type 
_em_entity_assembly.name 
_em_entity_assembly.details 
_em_entity_assembly.synonym 
_em_entity_assembly.oligomeric_details 
_em_entity_assembly.entity_id_list 
1 0 'MULTIPLE SOURCES' COMPLEX 
'HIV-2 capsid protein assembled into a lattice via liposome templating and then bound with Nup153 peptide.' 
;C-terminally hexahistidine tagged HIV-2 CA associated with a liposome decorated with NiNTA headgroups which results in the assembly of a lattice of CA. Nup153 peptide is subsequently introduced and binding is allowed to equilibrate.
;
? ? '1, 2' 
2 1 RECOMBINANT        COMPLEX 'HIV-2 capsid protein' ? ? ? 1      
3 1 SYNTHETIC          COMPLEX 'Nup153 peptide' ? ? ? 2      
# 
_em_imaging.entry_id                        9CNU 
_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              9CNU 
_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                9CNU 
_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              9CNU 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C6 
# 
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 222 ? A GLY 222 
2  1 Y 1 A GLY 223 ? A GLY 223 
3  1 Y 1 A PRO 224 ? A PRO 224 
4  1 Y 1 A GLY 225 ? A GLY 225 
5  1 Y 1 A GLN 226 ? A GLN 226 
6  1 Y 1 A LYS 227 ? A LYS 227 
7  1 Y 1 A ALA 228 ? A ALA 228 
8  1 Y 1 A ARG 229 ? A ARG 229 
9  1 Y 1 A LEU 230 ? A LEU 230 
10 1 Y 1 A MET 231 ? A MET 231 
11 1 Y 1 A GLY 232 ? A GLY 232 
12 1 Y 1 A SER 233 ? A SER 233 
13 1 Y 1 A SER 234 ? A SER 234 
14 1 Y 1 A HIS 235 ? A HIS 235 
15 1 Y 1 A HIS 236 ? A HIS 236 
16 1 Y 1 A HIS 237 ? A HIS 237 
17 1 Y 1 A HIS 238 ? A HIS 238 
18 1 Y 1 A HIS 239 ? A HIS 239 
19 1 Y 1 A HIS 240 ? A HIS 240 
20 1 Y 1 B PRO 1   ? B PRO 1   
21 1 Y 1 B ASN 10  ? B ASN 10  
22 1 Y 1 B SER 11  ? B SER 11  
23 1 Y 1 B SER 12  ? B SER 12  
24 1 Y 1 B THR 13  ? B THR 13  
25 1 Y 1 B PRO 14  ? B PRO 14  
26 1 Y 1 B ALA 15  ? B ALA 15  
27 1 Y 1 B GLY 16  ? B GLY 16  
28 1 Y 1 B ARG 17  ? B ARG 17  
29 1 Y 1 B LYS 18  ? B LYS 18  
30 1 Y 1 B ILE 19  ? B ILE 19  
31 1 Y 1 B LYS 20  ? B LYS 20  
32 1 Y 1 B THR 21  ? B THR 21  
33 1 Y 1 B ALA 22  ? B ALA 22  
34 1 Y 1 B VAL 23  ? B VAL 23  
35 1 Y 1 B ARG 24  ? B ARG 24  
36 1 Y 1 B ARG 25  ? B ARG 25  
37 1 Y 1 B ARG 26  ? B ARG 26  
38 1 Y 1 B LYS 27  ? B LYS 27  
# 
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 
IHP C1   C N N 158 
IHP C2   C N N 159 
IHP C3   C N N 160 
IHP C4   C N N 161 
IHP C5   C N N 162 
IHP C6   C N N 163 
IHP O11  O N N 164 
IHP P1   P N N 165 
IHP O21  O N N 166 
IHP O31  O N N 167 
IHP O41  O N N 168 
IHP O12  O N N 169 
IHP P2   P N N 170 
IHP O22  O N N 171 
IHP O32  O N N 172 
IHP O42  O N N 173 
IHP O13  O N N 174 
IHP P3   P N N 175 
IHP O23  O N N 176 
IHP O33  O N N 177 
IHP O43  O N N 178 
IHP O14  O N N 179 
IHP P4   P N N 180 
IHP O24  O N N 181 
IHP O34  O N N 182 
IHP O44  O N N 183 
IHP O15  O N N 184 
IHP P5   P N N 185 
IHP O25  O N N 186 
IHP O35  O N N 187 
IHP O45  O N N 188 
IHP O16  O N N 189 
IHP P6   P N N 190 
IHP O26  O N N 191 
IHP O36  O N N 192 
IHP O46  O N N 193 
IHP H1   H N N 194 
IHP H2   H N N 195 
IHP H3   H N N 196 
IHP H4   H N N 197 
IHP H5   H N N 198 
IHP H6   H N N 199 
IHP H31  H N N 200 
IHP H41  H N N 201 
IHP H32  H N N 202 
IHP H42  H N N 203 
IHP H33  H N N 204 
IHP H43  H N N 205 
IHP H34  H N N 206 
IHP H44  H N N 207 
IHP H35  H N N 208 
IHP H45  H N N 209 
IHP H36  H N N 210 
IHP H46  H N N 211 
ILE N    N N N 212 
ILE CA   C N S 213 
ILE C    C N N 214 
ILE O    O N N 215 
ILE CB   C N S 216 
ILE CG1  C N N 217 
ILE CG2  C N N 218 
ILE CD1  C N N 219 
ILE OXT  O N N 220 
ILE H    H N N 221 
ILE H2   H N N 222 
ILE HA   H N N 223 
ILE HB   H N N 224 
ILE HG12 H N N 225 
ILE HG13 H N N 226 
ILE HG21 H N N 227 
ILE HG22 H N N 228 
ILE HG23 H N N 229 
ILE HD11 H N N 230 
ILE HD12 H N N 231 
ILE HD13 H N N 232 
ILE HXT  H N N 233 
LEU N    N N N 234 
LEU CA   C N S 235 
LEU C    C N N 236 
LEU O    O N N 237 
LEU CB   C N N 238 
LEU CG   C N N 239 
LEU CD1  C N N 240 
LEU CD2  C N N 241 
LEU OXT  O N N 242 
LEU H    H N N 243 
LEU H2   H N N 244 
LEU HA   H N N 245 
LEU HB2  H N N 246 
LEU HB3  H N N 247 
LEU HG   H N N 248 
LEU HD11 H N N 249 
LEU HD12 H N N 250 
LEU HD13 H N N 251 
LEU HD21 H N N 252 
LEU HD22 H N N 253 
LEU HD23 H N N 254 
LEU HXT  H N N 255 
LYS N    N N N 256 
LYS CA   C N S 257 
LYS C    C N N 258 
LYS O    O N N 259 
LYS CB   C N N 260 
LYS CG   C N N 261 
LYS CD   C N N 262 
LYS CE   C N N 263 
LYS NZ   N N N 264 
LYS OXT  O N N 265 
LYS H    H N N 266 
LYS H2   H N N 267 
LYS HA   H N N 268 
LYS HB2  H N N 269 
LYS HB3  H N N 270 
LYS HG2  H N N 271 
LYS HG3  H N N 272 
LYS HD2  H N N 273 
LYS HD3  H N N 274 
LYS HE2  H N N 275 
LYS HE3  H N N 276 
LYS HZ1  H N N 277 
LYS HZ2  H N N 278 
LYS HZ3  H N N 279 
LYS HXT  H N N 280 
MET N    N N N 281 
MET CA   C N S 282 
MET C    C N N 283 
MET O    O N N 284 
MET CB   C N N 285 
MET CG   C N N 286 
MET SD   S N N 287 
MET CE   C N N 288 
MET OXT  O N N 289 
MET H    H N N 290 
MET H2   H N N 291 
MET HA   H N N 292 
MET HB2  H N N 293 
MET HB3  H N N 294 
MET HG2  H N N 295 
MET HG3  H N N 296 
MET HE1  H N N 297 
MET HE2  H N N 298 
MET HE3  H N N 299 
MET HXT  H N N 300 
PHE N    N N N 301 
PHE CA   C N S 302 
PHE C    C N N 303 
PHE O    O N N 304 
PHE CB   C N N 305 
PHE CG   C Y N 306 
PHE CD1  C Y N 307 
PHE CD2  C Y N 308 
PHE CE1  C Y N 309 
PHE CE2  C Y N 310 
PHE CZ   C Y N 311 
PHE OXT  O N N 312 
PHE H    H N N 313 
PHE H2   H N N 314 
PHE HA   H N N 315 
PHE HB2  H N N 316 
PHE HB3  H N N 317 
PHE HD1  H N N 318 
PHE HD2  H N N 319 
PHE HE1  H N N 320 
PHE HE2  H N N 321 
PHE HZ   H N N 322 
PHE HXT  H N N 323 
PRO N    N N N 324 
PRO CA   C N S 325 
PRO C    C N N 326 
PRO O    O N N 327 
PRO CB   C N N 328 
PRO CG   C N N 329 
PRO CD   C N N 330 
PRO OXT  O N N 331 
PRO H    H N N 332 
PRO HA   H N N 333 
PRO HB2  H N N 334 
PRO HB3  H N N 335 
PRO HG2  H N N 336 
PRO HG3  H N N 337 
PRO HD2  H N N 338 
PRO HD3  H N N 339 
PRO HXT  H N N 340 
SER N    N N N 341 
SER CA   C N S 342 
SER C    C N N 343 
SER O    O N N 344 
SER CB   C N N 345 
SER OG   O N N 346 
SER OXT  O N N 347 
SER H    H N N 348 
SER H2   H N N 349 
SER HA   H N N 350 
SER HB2  H N N 351 
SER HB3  H N N 352 
SER HG   H N N 353 
SER HXT  H N N 354 
THR N    N N N 355 
THR CA   C N S 356 
THR C    C N N 357 
THR O    O N N 358 
THR CB   C N R 359 
THR OG1  O N N 360 
THR CG2  C N N 361 
THR OXT  O N N 362 
THR H    H N N 363 
THR H2   H N N 364 
THR HA   H N N 365 
THR HB   H N N 366 
THR HG1  H N N 367 
THR HG21 H N N 368 
THR HG22 H N N 369 
THR HG23 H N N 370 
THR HXT  H N N 371 
TRP N    N N N 372 
TRP CA   C N S 373 
TRP C    C N N 374 
TRP O    O N N 375 
TRP CB   C N N 376 
TRP CG   C Y N 377 
TRP CD1  C Y N 378 
TRP CD2  C Y N 379 
TRP NE1  N Y N 380 
TRP CE2  C Y N 381 
TRP CE3  C Y N 382 
TRP CZ2  C Y N 383 
TRP CZ3  C Y N 384 
TRP CH2  C Y N 385 
TRP OXT  O N N 386 
TRP H    H N N 387 
TRP H2   H N N 388 
TRP HA   H N N 389 
TRP HB2  H N N 390 
TRP HB3  H N N 391 
TRP HD1  H N N 392 
TRP HE1  H N N 393 
TRP HE3  H N N 394 
TRP HZ2  H N N 395 
TRP HZ3  H N N 396 
TRP HH2  H N N 397 
TRP HXT  H N N 398 
TYR N    N N N 399 
TYR CA   C N S 400 
TYR C    C N N 401 
TYR O    O N N 402 
TYR CB   C N N 403 
TYR CG   C Y N 404 
TYR CD1  C Y N 405 
TYR CD2  C Y N 406 
TYR CE1  C Y N 407 
TYR CE2  C Y N 408 
TYR CZ   C Y N 409 
TYR OH   O N N 410 
TYR OXT  O N N 411 
TYR H    H N N 412 
TYR H2   H N N 413 
TYR HA   H N N 414 
TYR HB2  H N N 415 
TYR HB3  H N N 416 
TYR HD1  H N N 417 
TYR HD2  H N N 418 
TYR HE1  H N N 419 
TYR HE2  H N N 420 
TYR HH   H N N 421 
TYR HXT  H N N 422 
VAL N    N N N 423 
VAL CA   C N S 424 
VAL C    C N N 425 
VAL O    O N N 426 
VAL CB   C N N 427 
VAL CG1  C N N 428 
VAL CG2  C N N 429 
VAL OXT  O N N 430 
VAL H    H N N 431 
VAL H2   H N N 432 
VAL HA   H N N 433 
VAL HB   H N N 434 
VAL HG11 H N N 435 
VAL HG12 H N N 436 
VAL HG13 H N N 437 
VAL HG21 H N N 438 
VAL HG22 H N N 439 
VAL HG23 H N N 440 
VAL HXT  H N N 441 
# 
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 
IHP C1  C2   sing N N 150 
IHP C1  C6   sing N N 151 
IHP C1  O11  sing N N 152 
IHP C1  H1   sing N N 153 
IHP C2  C3   sing N N 154 
IHP C2  O12  sing N N 155 
IHP C2  H2   sing N N 156 
IHP C3  C4   sing N N 157 
IHP C3  O13  sing N N 158 
IHP C3  H3   sing N N 159 
IHP C4  C5   sing N N 160 
IHP C4  O14  sing N N 161 
IHP C4  H4   sing N N 162 
IHP C5  C6   sing N N 163 
IHP C5  O15  sing N N 164 
IHP C5  H5   sing N N 165 
IHP C6  O16  sing N N 166 
IHP C6  H6   sing N N 167 
IHP O11 P1   sing N N 168 
IHP P1  O21  doub N N 169 
IHP P1  O31  sing N N 170 
IHP P1  O41  sing N N 171 
IHP O31 H31  sing N N 172 
IHP O41 H41  sing N N 173 
IHP O12 P2   sing N N 174 
IHP P2  O22  doub N N 175 
IHP P2  O32  sing N N 176 
IHP P2  O42  sing N N 177 
IHP O32 H32  sing N N 178 
IHP O42 H42  sing N N 179 
IHP O13 P3   sing N N 180 
IHP P3  O23  doub N N 181 
IHP P3  O33  sing N N 182 
IHP P3  O43  sing N N 183 
IHP O33 H33  sing N N 184 
IHP O43 H43  sing N N 185 
IHP O14 P4   sing N N 186 
IHP P4  O24  doub N N 187 
IHP P4  O34  sing N N 188 
IHP P4  O44  sing N N 189 
IHP O34 H34  sing N N 190 
IHP O44 H44  sing N N 191 
IHP O15 P5   sing N N 192 
IHP P5  O25  doub N N 193 
IHP P5  O35  sing N N 194 
IHP P5  O45  sing N N 195 
IHP O35 H35  sing N N 196 
IHP O45 H45  sing N N 197 
IHP O16 P6   sing N N 198 
IHP P6  O26  doub N N 199 
IHP P6  O36  sing N N 200 
IHP P6  O46  sing N N 201 
IHP O36 H36  sing N N 202 
IHP O46 H46  sing N N 203 
ILE N   CA   sing N N 204 
ILE N   H    sing N N 205 
ILE N   H2   sing N N 206 
ILE CA  C    sing N N 207 
ILE CA  CB   sing N N 208 
ILE CA  HA   sing N N 209 
ILE C   O    doub N N 210 
ILE C   OXT  sing N N 211 
ILE CB  CG1  sing N N 212 
ILE CB  CG2  sing N N 213 
ILE CB  HB   sing N N 214 
ILE CG1 CD1  sing N N 215 
ILE CG1 HG12 sing N N 216 
ILE CG1 HG13 sing N N 217 
ILE CG2 HG21 sing N N 218 
ILE CG2 HG22 sing N N 219 
ILE CG2 HG23 sing N N 220 
ILE CD1 HD11 sing N N 221 
ILE CD1 HD12 sing N N 222 
ILE CD1 HD13 sing N N 223 
ILE OXT HXT  sing N N 224 
LEU N   CA   sing N N 225 
LEU N   H    sing N N 226 
LEU N   H2   sing N N 227 
LEU CA  C    sing N N 228 
LEU CA  CB   sing N N 229 
LEU CA  HA   sing N N 230 
LEU C   O    doub N N 231 
LEU C   OXT  sing N N 232 
LEU CB  CG   sing N N 233 
LEU CB  HB2  sing N N 234 
LEU CB  HB3  sing N N 235 
LEU CG  CD1  sing N N 236 
LEU CG  CD2  sing N N 237 
LEU CG  HG   sing N N 238 
LEU CD1 HD11 sing N N 239 
LEU CD1 HD12 sing N N 240 
LEU CD1 HD13 sing N N 241 
LEU CD2 HD21 sing N N 242 
LEU CD2 HD22 sing N N 243 
LEU CD2 HD23 sing N N 244 
LEU OXT HXT  sing N N 245 
LYS N   CA   sing N N 246 
LYS N   H    sing N N 247 
LYS N   H2   sing N N 248 
LYS CA  C    sing N N 249 
LYS CA  CB   sing N N 250 
LYS CA  HA   sing N N 251 
LYS C   O    doub N N 252 
LYS C   OXT  sing N N 253 
LYS CB  CG   sing N N 254 
LYS CB  HB2  sing N N 255 
LYS CB  HB3  sing N N 256 
LYS CG  CD   sing N N 257 
LYS CG  HG2  sing N N 258 
LYS CG  HG3  sing N N 259 
LYS CD  CE   sing N N 260 
LYS CD  HD2  sing N N 261 
LYS CD  HD3  sing N N 262 
LYS CE  NZ   sing N N 263 
LYS CE  HE2  sing N N 264 
LYS CE  HE3  sing N N 265 
LYS NZ  HZ1  sing N N 266 
LYS NZ  HZ2  sing N N 267 
LYS NZ  HZ3  sing N N 268 
LYS OXT HXT  sing N N 269 
MET N   CA   sing N N 270 
MET N   H    sing N N 271 
MET N   H2   sing N N 272 
MET CA  C    sing N N 273 
MET CA  CB   sing N N 274 
MET CA  HA   sing N N 275 
MET C   O    doub N N 276 
MET C   OXT  sing N N 277 
MET CB  CG   sing N N 278 
MET CB  HB2  sing N N 279 
MET CB  HB3  sing N N 280 
MET CG  SD   sing N N 281 
MET CG  HG2  sing N N 282 
MET CG  HG3  sing N N 283 
MET SD  CE   sing N N 284 
MET CE  HE1  sing N N 285 
MET CE  HE2  sing N N 286 
MET CE  HE3  sing N N 287 
MET OXT HXT  sing N N 288 
PHE N   CA   sing N N 289 
PHE N   H    sing N N 290 
PHE N   H2   sing N N 291 
PHE CA  C    sing N N 292 
PHE CA  CB   sing N N 293 
PHE CA  HA   sing N N 294 
PHE C   O    doub N N 295 
PHE C   OXT  sing N N 296 
PHE CB  CG   sing N N 297 
PHE CB  HB2  sing N N 298 
PHE CB  HB3  sing N N 299 
PHE CG  CD1  doub Y N 300 
PHE CG  CD2  sing Y N 301 
PHE CD1 CE1  sing Y N 302 
PHE CD1 HD1  sing N N 303 
PHE CD2 CE2  doub Y N 304 
PHE CD2 HD2  sing N N 305 
PHE CE1 CZ   doub Y N 306 
PHE CE1 HE1  sing N N 307 
PHE CE2 CZ   sing Y N 308 
PHE CE2 HE2  sing N N 309 
PHE CZ  HZ   sing N N 310 
PHE OXT HXT  sing N N 311 
PRO N   CA   sing N N 312 
PRO N   CD   sing N N 313 
PRO N   H    sing N N 314 
PRO CA  C    sing N N 315 
PRO CA  CB   sing N N 316 
PRO CA  HA   sing N N 317 
PRO C   O    doub N N 318 
PRO C   OXT  sing N N 319 
PRO CB  CG   sing N N 320 
PRO CB  HB2  sing N N 321 
PRO CB  HB3  sing N N 322 
PRO CG  CD   sing N N 323 
PRO CG  HG2  sing N N 324 
PRO CG  HG3  sing N N 325 
PRO CD  HD2  sing N N 326 
PRO CD  HD3  sing N N 327 
PRO OXT HXT  sing N N 328 
SER N   CA   sing N N 329 
SER N   H    sing N N 330 
SER N   H2   sing N N 331 
SER CA  C    sing N N 332 
SER CA  CB   sing N N 333 
SER CA  HA   sing N N 334 
SER C   O    doub N N 335 
SER C   OXT  sing N N 336 
SER CB  OG   sing N N 337 
SER CB  HB2  sing N N 338 
SER CB  HB3  sing N N 339 
SER OG  HG   sing N N 340 
SER OXT HXT  sing N N 341 
THR N   CA   sing N N 342 
THR N   H    sing N N 343 
THR N   H2   sing N N 344 
THR CA  C    sing N N 345 
THR CA  CB   sing N N 346 
THR CA  HA   sing N N 347 
THR C   O    doub N N 348 
THR C   OXT  sing N N 349 
THR CB  OG1  sing N N 350 
THR CB  CG2  sing N N 351 
THR CB  HB   sing N N 352 
THR OG1 HG1  sing N N 353 
THR CG2 HG21 sing N N 354 
THR CG2 HG22 sing N N 355 
THR CG2 HG23 sing N N 356 
THR OXT HXT  sing N N 357 
TRP N   CA   sing N N 358 
TRP N   H    sing N N 359 
TRP N   H2   sing N N 360 
TRP CA  C    sing N N 361 
TRP CA  CB   sing N N 362 
TRP CA  HA   sing N N 363 
TRP C   O    doub N N 364 
TRP C   OXT  sing N N 365 
TRP CB  CG   sing N N 366 
TRP CB  HB2  sing N N 367 
TRP CB  HB3  sing N N 368 
TRP CG  CD1  doub Y N 369 
TRP CG  CD2  sing Y N 370 
TRP CD1 NE1  sing Y N 371 
TRP CD1 HD1  sing N N 372 
TRP CD2 CE2  doub Y N 373 
TRP CD2 CE3  sing Y N 374 
TRP NE1 CE2  sing Y N 375 
TRP NE1 HE1  sing N N 376 
TRP CE2 CZ2  sing Y N 377 
TRP CE3 CZ3  doub Y N 378 
TRP CE3 HE3  sing N N 379 
TRP CZ2 CH2  doub Y N 380 
TRP CZ2 HZ2  sing N N 381 
TRP CZ3 CH2  sing Y N 382 
TRP CZ3 HZ3  sing N N 383 
TRP CH2 HH2  sing N N 384 
TRP OXT HXT  sing N N 385 
TYR N   CA   sing N N 386 
TYR N   H    sing N N 387 
TYR N   H2   sing N N 388 
TYR CA  C    sing N N 389 
TYR CA  CB   sing N N 390 
TYR CA  HA   sing N N 391 
TYR C   O    doub N N 392 
TYR C   OXT  sing N N 393 
TYR CB  CG   sing N N 394 
TYR CB  HB2  sing N N 395 
TYR CB  HB3  sing N N 396 
TYR CG  CD1  doub Y N 397 
TYR CG  CD2  sing Y N 398 
TYR CD1 CE1  sing Y N 399 
TYR CD1 HD1  sing N N 400 
TYR CD2 CE2  doub Y N 401 
TYR CD2 HD2  sing N N 402 
TYR CE1 CZ   doub Y N 403 
TYR CE1 HE1  sing N N 404 
TYR CE2 CZ   sing Y N 405 
TYR CE2 HE2  sing N N 406 
TYR CZ  OH   sing N N 407 
TYR OH  HH   sing N N 408 
TYR OXT HXT  sing N N 409 
VAL N   CA   sing N N 410 
VAL N   H    sing N N 411 
VAL N   H2   sing N N 412 
VAL CA  C    sing N N 413 
VAL CA  CB   sing N N 414 
VAL CA  HA   sing N N 415 
VAL C   O    doub N N 416 
VAL C   OXT  sing N N 417 
VAL CB  CG1  sing N N 418 
VAL CB  CG2  sing N N 419 
VAL CB  HB   sing N N 420 
VAL CG1 HG11 sing N N 421 
VAL CG1 HG12 sing N N 422 
VAL CG1 HG13 sing N N 423 
VAL CG2 HG21 sing N N 424 
VAL CG2 HG22 sing N N 425 
VAL CG2 HG23 sing N N 426 
VAL OXT HXT  sing N N 427 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-07-15 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9CNU 
_em_admin.last_update        2025-03-05 
_em_admin.map_release_date   2025-03-05 
_em_admin.title              'HIV-2 CA hexamer bound with Nup153 peptide; assembled with liposome 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                MEGADALTONS 
_em_entity_assembly_molwt.value                0.0269 
# 
loop_
_em_entity_assembly_naturalsource.cell 
_em_entity_assembly_naturalsource.cellular_location 
_em_entity_assembly_naturalsource.entity_assembly_id 
_em_entity_assembly_naturalsource.id 
_em_entity_assembly_naturalsource.ncbi_tax_id 
_em_entity_assembly_naturalsource.organism 
_em_entity_assembly_naturalsource.organelle 
_em_entity_assembly_naturalsource.organ 
_em_entity_assembly_naturalsource.strain 
_em_entity_assembly_naturalsource.tissue 
_em_entity_assembly_naturalsource.details 
? ? 2 2 11709 'Human immunodeficiency virus 2' ? ? GL-AN ? ? 
? ? 3 3 9606  'Homo sapiens'                   ? ? ?     ? ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   2 
_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    20 
_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   11931864 
_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 Yale University West Campus CryoEM Resource' 2  ? ? 1 SerialEM  ? 
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 final concentrations after subsequent addition. Nup153 peptide was then introduced to 400 uM final concentration.

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      Other 
_pdbx_initial_refinement_model.accession_code   9CLJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CNU 
_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   ? 98.911  79.005  124.051 1.00 30.00 ? 1   PRO A N   1 
ATOM   2    C CA  . PRO A 1 1   ? 99.985  79.472  124.930 1.00 30.00 ? 1   PRO A CA  1 
ATOM   3    C C   . PRO A 1 1   ? 99.603  79.359  126.409 1.00 30.00 ? 1   PRO A C   1 
ATOM   4    O O   . PRO A 1 1   ? 98.696  78.610  126.726 1.00 30.00 ? 1   PRO A O   1 
ATOM   5    C CB  . PRO A 1 1   ? 100.095 80.965  124.620 1.00 30.00 ? 1   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 1   ? 99.757  81.055  123.165 1.00 30.00 ? 1   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 1   ? 98.733  79.961  122.953 1.00 30.00 ? 1   PRO A CD  1 
ATOM   8    N N   . VAL A 1 2   ? 100.290 80.096  127.287 1.00 30.00 ? 2   VAL A N   1 
ATOM   9    C CA  . VAL A 1 2   ? 99.977  80.077  128.744 1.00 30.00 ? 2   VAL A CA  1 
ATOM   10   C C   . VAL A 1 2   ? 100.066 81.480  129.333 1.00 30.00 ? 2   VAL A C   1 
ATOM   11   O O   . VAL A 1 2   ? 100.944 82.226  128.893 1.00 30.00 ? 2   VAL A O   1 
ATOM   12   C CB  . VAL A 1 2   ? 100.903 79.128  129.518 1.00 30.00 ? 2   VAL A CB  1 
ATOM   13   C CG1 . VAL A 1 2   ? 100.451 78.978  130.962 1.00 30.00 ? 2   VAL A CG1 1 
ATOM   14   C CG2 . VAL A 1 2   ? 100.995 77.771  128.847 1.00 30.00 ? 2   VAL A CG2 1 
ATOM   15   N N   . GLN A 1 3   ? 99.184  81.827  130.271 1.00 30.00 ? 3   GLN A N   1 
ATOM   16   C CA  . GLN A 1 3   ? 99.222  83.115  131.013 1.00 30.00 ? 3   GLN A CA  1 
ATOM   17   C C   . GLN A 1 3   ? 99.068  82.748  132.485 1.00 30.00 ? 3   GLN A C   1 
ATOM   18   O O   . GLN A 1 3   ? 98.596  81.634  132.740 1.00 30.00 ? 3   GLN A O   1 
ATOM   19   C CB  . GLN A 1 3   ? 98.111  84.072  130.590 1.00 30.00 ? 3   GLN A CB  1 
ATOM   20   C CG  . GLN A 1 3   ? 96.713  83.558  130.894 1.00 30.00 ? 3   GLN A CG  1 
ATOM   21   C CD  . GLN A 1 3   ? 95.645  84.536  130.477 1.00 30.00 ? 3   GLN A CD  1 
ATOM   22   O OE1 . GLN A 1 3   ? 95.927  85.618  129.967 1.00 30.00 ? 3   GLN A OE1 1 
ATOM   23   N NE2 . GLN A 1 3   ? 94.398  84.158  130.699 1.00 30.00 ? 3   GLN A NE2 1 
ATOM   24   N N   . GLN A 1 4   ? 99.451  83.622  133.408 1.00 30.00 ? 4   GLN A N   1 
ATOM   25   C CA  . GLN A 1 4   ? 99.389  83.325  134.861 1.00 30.00 ? 4   GLN A CA  1 
ATOM   26   C C   . GLN A 1 4   ? 98.234  84.128  135.451 1.00 30.00 ? 4   GLN A C   1 
ATOM   27   O O   . GLN A 1 4   ? 97.794  85.070  134.776 1.00 30.00 ? 4   GLN A O   1 
ATOM   28   C CB  . GLN A 1 4   ? 100.714 83.652  135.541 1.00 30.00 ? 4   GLN A CB  1 
ATOM   29   C CG  . GLN A 1 4   ? 100.915 82.897  136.845 1.00 30.00 ? 4   GLN A CG  1 
ATOM   30   C CD  . GLN A 1 4   ? 102.273 83.133  137.454 1.00 30.00 ? 4   GLN A CD  1 
ATOM   31   O OE1 . GLN A 1 4   ? 103.091 83.886  136.933 1.00 30.00 ? 4   GLN A OE1 1 
ATOM   32   N NE2 . GLN A 1 4   ? 102.522 82.480  138.576 1.00 30.00 ? 4   GLN A NE2 1 
ATOM   33   N N   . THR A 1 5   ? 97.729  83.744  136.623 1.00 30.00 ? 5   THR A N   1 
ATOM   34   C CA  . THR A 1 5   ? 96.577  84.412  137.279 1.00 30.00 ? 5   THR A CA  1 
ATOM   35   C C   . THR A 1 5   ? 96.877  84.574  138.771 1.00 30.00 ? 5   THR A C   1 
ATOM   36   O O   . THR A 1 5   ? 97.813  83.904  139.253 1.00 30.00 ? 5   THR A O   1 
ATOM   37   C CB  . THR A 1 5   ? 95.294  83.616  137.028 1.00 30.00 ? 5   THR A CB  1 
ATOM   38   O OG1 . THR A 1 5   ? 95.427  82.367  137.704 1.00 30.00 ? 5   THR A OG1 1 
ATOM   39   C CG2 . THR A 1 5   ? 95.019  83.379  135.559 1.00 30.00 ? 5   THR A CG2 1 
ATOM   40   N N   . GLY A 1 6   ? 96.139  85.439  139.474 1.00 30.00 ? 6   GLY A N   1 
ATOM   41   C CA  . GLY A 1 6   ? 96.294  85.617  140.932 1.00 30.00 ? 6   GLY A CA  1 
ATOM   42   C C   . GLY A 1 6   ? 96.397  84.284  141.650 1.00 30.00 ? 6   GLY A C   1 
ATOM   43   O O   . GLY A 1 6   ? 95.637  83.366  141.278 1.00 30.00 ? 6   GLY A O   1 
ATOM   44   N N   . GLY A 1 7   ? 97.289  84.167  142.639 1.00 30.00 ? 7   GLY A N   1 
ATOM   45   C CA  . GLY A 1 7   ? 97.450  82.935  143.437 1.00 30.00 ? 7   GLY A CA  1 
ATOM   46   C C   . GLY A 1 7   ? 98.599  82.073  142.946 1.00 30.00 ? 7   GLY A C   1 
ATOM   47   O O   . GLY A 1 7   ? 98.895  81.069  143.622 1.00 30.00 ? 7   GLY A O   1 
ATOM   48   N N   . GLY A 1 8   ? 99.221  82.430  141.818 1.00 30.00 ? 8   GLY A N   1 
ATOM   49   C CA  . GLY A 1 8   ? 100.370 81.683  141.268 1.00 30.00 ? 8   GLY A CA  1 
ATOM   50   C C   . GLY A 1 8   ? 99.925  80.565  140.343 1.00 30.00 ? 8   GLY A C   1 
ATOM   51   O O   . GLY A 1 8   ? 100.784 79.741  139.976 1.00 30.00 ? 8   GLY A O   1 
ATOM   52   N N   . ASN A 1 9   ? 98.662  80.564  139.904 1.00 30.00 ? 9   ASN A N   1 
ATOM   53   C CA  . ASN A 1 9   ? 98.106  79.482  139.049 1.00 30.00 ? 9   ASN A CA  1 
ATOM   54   C C   . ASN A 1 9   ? 98.447  79.763  137.588 1.00 30.00 ? 9   ASN A C   1 
ATOM   55   O O   . ASN A 1 9   ? 98.725  80.922  137.287 1.00 30.00 ? 9   ASN A O   1 
ATOM   56   C CB  . ASN A 1 9   ? 96.587  79.371  139.163 1.00 30.00 ? 9   ASN A CB  1 
ATOM   57   C CG  . ASN A 1 9   ? 96.104  79.306  140.595 1.00 30.00 ? 9   ASN A CG  1 
ATOM   58   O OD1 . ASN A 1 9   ? 96.313  80.237  141.369 1.00 30.00 ? 9   ASN A OD1 1 
ATOM   59   N ND2 . ASN A 1 9   ? 95.445  78.217  140.951 1.00 30.00 ? 9   ASN A ND2 1 
ATOM   60   N N   . TYR A 1 10  ? 98.336  78.781  136.694 1.00 30.00 ? 10  TYR A N   1 
ATOM   61   C CA  . TYR A 1 10  ? 98.537  79.007  135.239 1.00 30.00 ? 10  TYR A CA  1 
ATOM   62   C C   . TYR A 1 10  ? 97.311  78.504  134.479 1.00 30.00 ? 10  TYR A C   1 
ATOM   63   O O   . TYR A 1 10  ? 96.551  77.702  135.056 1.00 30.00 ? 10  TYR A O   1 
ATOM   64   C CB  . TYR A 1 10  ? 99.813  78.339  134.739 1.00 30.00 ? 10  TYR A CB  1 
ATOM   65   C CG  . TYR A 1 10  ? 101.086 78.874  135.337 1.00 30.00 ? 10  TYR A CG  1 
ATOM   66   C CD1 . TYR A 1 10  ? 101.376 78.717  136.680 1.00 30.00 ? 10  TYR A CD1 1 
ATOM   67   C CD2 . TYR A 1 10  ? 101.984 79.582  134.559 1.00 30.00 ? 10  TYR A CD2 1 
ATOM   68   C CE1 . TYR A 1 10  ? 102.544 79.214  137.229 1.00 30.00 ? 10  TYR A CE1 1 
ATOM   69   C CE2 . TYR A 1 10  ? 103.153 80.093  135.093 1.00 30.00 ? 10  TYR A CE2 1 
ATOM   70   C CZ  . TYR A 1 10  ? 103.435 79.907  136.433 1.00 30.00 ? 10  TYR A CZ  1 
ATOM   71   O OH  . TYR A 1 10  ? 104.592 80.410  136.969 1.00 30.00 ? 10  TYR A OH  1 
ATOM   72   N N   . ILE A 1 11  ? 97.068  79.027  133.280 1.00 30.00 ? 11  ILE A N   1 
ATOM   73   C CA  . ILE A 1 11  ? 95.859  78.667  132.490 1.00 30.00 ? 11  ILE A CA  1 
ATOM   74   C C   . ILE A 1 11  ? 96.246  78.592  131.019 1.00 30.00 ? 11  ILE A C   1 
ATOM   75   O O   . ILE A 1 11  ? 97.301  79.142  130.674 1.00 30.00 ? 11  ILE A O   1 
ATOM   76   C CB  . ILE A 1 11  ? 94.763  79.715  132.752 1.00 30.00 ? 11  ILE A CB  1 
ATOM   77   C CG1 . ILE A 1 11  ? 93.403  79.302  132.184 1.00 30.00 ? 11  ILE A CG1 1 
ATOM   78   C CG2 . ILE A 1 11  ? 95.197  81.082  132.246 1.00 30.00 ? 11  ILE A CG2 1 
ATOM   79   C CD1 . ILE A 1 11  ? 92.283  80.257  132.512 1.00 30.00 ? 11  ILE A CD1 1 
ATOM   80   N N   . HIS A 1 12  ? 95.401  78.007  130.176 1.00 30.00 ? 12  HIS A N   1 
ATOM   81   C CA  . HIS A 1 12  ? 95.663  78.018  128.721 1.00 30.00 ? 12  HIS A CA  1 
ATOM   82   C C   . HIS A 1 12  ? 95.015  79.247  128.111 1.00 30.00 ? 12  HIS A C   1 
ATOM   83   O O   . HIS A 1 12  ? 93.767  79.345  128.105 1.00 30.00 ? 12  HIS A O   1 
ATOM   84   C CB  . HIS A 1 12  ? 94.998  76.867  127.975 1.00 30.00 ? 12  HIS A CB  1 
ATOM   85   C CG  . HIS A 1 12  ? 95.144  76.936  126.495 1.00 30.00 ? 12  HIS A CG  1 
ATOM   86   N ND1 . HIS A 1 12  ? 96.360  76.855  125.861 1.00 30.00 ? 12  HIS A ND1 1 
ATOM   87   C CD2 . HIS A 1 12  ? 94.232  77.033  125.526 1.00 30.00 ? 12  HIS A CD2 1 
ATOM   88   C CE1 . HIS A 1 12  ? 96.174  76.916  124.556 1.00 30.00 ? 12  HIS A CE1 1 
ATOM   89   N NE2 . HIS A 1 12  ? 94.892  77.034  124.328 1.00 30.00 ? 12  HIS A NE2 1 
ATOM   90   N N   . VAL A 1 13  ? 95.837  80.162  127.622 1.00 30.00 ? 13  VAL A N   1 
ATOM   91   C CA  . VAL A 1 13  ? 95.305  81.323  126.868 1.00 30.00 ? 13  VAL A CA  1 
ATOM   92   C C   . VAL A 1 13  ? 95.310  80.787  125.442 1.00 30.00 ? 13  VAL A C   1 
ATOM   93   O O   . VAL A 1 13  ? 95.933  79.745  125.251 1.00 30.00 ? 13  VAL A O   1 
ATOM   94   C CB  . VAL A 1 13  ? 96.161  82.585  127.047 1.00 30.00 ? 13  VAL A CB  1 
ATOM   95   C CG1 . VAL A 1 13  ? 97.620  82.340  126.724 1.00 30.00 ? 13  VAL A CG1 1 
ATOM   96   C CG2 . VAL A 1 13  ? 95.650  83.773  126.256 1.00 30.00 ? 13  VAL A CG2 1 
ATOM   97   N N   . PRO A 1 14  ? 94.550  81.316  124.474 1.00 30.00 ? 14  PRO A N   1 
ATOM   98   C CA  . PRO A 1 14  ? 94.612  80.777  123.127 1.00 30.00 ? 14  PRO A CA  1 
ATOM   99   C C   . PRO A 1 14  ? 95.724  81.336  122.241 1.00 30.00 ? 14  PRO A C   1 
ATOM   100  O O   . PRO A 1 14  ? 96.263  82.372  122.590 1.00 30.00 ? 14  PRO A O   1 
ATOM   101  C CB  . PRO A 1 14  ? 93.308  81.286  122.520 1.00 30.00 ? 14  PRO A CB  1 
ATOM   102  C CG  . PRO A 1 14  ? 92.471  81.731  123.682 1.00 30.00 ? 14  PRO A CG  1 
ATOM   103  C CD  . PRO A 1 14  ? 93.493  82.302  124.628 1.00 30.00 ? 14  PRO A CD  1 
ATOM   104  N N   . LEU A 1 15  ? 96.000  80.706  121.094 1.00 30.00 ? 15  LEU A N   1 
ATOM   105  C CA  . LEU A 1 15  ? 96.983  81.280  120.140 1.00 30.00 ? 15  LEU A CA  1 
ATOM   106  C C   . LEU A 1 15  ? 96.188  82.334  119.379 1.00 30.00 ? 15  LEU A C   1 
ATOM   107  O O   . LEU A 1 15  ? 94.945  82.292  119.484 1.00 30.00 ? 15  LEU A O   1 
ATOM   108  C CB  . LEU A 1 15  ? 97.580  80.196  119.236 1.00 30.00 ? 15  LEU A CB  1 
ATOM   109  C CG  . LEU A 1 15  ? 98.618  80.651  118.218 1.00 30.00 ? 15  LEU A CG  1 
ATOM   110  C CD1 . LEU A 1 15  ? 99.856  81.203  118.898 1.00 30.00 ? 15  LEU A CD1 1 
ATOM   111  C CD2 . LEU A 1 15  ? 99.013  79.481  117.360 1.00 30.00 ? 15  LEU A CD2 1 
ATOM   112  N N   . SER A 1 16  ? 96.835  83.224  118.636 1.00 30.00 ? 16  SER A N   1 
ATOM   113  C CA  . SER A 1 16  ? 96.132  84.384  118.042 1.00 30.00 ? 16  SER A CA  1 
ATOM   114  C C   . SER A 1 16  ? 95.846  84.242  116.547 1.00 30.00 ? 16  SER A C   1 
ATOM   115  O O   . SER A 1 16  ? 96.558  83.482  115.861 1.00 30.00 ? 16  SER A O   1 
ATOM   116  C CB  . SER A 1 16  ? 96.945  85.591  118.304 1.00 30.00 ? 16  SER A CB  1 
ATOM   117  O OG  . SER A 1 16  ? 96.353  86.741  117.734 1.00 30.00 ? 16  SER A OG  1 
ATOM   118  N N   . PRO A 1 17  ? 94.829  84.964  116.029 1.00 30.00 ? 17  PRO A N   1 
ATOM   119  C CA  . PRO A 1 17  ? 94.463  84.930  114.606 1.00 30.00 ? 17  PRO A CA  1 
ATOM   120  C C   . PRO A 1 17  ? 95.493  85.516  113.640 1.00 30.00 ? 17  PRO A C   1 
ATOM   121  O O   . PRO A 1 17  ? 95.336  85.320  112.449 1.00 30.00 ? 17  PRO A O   1 
ATOM   122  C CB  . PRO A 1 17  ? 93.193  85.768  114.584 1.00 30.00 ? 17  PRO A CB  1 
ATOM   123  C CG  . PRO A 1 17  ? 92.625  85.580  115.942 1.00 30.00 ? 17  PRO A CG  1 
ATOM   124  C CD  . PRO A 1 17  ? 93.854  85.739  116.794 1.00 30.00 ? 17  PRO A CD  1 
ATOM   125  N N   . ARG A 1 18  ? 96.507  86.193  114.159 1.00 30.00 ? 18  ARG A N   1 
ATOM   126  C CA  . ARG A 1 18  ? 97.517  86.880  113.326 1.00 30.00 ? 18  ARG A CA  1 
ATOM   127  C C   . ARG A 1 18  ? 98.814  86.085  113.270 1.00 30.00 ? 18  ARG A C   1 
ATOM   128  O O   . ARG A 1 18  ? 99.683  86.449  112.458 1.00 30.00 ? 18  ARG A O   1 
ATOM   129  C CB  . ARG A 1 18  ? 97.846  88.174  114.042 1.00 30.00 ? 18  ARG A CB  1 
ATOM   130  C CG  . ARG A 1 18  ? 96.639  89.012  114.430 1.00 30.00 ? 18  ARG A CG  1 
ATOM   131  C CD  . ARG A 1 18  ? 97.054  90.284  115.139 1.00 30.00 ? 18  ARG A CD  1 
ATOM   132  N NE  . ARG A 1 18  ? 97.802  91.163  114.250 1.00 30.00 ? 18  ARG A NE  1 
ATOM   133  C CZ  . ARG A 1 18  ? 97.454  92.402  113.922 1.00 30.00 ? 18  ARG A CZ  1 
ATOM   134  N NH1 . ARG A 1 18  ? 97.981  92.960  112.849 1.00 30.00 ? 18  ARG A NH1 1 
ATOM   135  N NH2 . ARG A 1 18  ? 96.559  93.072  114.630 1.00 30.00 ? 18  ARG A NH2 1 
ATOM   136  N N   . THR A 1 19  ? 98.936  85.048  114.091 1.00 30.00 ? 19  THR A N   1 
ATOM   137  C CA  . THR A 1 19  ? 100.173 84.243  114.207 1.00 30.00 ? 19  THR A CA  1 
ATOM   138  C C   . THR A 1 19  ? 99.960  82.962  113.415 1.00 30.00 ? 19  THR A C   1 
ATOM   139  O O   . THR A 1 19  ? 100.819 82.643  112.573 1.00 30.00 ? 19  THR A O   1 
ATOM   140  C CB  . THR A 1 19  ? 100.409 84.019  115.696 1.00 30.00 ? 19  THR A CB  1 
ATOM   141  O OG1 . THR A 1 19  ? 100.530 85.303  116.303 1.00 30.00 ? 19  THR A OG1 1 
ATOM   142  C CG2 . THR A 1 19  ? 101.630 83.190  116.004 1.00 30.00 ? 19  THR A CG2 1 
ATOM   143  N N   . LEU A 1 20  ? 98.869  82.252  113.688 1.00 30.00 ? 20  LEU A N   1 
ATOM   144  C CA  . LEU A 1 20  ? 98.475  81.093  112.859 1.00 30.00 ? 20  LEU A CA  1 
ATOM   145  C C   . LEU A 1 20  ? 98.579  81.501  111.398 1.00 30.00 ? 20  LEU A C   1 
ATOM   146  O O   . LEU A 1 20  ? 99.213  80.775  110.623 1.00 30.00 ? 20  LEU A O   1 
ATOM   147  C CB  . LEU A 1 20  ? 97.004  80.829  113.158 1.00 30.00 ? 20  LEU A CB  1 
ATOM   148  C CG  . LEU A 1 20  ? 96.640  80.203  114.494 1.00 30.00 ? 20  LEU A CG  1 
ATOM   149  C CD1 . LEU A 1 20  ? 95.143  79.982  114.566 1.00 30.00 ? 20  LEU A CD1 1 
ATOM   150  C CD2 . LEU A 1 20  ? 97.343  78.877  114.648 1.00 30.00 ? 20  LEU A CD2 1 
ATOM   151  N N   . ASN A 1 21  ? 98.044  82.673  111.075 1.00 30.00 ? 21  ASN A N   1 
ATOM   152  C CA  . ASN A 1 21  ? 97.954  83.172  109.686 1.00 30.00 ? 21  ASN A CA  1 
ATOM   153  C C   . ASN A 1 21  ? 99.314  83.548  109.115 1.00 30.00 ? 21  ASN A C   1 
ATOM   154  O O   . ASN A 1 21  ? 99.562  83.251  107.938 1.00 30.00 ? 21  ASN A O   1 
ATOM   155  C CB  . ASN A 1 21  ? 97.092  84.420  109.741 1.00 30.00 ? 21  ASN A CB  1 
ATOM   156  C CG  . ASN A 1 21  ? 96.906  85.104  108.410 1.00 30.00 ? 21  ASN A CG  1 
ATOM   157  O OD1 . ASN A 1 21  ? 96.375  84.518  107.470 1.00 30.00 ? 21  ASN A OD1 1 
ATOM   158  N ND2 . ASN A 1 21  ? 97.328  86.353  108.333 1.00 30.00 ? 21  ASN A ND2 1 
ATOM   159  N N   . ALA A 1 22  ? 100.169 84.152  109.927 1.00 30.00 ? 22  ALA A N   1 
ATOM   160  C CA  . ALA A 1 22  ? 101.497 84.604  109.476 1.00 30.00 ? 22  ALA A CA  1 
ATOM   161  C C   . ALA A 1 22  ? 102.372 83.383  109.235 1.00 30.00 ? 22  ALA A C   1 
ATOM   162  O O   . ALA A 1 22  ? 103.193 83.412  108.299 1.00 30.00 ? 22  ALA A O   1 
ATOM   163  C CB  . ALA A 1 22  ? 102.063 85.452  110.550 1.00 30.00 ? 22  ALA A CB  1 
ATOM   164  N N   . TRP A 1 23  ? 102.180 82.348  110.042 1.00 30.00 ? 23  TRP A N   1 
ATOM   165  C CA  . TRP A 1 23  ? 102.912 81.078  109.868 1.00 30.00 ? 23  TRP A CA  1 
ATOM   166  C C   . TRP A 1 23  ? 102.460 80.433  108.570 1.00 30.00 ? 23  TRP A C   1 
ATOM   167  O O   . TRP A 1 23  ? 103.319 80.064  107.756 1.00 30.00 ? 23  TRP A O   1 
ATOM   168  C CB  . TRP A 1 23  ? 102.541 80.188  111.041 1.00 30.00 ? 23  TRP A CB  1 
ATOM   169  C CG  . TRP A 1 23  ? 102.859 78.754  110.810 1.00 30.00 ? 23  TRP A CG  1 
ATOM   170  C CD1 . TRP A 1 23  ? 101.987 77.710  110.809 1.00 30.00 ? 23  TRP A CD1 1 
ATOM   171  C CD2 . TRP A 1 23  ? 104.144 78.215  110.493 1.00 30.00 ? 23  TRP A CD2 1 
ATOM   172  N NE1 . TRP A 1 23  ? 102.650 76.550  110.528 1.00 30.00 ? 23  TRP A NE1 1 
ATOM   173  C CE2 . TRP A 1 23  ? 103.975 76.829  110.330 1.00 30.00 ? 23  TRP A CE2 1 
ATOM   174  C CE3 . TRP A 1 23  ? 105.411 78.773  110.335 1.00 30.00 ? 23  TRP A CE3 1 
ATOM   175  C CZ2 . TRP A 1 23  ? 105.038 75.988  110.021 1.00 30.00 ? 23  TRP A CZ2 1 
ATOM   176  C CZ3 . TRP A 1 23  ? 106.456 77.942  110.026 1.00 30.00 ? 23  TRP A CZ3 1 
ATOM   177  C CH2 . TRP A 1 23  ? 106.273 76.570  109.875 1.00 30.00 ? 23  TRP A CH2 1 
ATOM   178  N N   . VAL A 1 24  ? 101.152 80.350  108.381 1.00 30.00 ? 24  VAL A N   1 
ATOM   179  C CA  . VAL A 1 24  ? 100.564 79.816  107.127 1.00 30.00 ? 24  VAL A CA  1 
ATOM   180  C C   . VAL A 1 24  ? 101.203 80.508  105.927 1.00 30.00 ? 24  VAL A C   1 
ATOM   181  O O   . VAL A 1 24  ? 101.578 79.802  104.968 1.00 30.00 ? 24  VAL A O   1 
ATOM   182  C CB  . VAL A 1 24  ? 99.051  80.058  107.189 1.00 30.00 ? 24  VAL A CB  1 
ATOM   183  C CG1 . VAL A 1 24  ? 98.404  80.015  105.821 1.00 30.00 ? 24  VAL A CG1 1 
ATOM   184  C CG2 . VAL A 1 24  ? 98.363  79.093  108.137 1.00 30.00 ? 24  VAL A CG2 1 
ATOM   185  N N   . LYS A 1 25  ? 101.368 81.825  106.001 1.00 30.00 ? 25  LYS A N   1 
ATOM   186  C CA  . LYS A 1 25  ? 101.899 82.635  104.881 1.00 30.00 ? 25  LYS A CA  1 
ATOM   187  C C   . LYS A 1 25  ? 103.406 82.452  104.722 1.00 30.00 ? 25  LYS A C   1 
ATOM   188  O O   . LYS A 1 25  ? 103.858 82.341  103.584 1.00 30.00 ? 25  LYS A O   1 
ATOM   189  C CB  . LYS A 1 25  ? 101.622 84.092  105.216 1.00 30.00 ? 25  LYS A CB  1 
ATOM   190  C CG  . LYS A 1 25  ? 100.185 84.549  105.062 1.00 30.00 ? 25  LYS A CG  1 
ATOM   191  C CD  . LYS A 1 25  ? 100.014 85.977  105.495 1.00 30.00 ? 25  LYS A CD  1 
ATOM   192  C CE  . LYS A 1 25  ? 98.640  86.525  105.191 1.00 30.00 ? 25  LYS A CE  1 
ATOM   193  N NZ  . LYS A 1 25  ? 98.526  87.942  105.603 1.00 30.00 ? 25  LYS A NZ  1 
ATOM   194  N N   . LEU A 1 26  ? 104.152 82.434  105.820 1.00 30.00 ? 26  LEU A N   1 
ATOM   195  C CA  . LEU A 1 26  ? 105.623 82.248  105.795 1.00 30.00 ? 26  LEU A CA  1 
ATOM   196  C C   . LEU A 1 26  ? 105.912 80.896  105.152 1.00 30.00 ? 26  LEU A C   1 
ATOM   197  O O   . LEU A 1 26  ? 106.869 80.799  104.384 1.00 30.00 ? 26  LEU A O   1 
ATOM   198  C CB  . LEU A 1 26  ? 106.081 82.298  107.249 1.00 30.00 ? 26  LEU A CB  1 
ATOM   199  C CG  . LEU A 1 26  ? 107.529 81.958  107.546 1.00 30.00 ? 26  LEU A CG  1 
ATOM   200  C CD1 . LEU A 1 26  ? 108.441 83.104  107.166 1.00 30.00 ? 26  LEU A CD1 1 
ATOM   201  C CD2 . LEU A 1 26  ? 107.669 81.617  109.012 1.00 30.00 ? 26  LEU A CD2 1 
ATOM   202  N N   . VAL A 1 27  ? 105.100 79.892  105.454 1.00 30.00 ? 27  VAL A N   1 
ATOM   203  C CA  . VAL A 1 27  ? 105.248 78.520  104.898 1.00 30.00 ? 27  VAL A CA  1 
ATOM   204  C C   . VAL A 1 27  ? 104.900 78.499  103.413 1.00 30.00 ? 27  VAL A C   1 
ATOM   205  O O   . VAL A 1 27  ? 105.451 77.647  102.697 1.00 30.00 ? 27  VAL A O   1 
ATOM   206  C CB  . VAL A 1 27  ? 104.302 77.595  105.670 1.00 30.00 ? 27  VAL A CB  1 
ATOM   207  C CG1 . VAL A 1 27  ? 104.056 76.282  104.955 1.00 30.00 ? 27  VAL A CG1 1 
ATOM   208  C CG2 . VAL A 1 27  ? 104.799 77.330  107.074 1.00 30.00 ? 27  VAL A CG2 1 
ATOM   209  N N   . GLU A 1 28  ? 103.999 79.369  102.970 1.00 30.00 ? 28  GLU A N   1 
ATOM   210  C CA  . GLU A 1 28  ? 103.482 79.343  101.580 1.00 30.00 ? 28  GLU A CA  1 
ATOM   211  C C   . GLU A 1 28  ? 104.221 80.314  100.671 1.00 30.00 ? 28  GLU A C   1 
ATOM   212  O O   . GLU A 1 28  ? 104.697 79.878  99.610  1.00 30.00 ? 28  GLU A O   1 
ATOM   213  C CB  . GLU A 1 28  ? 102.035 79.798  101.668 1.00 30.00 ? 28  GLU A CB  1 
ATOM   214  C CG  . GLU A 1 28  ? 101.219 79.510  100.424 1.00 30.00 ? 28  GLU A CG  1 
ATOM   215  C CD  . GLU A 1 28  ? 101.313 80.521  99.295  1.00 30.00 ? 28  GLU A CD  1 
ATOM   216  O OE1 . GLU A 1 28  ? 102.019 81.528  99.458  1.00 30.00 ? 28  GLU A OE1 1 
ATOM   217  O OE2 . GLU A 1 28  ? 100.670 80.293  98.250  1.00 30.00 ? 28  GLU A OE2 1 
ATOM   218  N N   . ASP A 1 29  ? 104.295 81.576  101.069 1.00 30.00 ? 29  ASP A N   1 
ATOM   219  C CA  . ASP A 1 29  ? 104.949 82.641  100.280 1.00 30.00 ? 29  ASP A CA  1 
ATOM   220  C C   . ASP A 1 29  ? 106.416 82.289  100.099 1.00 30.00 ? 29  ASP A C   1 
ATOM   221  O O   . ASP A 1 29  ? 106.936 82.464  98.980  1.00 30.00 ? 29  ASP A O   1 
ATOM   222  C CB  . ASP A 1 29  ? 104.865 83.953  101.045 1.00 30.00 ? 29  ASP A CB  1 
ATOM   223  C CG  . ASP A 1 29  ? 103.456 84.421  101.355 1.00 30.00 ? 29  ASP A CG  1 
ATOM   224  O OD1 . ASP A 1 29  ? 102.507 83.712  100.987 1.00 30.00 ? 29  ASP A OD1 1 
ATOM   225  O OD2 . ASP A 1 29  ? 103.325 85.498  101.960 1.00 30.00 ? 29  ASP A OD2 1 
ATOM   226  N N   . LYS A 1 30  ? 107.042 81.800  101.164 1.00 30.00 ? 30  LYS A N   1 
ATOM   227  C CA  . LYS A 1 30  ? 108.480 81.454  101.146 1.00 30.00 ? 30  LYS A CA  1 
ATOM   228  C C   . LYS A 1 30  ? 108.633 79.999  100.721 1.00 30.00 ? 30  LYS A C   1 
ATOM   229  O O   . LYS A 1 30  ? 109.770 79.604  100.396 1.00 30.00 ? 30  LYS A O   1 
ATOM   230  C CB  . LYS A 1 30  ? 109.044 81.631  102.548 1.00 30.00 ? 30  LYS A CB  1 
ATOM   231  C CG  . LYS A 1 30  ? 108.632 82.900  103.275 1.00 30.00 ? 30  LYS A CG  1 
ATOM   232  C CD  . LYS A 1 30  ? 108.999 84.153  102.541 1.00 30.00 ? 30  LYS A CD  1 
ATOM   233  C CE  . LYS A 1 30  ? 108.637 85.396  103.319 1.00 30.00 ? 30  LYS A CE  1 
ATOM   234  N NZ  . LYS A 1 30  ? 108.977 86.618  102.557 1.00 30.00 ? 30  LYS A NZ  1 
ATOM   235  N N   . LYS A 1 31  ? 107.540 79.235  100.748 1.00 30.00 ? 31  LYS A N   1 
ATOM   236  C CA  . LYS A 1 31  ? 107.555 77.822  100.303 1.00 30.00 ? 31  LYS A CA  1 
ATOM   237  C C   . LYS A 1 31  ? 108.612 77.070  101.107 1.00 30.00 ? 31  LYS A C   1 
ATOM   238  O O   . LYS A 1 31  ? 109.563 76.551  100.488 1.00 30.00 ? 31  LYS A O   1 
ATOM   239  C CB  . LYS A 1 31  ? 107.855 77.795  98.811  1.00 30.00 ? 31  LYS A CB  1 
ATOM   240  C CG  . LYS A 1 31  ? 106.874 78.581  97.954  1.00 30.00 ? 31  LYS A CG  1 
ATOM   241  C CD  . LYS A 1 31  ? 107.230 78.617  96.488  1.00 30.00 ? 31  LYS A CD  1 
ATOM   242  C CE  . LYS A 1 31  ? 108.556 79.290  96.205  1.00 30.00 ? 31  LYS A CE  1 
ATOM   243  N NZ  . LYS A 1 31  ? 108.578 80.693  96.681  1.00 30.00 ? 31  LYS A NZ  1 
ATOM   244  N N   . PHE A 1 32  ? 108.462 77.015  102.427 1.00 30.00 ? 32  PHE A N   1 
ATOM   245  C CA  . PHE A 1 32  ? 109.427 76.350  103.338 1.00 30.00 ? 32  PHE A CA  1 
ATOM   246  C C   . PHE A 1 32  ? 110.819 76.923  103.094 1.00 30.00 ? 32  PHE A C   1 
ATOM   247  O O   . PHE A 1 32  ? 111.788 76.146  102.985 1.00 30.00 ? 32  PHE A O   1 
ATOM   248  C CB  . PHE A 1 32  ? 109.402 74.833  103.166 1.00 30.00 ? 32  PHE A CB  1 
ATOM   249  C CG  . PHE A 1 32  ? 108.226 74.176  103.817 1.00 30.00 ? 32  PHE A CG  1 
ATOM   250  C CD1 . PHE A 1 32  ? 108.029 74.274  105.180 1.00 30.00 ? 32  PHE A CD1 1 
ATOM   251  C CD2 . PHE A 1 32  ? 107.319 73.469  103.061 1.00 30.00 ? 32  PHE A CD2 1 
ATOM   252  C CE1 . PHE A 1 32  ? 106.940 73.667  105.778 1.00 30.00 ? 32  PHE A CE1 1 
ATOM   253  C CE2 . PHE A 1 32  ? 106.236 72.864  103.663 1.00 30.00 ? 32  PHE A CE2 1 
ATOM   254  C CZ  . PHE A 1 32  ? 106.050 72.964  105.012 1.00 30.00 ? 32  PHE A CZ  1 
ATOM   255  N N   . GLY A 1 33  ? 110.918 78.245  102.982 1.00 30.00 ? 33  GLY A N   1 
ATOM   256  C CA  . GLY A 1 33  ? 112.240 78.880  102.893 1.00 30.00 ? 33  GLY A CA  1 
ATOM   257  C C   . GLY A 1 33  ? 112.924 78.628  104.220 1.00 30.00 ? 33  GLY A C   1 
ATOM   258  O O   . GLY A 1 33  ? 112.213 78.332  105.186 1.00 30.00 ? 33  GLY A O   1 
ATOM   259  N N   . ALA A 1 34  ? 114.254 78.584  104.272 1.00 30.00 ? 34  ALA A N   1 
ATOM   260  C CA  . ALA A 1 34  ? 115.022 78.367  105.521 1.00 30.00 ? 34  ALA A CA  1 
ATOM   261  C C   . ALA A 1 34  ? 114.461 79.205  106.665 1.00 30.00 ? 34  ALA A C   1 
ATOM   262  O O   . ALA A 1 34  ? 114.457 78.712  107.810 1.00 30.00 ? 34  ALA A O   1 
ATOM   263  C CB  . ALA A 1 34  ? 116.433 78.762  105.281 1.00 30.00 ? 34  ALA A CB  1 
ATOM   264  N N   . GLU A 1 35  ? 114.010 80.420  106.368 1.00 30.00 ? 35  GLU A N   1 
ATOM   265  C CA  . GLU A 1 35  ? 113.518 81.384  107.385 1.00 30.00 ? 35  GLU A CA  1 
ATOM   266  C C   . GLU A 1 35  ? 112.239 80.903  108.057 1.00 30.00 ? 35  GLU A C   1 
ATOM   267  O O   . GLU A 1 35  ? 111.843 81.495  109.077 1.00 30.00 ? 35  GLU A O   1 
ATOM   268  C CB  . GLU A 1 35  ? 113.202 82.715  106.726 1.00 30.00 ? 35  GLU A CB  1 
ATOM   269  C CG  . GLU A 1 35  ? 112.203 82.690  105.586 1.00 30.00 ? 35  GLU A CG  1 
ATOM   270  C CD  . GLU A 1 35  ? 112.813 82.521  104.207 1.00 30.00 ? 35  GLU A CD  1 
ATOM   271  O OE1 . GLU A 1 35  ? 114.027 82.286  104.125 1.00 30.00 ? 35  GLU A OE1 1 
ATOM   272  O OE2 . GLU A 1 35  ? 112.086 82.700  103.220 1.00 30.00 ? 35  GLU A OE2 1 
ATOM   273  N N   . VAL A 1 36  ? 111.584 79.915  107.473 1.00 30.00 ? 36  VAL A N   1 
ATOM   274  C CA  . VAL A 1 36  ? 110.319 79.373  108.025 1.00 30.00 ? 36  VAL A CA  1 
ATOM   275  C C   . VAL A 1 36  ? 110.590 78.864  109.441 1.00 30.00 ? 36  VAL A C   1 
ATOM   276  O O   . VAL A 1 36  ? 109.694 79.011  110.290 1.00 30.00 ? 36  VAL A O   1 
ATOM   277  C CB  . VAL A 1 36  ? 109.770 78.292  107.090 1.00 30.00 ? 36  VAL A CB  1 
ATOM   278  C CG1 . VAL A 1 36  ? 108.691 77.454  107.748 1.00 30.00 ? 36  VAL A CG1 1 
ATOM   279  C CG2 . VAL A 1 36  ? 109.243 78.913  105.808 1.00 30.00 ? 36  VAL A CG2 1 
ATOM   280  N N   . VAL A 1 37  ? 111.768 78.294  109.689 1.00 30.00 ? 37  VAL A N   1 
ATOM   281  C CA  . VAL A 1 37  ? 112.111 77.686  111.007 1.00 30.00 ? 37  VAL A CA  1 
ATOM   282  C C   . VAL A 1 37  ? 112.138 78.728  112.139 1.00 30.00 ? 37  VAL A C   1 
ATOM   283  O O   . VAL A 1 37  ? 111.528 78.442  113.177 1.00 30.00 ? 37  VAL A O   1 
ATOM   284  C CB  . VAL A 1 37  ? 113.474 76.982  110.875 1.00 30.00 ? 37  VAL A CB  1 
ATOM   285  C CG1 . VAL A 1 37  ? 113.846 76.248  112.146 1.00 30.00 ? 37  VAL A CG1 1 
ATOM   286  C CG2 . VAL A 1 37  ? 113.507 76.015  109.706 1.00 30.00 ? 37  VAL A CG2 1 
ATOM   287  N N   . PRO A 1 38  ? 112.842 79.881  112.032 1.00 30.00 ? 38  PRO A N   1 
ATOM   288  C CA  . PRO A 1 38  ? 112.789 80.973  113.046 1.00 30.00 ? 38  PRO A CA  1 
ATOM   289  C C   . PRO A 1 38  ? 111.488 81.768  112.995 1.00 30.00 ? 38  PRO A C   1 
ATOM   290  O O   . PRO A 1 38  ? 111.147 82.354  113.987 1.00 30.00 ? 38  PRO A O   1 
ATOM   291  C CB  . PRO A 1 38  ? 113.983 81.837  112.640 1.00 30.00 ? 38  PRO A CB  1 
ATOM   292  C CG  . PRO A 1 38  ? 114.141 81.621  111.174 1.00 30.00 ? 38  PRO A CG  1 
ATOM   293  C CD  . PRO A 1 38  ? 113.856 80.152  111.011 1.00 30.00 ? 38  PRO A CD  1 
ATOM   294  N N   . GLY A 1 39  ? 110.867 81.861  111.821 1.00 30.00 ? 39  GLY A N   1 
ATOM   295  C CA  . GLY A 1 39  ? 109.555 82.515  111.721 1.00 30.00 ? 39  GLY A CA  1 
ATOM   296  C C   . GLY A 1 39  ? 108.595 81.714  112.571 1.00 30.00 ? 39  GLY A C   1 
ATOM   297  O O   . GLY A 1 39  ? 107.850 82.325  113.315 1.00 30.00 ? 39  GLY A O   1 
ATOM   298  N N   . PHE A 1 40  ? 108.695 80.386  112.547 1.00 30.00 ? 40  PHE A N   1 
ATOM   299  C CA  . PHE A 1 40  ? 107.850 79.475  113.357 1.00 30.00 ? 40  PHE A CA  1 
ATOM   300  C C   . PHE A 1 40  ? 108.166 79.610  114.842 1.00 30.00 ? 40  PHE A C   1 
ATOM   301  O O   . PHE A 1 40  ? 107.215 79.753  115.626 1.00 30.00 ? 40  PHE A O   1 
ATOM   302  C CB  . PHE A 1 40  ? 108.178 78.045  112.949 1.00 30.00 ? 40  PHE A CB  1 
ATOM   303  C CG  . PHE A 1 40  ? 107.708 76.952  113.868 1.00 30.00 ? 40  PHE A CG  1 
ATOM   304  C CD1 . PHE A 1 40  ? 106.366 76.773  114.144 1.00 30.00 ? 40  PHE A CD1 1 
ATOM   305  C CD2 . PHE A 1 40  ? 108.621 76.077  114.423 1.00 30.00 ? 40  PHE A CD2 1 
ATOM   306  C CE1 . PHE A 1 40  ? 105.952 75.751  114.979 1.00 30.00 ? 40  PHE A CE1 1 
ATOM   307  C CE2 . PHE A 1 40  ? 108.203 75.054  115.252 1.00 30.00 ? 40  PHE A CE2 1 
ATOM   308  C CZ  . PHE A 1 40  ? 106.871 74.895  115.532 1.00 30.00 ? 40  PHE A CZ  1 
ATOM   309  N N   . GLN A 1 41  ? 109.444 79.556  115.215 1.00 30.00 ? 41  GLN A N   1 
ATOM   310  C CA  . GLN A 1 41  ? 109.910 79.603  116.621 1.00 30.00 ? 41  GLN A CA  1 
ATOM   311  C C   . GLN A 1 41  ? 109.449 80.883  117.304 1.00 30.00 ? 41  GLN A C   1 
ATOM   312  O O   . GLN A 1 41  ? 108.986 80.799  118.458 1.00 30.00 ? 41  GLN A O   1 
ATOM   313  C CB  . GLN A 1 41  ? 111.430 79.609  116.574 1.00 30.00 ? 41  GLN A CB  1 
ATOM   314  C CG  . GLN A 1 41  ? 112.103 79.688  117.930 1.00 30.00 ? 41  GLN A CG  1 
ATOM   315  C CD  . GLN A 1 41  ? 113.603 79.693  117.781 1.00 30.00 ? 41  GLN A CD  1 
ATOM   316  O OE1 . GLN A 1 41  ? 114.136 79.614  116.678 1.00 30.00 ? 41  GLN A OE1 1 
ATOM   317  N NE2 . GLN A 1 41  ? 114.300 79.782  118.899 1.00 30.00 ? 41  GLN A NE2 1 
ATOM   318  N N   . ALA A 1 42  ? 109.597 82.020  116.631 1.00 30.00 ? 42  ALA A N   1 
ATOM   319  C CA  . ALA A 1 42  ? 109.229 83.343  117.174 1.00 30.00 ? 42  ALA A CA  1 
ATOM   320  C C   . ALA A 1 42  ? 107.719 83.450  117.339 1.00 30.00 ? 42  ALA A C   1 
ATOM   321  O O   . ALA A 1 42  ? 107.271 83.993  118.367 1.00 30.00 ? 42  ALA A O   1 
ATOM   322  C CB  . ALA A 1 42  ? 109.701 84.361  116.199 1.00 30.00 ? 42  ALA A CB  1 
ATOM   323  N N   . LEU A 1 43  ? 106.973 82.961  116.353 1.00 30.00 ? 43  LEU A N   1 
ATOM   324  C CA  . LEU A 1 43  ? 105.493 83.010  116.363 1.00 30.00 ? 43  LEU A CA  1 
ATOM   325  C C   . LEU A 1 43  ? 104.983 82.079  117.459 1.00 30.00 ? 43  LEU A C   1 
ATOM   326  O O   . LEU A 1 43  ? 103.843 82.279  117.908 1.00 30.00 ? 43  LEU A O   1 
ATOM   327  C CB  . LEU A 1 43  ? 105.033 82.535  114.987 1.00 30.00 ? 43  LEU A CB  1 
ATOM   328  C CG  . LEU A 1 43  ? 105.246 83.503  113.828 1.00 30.00 ? 43  LEU A CG  1 
ATOM   329  C CD1 . LEU A 1 43  ? 104.789 82.880  112.525 1.00 30.00 ? 43  LEU A CD1 1 
ATOM   330  C CD2 . LEU A 1 43  ? 104.507 84.803  114.060 1.00 30.00 ? 43  LEU A CD2 1 
ATOM   331  N N   . SER A 1 44  ? 105.802 81.124  117.897 1.00 30.00 ? 44  SER A N   1 
ATOM   332  C CA  . SER A 1 44  ? 105.411 80.096  118.890 1.00 30.00 ? 44  SER A CA  1 
ATOM   333  C C   . SER A 1 44  ? 106.165 80.225  120.212 1.00 30.00 ? 44  SER A C   1 
ATOM   334  O O   . SER A 1 44  ? 106.218 79.224  120.949 1.00 30.00 ? 44  SER A O   1 
ATOM   335  C CB  . SER A 1 44  ? 105.702 78.779  118.306 1.00 30.00 ? 44  SER A CB  1 
ATOM   336  O OG  . SER A 1 44  ? 107.097 78.592  118.213 1.00 30.00 ? 44  SER A OG  1 
ATOM   337  N N   . GLU A 1 45  ? 106.754 81.380  120.504 1.00 30.00 ? 45  GLU A N   1 
ATOM   338  C CA  . GLU A 1 45  ? 107.572 81.526  121.732 1.00 30.00 ? 45  GLU A CA  1 
ATOM   339  C C   . GLU A 1 45  ? 106.605 81.808  122.884 1.00 30.00 ? 45  GLU A C   1 
ATOM   340  O O   . GLU A 1 45  ? 105.903 82.835  122.812 1.00 30.00 ? 45  GLU A O   1 
ATOM   341  C CB  . GLU A 1 45  ? 108.619 82.613  121.516 1.00 30.00 ? 45  GLU A CB  1 
ATOM   342  C CG  . GLU A 1 45  ? 109.640 82.701  122.631 1.00 30.00 ? 45  GLU A CG  1 
ATOM   343  C CD  . GLU A 1 45  ? 110.655 81.573  122.659 1.00 30.00 ? 45  GLU A CD  1 
ATOM   344  O OE1 . GLU A 1 45  ? 110.613 80.719  121.755 1.00 30.00 ? 45  GLU A OE1 1 
ATOM   345  O OE2 . GLU A 1 45  ? 111.471 81.541  123.598 1.00 30.00 ? 45  GLU A OE2 1 
ATOM   346  N N   . GLY A 1 46  ? 106.561 80.933  123.894 1.00 30.00 ? 46  GLY A N   1 
ATOM   347  C CA  . GLY A 1 46  ? 105.597 81.049  125.007 1.00 30.00 ? 46  GLY A CA  1 
ATOM   348  C C   . GLY A 1 46  ? 104.366 80.205  124.727 1.00 30.00 ? 46  GLY A C   1 
ATOM   349  O O   . GLY A 1 46  ? 103.411 80.291  125.524 1.00 30.00 ? 46  GLY A O   1 
ATOM   350  N N   . CYS A 1 47  ? 104.378 79.413  123.649 1.00 30.00 ? 47  CYS A N   1 
ATOM   351  C CA  . CYS A 1 47  ? 103.235 78.551  123.242 1.00 30.00 ? 47  CYS A CA  1 
ATOM   352  C C   . CYS A 1 47  ? 103.281 77.178  123.897 1.00 30.00 ? 47  CYS A C   1 
ATOM   353  O O   . CYS A 1 47  ? 104.297 76.874  124.554 1.00 30.00 ? 47  CYS A O   1 
ATOM   354  C CB  . CYS A 1 47  ? 103.249 78.216  121.757 1.00 30.00 ? 47  CYS A CB  1 
ATOM   355  S SG  . CYS A 1 47  ? 102.419 79.434  120.712 1.00 30.00 ? 47  CYS A SG  1 
ATOM   356  N N   . THR A 1 48  ? 102.224 76.388  123.719 1.00 30.00 ? 48  THR A N   1 
ATOM   357  C CA  . THR A 1 48  ? 102.180 74.984  124.185 1.00 30.00 ? 48  THR A CA  1 
ATOM   358  C C   . THR A 1 48  ? 102.057 74.109  122.936 1.00 30.00 ? 48  THR A C   1 
ATOM   359  O O   . THR A 1 48  ? 101.664 74.636  121.879 1.00 30.00 ? 48  THR A O   1 
ATOM   360  C CB  . THR A 1 48  ? 101.016 74.745  125.145 1.00 30.00 ? 48  THR A CB  1 
ATOM   361  O OG1 . THR A 1 48  ? 99.808  74.831  124.399 1.00 30.00 ? 48  THR A OG1 1 
ATOM   362  C CG2 . THR A 1 48  ? 100.971 75.732  126.288 1.00 30.00 ? 48  THR A CG2 1 
ATOM   363  N N   . PRO A 1 49  ? 102.356 72.800  123.020 1.00 30.00 ? 49  PRO A N   1 
ATOM   364  C CA  . PRO A 1 49  ? 102.298 71.908  121.863 1.00 30.00 ? 49  PRO A CA  1 
ATOM   365  C C   . PRO A 1 49  ? 100.964 71.897  121.112 1.00 30.00 ? 49  PRO A C   1 
ATOM   366  O O   . PRO A 1 49  ? 100.986 71.736  119.913 1.00 30.00 ? 49  PRO A O   1 
ATOM   367  C CB  . PRO A 1 49  ? 102.420 70.544  122.533 1.00 30.00 ? 49  PRO A CB  1 
ATOM   368  C CG  . PRO A 1 49  ? 103.260 70.787  123.741 1.00 30.00 ? 49  PRO A CG  1 
ATOM   369  C CD  . PRO A 1 49  ? 102.720 72.096  124.252 1.00 30.00 ? 49  PRO A CD  1 
ATOM   370  N N   . TYR A 1 50  ? 99.850  72.057  121.822 1.00 30.00 ? 50  TYR A N   1 
ATOM   371  C CA  . TYR A 1 50  ? 98.484  72.030  121.244 1.00 30.00 ? 50  TYR A CA  1 
ATOM   372  C C   . TYR A 1 50  ? 98.353  73.058  120.129 1.00 30.00 ? 50  TYR A C   1 
ATOM   373  O O   . TYR A 1 50  ? 97.839  72.723  119.048 1.00 30.00 ? 50  TYR A O   1 
ATOM   374  C CB  . TYR A 1 50  ? 97.539  72.391  122.384 1.00 30.00 ? 50  TYR A CB  1 
ATOM   375  C CG  . TYR A 1 50  ? 96.100  72.654  122.040 1.00 30.00 ? 50  TYR A CG  1 
ATOM   376  C CD1 . TYR A 1 50  ? 95.303  71.685  121.465 1.00 30.00 ? 50  TYR A CD1 1 
ATOM   377  C CD2 . TYR A 1 50  ? 95.525  73.871  122.348 1.00 30.00 ? 50  TYR A CD2 1 
ATOM   378  C CE1 . TYR A 1 50  ? 93.972  71.928  121.177 1.00 30.00 ? 50  TYR A CE1 1 
ATOM   379  C CE2 . TYR A 1 50  ? 94.198  74.133  122.065 1.00 30.00 ? 50  TYR A CE2 1 
ATOM   380  C CZ  . TYR A 1 50  ? 93.418  73.157  121.481 1.00 30.00 ? 50  TYR A CZ  1 
ATOM   381  O OH  . TYR A 1 50  ? 92.106  73.423  121.196 1.00 30.00 ? 50  TYR A OH  1 
ATOM   382  N N   . ASP A 1 51  ? 98.905  74.246  120.338 1.00 30.00 ? 51  ASP A N   1 
ATOM   383  C CA  . ASP A 1 51  ? 98.804  75.358  119.368 1.00 30.00 ? 51  ASP A CA  1 
ATOM   384  C C   . ASP A 1 51  ? 99.845  75.187  118.277 1.00 30.00 ? 51  ASP A C   1 
ATOM   385  O O   . ASP A 1 51  ? 99.561  75.549  117.123 1.00 30.00 ? 51  ASP A O   1 
ATOM   386  C CB  . ASP A 1 51  ? 99.169  76.644  120.072 1.00 30.00 ? 51  ASP A CB  1 
ATOM   387  C CG  . ASP A 1 51  ? 98.575  76.730  121.454 1.00 30.00 ? 51  ASP A CG  1 
ATOM   388  O OD1 . ASP A 1 51  ? 97.360  76.933  121.565 1.00 30.00 ? 51  ASP A OD1 1 
ATOM   389  O OD2 . ASP A 1 51  ? 99.320  76.446  122.380 1.00 30.00 ? 51  ASP A OD2 1 
ATOM   390  N N   . ILE A 1 52  ? 101.018 74.690  118.654 1.00 30.00 ? 52  ILE A N   1 
ATOM   391  C CA  . ILE A 1 52  ? 102.110 74.433  117.684 1.00 30.00 ? 52  ILE A CA  1 
ATOM   392  C C   . ILE A 1 52  ? 101.523 73.475  116.655 1.00 30.00 ? 52  ILE A C   1 
ATOM   393  O O   . ILE A 1 52  ? 101.767 73.677  115.456 1.00 30.00 ? 52  ILE A O   1 
ATOM   394  C CB  . ILE A 1 52  ? 103.325 73.846  118.415 1.00 30.00 ? 52  ILE A CB  1 
ATOM   395  C CG1 . ILE A 1 52  ? 103.919 74.829  119.423 1.00 30.00 ? 52  ILE A CG1 1 
ATOM   396  C CG2 . ILE A 1 52  ? 104.356 73.390  117.412 1.00 30.00 ? 52  ILE A CG2 1 
ATOM   397  C CD1 . ILE A 1 52  ? 104.990 74.233  120.297 1.00 30.00 ? 52  ILE A CD1 1 
ATOM   398  N N   . ASN A 1 53  ? 100.748 72.495  117.114 1.00 30.00 ? 53  ASN A N   1 
ATOM   399  C CA  . ASN A 1 53  ? 100.054 71.551  116.211 1.00 30.00 ? 53  ASN A CA  1 
ATOM   400  C C   . ASN A 1 53  ? 99.048  72.311  115.355 1.00 30.00 ? 53  ASN A C   1 
ATOM   401  O O   . ASN A 1 53  ? 99.117  72.167  114.126 1.00 30.00 ? 53  ASN A O   1 
ATOM   402  C CB  . ASN A 1 53  ? 99.203  70.538  116.958 1.00 30.00 ? 53  ASN A CB  1 
ATOM   403  C CG  . ASN A 1 53  ? 99.956  69.579  117.846 1.00 30.00 ? 53  ASN A CG  1 
ATOM   404  O OD1 . ASN A 1 53  ? 101.176 69.560  117.863 1.00 30.00 ? 53  ASN A OD1 1 
ATOM   405  N ND2 . ASN A 1 53  ? 99.225  68.748  118.564 1.00 30.00 ? 53  ASN A ND2 1 
ATOM   406  N N   . GLN A 1 54  ? 98.137  73.077  115.968 1.00 30.00 ? 54  GLN A N   1 
ATOM   407  C CA  . GLN A 1 54  ? 97.047  73.774  115.234 1.00 30.00 ? 54  GLN A CA  1 
ATOM   408  C C   . GLN A 1 54  ? 97.612  74.680  114.152 1.00 30.00 ? 54  GLN A C   1 
ATOM   409  O O   . GLN A 1 54  ? 96.938  74.837  113.144 1.00 30.00 ? 54  GLN A O   1 
ATOM   410  C CB  . GLN A 1 54  ? 96.269  74.727  116.129 1.00 30.00 ? 54  GLN A CB  1 
ATOM   411  C CG  . GLN A 1 54  ? 95.321  74.046  117.096 1.00 30.00 ? 54  GLN A CG  1 
ATOM   412  C CD  . GLN A 1 54  ? 94.626  75.054  117.975 1.00 30.00 ? 54  GLN A CD  1 
ATOM   413  O OE1 . GLN A 1 54  ? 94.870  76.254  117.894 1.00 30.00 ? 54  GLN A OE1 1 
ATOM   414  N NE2 . GLN A 1 54  ? 93.751  74.567  118.835 1.00 30.00 ? 54  GLN A NE2 1 
ATOM   415  N N   . MET A 1 55  ? 98.733  75.341  114.417 1.00 30.00 ? 55  MET A N   1 
ATOM   416  C CA  . MET A 1 55  ? 99.408  76.220  113.437 1.00 30.00 ? 55  MET A CA  1 
ATOM   417  C C   . MET A 1 55  ? 99.811  75.382  112.233 1.00 30.00 ? 55  MET A C   1 
ATOM   418  O O   . MET A 1 55  ? 99.424  75.732  111.103 1.00 30.00 ? 55  MET A O   1 
ATOM   419  C CB  . MET A 1 55  ? 100.702 76.726  114.052 1.00 30.00 ? 55  MET A CB  1 
ATOM   420  C CG  . MET A 1 55  ? 100.596 77.966  114.867 1.00 30.00 ? 55  MET A CG  1 
ATOM   421  S SD  . MET A 1 55  ? 102.193 78.299  115.630 1.00 30.00 ? 55  MET A SD  1 
ATOM   422  C CE  . MET A 1 55  ? 102.987 79.222  114.319 1.00 30.00 ? 55  MET A CE  1 
ATOM   423  N N   . LEU A 1 56  ? 100.561 74.313  112.487 1.00 30.00 ? 56  LEU A N   1 
ATOM   424  C CA  . LEU A 1 56  ? 101.062 73.403  111.432 1.00 30.00 ? 56  LEU A CA  1 
ATOM   425  C C   . LEU A 1 56  ? 99.878  72.805  110.677 1.00 30.00 ? 56  LEU A C   1 
ATOM   426  O O   . LEU A 1 56  ? 99.988  72.643  109.448 1.00 30.00 ? 56  LEU A O   1 
ATOM   427  C CB  . LEU A 1 56  ? 101.850 72.312  112.151 1.00 30.00 ? 56  LEU A CB  1 
ATOM   428  C CG  . LEU A 1 56  ? 103.159 72.720  112.812 1.00 30.00 ? 56  LEU A CG  1 
ATOM   429  C CD1 . LEU A 1 56  ? 103.681 71.581  113.661 1.00 30.00 ? 56  LEU A CD1 1 
ATOM   430  C CD2 . LEU A 1 56  ? 104.187 73.110  111.772 1.00 30.00 ? 56  LEU A CD2 1 
ATOM   431  N N   . ASN A 1 57  ? 98.794  72.488  111.384 1.00 30.00 ? 57  ASN A N   1 
ATOM   432  C CA  . ASN A 1 57  ? 97.582  71.883  110.780 1.00 30.00 ? 57  ASN A CA  1 
ATOM   433  C C   . ASN A 1 57  ? 96.900  72.860  109.832 1.00 30.00 ? 57  ASN A C   1 
ATOM   434  O O   . ASN A 1 57  ? 96.565  72.449  108.714 1.00 30.00 ? 57  ASN A O   1 
ATOM   435  C CB  . ASN A 1 57  ? 96.550  71.518  111.831 1.00 30.00 ? 57  ASN A CB  1 
ATOM   436  C CG  . ASN A 1 57  ? 96.810  70.191  112.489 1.00 30.00 ? 57  ASN A CG  1 
ATOM   437  O OD1 . ASN A 1 57  ? 96.813  69.176  111.812 1.00 30.00 ? 57  ASN A OD1 1 
ATOM   438  N ND2 . ASN A 1 57  ? 96.989  70.185  113.796 1.00 30.00 ? 57  ASN A ND2 1 
ATOM   439  N N   . CYS A 1 58  ? 96.689  74.098  110.266 1.00 30.00 ? 58  CYS A N   1 
ATOM   440  C CA  . CYS A 1 58  ? 95.967  75.111  109.464 1.00 30.00 ? 58  CYS A CA  1 
ATOM   441  C C   . CYS A 1 58  ? 96.581  75.189  108.072 1.00 30.00 ? 58  CYS A C   1 
ATOM   442  O O   . CYS A 1 58  ? 95.827  75.397  107.109 1.00 30.00 ? 58  CYS A O   1 
ATOM   443  C CB  . CYS A 1 58  ? 96.086  76.470  110.113 1.00 30.00 ? 58  CYS A CB  1 
ATOM   444  S SG  . CYS A 1 58  ? 95.111  76.635  111.626 1.00 30.00 ? 58  CYS A SG  1 
ATOM   445  N N   . VAL A 1 59  ? 97.900  75.056  107.973 1.00 30.00 ? 59  VAL A N   1 
ATOM   446  C CA  . VAL A 1 59  ? 98.552  75.021  106.639 1.00 30.00 ? 59  VAL A CA  1 
ATOM   447  C C   . VAL A 1 59  ? 97.850  73.893  105.887 1.00 30.00 ? 59  VAL A C   1 
ATOM   448  O O   . VAL A 1 59  ? 97.812  72.774  106.436 1.00 30.00 ? 59  VAL A O   1 
ATOM   449  C CB  . VAL A 1 59  ? 100.065 74.787  106.765 1.00 30.00 ? 59  VAL A CB  1 
ATOM   450  C CG1 . VAL A 1 59  ? 100.728 74.651  105.410 1.00 30.00 ? 59  VAL A CG1 1 
ATOM   451  C CG2 . VAL A 1 59  ? 100.748 75.872  107.578 1.00 30.00 ? 59  VAL A CG2 1 
ATOM   452  N N   . GLY A 1 60  ? 97.328  74.159  104.689 1.00 30.00 ? 60  GLY A N   1 
ATOM   453  C CA  . GLY A 1 60  ? 96.539  73.167  103.934 1.00 30.00 ? 60  GLY A CA  1 
ATOM   454  C C   . GLY A 1 60  ? 97.224  72.710  102.672 1.00 30.00 ? 60  GLY A C   1 
ATOM   455  O O   . GLY A 1 60  ? 96.588  71.968  101.899 1.00 30.00 ? 60  GLY A O   1 
ATOM   456  N N   . ASP A 1 61  ? 98.464  73.134  102.468 1.00 30.00 ? 61  ASP A N   1 
ATOM   457  C CA  . ASP A 1 61  ? 99.202  72.832  101.224 1.00 30.00 ? 61  ASP A CA  1 
ATOM   458  C C   . ASP A 1 61  ? 100.623 72.444  101.607 1.00 30.00 ? 61  ASP A C   1 
ATOM   459  O O   . ASP A 1 61  ? 100.941 72.547  102.807 1.00 30.00 ? 61  ASP A O   1 
ATOM   460  C CB  . ASP A 1 61  ? 99.163  74.033  100.297 1.00 30.00 ? 61  ASP A CB  1 
ATOM   461  C CG  . ASP A 1 61  ? 99.145  73.655  98.829  1.00 30.00 ? 61  ASP A CG  1 
ATOM   462  O OD1 . ASP A 1 61  ? 100.096 72.989  98.382  1.00 30.00 ? 61  ASP A OD1 1 
ATOM   463  O OD2 . ASP A 1 61  ? 98.168  74.019  98.147  1.00 30.00 ? 61  ASP A OD2 1 
ATOM   464  N N   . HIS A 1 62  ? 101.415 71.964  100.650 1.00 30.00 ? 62  HIS A N   1 
ATOM   465  C CA  . HIS A 1 62  ? 102.769 71.473  100.976 1.00 30.00 ? 62  HIS A CA  1 
ATOM   466  C C   . HIS A 1 62  ? 102.540 70.377  102.006 1.00 30.00 ? 62  HIS A C   1 
ATOM   467  O O   . HIS A 1 62  ? 103.319 70.277  102.977 1.00 30.00 ? 62  HIS A O   1 
ATOM   468  C CB  . HIS A 1 62  ? 103.615 72.582  101.592 1.00 30.00 ? 62  HIS A CB  1 
ATOM   469  C CG  . HIS A 1 62  ? 103.659 73.884  100.883 1.00 30.00 ? 62  HIS A CG  1 
ATOM   470  N ND1 . HIS A 1 62  ? 104.257 74.063  99.658  1.00 30.00 ? 62  HIS A ND1 1 
ATOM   471  C CD2 . HIS A 1 62  ? 103.258 75.088  101.282 1.00 30.00 ? 62  HIS A CD2 1 
ATOM   472  C CE1 . HIS A 1 62  ? 104.166 75.336  99.316  1.00 30.00 ? 62  HIS A CE1 1 
ATOM   473  N NE2 . HIS A 1 62  ? 103.560 75.975  100.287 1.00 30.00 ? 62  HIS A NE2 1 
ATOM   474  N N   . GLN A 1 63  ? 101.481 69.591  101.818 1.00 30.00 ? 63  GLN A N   1 
ATOM   475  C CA  . GLN A 1 63  ? 101.084 68.558  102.805 1.00 30.00 ? 63  GLN A CA  1 
ATOM   476  C C   . GLN A 1 63  ? 102.027 67.360  102.692 1.00 30.00 ? 63  GLN A C   1 
ATOM   477  O O   . GLN A 1 63  ? 101.923 66.470  103.551 1.00 30.00 ? 63  GLN A O   1 
ATOM   478  C CB  . GLN A 1 63  ? 99.617  68.211  102.581 1.00 30.00 ? 63  GLN A CB  1 
ATOM   479  C CG  . GLN A 1 63  ? 98.651  69.297  103.011 1.00 30.00 ? 63  GLN A CG  1 
ATOM   480  C CD  . GLN A 1 63  ? 98.763  69.529  104.493 1.00 30.00 ? 63  GLN A CD  1 
ATOM   481  O OE1 . GLN A 1 63  ? 98.667  68.601  105.287 1.00 30.00 ? 63  GLN A OE1 1 
ATOM   482  N NE2 . GLN A 1 63  ? 99.050  70.760  104.874 1.00 30.00 ? 63  GLN A NE2 1 
ATOM   483  N N   . ALA A 1 64  ? 102.898 67.316  101.686 1.00 30.00 ? 64  ALA A N   1 
ATOM   484  C CA  . ALA A 1 64  ? 103.947 66.282  101.568 1.00 30.00 ? 64  ALA A CA  1 
ATOM   485  C C   . ALA A 1 64  ? 105.022 66.560  102.609 1.00 30.00 ? 64  ALA A C   1 
ATOM   486  O O   . ALA A 1 64  ? 105.527 65.593  103.200 1.00 30.00 ? 64  ALA A O   1 
ATOM   487  C CB  . ALA A 1 64  ? 104.553 66.343  100.210 1.00 30.00 ? 64  ALA A CB  1 
ATOM   488  N N   . ALA A 1 65  ? 105.334 67.833  102.835 1.00 30.00 ? 65  ALA A N   1 
ATOM   489  C CA  . ALA A 1 65  ? 106.389 68.253  103.776 1.00 30.00 ? 65  ALA A CA  1 
ATOM   490  C C   . ALA A 1 65  ? 105.858 68.196  105.200 1.00 30.00 ? 65  ALA A C   1 
ATOM   491  O O   . ALA A 1 65  ? 106.642 67.903  106.111 1.00 30.00 ? 65  ALA A O   1 
ATOM   492  C CB  . ALA A 1 65  ? 106.753 69.651  103.438 1.00 30.00 ? 65  ALA A CB  1 
ATOM   493  N N   . MET A 1 66  ? 104.580 68.510  105.376 1.00 30.00 ? 66  MET A N   1 
ATOM   494  C CA  . MET A 1 66  ? 103.941 68.467  106.708 1.00 30.00 ? 66  MET A CA  1 
ATOM   495  C C   . MET A 1 66  ? 103.963 67.007  107.144 1.00 30.00 ? 66  MET A C   1 
ATOM   496  O O   . MET A 1 66  ? 104.129 66.758  108.342 1.00 30.00 ? 66  MET A O   1 
ATOM   497  C CB  . MET A 1 66  ? 102.509 68.977  106.642 1.00 30.00 ? 66  MET A CB  1 
ATOM   498  C CG  . MET A 1 66  ? 102.381 70.471  106.441 1.00 30.00 ? 66  MET A CG  1 
ATOM   499  S SD  . MET A 1 66  ? 102.629 71.413  107.950 1.00 30.00 ? 66  MET A SD  1 
ATOM   500  C CE  . MET A 1 66  ? 104.095 72.349  107.536 1.00 30.00 ? 66  MET A CE  1 
ATOM   501  N N   . GLN A 1 67  ? 103.917 66.054  106.215 1.00 30.00 ? 67  GLN A N   1 
ATOM   502  C CA  . GLN A 1 67  ? 104.006 64.618  106.581 1.00 30.00 ? 67  GLN A CA  1 
ATOM   503  C C   . GLN A 1 67  ? 105.448 64.263  106.936 1.00 30.00 ? 67  GLN A C   1 
ATOM   504  O O   . GLN A 1 67  ? 105.635 63.451  107.854 1.00 30.00 ? 67  GLN A O   1 
ATOM   505  C CB  . GLN A 1 67  ? 103.566 63.729  105.431 1.00 30.00 ? 67  GLN A CB  1 
ATOM   506  C CG  . GLN A 1 67  ? 103.552 62.255  105.785 1.00 30.00 ? 67  GLN A CG  1 
ATOM   507  C CD  . GLN A 1 67  ? 102.530 61.958  106.853 1.00 30.00 ? 67  GLN A CD  1 
ATOM   508  O OE1 . GLN A 1 67  ? 101.347 62.252  106.701 1.00 30.00 ? 67  GLN A OE1 1 
ATOM   509  N NE2 . GLN A 1 67  ? 102.988 61.405  107.962 1.00 30.00 ? 67  GLN A NE2 1 
ATOM   510  N N   . ILE A 1 68  ? 106.427 64.827  106.229 1.00 30.00 ? 68  ILE A N   1 
ATOM   511  C CA  . ILE A 1 68  ? 107.863 64.600  106.554 1.00 30.00 ? 68  ILE A CA  1 
ATOM   512  C C   . ILE A 1 68  ? 108.076 65.105  107.978 1.00 30.00 ? 68  ILE A C   1 
ATOM   513  O O   . ILE A 1 68  ? 108.704 64.381  108.767 1.00 30.00 ? 68  ILE A O   1 
ATOM   514  C CB  . ILE A 1 68  ? 108.776 65.316  105.544 1.00 30.00 ? 68  ILE A CB  1 
ATOM   515  C CG1 . ILE A 1 68  ? 108.700 64.666  104.163 1.00 30.00 ? 68  ILE A CG1 1 
ATOM   516  C CG2 . ILE A 1 68  ? 110.204 65.372  106.055 1.00 30.00 ? 68  ILE A CG2 1 
ATOM   517  C CD1 . ILE A 1 68  ? 109.373 65.458  103.074 1.00 30.00 ? 68  ILE A CD1 1 
ATOM   518  N N   . ILE A 1 69  ? 107.535 66.280  108.302 1.00 30.00 ? 69  ILE A N   1 
ATOM   519  C CA  . ILE A 1 69  ? 107.625 66.848  109.675 1.00 30.00 ? 69  ILE A CA  1 
ATOM   520  C C   . ILE A 1 69  ? 106.980 65.851  110.633 1.00 30.00 ? 69  ILE A C   1 
ATOM   521  O O   . ILE A 1 69  ? 107.562 65.629  111.705 1.00 30.00 ? 69  ILE A O   1 
ATOM   522  C CB  . ILE A 1 69  ? 106.934 68.221  109.764 1.00 30.00 ? 69  ILE A CB  1 
ATOM   523  C CG1 . ILE A 1 69  ? 107.662 69.279  108.936 1.00 30.00 ? 69  ILE A CG1 1 
ATOM   524  C CG2 . ILE A 1 69  ? 106.786 68.657  111.210 1.00 30.00 ? 69  ILE A CG2 1 
ATOM   525  C CD1 . ILE A 1 69  ? 106.886 70.552  108.764 1.00 30.00 ? 69  ILE A CD1 1 
ATOM   526  N N   . ARG A 1 70  ? 105.846 65.248  110.262 1.00 30.00 ? 70  ARG A N   1 
ATOM   527  C CA  . ARG A 1 70  ? 105.099 64.363  111.195 1.00 30.00 ? 70  ARG A CA  1 
ATOM   528  C C   . ARG A 1 70  ? 105.877 63.073  111.420 1.00 30.00 ? 70  ARG A C   1 
ATOM   529  O O   . ARG A 1 70  ? 105.833 62.568  112.541 1.00 30.00 ? 70  ARG A O   1 
ATOM   530  C CB  . ARG A 1 70  ? 103.709 64.055  110.643 1.00 30.00 ? 70  ARG A CB  1 
ATOM   531  C CG  . ARG A 1 70  ? 102.857 63.175  111.543 1.00 30.00 ? 70  ARG A CG  1 
ATOM   532  C CD  . ARG A 1 70  ? 102.539 63.831  112.870 1.00 30.00 ? 70  ARG A CD  1 
ATOM   533  N NE  . ARG A 1 70  ? 102.051 62.867  113.844 1.00 30.00 ? 70  ARG A NE  1 
ATOM   534  C CZ  . ARG A 1 70  ? 101.706 63.153  115.095 1.00 30.00 ? 70  ARG A CZ  1 
ATOM   535  N NH1 . ARG A 1 70  ? 101.551 62.174  115.967 1.00 30.00 ? 70  ARG A NH1 1 
ATOM   536  N NH2 . ARG A 1 70  ? 101.530 64.406  115.482 1.00 30.00 ? 70  ARG A NH2 1 
ATOM   537  N N   . GLU A 1 71  ? 106.580 62.591  110.405 1.00 30.00 ? 71  GLU A N   1 
ATOM   538  C CA  . GLU A 1 71  ? 107.399 61.366  110.525 1.00 30.00 ? 71  GLU A CA  1 
ATOM   539  C C   . GLU A 1 71  ? 108.589 61.684  111.426 1.00 30.00 ? 71  GLU A C   1 
ATOM   540  O O   . GLU A 1 71  ? 108.922 60.835  112.259 1.00 30.00 ? 71  GLU A O   1 
ATOM   541  C CB  . GLU A 1 71  ? 107.834 60.945  109.131 1.00 30.00 ? 71  GLU A CB  1 
ATOM   542  C CG  . GLU A 1 71  ? 106.688 60.453  108.271 1.00 30.00 ? 71  GLU A CG  1 
ATOM   543  C CD  . GLU A 1 71  ? 107.016 60.284  106.798 1.00 30.00 ? 71  GLU A CD  1 
ATOM   544  O OE1 . GLU A 1 71  ? 108.165 60.570  106.410 1.00 30.00 ? 71  GLU A OE1 1 
ATOM   545  O OE2 . GLU A 1 71  ? 106.120 59.859  106.044 1.00 30.00 ? 71  GLU A OE2 1 
ATOM   546  N N   . ILE A 1 72  ? 109.182 62.869  111.275 1.00 30.00 ? 72  ILE A N   1 
ATOM   547  C CA  . ILE A 1 72  ? 110.333 63.313  112.113 1.00 30.00 ? 72  ILE A CA  1 
ATOM   548  C C   . ILE A 1 72  ? 109.857 63.477  113.557 1.00 30.00 ? 72  ILE A C   1 
ATOM   549  O O   . ILE A 1 72  ? 110.617 63.104  114.443 1.00 30.00 ? 72  ILE A O   1 
ATOM   550  C CB  . ILE A 1 72  ? 110.932 64.620  111.562 1.00 30.00 ? 72  ILE A CB  1 
ATOM   551  C CG1 . ILE A 1 72  ? 111.596 64.421  110.198 1.00 30.00 ? 72  ILE A CG1 1 
ATOM   552  C CG2 . ILE A 1 72  ? 111.894 65.245  112.559 1.00 30.00 ? 72  ILE A CG2 1 
ATOM   553  C CD1 . ILE A 1 72  ? 112.853 63.595  110.236 1.00 30.00 ? 72  ILE A CD1 1 
ATOM   554  N N   . ILE A 1 73  ? 108.656 64.013  113.780 1.00 30.00 ? 73  ILE A N   1 
ATOM   555  C CA  . ILE A 1 73  ? 108.105 64.251  115.149 1.00 30.00 ? 73  ILE A CA  1 
ATOM   556  C C   . ILE A 1 73  ? 107.898 62.906  115.842 1.00 30.00 ? 73  ILE A C   1 
ATOM   557  O O   . ILE A 1 73  ? 108.152 62.846  117.053 1.00 30.00 ? 73  ILE A O   1 
ATOM   558  C CB  . ILE A 1 73  ? 106.779 65.029  115.077 1.00 30.00 ? 73  ILE A CB  1 
ATOM   559  C CG1 . ILE A 1 73  ? 106.986 66.489  114.677 1.00 30.00 ? 73  ILE A CG1 1 
ATOM   560  C CG2 . ILE A 1 73  ? 106.017 64.928  116.389 1.00 30.00 ? 73  ILE A CG2 1 
ATOM   561  C CD1 . ILE A 1 73  ? 105.729 67.167  114.197 1.00 30.00 ? 73  ILE A CD1 1 
ATOM   562  N N   . ASN A 1 74  ? 107.427 61.886  115.122 1.00 30.00 ? 74  ASN A N   1 
ATOM   563  C CA  . ASN A 1 74  ? 107.123 60.546  115.686 1.00 30.00 ? 74  ASN A CA  1 
ATOM   564  C C   . ASN A 1 74  ? 108.433 59.838  116.017 1.00 30.00 ? 74  ASN A C   1 
ATOM   565  O O   . ASN A 1 74  ? 108.427 59.025  116.955 1.00 30.00 ? 74  ASN A O   1 
ATOM   566  C CB  . ASN A 1 74  ? 106.324 59.719  114.683 1.00 30.00 ? 74  ASN A CB  1 
ATOM   567  C CG  . ASN A 1 74  ? 105.009 60.354  114.286 1.00 30.00 ? 74  ASN A CG  1 
ATOM   568  O OD1 . ASN A 1 74  ? 104.619 61.384  114.827 1.00 30.00 ? 74  ASN A OD1 1 
ATOM   569  N ND2 . ASN A 1 74  ? 104.305 59.731  113.357 1.00 30.00 ? 74  ASN A ND2 1 
ATOM   570  N N   . ASP A 1 75  ? 109.495 60.102  115.258 1.00 30.00 ? 75  ASP A N   1 
ATOM   571  C CA  . ASP A 1 75  ? 110.838 59.503  115.448 1.00 30.00 ? 75  ASP A CA  1 
ATOM   572  C C   . ASP A 1 75  ? 111.498 60.072  116.700 1.00 30.00 ? 75  ASP A C   1 
ATOM   573  O O   . ASP A 1 75  ? 112.026 59.275  117.490 1.00 30.00 ? 75  ASP A O   1 
ATOM   574  C CB  . ASP A 1 75  ? 111.716 59.812  114.242 1.00 30.00 ? 75  ASP A CB  1 
ATOM   575  C CG  . ASP A 1 75  ? 111.216 59.226  112.937 1.00 30.00 ? 75  ASP A CG  1 
ATOM   576  O OD1 . ASP A 1 75  ? 110.191 58.521  112.965 1.00 30.00 ? 75  ASP A OD1 1 
ATOM   577  O OD2 . ASP A 1 75  ? 111.842 59.505  111.899 1.00 30.00 ? 75  ASP A OD2 1 
ATOM   578  N N   . GLU A 1 76  ? 111.452 61.391  116.879 1.00 30.00 ? 76  GLU A N   1 
ATOM   579  C CA  . GLU A 1 76  ? 112.062 62.066  118.051 1.00 30.00 ? 76  GLU A CA  1 
ATOM   580  C C   . GLU A 1 76  ? 111.290 61.631  119.294 1.00 30.00 ? 76  GLU A C   1 
ATOM   581  O O   . GLU A 1 76  ? 111.923 61.489  120.352 1.00 30.00 ? 76  GLU A O   1 
ATOM   582  C CB  . GLU A 1 76  ? 111.986 63.581  117.891 1.00 30.00 ? 76  GLU A CB  1 
ATOM   583  C CG  . GLU A 1 76  ? 112.712 64.140  116.682 1.00 30.00 ? 76  GLU A CG  1 
ATOM   584  C CD  . GLU A 1 76  ? 114.218 63.965  116.691 1.00 30.00 ? 76  GLU A CD  1 
ATOM   585  O OE1 . GLU A 1 76  ? 114.861 64.467  117.629 1.00 30.00 ? 76  GLU A OE1 1 
ATOM   586  O OE2 . GLU A 1 76  ? 114.743 63.342  115.750 1.00 30.00 ? 76  GLU A OE2 1 
ATOM   587  N N   . ALA A 1 77  ? 109.972 61.464  119.175 1.00 30.00 ? 77  ALA A N   1 
ATOM   588  C CA  . ALA A 1 77  ? 109.095 61.040  120.289 1.00 30.00 ? 77  ALA A CA  1 
ATOM   589  C C   . ALA A 1 77  ? 109.411 59.603  120.696 1.00 30.00 ? 77  ALA A C   1 
ATOM   590  O O   . ALA A 1 77  ? 109.304 59.312  121.897 1.00 30.00 ? 77  ALA A O   1 
ATOM   591  C CB  . ALA A 1 77  ? 107.667 61.155  119.854 1.00 30.00 ? 77  ALA A CB  1 
ATOM   592  N N   . ALA A 1 78  ? 109.734 58.734  119.737 1.00 30.00 ? 78  ALA A N   1 
ATOM   593  C CA  . ALA A 1 78  ? 110.039 57.307  119.990 1.00 30.00 ? 78  ALA A CA  1 
ATOM   594  C C   . ALA A 1 78  ? 111.372 57.203  120.727 1.00 30.00 ? 78  ALA A C   1 
ATOM   595  O O   . ALA A 1 78  ? 111.570 56.184  121.403 1.00 30.00 ? 78  ALA A O   1 
ATOM   596  C CB  . ALA A 1 78  ? 110.094 56.596  118.672 1.00 30.00 ? 78  ALA A CB  1 
ATOM   597  N N   . ASP A 1 79  ? 112.268 58.171  120.543 1.00 30.00 ? 79  ASP A N   1 
ATOM   598  C CA  . ASP A 1 79  ? 113.585 58.251  121.221 1.00 30.00 ? 79  ASP A CA  1 
ATOM   599  C C   . ASP A 1 79  ? 113.372 58.687  122.668 1.00 30.00 ? 79  ASP A C   1 
ATOM   600  O O   . ASP A 1 79  ? 114.046 58.135  123.548 1.00 30.00 ? 79  ASP A O   1 
ATOM   601  C CB  . ASP A 1 79  ? 114.495 59.246  120.513 1.00 30.00 ? 79  ASP A CB  1 
ATOM   602  C CG  . ASP A 1 79  ? 114.727 58.946  119.044 1.00 30.00 ? 79  ASP A CG  1 
ATOM   603  O OD1 . ASP A 1 79  ? 114.202 57.924  118.564 1.00 30.00 ? 79  ASP A OD1 1 
ATOM   604  O OD2 . ASP A 1 79  ? 115.413 59.750  118.388 1.00 30.00 ? 79  ASP A OD2 1 
ATOM   605  N N   . TRP A 1 80  ? 112.472 59.642  122.903 1.00 30.00 ? 80  TRP A N   1 
ATOM   606  C CA  . TRP A 1 80  ? 112.155 60.119  124.272 1.00 30.00 ? 80  TRP A CA  1 
ATOM   607  C C   . TRP A 1 80  ? 111.596 58.933  125.056 1.00 30.00 ? 80  TRP A C   1 
ATOM   608  O O   . TRP A 1 80  ? 111.972 58.772  126.219 1.00 30.00 ? 80  TRP A O   1 
ATOM   609  C CB  . TRP A 1 80  ? 111.181 61.298  124.214 1.00 30.00 ? 80  TRP A CB  1 
ATOM   610  C CG  . TRP A 1 80  ? 110.796 61.841  125.552 1.00 30.00 ? 80  TRP A CG  1 
ATOM   611  C CD1 . TRP A 1 80  ? 110.082 61.212  126.529 1.00 30.00 ? 80  TRP A CD1 1 
ATOM   612  C CD2 . TRP A 1 80  ? 111.166 63.120  126.088 1.00 30.00 ? 80  TRP A CD2 1 
ATOM   613  N NE1 . TRP A 1 80  ? 109.955 62.026  127.621 1.00 30.00 ? 80  TRP A NE1 1 
ATOM   614  C CE2 . TRP A 1 80  ? 110.616 63.199  127.382 1.00 30.00 ? 80  TRP A CE2 1 
ATOM   615  C CE3 . TRP A 1 80  ? 111.898 64.203  125.597 1.00 30.00 ? 80  TRP A CE3 1 
ATOM   616  C CZ2 . TRP A 1 80  ? 110.774 64.323  128.187 1.00 30.00 ? 80  TRP A CZ2 1 
ATOM   617  C CZ3 . TRP A 1 80  ? 112.056 65.311  126.395 1.00 30.00 ? 80  TRP A CZ3 1 
ATOM   618  C CH2 . TRP A 1 80  ? 111.499 65.370  127.671 1.00 30.00 ? 80  TRP A CH2 1 
ATOM   619  N N   . ASP A 1 81  ? 110.743 58.124  124.434 1.00 30.00 ? 81  ASP A N   1 
ATOM   620  C CA  . ASP A 1 81  ? 110.191 56.902  125.068 1.00 30.00 ? 81  ASP A CA  1 
ATOM   621  C C   . ASP A 1 81  ? 111.325 55.905  125.300 1.00 30.00 ? 81  ASP A C   1 
ATOM   622  O O   . ASP A 1 81  ? 111.362 55.315  126.395 1.00 30.00 ? 81  ASP A O   1 
ATOM   623  C CB  . ASP A 1 81  ? 109.111 56.307  124.168 1.00 30.00 ? 81  ASP A CB  1 
ATOM   624  C CG  . ASP A 1 81  ? 107.763 56.995  124.277 1.00 30.00 ? 81  ASP A CG  1 
ATOM   625  O OD1 . ASP A 1 81  ? 107.635 57.883  125.129 1.00 30.00 ? 81  ASP A OD1 1 
ATOM   626  O OD2 . ASP A 1 81  ? 106.864 56.647  123.490 1.00 30.00 ? 81  ASP A OD2 1 
ATOM   627  N N   . ALA A 1 82  ? 112.233 55.753  124.335 1.00 30.00 ? 82  ALA A N   1 
ATOM   628  C CA  . ALA A 1 82  ? 113.349 54.781  124.389 1.00 30.00 ? 82  ALA A CA  1 
ATOM   629  C C   . ALA A 1 82  ? 114.350 55.131  125.490 1.00 30.00 ? 82  ALA A C   1 
ATOM   630  O O   . ALA A 1 82  ? 114.838 54.193  126.148 1.00 30.00 ? 82  ALA A O   1 
ATOM   631  C CB  . ALA A 1 82  ? 114.035 54.778  123.053 1.00 30.00 ? 82  ALA A CB  1 
ATOM   632  N N   . GLN A 1 83  ? 114.637 56.419  125.693 1.00 30.00 ? 83  GLN A N   1 
ATOM   633  C CA  . GLN A 1 83  ? 115.672 56.876  126.655 1.00 30.00 ? 83  GLN A CA  1 
ATOM   634  C C   . GLN A 1 83  ? 115.083 56.982  128.057 1.00 30.00 ? 83  GLN A C   1 
ATOM   635  O O   . GLN A 1 83  ? 115.797 56.643  129.020 1.00 30.00 ? 83  GLN A O   1 
ATOM   636  C CB  . GLN A 1 83  ? 116.170 58.253  126.229 1.00 30.00 ? 83  GLN A CB  1 
ATOM   637  C CG  . GLN A 1 83  ? 116.864 58.254  124.876 1.00 30.00 ? 83  GLN A CG  1 
ATOM   638  C CD  . GLN A 1 83  ? 117.009 59.642  124.304 1.00 30.00 ? 83  GLN A CD  1 
ATOM   639  O OE1 . GLN A 1 83  ? 116.616 60.634  124.912 1.00 30.00 ? 83  GLN A OE1 1 
ATOM   640  N NE2 . GLN A 1 83  ? 117.579 59.719  123.113 1.00 30.00 ? 83  GLN A NE2 1 
ATOM   641  N N   . HIS A 1 84  ? 113.833 57.429  128.164 1.00 30.00 ? 84  HIS A N   1 
ATOM   642  C CA  . HIS A 1 84  ? 113.177 57.621  129.483 1.00 30.00 ? 84  HIS A CA  1 
ATOM   643  C C   . HIS A 1 84  ? 112.853 56.242  130.058 1.00 30.00 ? 84  HIS A C   1 
ATOM   644  O O   . HIS A 1 84  ? 112.599 55.299  129.276 1.00 30.00 ? 84  HIS A O   1 
ATOM   645  C CB  . HIS A 1 84  ? 111.992 58.579  129.339 1.00 30.00 ? 84  HIS A CB  1 
ATOM   646  C CG  . HIS A 1 84  ? 112.423 59.995  129.160 1.00 30.00 ? 84  HIS A CG  1 
ATOM   647  N ND1 . HIS A 1 84  ? 113.283 60.425  128.173 1.00 30.00 ? 84  HIS A ND1 1 
ATOM   648  C CD2 . HIS A 1 84  ? 112.140 61.074  129.895 1.00 30.00 ? 84  HIS A CD2 1 
ATOM   649  C CE1 . HIS A 1 84  ? 113.484 61.726  128.304 1.00 30.00 ? 84  HIS A CE1 1 
ATOM   650  N NE2 . HIS A 1 84  ? 112.799 62.141  129.345 1.00 30.00 ? 84  HIS A NE2 1 
ATOM   651  N N   . PRO A 1 85  ? 112.841 56.076  131.397 1.00 30.00 ? 85  PRO A N   1 
ATOM   652  C CA  . PRO A 1 85  ? 112.663 54.760  132.014 1.00 30.00 ? 85  PRO A CA  1 
ATOM   653  C C   . PRO A 1 85  ? 111.214 54.351  132.296 1.00 30.00 ? 85  PRO A C   1 
ATOM   654  O O   . PRO A 1 85  ? 111.037 53.288  132.860 1.00 30.00 ? 85  PRO A O   1 
ATOM   655  C CB  . PRO A 1 85  ? 113.384 54.984  133.347 1.00 30.00 ? 85  PRO A CB  1 
ATOM   656  C CG  . PRO A 1 85  ? 113.007 56.399  133.717 1.00 30.00 ? 85  PRO A CG  1 
ATOM   657  C CD  . PRO A 1 85  ? 112.965 57.140  132.397 1.00 30.00 ? 85  PRO A CD  1 
ATOM   658  N N   . ILE A 1 86  ? 110.233 55.183  131.934 1.00 30.00 ? 86  ILE A N   1 
ATOM   659  C CA  . ILE A 1 86  ? 108.798 54.905  132.241 1.00 30.00 ? 86  ILE A CA  1 
ATOM   660  C C   . ILE A 1 86  ? 108.771 54.351  133.670 1.00 30.00 ? 86  ILE A C   1 
ATOM   661  O O   . ILE A 1 86  ? 108.466 53.159  133.860 1.00 30.00 ? 86  ILE A O   1 
ATOM   662  C CB  . ILE A 1 86  ? 108.136 54.010  131.164 1.00 30.00 ? 86  ILE A CB  1 
ATOM   663  C CG1 . ILE A 1 86  ? 106.651 53.771  131.453 1.00 30.00 ? 86  ILE A CG1 1 
ATOM   664  C CG2 . ILE A 1 86  ? 108.877 52.698  130.935 1.00 30.00 ? 86  ILE A CG2 1 
ATOM   665  C CD1 . ILE A 1 86  ? 105.837 55.038  131.551 1.00 30.00 ? 86  ILE A CD1 1 
ATOM   666  N N   . PRO A 1 87  ? 109.011 55.189  134.699 1.00 30.00 ? 87  PRO A N   1 
ATOM   667  C CA  . PRO A 1 87  ? 109.095 54.703  136.081 1.00 30.00 ? 87  PRO A CA  1 
ATOM   668  C C   . PRO A 1 87  ? 107.806 54.036  136.578 1.00 30.00 ? 87  PRO A C   1 
ATOM   669  O O   . PRO A 1 87  ? 106.851 53.974  135.823 1.00 30.00 ? 87  PRO A O   1 
ATOM   670  C CB  . PRO A 1 87  ? 109.365 55.981  136.891 1.00 30.00 ? 87  PRO A CB  1 
ATOM   671  C CG  . PRO A 1 87  ? 108.833 57.093  136.019 1.00 30.00 ? 87  PRO A CG  1 
ATOM   672  C CD  . PRO A 1 87  ? 109.158 56.643  134.613 1.00 30.00 ? 87  PRO A CD  1 
ATOM   673  N N   . GLY A 1 88  ? 107.785 53.599  137.840 1.00 30.00 ? 88  GLY A N   1 
ATOM   674  C CA  . GLY A 1 88  ? 106.612 52.922  138.423 1.00 30.00 ? 88  GLY A CA  1 
ATOM   675  C C   . GLY A 1 88  ? 105.385 53.810  138.346 1.00 30.00 ? 88  GLY A C   1 
ATOM   676  O O   . GLY A 1 88  ? 105.548 55.044  138.436 1.00 30.00 ? 88  GLY A O   1 
ATOM   677  N N   . PRO A 1 89  ? 104.159 53.263  138.185 1.00 30.00 ? 89  PRO A N   1 
ATOM   678  C CA  . PRO A 1 89  ? 102.970 54.096  137.999 1.00 30.00 ? 89  PRO A CA  1 
ATOM   679  C C   . PRO A 1 89  ? 102.798 55.113  139.132 1.00 30.00 ? 89  PRO A C   1 
ATOM   680  O O   . PRO A 1 89  ? 103.050 54.753  140.268 1.00 30.00 ? 89  PRO A O   1 
ATOM   681  C CB  . PRO A 1 89  ? 101.806 53.097  138.022 1.00 30.00 ? 89  PRO A CB  1 
ATOM   682  C CG  . PRO A 1 89  ? 102.436 51.787  137.607 1.00 30.00 ? 89  PRO A CG  1 
ATOM   683  C CD  . PRO A 1 89  ? 103.840 51.835  138.172 1.00 30.00 ? 89  PRO A CD  1 
ATOM   684  N N   . LEU A 1 90  ? 102.372 56.334  138.803 1.00 30.00 ? 90  LEU A N   1 
ATOM   685  C CA  . LEU A 1 90  ? 102.181 57.422  139.801 1.00 30.00 ? 90  LEU A CA  1 
ATOM   686  C C   . LEU A 1 90  ? 100.689 57.534  140.126 1.00 30.00 ? 90  LEU A C   1 
ATOM   687  O O   . LEU A 1 90  ? 99.873  57.049  139.317 1.00 30.00 ? 90  LEU A O   1 
ATOM   688  C CB  . LEU A 1 90  ? 102.758 58.741  139.265 1.00 30.00 ? 90  LEU A CB  1 
ATOM   689  C CG  . LEU A 1 90  ? 102.404 59.142  137.833 1.00 30.00 ? 90  LEU A CG  1 
ATOM   690  C CD1 . LEU A 1 90  ? 101.080 59.881  137.767 1.00 30.00 ? 90  LEU A CD1 1 
ATOM   691  C CD2 . LEU A 1 90  ? 103.509 59.990  137.234 1.00 30.00 ? 90  LEU A CD2 1 
ATOM   692  N N   . PRO A 1 91  ? 100.295 58.132  141.271 1.00 30.00 ? 91  PRO A N   1 
ATOM   693  C CA  . PRO A 1 91  ? 98.890  58.195  141.673 1.00 30.00 ? 91  PRO A CA  1 
ATOM   694  C C   . PRO A 1 91  ? 98.097  59.136  140.761 1.00 30.00 ? 91  PRO A C   1 
ATOM   695  O O   . PRO A 1 91  ? 98.718  59.858  140.014 1.00 30.00 ? 91  PRO A O   1 
ATOM   696  C CB  . PRO A 1 91  ? 98.909  58.764  143.100 1.00 30.00 ? 91  PRO A CB  1 
ATOM   697  C CG  . PRO A 1 91  ? 100.362 58.702  143.525 1.00 30.00 ? 91  PRO A CG  1 
ATOM   698  C CD  . PRO A 1 91  ? 101.160 58.797  142.243 1.00 30.00 ? 91  PRO A CD  1 
ATOM   699  N N   . ALA A 1 92  ? 96.765  59.093  140.816 1.00 30.00 ? 92  ALA A N   1 
ATOM   700  C CA  . ALA A 1 92  ? 95.900  59.983  140.011 1.00 30.00 ? 92  ALA A CA  1 
ATOM   701  C C   . ALA A 1 92  ? 96.227  61.430  140.381 1.00 30.00 ? 92  ALA A C   1 
ATOM   702  O O   . ALA A 1 92  ? 96.303  62.264  139.460 1.00 30.00 ? 92  ALA A O   1 
ATOM   703  C CB  . ALA A 1 92  ? 94.454  59.657  140.265 1.00 30.00 ? 92  ALA A CB  1 
ATOM   704  N N   . GLY A 1 93  ? 96.399  61.721  141.674 1.00 30.00 ? 93  GLY A N   1 
ATOM   705  C CA  . GLY A 1 93  ? 96.800  63.065  142.133 1.00 30.00 ? 93  GLY A CA  1 
ATOM   706  C C   . GLY A 1 93  ? 97.941  63.604  141.289 1.00 30.00 ? 93  GLY A C   1 
ATOM   707  O O   . GLY A 1 93  ? 97.878  64.794  140.924 1.00 30.00 ? 93  GLY A O   1 
ATOM   708  N N   . GLN A 1 94  ? 98.944  62.775  140.974 1.00 30.00 ? 94  GLN A N   1 
ATOM   709  C CA  . GLN A 1 94  ? 100.122 63.174  140.162 1.00 30.00 ? 94  GLN A CA  1 
ATOM   710  C C   . GLN A 1 94  ? 99.776  62.994  138.682 1.00 30.00 ? 94  GLN A C   1 
ATOM   711  O O   . GLN A 1 94  ? 98.915  62.142  138.388 1.00 30.00 ? 94  GLN A O   1 
ATOM   712  C CB  . GLN A 1 94  ? 101.340 62.335  140.547 1.00 30.00 ? 94  GLN A CB  1 
ATOM   713  C CG  . GLN A 1 94  ? 102.588 62.686  139.751 1.00 30.00 ? 94  GLN A CG  1 
ATOM   714  C CD  . GLN A 1 94  ? 103.850 62.083  140.318 1.00 30.00 ? 94  GLN A CD  1 
ATOM   715  O OE1 . GLN A 1 94  ? 103.841 61.416  141.349 1.00 30.00 ? 94  GLN A OE1 1 
ATOM   716  N NE2 . GLN A 1 94  ? 104.960 62.333  139.644 1.00 30.00 ? 94  GLN A NE2 1 
ATOM   717  N N   . LEU A 1 95  ? 100.436 63.734  137.784 1.00 30.00 ? 95  LEU A N   1 
ATOM   718  C CA  . LEU A 1 95  ? 100.180 63.654  136.320 1.00 30.00 ? 95  LEU A CA  1 
ATOM   719  C C   . LEU A 1 95  ? 101.192 62.694  135.692 1.00 30.00 ? 95  LEU A C   1 
ATOM   720  O O   . LEU A 1 95  ? 102.328 62.635  136.198 1.00 30.00 ? 95  LEU A O   1 
ATOM   721  C CB  . LEU A 1 95  ? 100.279 65.061  135.723 1.00 30.00 ? 95  LEU A CB  1 
ATOM   722  C CG  . LEU A 1 95  ? 100.110 65.175  134.209 1.00 30.00 ? 95  LEU A CG  1 
ATOM   723  C CD1 . LEU A 1 95  ? 98.749  64.677  133.758 1.00 30.00 ? 95  LEU A CD1 1 
ATOM   724  C CD2 . LEU A 1 95  ? 100.296 66.617  133.769 1.00 30.00 ? 95  LEU A CD2 1 
ATOM   725  N N   . ARG A 1 96  ? 100.810 61.997  134.621 1.00 30.00 ? 96  ARG A N   1 
ATOM   726  C CA  . ARG A 1 96  ? 101.667 60.974  133.968 1.00 30.00 ? 96  ARG A CA  1 
ATOM   727  C C   . ARG A 1 96  ? 103.030 61.540  133.590 1.00 30.00 ? 96  ARG A C   1 
ATOM   728  O O   . ARG A 1 96  ? 103.056 62.618  132.985 1.00 30.00 ? 96  ARG A O   1 
ATOM   729  C CB  . ARG A 1 96  ? 101.076 60.529  132.630 1.00 30.00 ? 96  ARG A CB  1 
ATOM   730  C CG  . ARG A 1 96  ? 99.642  60.029  132.681 1.00 30.00 ? 96  ARG A CG  1 
ATOM   731  C CD  . ARG A 1 96  ? 99.163  59.625  131.298 1.00 30.00 ? 96  ARG A CD  1 
ATOM   732  N NE  . ARG A 1 96  ? 99.380  60.627  130.259 1.00 30.00 ? 96  ARG A NE  1 
ATOM   733  C CZ  . ARG A 1 96  ? 98.854  61.849  130.232 1.00 30.00 ? 96  ARG A CZ  1 
ATOM   734  N NH1 . ARG A 1 96  ? 98.127  62.304  131.236 1.00 30.00 ? 96  ARG A NH1 1 
ATOM   735  N NH2 . ARG A 1 96  ? 99.034  62.612  129.169 1.00 30.00 ? 96  ARG A NH2 1 
ATOM   736  N N   . ASP A 1 97  ? 104.125 60.865  133.946 1.00 30.00 ? 97  ASP A N   1 
ATOM   737  C CA  . ASP A 1 97  ? 105.461 61.294  133.470 1.00 30.00 ? 97  ASP A CA  1 
ATOM   738  C C   . ASP A 1 97  ? 105.268 61.566  131.980 1.00 30.00 ? 97  ASP A C   1 
ATOM   739  O O   . ASP A 1 97  ? 104.896 60.615  131.264 1.00 30.00 ? 97  ASP A O   1 
ATOM   740  C CB  . ASP A 1 97  ? 106.527 60.241  133.755 1.00 30.00 ? 97  ASP A CB  1 
ATOM   741  C CG  . ASP A 1 97  ? 107.917 60.583  133.246 1.00 30.00 ? 97  ASP A CG  1 
ATOM   742  O OD1 . ASP A 1 97  ? 108.081 61.667  132.659 1.00 30.00 ? 97  ASP A OD1 1 
ATOM   743  O OD2 . ASP A 1 97  ? 108.826 59.754  133.439 1.00 30.00 ? 97  ASP A OD2 1 
ATOM   744  N N   . PRO A 1 98  ? 105.486 62.791  131.465 1.00 30.00 ? 98  PRO A N   1 
ATOM   745  C CA  . PRO A 1 98  ? 105.183 63.079  130.068 1.00 30.00 ? 98  PRO A CA  1 
ATOM   746  C C   . PRO A 1 98  ? 105.847 62.086  129.113 1.00 30.00 ? 98  PRO A C   1 
ATOM   747  O O   . PRO A 1 98  ? 107.017 61.805  129.299 1.00 30.00 ? 98  PRO A O   1 
ATOM   748  C CB  . PRO A 1 98  ? 105.770 64.472  129.831 1.00 30.00 ? 98  PRO A CB  1 
ATOM   749  C CG  . PRO A 1 98  ? 106.660 64.730  131.026 1.00 30.00 ? 98  PRO A CG  1 
ATOM   750  C CD  . PRO A 1 98  ? 106.019 63.957  132.156 1.00 30.00 ? 98  PRO A CD  1 
ATOM   751  N N   . ARG A 1 99  ? 105.095 61.591  128.131 1.00 30.00 ? 99  ARG A N   1 
ATOM   752  C CA  . ARG A 1 99  ? 105.600 60.622  127.127 1.00 30.00 ? 99  ARG A CA  1 
ATOM   753  C C   . ARG A 1 99  ? 105.612 61.310  125.767 1.00 30.00 ? 99  ARG A C   1 
ATOM   754  O O   . ARG A 1 99  ? 105.288 62.505  125.712 1.00 30.00 ? 99  ARG A O   1 
ATOM   755  C CB  . ARG A 1 99  ? 104.717 59.376  127.073 1.00 30.00 ? 99  ARG A CB  1 
ATOM   756  C CG  . ARG A 1 99  ? 104.500 58.699  128.418 1.00 30.00 ? 99  ARG A CG  1 
ATOM   757  C CD  . ARG A 1 99  ? 105.790 58.341  129.131 1.00 30.00 ? 99  ARG A CD  1 
ATOM   758  N NE  . ARG A 1 99  ? 106.643 57.458  128.349 1.00 30.00 ? 99  ARG A NE  1 
ATOM   759  C CZ  . ARG A 1 99  ? 107.832 57.010  128.735 1.00 30.00 ? 99  ARG A CZ  1 
ATOM   760  N NH1 . ARG A 1 99  ? 108.508 56.193  127.950 1.00 30.00 ? 99  ARG A NH1 1 
ATOM   761  N NH2 . ARG A 1 99  ? 108.349 57.370  129.898 1.00 30.00 ? 99  ARG A NH2 1 
ATOM   762  N N   . GLY A 1 100 ? 105.990 60.596  124.716 1.00 30.00 ? 100 GLY A N   1 
ATOM   763  C CA  . GLY A 1 100 ? 106.115 61.193  123.380 1.00 30.00 ? 100 GLY A CA  1 
ATOM   764  C C   . GLY A 1 100 ? 104.831 61.517  122.686 1.00 30.00 ? 100 GLY A C   1 
ATOM   765  O O   . GLY A 1 100 ? 104.828 62.456  121.899 1.00 30.00 ? 100 GLY A O   1 
ATOM   766  N N   . SER A 1 101 ? 103.813 60.701  122.869 1.00 30.00 ? 101 SER A N   1 
ATOM   767  C CA  . SER A 1 101 ? 102.503 61.050  122.302 1.00 30.00 ? 101 SER A CA  1 
ATOM   768  C C   . SER A 1 101 ? 102.102 62.348  122.996 1.00 30.00 ? 101 SER A C   1 
ATOM   769  O O   . SER A 1 101 ? 101.684 63.235  122.298 1.00 30.00 ? 101 SER A O   1 
ATOM   770  C CB  . SER A 1 101 ? 101.532 59.961  122.504 1.00 30.00 ? 101 SER A CB  1 
ATOM   771  O OG  . SER A 1 101 ? 102.095 58.710  122.141 1.00 30.00 ? 101 SER A OG  1 
ATOM   772  N N   . ASP A 1 102 ? 102.376 62.489  124.294 1.00 30.00 ? 102 ASP A N   1 
ATOM   773  C CA  . ASP A 1 102 ? 101.970 63.674  125.096 1.00 30.00 ? 102 ASP A CA  1 
ATOM   774  C C   . ASP A 1 102 ? 102.664 64.967  124.649 1.00 30.00 ? 102 ASP A C   1 
ATOM   775  O O   . ASP A 1 102 ? 101.960 65.993  124.577 1.00 30.00 ? 102 ASP A O   1 
ATOM   776  C CB  . ASP A 1 102 ? 102.292 63.442  126.569 1.00 30.00 ? 102 ASP A CB  1 
ATOM   777  C CG  . ASP A 1 102 ? 101.692 62.175  127.153 1.00 30.00 ? 102 ASP A CG  1 
ATOM   778  O OD1 . ASP A 1 102 ? 100.993 61.457  126.416 1.00 30.00 ? 102 ASP A OD1 1 
ATOM   779  O OD2 . ASP A 1 102 ? 101.941 61.913  128.343 1.00 30.00 ? 102 ASP A OD2 1 
ATOM   780  N N   . ILE A 1 103 ? 103.972 64.944  124.364 1.00 30.00 ? 103 ILE A N   1 
ATOM   781  C CA  . ILE A 1 103 ? 104.754 66.170  124.002 1.00 30.00 ? 103 ILE A CA  1 
ATOM   782  C C   . ILE A 1 103 ? 104.455 66.497  122.542 1.00 30.00 ? 103 ILE A C   1 
ATOM   783  O O   . ILE A 1 103 ? 104.192 67.679  122.251 1.00 30.00 ? 103 ILE A O   1 
ATOM   784  C CB  . ILE A 1 103 ? 106.259 65.949  124.236 1.00 30.00 ? 103 ILE A CB  1 
ATOM   785  C CG1 . ILE A 1 103 ? 106.563 65.669  125.709 1.00 30.00 ? 103 ILE A CG1 1 
ATOM   786  C CG2 . ILE A 1 103 ? 107.066 67.123  123.708 1.00 30.00 ? 103 ILE A CG2 1 
ATOM   787  C CD1 . ILE A 1 103 ? 107.976 65.213  125.970 1.00 30.00 ? 103 ILE A CD1 1 
ATOM   788  N N   . ALA A 1 104 ? 104.505 65.499  121.663 1.00 30.00 ? 104 ALA A N   1 
ATOM   789  C CA  . ALA A 1 104 ? 104.128 65.648  120.241 1.00 30.00 ? 104 ALA A CA  1 
ATOM   790  C C   . ALA A 1 104 ? 102.772 66.333  120.213 1.00 30.00 ? 104 ALA A C   1 
ATOM   791  O O   . ALA A 1 104 ? 102.544 67.162  119.312 1.00 30.00 ? 104 ALA A O   1 
ATOM   792  C CB  . ALA A 1 104 ? 104.048 64.317  119.564 1.00 30.00 ? 104 ALA A CB  1 
ATOM   793  N N   . GLY A 1 105 ? 101.958 66.186  121.270 1.00 30.00 ? 105 GLY A N   1 
ATOM   794  C CA  . GLY A 1 105 ? 100.711 66.970  121.426 1.00 30.00 ? 105 GLY A CA  1 
ATOM   795  C C   . GLY A 1 105 ? 99.447  66.216  121.072 1.00 30.00 ? 105 GLY A C   1 
ATOM   796  O O   . GLY A 1 105 ? 98.413  66.891  120.901 1.00 30.00 ? 105 GLY A O   1 
ATOM   797  N N   . THR A 1 106 ? 99.471  64.886  121.053 1.00 30.00 ? 106 THR A N   1 
ATOM   798  C CA  . THR A 1 106 ? 98.314  64.072  120.606 1.00 30.00 ? 106 THR A CA  1 
ATOM   799  C C   . THR A 1 106 ? 97.545  63.485  121.784 1.00 30.00 ? 106 THR A C   1 
ATOM   800  O O   . THR A 1 106 ? 96.449  63.992  122.075 1.00 30.00 ? 106 THR A O   1 
ATOM   801  C CB  . THR A 1 106 ? 98.815  62.933  119.718 1.00 30.00 ? 106 THR A CB  1 
ATOM   802  O OG1 . THR A 1 106 ? 99.331  63.516  118.522 1.00 30.00 ? 106 THR A OG1 1 
ATOM   803  C CG2 . THR A 1 106 ? 97.741  61.925  119.375 1.00 30.00 ? 106 THR A CG2 1 
ATOM   804  N N   . THR A 1 107 ? 98.106  62.486  122.455 1.00 30.00 ? 107 THR A N   1 
ATOM   805  C CA  . THR A 1 107 ? 97.429  61.759  123.554 1.00 30.00 ? 107 THR A CA  1 
ATOM   806  C C   . THR A 1 107 ? 97.029  62.704  124.680 1.00 30.00 ? 107 THR A C   1 
ATOM   807  O O   . THR A 1 107 ? 95.936  62.502  125.245 1.00 30.00 ? 107 THR A O   1 
ATOM   808  C CB  . THR A 1 107 ? 98.400  60.718  124.104 1.00 30.00 ? 107 THR A CB  1 
ATOM   809  O OG1 . THR A 1 107 ? 98.729  59.843  123.025 1.00 30.00 ? 107 THR A OG1 1 
ATOM   810  C CG2 . THR A 1 107 ? 97.844  59.927  125.266 1.00 30.00 ? 107 THR A CG2 1 
ATOM   811  N N   . SER A 1 108 ? 97.862  63.692  124.991 1.00 30.00 ? 108 SER A N   1 
ATOM   812  C CA  . SER A 1 108 ? 97.641  64.595  126.145 1.00 30.00 ? 108 SER A CA  1 
ATOM   813  C C   . SER A 1 108 ? 96.681  65.740  125.840 1.00 30.00 ? 108 SER A C   1 
ATOM   814  O O   . SER A 1 108 ? 96.397  65.971  124.649 1.00 30.00 ? 108 SER A O   1 
ATOM   815  C CB  . SER A 1 108 ? 98.941  65.162  126.572 1.00 30.00 ? 108 SER A CB  1 
ATOM   816  O OG  . SER A 1 108 ? 98.775  66.034  127.676 1.00 30.00 ? 108 SER A OG  1 
ATOM   817  N N   . THR A 1 109 ? 96.223  66.435  126.882 1.00 30.00 ? 109 THR A N   1 
ATOM   818  C CA  . THR A 1 109 ? 95.348  67.622  126.752 1.00 30.00 ? 109 THR A CA  1 
ATOM   819  C C   . THR A 1 109 ? 96.250  68.852  126.714 1.00 30.00 ? 109 THR A C   1 
ATOM   820  O O   . THR A 1 109 ? 97.460  68.654  126.570 1.00 30.00 ? 109 THR A O   1 
ATOM   821  C CB  . THR A 1 109 ? 94.407  67.737  127.949 1.00 30.00 ? 109 THR A CB  1 
ATOM   822  O OG1 . THR A 1 109 ? 95.194  68.202  129.045 1.00 30.00 ? 109 THR A OG1 1 
ATOM   823  C CG2 . THR A 1 109 ? 93.727  66.434  128.302 1.00 30.00 ? 109 THR A CG2 1 
ATOM   824  N N   . VAL A 1 110 ? 95.700  70.058  126.860 1.00 30.00 ? 110 VAL A N   1 
ATOM   825  C CA  . VAL A 1 110 ? 96.513  71.307  126.916 1.00 30.00 ? 110 VAL A CA  1 
ATOM   826  C C   . VAL A 1 110 ? 96.779  71.657  128.379 1.00 30.00 ? 110 VAL A C   1 
ATOM   827  O O   . VAL A 1 110 ? 97.805  72.285  128.632 1.00 30.00 ? 110 VAL A O   1 
ATOM   828  C CB  . VAL A 1 110 ? 95.797  72.470  126.213 1.00 30.00 ? 110 VAL A CB  1 
ATOM   829  C CG1 . VAL A 1 110 ? 94.590  72.956  126.995 1.00 30.00 ? 110 VAL A CG1 1 
ATOM   830  C CG2 . VAL A 1 110 ? 96.735  73.628  125.940 1.00 30.00 ? 110 VAL A CG2 1 
ATOM   831  N N   . GLU A 1 111 ? 95.905  71.251  129.300 1.00 30.00 ? 111 GLU A N   1 
ATOM   832  C CA  . GLU A 1 111 ? 96.024  71.618  130.736 1.00 30.00 ? 111 GLU A CA  1 
ATOM   833  C C   . GLU A 1 111 ? 97.096  70.764  131.407 1.00 30.00 ? 111 GLU A C   1 
ATOM   834  O O   . GLU A 1 111 ? 97.608  71.194  132.455 1.00 30.00 ? 111 GLU A O   1 
ATOM   835  C CB  . GLU A 1 111 ? 94.700  71.401  131.459 1.00 30.00 ? 111 GLU A CB  1 
ATOM   836  C CG  . GLU A 1 111 ? 93.554  72.226  130.904 1.00 30.00 ? 111 GLU A CG  1 
ATOM   837  C CD  . GLU A 1 111 ? 92.826  71.638  129.708 1.00 30.00 ? 111 GLU A CD  1 
ATOM   838  O OE1 . GLU A 1 111 ? 93.184  70.527  129.280 1.00 30.00 ? 111 GLU A OE1 1 
ATOM   839  O OE2 . GLU A 1 111 ? 91.900  72.300  129.204 1.00 30.00 ? 111 GLU A OE2 1 
ATOM   840  N N   . GLU A 1 112 ? 97.403  69.600  130.839 1.00 30.00 ? 112 GLU A N   1 
ATOM   841  C CA  . GLU A 1 112 ? 98.428  68.676  131.384 1.00 30.00 ? 112 GLU A CA  1 
ATOM   842  C C   . GLU A 1 112 ? 99.783  69.103  130.832 1.00 30.00 ? 112 GLU A C   1 
ATOM   843  O O   . GLU A 1 112 ? 100.783 68.867  131.518 1.00 30.00 ? 112 GLU A O   1 
ATOM   844  C CB  . GLU A 1 112 ? 98.095  67.260  130.939 1.00 30.00 ? 112 GLU A CB  1 
ATOM   845  C CG  . GLU A 1 112 ? 96.785  66.738  131.488 1.00 30.00 ? 112 GLU A CG  1 
ATOM   846  C CD  . GLU A 1 112 ? 96.272  65.483  130.805 1.00 30.00 ? 112 GLU A CD  1 
ATOM   847  O OE1 . GLU A 1 112 ? 96.927  65.014  129.860 1.00 30.00 ? 112 GLU A OE1 1 
ATOM   848  O OE2 . GLU A 1 112 ? 95.217  64.978  131.225 1.00 30.00 ? 112 GLU A OE2 1 
ATOM   849  N N   . GLN A 1 113 ? 99.814  69.662  129.623 1.00 30.00 ? 113 GLN A N   1 
ATOM   850  C CA  . GLN A 1 113 ? 101.047 70.179  128.980 1.00 30.00 ? 113 GLN A CA  1 
ATOM   851  C C   . GLN A 1 113 ? 101.514 71.395  129.781 1.00 30.00 ? 113 GLN A C   1 
ATOM   852  O O   . GLN A 1 113 ? 102.721 71.467  130.092 1.00 30.00 ? 113 GLN A O   1 
ATOM   853  C CB  . GLN A 1 113 ? 100.724 70.506  127.524 1.00 30.00 ? 113 GLN A CB  1 
ATOM   854  C CG  . GLN A 1 113 ? 100.401 69.279  126.688 1.00 30.00 ? 113 GLN A CG  1 
ATOM   855  C CD  . GLN A 1 113 ? 99.798  69.637  125.355 1.00 30.00 ? 113 GLN A CD  1 
ATOM   856  O OE1 . GLN A 1 113 ? 99.595  70.803  125.037 1.00 30.00 ? 113 GLN A OE1 1 
ATOM   857  N NE2 . GLN A 1 113 ? 99.489  68.626  124.565 1.00 30.00 ? 113 GLN A NE2 1 
ATOM   858  N N   . ILE A 1 114 ? 100.588 72.280  130.153 1.00 30.00 ? 114 ILE A N   1 
ATOM   859  C CA  . ILE A 1 114 ? 100.895 73.495  130.963 1.00 30.00 ? 114 ILE A CA  1 
ATOM   860  C C   . ILE A 1 114 ? 101.322 73.055  132.362 1.00 30.00 ? 114 ILE A C   1 
ATOM   861  O O   . ILE A 1 114 ? 102.273 73.643  132.900 1.00 30.00 ? 114 ILE A O   1 
ATOM   862  C CB  . ILE A 1 114 ? 99.661  74.414  131.010 1.00 30.00 ? 114 ILE A CB  1 
ATOM   863  C CG1 . ILE A 1 114 ? 99.279  74.888  129.606 1.00 30.00 ? 114 ILE A CG1 1 
ATOM   864  C CG2 . ILE A 1 114 ? 99.886  75.583  131.953 1.00 30.00 ? 114 ILE A CG2 1 
ATOM   865  C CD1 . ILE A 1 114 ? 98.040  75.742  129.545 1.00 30.00 ? 114 ILE A CD1 1 
ATOM   866  N N   . GLN A 1 115 ? 100.548 72.157  132.976 1.00 30.00 ? 115 GLN A N   1 
ATOM   867  C CA  . GLN A 1 115 ? 100.851 71.638  134.332 1.00 30.00 ? 115 GLN A CA  1 
ATOM   868  C C   . GLN A 1 115 ? 102.322 71.239  134.393 1.00 30.00 ? 115 GLN A C   1 
ATOM   869  O O   . GLN A 1 115 ? 103.031 71.784  135.250 1.00 30.00 ? 115 GLN A O   1 
ATOM   870  C CB  . GLN A 1 115 ? 99.949  70.452  134.648 1.00 30.00 ? 115 GLN A CB  1 
ATOM   871  C CG  . GLN A 1 115 ? 100.335 69.719  135.921 1.00 30.00 ? 115 GLN A CG  1 
ATOM   872  C CD  . GLN A 1 115 ? 99.276  68.740  136.362 1.00 30.00 ? 115 GLN A CD  1 
ATOM   873  O OE1 . GLN A 1 115 ? 98.214  68.622  135.755 1.00 30.00 ? 115 GLN A OE1 1 
ATOM   874  N NE2 . GLN A 1 115 ? 99.559  68.034  137.444 1.00 30.00 ? 115 GLN A NE2 1 
ATOM   875  N N   . TRP A 1 116 ? 102.757 70.342  133.507 1.00 30.00 ? 116 TRP A N   1 
ATOM   876  C CA  . TRP A 1 116 ? 104.168 69.886  133.472 1.00 30.00 ? 116 TRP A CA  1 
ATOM   877  C C   . TRP A 1 116 ? 105.062 71.107  133.293 1.00 30.00 ? 116 TRP A C   1 
ATOM   878  O O   . TRP A 1 116 ? 106.003 71.240  134.080 1.00 30.00 ? 116 TRP A O   1 
ATOM   879  C CB  . TRP A 1 116 ? 104.426 68.912  132.322 1.00 30.00 ? 116 TRP A CB  1 
ATOM   880  C CG  . TRP A 1 116 ? 103.734 67.589  132.392 1.00 30.00 ? 116 TRP A CG  1 
ATOM   881  C CD1 . TRP A 1 116 ? 103.738 66.715  133.435 1.00 30.00 ? 116 TRP A CD1 1 
ATOM   882  C CD2 . TRP A 1 116 ? 103.067 66.915  131.312 1.00 30.00 ? 116 TRP A CD2 1 
ATOM   883  N NE1 . TRP A 1 116 ? 103.052 65.580  133.107 1.00 30.00 ? 116 TRP A NE1 1 
ATOM   884  C CE2 . TRP A 1 116 ? 102.631 65.671  131.808 1.00 30.00 ? 116 TRP A CE2 1 
ATOM   885  C CE3 . TRP A 1 116 ? 102.767 67.255  129.990 1.00 30.00 ? 116 TRP A CE3 1 
ATOM   886  C CZ2 . TRP A 1 116 ? 101.906 64.773  131.028 1.00 30.00 ? 116 TRP A CZ2 1 
ATOM   887  C CZ3 . TRP A 1 116 ? 102.052 66.367  129.219 1.00 30.00 ? 116 TRP A CZ3 1 
ATOM   888  C CH2 . TRP A 1 116 ? 101.629 65.143  129.733 1.00 30.00 ? 116 TRP A CH2 1 
ATOM   889  N N   . MET A 1 117 ? 104.715 72.007  132.373 1.00 30.00 ? 117 MET A N   1 
ATOM   890  C CA  . MET A 1 117 ? 105.549 73.189  132.028 1.00 30.00 ? 117 MET A CA  1 
ATOM   891  C C   . MET A 1 117 ? 105.801 74.056  133.259 1.00 30.00 ? 117 MET A C   1 
ATOM   892  O O   . MET A 1 117 ? 106.920 74.595  133.360 1.00 30.00 ? 117 MET A O   1 
ATOM   893  C CB  . MET A 1 117 ? 104.843 74.016  130.953 1.00 30.00 ? 117 MET A CB  1 
ATOM   894  C CG  . MET A 1 117 ? 105.159 73.580  129.545 1.00 30.00 ? 117 MET A CG  1 
ATOM   895  S SD  . MET A 1 117 ? 103.997 74.260  128.337 1.00 30.00 ? 117 MET A SD  1 
ATOM   896  C CE  . MET A 1 117 ? 104.771 75.833  127.976 1.00 30.00 ? 117 MET A CE  1 
ATOM   897  N N   . TYR A 1 118 ? 104.819 74.194  134.143 1.00 30.00 ? 118 TYR A N   1 
ATOM   898  C CA  . TYR A 1 118 ? 104.921 75.051  135.350 1.00 30.00 ? 118 TYR A CA  1 
ATOM   899  C C   . TYR A 1 118 ? 104.818 74.160  136.587 1.00 30.00 ? 118 TYR A C   1 
ATOM   900  O O   . TYR A 1 118 ? 104.432 74.664  137.659 1.00 30.00 ? 118 TYR A O   1 
ATOM   901  C CB  . TYR A 1 118 ? 103.858 76.135  135.218 1.00 30.00 ? 118 TYR A CB  1 
ATOM   902  C CG  . TYR A 1 118 ? 104.035 76.942  133.962 1.00 30.00 ? 118 TYR A CG  1 
ATOM   903  C CD1 . TYR A 1 118 ? 105.126 77.774  133.800 1.00 30.00 ? 118 TYR A CD1 1 
ATOM   904  C CD2 . TYR A 1 118 ? 103.185 76.778  132.887 1.00 30.00 ? 118 TYR A CD2 1 
ATOM   905  C CE1 . TYR A 1 118 ? 105.318 78.495  132.635 1.00 30.00 ? 118 TYR A CE1 1 
ATOM   906  C CE2 . TYR A 1 118 ? 103.371 77.476  131.709 1.00 30.00 ? 118 TYR A CE2 1 
ATOM   907  C CZ  . TYR A 1 118 ? 104.436 78.343  131.583 1.00 30.00 ? 118 TYR A CZ  1 
ATOM   908  O OH  . TYR A 1 118 ? 104.608 79.036  130.413 1.00 30.00 ? 118 TYR A OH  1 
ATOM   909  N N   . ARG A 1 119 ? 105.161 72.879  136.441 1.00 30.00 ? 119 ARG A N   1 
ATOM   910  C CA  . ARG A 1 119 ? 105.137 71.920  137.572 1.00 30.00 ? 119 ARG A CA  1 
ATOM   911  C C   . ARG A 1 119 ? 106.287 72.284  138.507 1.00 30.00 ? 119 ARG A C   1 
ATOM   912  O O   . ARG A 1 119 ? 107.420 72.416  138.014 1.00 30.00 ? 119 ARG A O   1 
ATOM   913  C CB  . ARG A 1 119 ? 105.295 70.488  137.066 1.00 30.00 ? 119 ARG A CB  1 
ATOM   914  C CG  . ARG A 1 119 ? 105.498 69.444  138.153 1.00 30.00 ? 119 ARG A CG  1 
ATOM   915  C CD  . ARG A 1 119 ? 105.351 68.060  137.557 1.00 30.00 ? 119 ARG A CD  1 
ATOM   916  N NE  . ARG A 1 119 ? 106.241 67.854  136.424 1.00 30.00 ? 119 ARG A NE  1 
ATOM   917  C CZ  . ARG A 1 119 ? 106.273 66.762  135.671 1.00 30.00 ? 119 ARG A CZ  1 
ATOM   918  N NH1 . ARG A 1 119 ? 105.793 65.616  136.120 1.00 30.00 ? 119 ARG A NH1 1 
ATOM   919  N NH2 . ARG A 1 119 ? 106.786 66.823  134.455 1.00 30.00 ? 119 ARG A NH2 1 
ATOM   920  N N   . PRO A 1 120 ? 106.055 72.449  139.823 1.00 30.00 ? 120 PRO A N   1 
ATOM   921  C CA  . PRO A 1 120 ? 107.115 72.872  140.725 1.00 30.00 ? 120 PRO A CA  1 
ATOM   922  C C   . PRO A 1 120 ? 108.241 71.837  140.762 1.00 30.00 ? 120 PRO A C   1 
ATOM   923  O O   . PRO A 1 120 ? 109.381 72.231  140.685 1.00 30.00 ? 120 PRO A O   1 
ATOM   924  C CB  . PRO A 1 120 ? 106.435 72.944  142.097 1.00 30.00 ? 120 PRO A CB  1 
ATOM   925  C CG  . PRO A 1 120 ? 104.961 73.039  141.785 1.00 30.00 ? 120 PRO A CG  1 
ATOM   926  C CD  . PRO A 1 120 ? 104.788 72.232  140.519 1.00 30.00 ? 120 PRO A CD  1 
ATOM   927  N N   . GLN A 1 121 ? 107.901 70.554  140.858 1.00 30.00 ? 121 GLN A N   1 
ATOM   928  C CA  . GLN A 1 121 ? 108.906 69.465  140.953 1.00 30.00 ? 121 GLN A CA  1 
ATOM   929  C C   . GLN A 1 121 ? 109.925 69.584  139.821 1.00 30.00 ? 121 GLN A C   1 
ATOM   930  O O   . GLN A 1 121 ? 111.120 69.701  140.130 1.00 30.00 ? 121 GLN A O   1 
ATOM   931  C CB  . GLN A 1 121 ? 108.207 68.110  140.878 1.00 30.00 ? 121 GLN A CB  1 
ATOM   932  C CG  . GLN A 1 121 ? 109.165 66.930  140.929 1.00 30.00 ? 121 GLN A CG  1 
ATOM   933  C CD  . GLN A 1 121 ? 110.064 66.985  142.138 1.00 30.00 ? 121 GLN A CD  1 
ATOM   934  O OE1 . GLN A 1 121 ? 111.285 67.058  142.024 1.00 30.00 ? 121 GLN A OE1 1 
ATOM   935  N NE2 . GLN A 1 121 ? 109.460 66.965  143.315 1.00 30.00 ? 121 GLN A NE2 1 
ATOM   936  N N   . ASN A 1 122 ? 109.480 69.547  138.570 1.00 30.00 ? 122 ASN A N   1 
ATOM   937  C CA  . ASN A 1 122 ? 110.361 69.589  137.376 1.00 30.00 ? 122 ASN A CA  1 
ATOM   938  C C   . ASN A 1 122 ? 109.634 70.316  136.242 1.00 30.00 ? 122 ASN A C   1 
ATOM   939  O O   . ASN A 1 122 ? 109.023 69.638  135.410 1.00 30.00 ? 122 ASN A O   1 
ATOM   940  C CB  . ASN A 1 122 ? 110.825 68.183  136.997 1.00 30.00 ? 122 ASN A CB  1 
ATOM   941  C CG  . ASN A 1 122 ? 109.691 67.203  136.792 1.00 30.00 ? 122 ASN A CG  1 
ATOM   942  O OD1 . ASN A 1 122 ? 108.890 66.971  137.694 1.00 30.00 ? 122 ASN A OD1 1 
ATOM   943  N ND2 . ASN A 1 122 ? 109.617 66.628  135.604 1.00 30.00 ? 122 ASN A ND2 1 
ATOM   944  N N   . PRO A 1 123 ? 109.667 71.658  136.157 1.00 30.00 ? 123 PRO A N   1 
ATOM   945  C CA  . PRO A 1 123 ? 108.988 72.313  135.060 1.00 30.00 ? 123 PRO A CA  1 
ATOM   946  C C   . PRO A 1 123 ? 109.625 71.757  133.782 1.00 30.00 ? 123 PRO A C   1 
ATOM   947  O O   . PRO A 1 123 ? 110.832 71.862  133.661 1.00 30.00 ? 123 PRO A O   1 
ATOM   948  C CB  . PRO A 1 123 ? 109.252 73.803  135.303 1.00 30.00 ? 123 PRO A CB  1 
ATOM   949  C CG  . PRO A 1 123 ? 110.458 73.838  136.220 1.00 30.00 ? 123 PRO A CG  1 
ATOM   950  C CD  . PRO A 1 123 ? 110.372 72.574  137.047 1.00 30.00 ? 123 PRO A CD  1 
ATOM   951  N N   . VAL A 1 124 ? 108.824 71.196  132.873 1.00 30.00 ? 124 VAL A N   1 
ATOM   952  C CA  . VAL A 1 124 ? 109.330 70.572  131.616 1.00 30.00 ? 124 VAL A CA  1 
ATOM   953  C C   . VAL A 1 124 ? 108.881 71.440  130.444 1.00 30.00 ? 124 VAL A C   1 
ATOM   954  O O   . VAL A 1 124 ? 107.691 71.745  130.382 1.00 30.00 ? 124 VAL A O   1 
ATOM   955  C CB  . VAL A 1 124 ? 108.819 69.132  131.438 1.00 30.00 ? 124 VAL A CB  1 
ATOM   956  C CG1 . VAL A 1 124 ? 109.107 68.590  130.048 1.00 30.00 ? 124 VAL A CG1 1 
ATOM   957  C CG2 . VAL A 1 124 ? 109.361 68.191  132.495 1.00 30.00 ? 124 VAL A CG2 1 
ATOM   958  N N   . PRO A 1 125 ? 109.773 71.808  129.504 1.00 30.00 ? 125 PRO A N   1 
ATOM   959  C CA  . PRO A 1 125 ? 109.412 72.665  128.386 1.00 30.00 ? 125 PRO A CA  1 
ATOM   960  C C   . PRO A 1 125 ? 108.842 71.811  127.253 1.00 30.00 ? 125 PRO A C   1 
ATOM   961  O O   . PRO A 1 125 ? 109.463 71.718  126.214 1.00 30.00 ? 125 PRO A O   1 
ATOM   962  C CB  . PRO A 1 125 ? 110.763 73.276  128.027 1.00 30.00 ? 125 PRO A CB  1 
ATOM   963  C CG  . PRO A 1 125 ? 111.731 72.144  128.248 1.00 30.00 ? 125 PRO A CG  1 
ATOM   964  C CD  . PRO A 1 125 ? 111.183 71.418  129.457 1.00 30.00 ? 125 PRO A CD  1 
ATOM   965  N N   . VAL A 1 126 ? 107.661 71.237  127.463 1.00 30.00 ? 126 VAL A N   1 
ATOM   966  C CA  . VAL A 1 126 ? 107.032 70.342  126.457 1.00 30.00 ? 126 VAL A CA  1 
ATOM   967  C C   . VAL A 1 126 ? 106.867 71.166  125.186 1.00 30.00 ? 126 VAL A C   1 
ATOM   968  O O   . VAL A 1 126 ? 107.083 70.620  124.102 1.00 30.00 ? 126 VAL A O   1 
ATOM   969  C CB  . VAL A 1 126 ? 105.704 69.745  126.950 1.00 30.00 ? 126 VAL A CB  1 
ATOM   970  C CG1 . VAL A 1 126 ? 105.902 68.880  128.182 1.00 30.00 ? 126 VAL A CG1 1 
ATOM   971  C CG2 . VAL A 1 126 ? 104.651 70.806  127.213 1.00 30.00 ? 126 VAL A CG2 1 
ATOM   972  N N   . GLY A 1 127 ? 106.545 72.444  125.313 1.00 30.00 ? 127 GLY A N   1 
ATOM   973  C CA  . GLY A 1 127 ? 106.339 73.311  124.147 1.00 30.00 ? 127 GLY A CA  1 
ATOM   974  C C   . GLY A 1 127 ? 107.613 73.470  123.357 1.00 30.00 ? 127 GLY A C   1 
ATOM   975  O O   . GLY A 1 127 ? 107.557 73.309  122.133 1.00 30.00 ? 127 GLY A O   1 
ATOM   976  N N   . ASN A 1 128 ? 108.734 73.722  124.024 1.00 30.00 ? 128 ASN A N   1 
ATOM   977  C CA  . ASN A 1 128 ? 110.035 73.962  123.352 1.00 30.00 ? 128 ASN A CA  1 
ATOM   978  C C   . ASN A 1 128 ? 110.565 72.671  122.728 1.00 30.00 ? 128 ASN A C   1 
ATOM   979  O O   . ASN A 1 128 ? 111.115 72.744  121.614 1.00 30.00 ? 128 ASN A O   1 
ATOM   980  C CB  . ASN A 1 128 ? 111.048 74.495  124.355 1.00 30.00 ? 128 ASN A CB  1 
ATOM   981  C CG  . ASN A 1 128 ? 110.608 75.773  125.031 1.00 30.00 ? 128 ASN A CG  1 
ATOM   982  O OD1 . ASN A 1 128 ? 109.555 76.322  124.719 1.00 30.00 ? 128 ASN A OD1 1 
ATOM   983  N ND2 . ASN A 1 128 ? 111.419 76.263  125.951 1.00 30.00 ? 128 ASN A ND2 1 
ATOM   984  N N   . ILE A 1 129 ? 110.423 71.540  123.417 1.00 30.00 ? 129 ILE A N   1 
ATOM   985  C CA  . ILE A 1 129 ? 110.976 70.234  122.955 1.00 30.00 ? 129 ILE A CA  1 
ATOM   986  C C   . ILE A 1 129 ? 110.295 69.807  121.656 1.00 30.00 ? 129 ILE A C   1 
ATOM   987  O O   . ILE A 1 129 ? 111.014 69.428  120.712 1.00 30.00 ? 129 ILE A O   1 
ATOM   988  C CB  . ILE A 1 129 ? 110.759 69.187  124.059 1.00 30.00 ? 129 ILE A CB  1 
ATOM   989  C CG1 . ILE A 1 129 ? 111.537 69.529  125.329 1.00 30.00 ? 129 ILE A CG1 1 
ATOM   990  C CG2 . ILE A 1 129 ? 111.100 67.794  123.563 1.00 30.00 ? 129 ILE A CG2 1 
ATOM   991  C CD1 . ILE A 1 129 ? 111.016 68.838  126.560 1.00 30.00 ? 129 ILE A CD1 1 
ATOM   992  N N   . TYR A 1 130 ? 108.967 69.876  121.604 1.00 30.00 ? 130 TYR A N   1 
ATOM   993  C CA  . TYR A 1 130 ? 108.188 69.481  120.405 1.00 30.00 ? 130 TYR A CA  1 
ATOM   994  C C   . TYR A 1 130 ? 108.547 70.426  119.266 1.00 30.00 ? 130 TYR A C   1 
ATOM   995  O O   . TYR A 1 130 ? 108.727 69.962  118.126 1.00 30.00 ? 130 TYR A O   1 
ATOM   996  C CB  . TYR A 1 130 ? 106.702 69.552  120.731 1.00 30.00 ? 130 TYR A CB  1 
ATOM   997  C CG  . TYR A 1 130 ? 105.786 69.389  119.552 1.00 30.00 ? 130 TYR A CG  1 
ATOM   998  C CD1 . TYR A 1 130 ? 105.862 68.271  118.747 1.00 30.00 ? 130 TYR A CD1 1 
ATOM   999  C CD2 . TYR A 1 130 ? 104.821 70.335  119.266 1.00 30.00 ? 130 TYR A CD2 1 
ATOM   1000 C CE1 . TYR A 1 130 ? 105.018 68.105  117.666 1.00 30.00 ? 130 TYR A CE1 1 
ATOM   1001 C CE2 . TYR A 1 130 ? 103.967 70.183  118.191 1.00 30.00 ? 130 TYR A CE2 1 
ATOM   1002 C CZ  . TYR A 1 130 ? 104.066 69.063  117.387 1.00 30.00 ? 130 TYR A CZ  1 
ATOM   1003 O OH  . TYR A 1 130 ? 103.241 68.884  116.309 1.00 30.00 ? 130 TYR A OH  1 
ATOM   1004 N N   . ARG A 1 131 ? 108.680 71.710  119.580 1.00 30.00 ? 131 ARG A N   1 
ATOM   1005 C CA  . ARG A 1 131 ? 109.018 72.753  118.584 1.00 30.00 ? 131 ARG A CA  1 
ATOM   1006 C C   . ARG A 1 131 ? 110.391 72.463  117.980 1.00 30.00 ? 131 ARG A C   1 
ATOM   1007 O O   . ARG A 1 131 ? 110.550 72.662  116.765 1.00 30.00 ? 131 ARG A O   1 
ATOM   1008 C CB  . ARG A 1 131 ? 108.993 74.074  119.340 1.00 30.00 ? 131 ARG A CB  1 
ATOM   1009 C CG  . ARG A 1 131 ? 109.232 75.311  118.495 1.00 30.00 ? 131 ARG A CG  1 
ATOM   1010 C CD  . ARG A 1 131 ? 109.028 76.551  119.339 1.00 30.00 ? 131 ARG A CD  1 
ATOM   1011 N NE  . ARG A 1 131 ? 109.914 76.600  120.488 1.00 30.00 ? 131 ARG A NE  1 
ATOM   1012 C CZ  . ARG A 1 131 ? 109.912 77.558  121.401 1.00 30.00 ? 131 ARG A CZ  1 
ATOM   1013 N NH1 . ARG A 1 131 ? 108.821 78.266  121.623 1.00 30.00 ? 131 ARG A NH1 1 
ATOM   1014 N NH2 . ARG A 1 131 ? 110.994 77.779  122.124 1.00 30.00 ? 131 ARG A NH2 1 
ATOM   1015 N N   . ARG A 1 132 ? 111.348 72.023  118.797 1.00 30.00 ? 132 ARG A N   1 
ATOM   1016 C CA  . ARG A 1 132 ? 112.718 71.692  118.332 1.00 30.00 ? 132 ARG A CA  1 
ATOM   1017 C C   . ARG A 1 132 ? 112.660 70.523  117.357 1.00 30.00 ? 132 ARG A C   1 
ATOM   1018 O O   . ARG A 1 132 ? 113.312 70.602  116.297 1.00 30.00 ? 132 ARG A O   1 
ATOM   1019 C CB  . ARG A 1 132 ? 113.572 71.285  119.527 1.00 30.00 ? 132 ARG A CB  1 
ATOM   1020 C CG  . ARG A 1 132 ? 114.979 70.834  119.173 1.00 30.00 ? 132 ARG A CG  1 
ATOM   1021 C CD  . ARG A 1 132 ? 115.596 70.126  120.357 1.00 30.00 ? 132 ARG A CD  1 
ATOM   1022 N NE  . ARG A 1 132 ? 115.490 70.949  121.551 1.00 30.00 ? 132 ARG A NE  1 
ATOM   1023 C CZ  . ARG A 1 132 ? 114.839 70.606  122.656 1.00 30.00 ? 132 ARG A CZ  1 
ATOM   1024 N NH1 . ARG A 1 132 ? 114.654 69.335  122.964 1.00 30.00 ? 132 ARG A NH1 1 
ATOM   1025 N NH2 . ARG A 1 132 ? 114.393 71.547  123.469 1.00 30.00 ? 132 ARG A NH2 1 
ATOM   1026 N N   . TRP A 1 133 ? 111.884 69.495  117.690 1.00 30.00 ? 133 TRP A N   1 
ATOM   1027 C CA  . TRP A 1 133 ? 111.735 68.298  116.830 1.00 30.00 ? 133 TRP A CA  1 
ATOM   1028 C C   . TRP A 1 133 ? 111.235 68.767  115.471 1.00 30.00 ? 133 TRP A C   1 
ATOM   1029 O O   . TRP A 1 133 ? 111.606 68.162  114.451 1.00 30.00 ? 133 TRP A O   1 
ATOM   1030 C CB  . TRP A 1 133 ? 110.727 67.336  117.446 1.00 30.00 ? 133 TRP A CB  1 
ATOM   1031 C CG  . TRP A 1 133 ? 111.075 66.789  118.791 1.00 30.00 ? 133 TRP A CG  1 
ATOM   1032 C CD1 . TRP A 1 133 ? 112.230 66.961  119.493 1.00 30.00 ? 133 TRP A CD1 1 
ATOM   1033 C CD2 . TRP A 1 133 ? 110.206 66.015  119.631 1.00 30.00 ? 133 TRP A CD2 1 
ATOM   1034 N NE1 . TRP A 1 133 ? 112.151 66.317  120.697 1.00 30.00 ? 133 TRP A NE1 1 
ATOM   1035 C CE2 . TRP A 1 133 ? 110.920 65.730  120.811 1.00 30.00 ? 133 TRP A CE2 1 
ATOM   1036 C CE3 . TRP A 1 133 ? 108.905 65.523  119.495 1.00 30.00 ? 133 TRP A CE3 1 
ATOM   1037 C CZ2 . TRP A 1 133 ? 110.372 64.977  121.847 1.00 30.00 ? 133 TRP A CZ2 1 
ATOM   1038 C CZ3 . TRP A 1 133 ? 108.364 64.782  120.519 1.00 30.00 ? 133 TRP A CZ3 1 
ATOM   1039 C CH2 . TRP A 1 133 ? 109.089 64.515  121.678 1.00 30.00 ? 133 TRP A CH2 1 
ATOM   1040 N N   . ILE A 1 134 ? 110.366 69.772  115.475 1.00 30.00 ? 134 ILE A N   1 
ATOM   1041 C CA  . ILE A 1 134 ? 109.767 70.307  114.224 1.00 30.00 ? 134 ILE A CA  1 
ATOM   1042 C C   . ILE A 1 134 ? 110.792 71.064  113.399 1.00 30.00 ? 134 ILE A C   1 
ATOM   1043 O O   . ILE A 1 134 ? 110.768 70.926  112.178 1.00 30.00 ? 134 ILE A O   1 
ATOM   1044 C CB  . ILE A 1 134 ? 108.577 71.226  114.554 1.00 30.00 ? 134 ILE A CB  1 
ATOM   1045 C CG1 . ILE A 1 134 ? 107.438 70.447  115.205 1.00 30.00 ? 134 ILE A CG1 1 
ATOM   1046 C CG2 . ILE A 1 134 ? 108.097 71.968  113.318 1.00 30.00 ? 134 ILE A CG2 1 
ATOM   1047 C CD1 . ILE A 1 134 ? 106.459 71.314  115.934 1.00 30.00 ? 134 ILE A CD1 1 
ATOM   1048 N N   . GLN A 1 135 ? 111.628 71.854  114.053 1.00 30.00 ? 135 GLN A N   1 
ATOM   1049 C CA  . GLN A 1 135 ? 112.638 72.660  113.336 1.00 30.00 ? 135 GLN A CA  1 
ATOM   1050 C C   . GLN A 1 135 ? 113.466 71.661  112.531 1.00 30.00 ? 135 GLN A C   1 
ATOM   1051 O O   . GLN A 1 135 ? 113.860 72.010  111.418 1.00 30.00 ? 135 GLN A O   1 
ATOM   1052 C CB  . GLN A 1 135 ? 113.402 73.502  114.348 1.00 30.00 ? 135 GLN A CB  1 
ATOM   1053 C CG  . GLN A 1 135 ? 112.552 74.628  114.917 1.00 30.00 ? 135 GLN A CG  1 
ATOM   1054 C CD  . GLN A 1 135 ? 113.231 75.396  116.021 1.00 30.00 ? 135 GLN A CD  1 
ATOM   1055 O OE1 . GLN A 1 135 ? 114.370 75.120  116.391 1.00 30.00 ? 135 GLN A OE1 1 
ATOM   1056 N NE2 . GLN A 1 135 ? 112.523 76.375  116.557 1.00 30.00 ? 135 GLN A NE2 1 
ATOM   1057 N N   . ILE A 1 136 ? 113.676 70.457  113.063 1.00 30.00 ? 136 ILE A N   1 
ATOM   1058 C CA  . ILE A 1 136 ? 114.415 69.375  112.352 1.00 30.00 ? 136 ILE A CA  1 
ATOM   1059 C C   . ILE A 1 136 ? 113.637 68.952  111.103 1.00 30.00 ? 136 ILE A C   1 
ATOM   1060 O O   . ILE A 1 136 ? 114.259 68.884  110.028 1.00 30.00 ? 136 ILE A O   1 
ATOM   1061 C CB  . ILE A 1 136 ? 114.608 68.186  113.306 1.00 30.00 ? 136 ILE A CB  1 
ATOM   1062 C CG1 . ILE A 1 136 ? 115.389 68.583  114.559 1.00 30.00 ? 136 ILE A CG1 1 
ATOM   1063 C CG2 . ILE A 1 136 ? 115.259 67.016  112.588 1.00 30.00 ? 136 ILE A CG2 1 
ATOM   1064 C CD1 . ILE A 1 136 ? 115.368 67.541  115.643 1.00 30.00 ? 136 ILE A CD1 1 
ATOM   1065 N N   . GLY A 1 137 ? 112.331 68.694  111.231 1.00 30.00 ? 137 GLY A N   1 
ATOM   1066 C CA  . GLY A 1 137 ? 111.482 68.296  110.090 1.00 30.00 ? 137 GLY A CA  1 
ATOM   1067 C C   . GLY A 1 137 ? 111.391 69.423  109.081 1.00 30.00 ? 137 GLY A C   1 
ATOM   1068 O O   . GLY A 1 137 ? 111.533 69.138  107.880 1.00 30.00 ? 137 GLY A O   1 
ATOM   1069 N N   . LEU A 1 138 ? 111.214 70.660  109.545 1.00 30.00 ? 138 LEU A N   1 
ATOM   1070 C CA  . LEU A 1 138 ? 111.137 71.863  108.680 1.00 30.00 ? 138 LEU A CA  1 
ATOM   1071 C C   . LEU A 1 138 ? 112.474 72.038  107.968 1.00 30.00 ? 138 LEU A C   1 
ATOM   1072 O O   . LEU A 1 138 ? 112.462 72.340  106.768 1.00 30.00 ? 138 LEU A O   1 
ATOM   1073 C CB  . LEU A 1 138 ? 110.874 73.076  109.572 1.00 30.00 ? 138 LEU A CB  1 
ATOM   1074 C CG  . LEU A 1 138 ? 109.432 73.340  109.986 1.00 30.00 ? 138 LEU A CG  1 
ATOM   1075 C CD1 . LEU A 1 138 ? 109.376 74.450  111.018 1.00 30.00 ? 138 LEU A CD1 1 
ATOM   1076 C CD2 . LEU A 1 138 ? 108.593 73.719  108.782 1.00 30.00 ? 138 LEU A CD2 1 
ATOM   1077 N N   . GLN A 1 139 ? 113.579 71.850  108.687 1.00 30.00 ? 139 GLN A N   1 
ATOM   1078 C CA  . GLN A 1 139 ? 114.940 72.018  108.122 1.00 30.00 ? 139 GLN A CA  1 
ATOM   1079 C C   . GLN A 1 139 ? 115.150 70.966  107.040 1.00 30.00 ? 139 GLN A C   1 
ATOM   1080 O O   . GLN A 1 139 ? 115.675 71.316  105.973 1.00 30.00 ? 139 GLN A O   1 
ATOM   1081 C CB  . GLN A 1 139 ? 115.987 71.897  109.224 1.00 30.00 ? 139 GLN A CB  1 
ATOM   1082 C CG  . GLN A 1 139 ? 116.218 73.198  109.974 1.00 30.00 ? 139 GLN A CG  1 
ATOM   1083 C CD  . GLN A 1 139 ? 117.137 73.023  111.156 1.00 30.00 ? 139 GLN A CD  1 
ATOM   1084 O OE1 . GLN A 1 139 ? 117.626 71.932  111.432 1.00 30.00 ? 139 GLN A OE1 1 
ATOM   1085 N NE2 . GLN A 1 139 ? 117.380 74.109  111.869 1.00 30.00 ? 139 GLN A NE2 1 
ATOM   1086 N N   . LYS A 1 140 ? 114.708 69.739  107.283 1.00 30.00 ? 140 LYS A N   1 
ATOM   1087 C CA  . LYS A 1 140 ? 114.836 68.656  106.283 1.00 30.00 ? 140 LYS A CA  1 
ATOM   1088 C C   . LYS A 1 140 ? 114.061 69.089  105.043 1.00 30.00 ? 140 LYS A C   1 
ATOM   1089 O O   . LYS A 1 140 ? 114.606 68.936  103.946 1.00 30.00 ? 140 LYS A O   1 
ATOM   1090 C CB  . LYS A 1 140 ? 114.268 67.365  106.861 1.00 30.00 ? 140 LYS A CB  1 
ATOM   1091 C CG  . LYS A 1 140 ? 114.601 66.098  106.093 1.00 30.00 ? 140 LYS A CG  1 
ATOM   1092 C CD  . LYS A 1 140 ? 116.088 65.860  105.992 1.00 30.00 ? 140 LYS A CD  1 
ATOM   1093 C CE  . LYS A 1 140 ? 116.447 64.449  105.585 1.00 30.00 ? 140 LYS A CE  1 
ATOM   1094 N NZ  . LYS A 1 140 ? 116.131 63.479  106.660 1.00 30.00 ? 140 LYS A NZ  1 
ATOM   1095 N N   . CYS A 1 141 ? 112.869 69.660  105.222 1.00 30.00 ? 141 CYS A N   1 
ATOM   1096 C CA  . CYS A 1 141 ? 112.003 70.119  104.106 1.00 30.00 ? 141 CYS A CA  1 
ATOM   1097 C C   . CYS A 1 141 ? 112.670 71.255  103.332 1.00 30.00 ? 141 CYS A C   1 
ATOM   1098 O O   . CYS A 1 141 ? 112.586 71.234  102.101 1.00 30.00 ? 141 CYS A O   1 
ATOM   1099 C CB  . CYS A 1 141 ? 110.680 70.636  104.638 1.00 30.00 ? 141 CYS A CB  1 
ATOM   1100 S SG  . CYS A 1 141 ? 109.776 69.416  105.618 1.00 30.00 ? 141 CYS A SG  1 
ATOM   1101 N N   . VAL A 1 142 ? 113.179 72.278  104.022 1.00 30.00 ? 142 VAL A N   1 
ATOM   1102 C CA  . VAL A 1 142 ? 113.941 73.379  103.368 1.00 30.00 ? 142 VAL A CA  1 
ATOM   1103 C C   . VAL A 1 142 ? 114.906 72.719  102.393 1.00 30.00 ? 142 VAL A C   1 
ATOM   1104 O O   . VAL A 1 142 ? 114.891 73.084  101.205 1.00 30.00 ? 142 VAL A O   1 
ATOM   1105 C CB  . VAL A 1 142 ? 114.722 74.215  104.395 1.00 30.00 ? 142 VAL A CB  1 
ATOM   1106 C CG1 . VAL A 1 142 ? 115.729 75.133  103.731 1.00 30.00 ? 142 VAL A CG1 1 
ATOM   1107 C CG2 . VAL A 1 142 ? 113.817 75.012  105.315 1.00 30.00 ? 142 VAL A CG2 1 
ATOM   1108 N N   . ARG A 1 143 ? 115.715 71.789  102.895 1.00 30.00 ? 143 ARG A N   1 
ATOM   1109 C CA  . ARG A 1 143 ? 116.728 71.074  102.087 1.00 30.00 ? 143 ARG A CA  1 
ATOM   1110 C C   . ARG A 1 143 ? 116.051 70.244  100.996 1.00 30.00 ? 143 ARG A C   1 
ATOM   1111 O O   . ARG A 1 143 ? 116.524 70.315  99.859  1.00 30.00 ? 143 ARG A O   1 
ATOM   1112 C CB  . ARG A 1 143 ? 117.535 70.211  103.047 1.00 30.00 ? 143 ARG A CB  1 
ATOM   1113 C CG  . ARG A 1 143 ? 118.656 69.399  102.425 1.00 30.00 ? 143 ARG A CG  1 
ATOM   1114 C CD  . ARG A 1 143 ? 118.969 68.270  103.381 1.00 30.00 ? 143 ARG A CD  1 
ATOM   1115 N NE  . ARG A 1 143 ? 119.255 68.761  104.720 1.00 30.00 ? 143 ARG A NE  1 
ATOM   1116 C CZ  . ARG A 1 143 ? 119.457 67.995  105.785 1.00 30.00 ? 143 ARG A CZ  1 
ATOM   1117 N NH1 . ARG A 1 143 ? 119.896 68.539  106.905 1.00 30.00 ? 143 ARG A NH1 1 
ATOM   1118 N NH2 . ARG A 1 143 ? 119.209 66.697  105.743 1.00 30.00 ? 143 ARG A NH2 1 
ATOM   1119 N N   . MET A 1 144 ? 114.973 69.518  101.299 1.00 30.00 ? 144 MET A N   1 
ATOM   1120 C CA  . MET A 1 144 ? 114.292 68.647  100.305 1.00 30.00 ? 144 MET A CA  1 
ATOM   1121 C C   . MET A 1 144 ? 113.788 69.550  99.183  1.00 30.00 ? 144 MET A C   1 
ATOM   1122 O O   . MET A 1 144 ? 113.859 69.125  98.013  1.00 30.00 ? 144 MET A O   1 
ATOM   1123 C CB  . MET A 1 144 ? 113.070 67.932  100.885 1.00 30.00 ? 144 MET A CB  1 
ATOM   1124 C CG  . MET A 1 144 ? 113.352 66.809  101.865 1.00 30.00 ? 144 MET A CG  1 
ATOM   1125 S SD  . MET A 1 144 ? 114.619 65.646  101.337 1.00 30.00 ? 144 MET A SD  1 
ATOM   1126 C CE  . MET A 1 144 ? 116.043 66.313  102.198 1.00 30.00 ? 144 MET A CE  1 
ATOM   1127 N N   . TYR A 1 145 ? 113.305 70.745  99.524  1.00 30.00 ? 145 TYR A N   1 
ATOM   1128 C CA  . TYR A 1 145 ? 112.722 71.708  98.560  1.00 30.00 ? 145 TYR A CA  1 
ATOM   1129 C C   . TYR A 1 145 ? 113.778 72.617  97.942  1.00 30.00 ? 145 TYR A C   1 
ATOM   1130 O O   . TYR A 1 145 ? 113.449 73.286  96.942  1.00 30.00 ? 145 TYR A O   1 
ATOM   1131 C CB  . TYR A 1 145 ? 111.759 72.635  99.296  1.00 30.00 ? 145 TYR A CB  1 
ATOM   1132 C CG  . TYR A 1 145 ? 110.318 72.205  99.339  1.00 30.00 ? 145 TYR A CG  1 
ATOM   1133 C CD1 . TYR A 1 145 ? 109.549 72.172  98.192  1.00 30.00 ? 145 TYR A CD1 1 
ATOM   1134 C CD2 . TYR A 1 145 ? 109.727 71.816  100.526 1.00 30.00 ? 145 TYR A CD2 1 
ATOM   1135 C CE1 . TYR A 1 145 ? 108.220 71.788  98.225  1.00 30.00 ? 145 TYR A CE1 1 
ATOM   1136 C CE2 . TYR A 1 145 ? 108.405 71.417  100.575 1.00 30.00 ? 145 TYR A CE2 1 
ATOM   1137 C CZ  . TYR A 1 145 ? 107.646 71.404  99.422  1.00 30.00 ? 145 TYR A CZ  1 
ATOM   1138 O OH  . TYR A 1 145 ? 106.333 71.009  99.468  1.00 30.00 ? 145 TYR A OH  1 
ATOM   1139 N N   . ASN A 1 146 ? 114.994 72.654  98.490  1.00 30.00 ? 146 ASN A N   1 
ATOM   1140 C CA  . ASN A 1 146 ? 116.000 73.625  97.996  1.00 30.00 ? 146 ASN A CA  1 
ATOM   1141 C C   . ASN A 1 146 ? 115.995 73.505  96.475  1.00 30.00 ? 146 ASN A C   1 
ATOM   1142 O O   . ASN A 1 146 ? 116.188 72.384  95.964  1.00 30.00 ? 146 ASN A O   1 
ATOM   1143 C CB  . ASN A 1 146 ? 117.397 73.418  98.575  1.00 30.00 ? 146 ASN A CB  1 
ATOM   1144 C CG  . ASN A 1 146 ? 118.290 74.632  98.450  1.00 30.00 ? 146 ASN A CG  1 
ATOM   1145 O OD1 . ASN A 1 146 ? 117.955 75.706  98.939  1.00 30.00 ? 146 ASN A OD1 1 
ATOM   1146 N ND2 . ASN A 1 146 ? 119.433 74.472  97.809  1.00 30.00 ? 146 ASN A ND2 1 
ATOM   1147 N N   . PRO A 1 147 ? 115.794 74.610  95.736  1.00 30.00 ? 147 PRO A N   1 
ATOM   1148 C CA  . PRO A 1 147 ? 115.681 74.546  94.284  1.00 30.00 ? 147 PRO A CA  1 
ATOM   1149 C C   . PRO A 1 147 ? 116.968 74.067  93.616  1.00 30.00 ? 147 PRO A C   1 
ATOM   1150 O O   . PRO A 1 147 ? 116.868 73.359  92.631  1.00 30.00 ? 147 PRO A O   1 
ATOM   1151 C CB  . PRO A 1 147 ? 115.450 76.011  93.908  1.00 30.00 ? 147 PRO A CB  1 
ATOM   1152 C CG  . PRO A 1 147 ? 116.069 76.794  95.027  1.00 30.00 ? 147 PRO A CG  1 
ATOM   1153 C CD  . PRO A 1 147 ? 115.720 75.977  96.245  1.00 30.00 ? 147 PRO A CD  1 
ATOM   1154 N N   . THR A 1 148 ? 118.122 74.458  94.153  1.00 30.00 ? 148 THR A N   1 
ATOM   1155 C CA  . THR A 1 148 ? 119.437 74.167  93.537  1.00 30.00 ? 148 THR A CA  1 
ATOM   1156 C C   . THR A 1 148 ? 120.370 73.517  94.554  1.00 30.00 ? 148 THR A C   1 
ATOM   1157 O O   . THR A 1 148 ? 119.852 73.012  95.566  1.00 30.00 ? 148 THR A O   1 
ATOM   1158 C CB  . THR A 1 148 ? 120.018 75.494  93.039  1.00 30.00 ? 148 THR A CB  1 
ATOM   1159 O OG1 . THR A 1 148 ? 121.080 75.257  92.115  1.00 30.00 ? 148 THR A OG1 1 
ATOM   1160 C CG2 . THR A 1 148 ? 120.513 76.378  94.164  1.00 30.00 ? 148 THR A CG2 1 
ATOM   1161 N N   . ASN A 1 149 ? 121.675 73.483  94.284  1.00 30.00 ? 149 ASN A N   1 
ATOM   1162 C CA  . ASN A 1 149 ? 122.699 73.009  95.242  1.00 30.00 ? 149 ASN A CA  1 
ATOM   1163 C C   . ASN A 1 149 ? 123.827 74.039  95.171  1.00 30.00 ? 149 ASN A C   1 
ATOM   1164 O O   . ASN A 1 149 ? 123.995 74.631  94.089  1.00 30.00 ? 149 ASN A O   1 
ATOM   1165 C CB  . ASN A 1 149 ? 123.130 71.580  94.929  1.00 30.00 ? 149 ASN A CB  1 
ATOM   1166 C CG  . ASN A 1 149 ? 123.997 70.970  96.009  1.00 30.00 ? 149 ASN A CG  1 
ATOM   1167 O OD1 . ASN A 1 149 ? 124.252 71.590  97.038  1.00 30.00 ? 149 ASN A OD1 1 
ATOM   1168 N ND2 . ASN A 1 149 ? 124.438 69.742  95.793  1.00 30.00 ? 149 ASN A ND2 1 
ATOM   1169 N N   . ILE A 1 150 ? 124.574 74.241  96.252  1.00 30.00 ? 150 ILE A N   1 
ATOM   1170 C CA  . ILE A 1 150 ? 125.642 75.280  96.331  1.00 30.00 ? 150 ILE A CA  1 
ATOM   1171 C C   . ILE A 1 150 ? 126.703 75.042  95.256  1.00 30.00 ? 150 ILE A C   1 
ATOM   1172 O O   . ILE A 1 150 ? 127.286 76.038  94.784  1.00 30.00 ? 150 ILE A O   1 
ATOM   1173 C CB  . ILE A 1 150 ? 126.259 75.251  97.736  1.00 30.00 ? 150 ILE A CB  1 
ATOM   1174 C CG1 . ILE A 1 150 ? 127.043 76.531  98.020  1.00 30.00 ? 150 ILE A CG1 1 
ATOM   1175 C CG2 . ILE A 1 150 ? 127.109 74.008  97.941  1.00 30.00 ? 150 ILE A CG2 1 
ATOM   1176 C CD1 . ILE A 1 150 ? 127.423 76.684  99.459  1.00 30.00 ? 150 ILE A CD1 1 
ATOM   1177 N N   . LEU A 1 151 ? 126.992 73.783  94.932  1.00 30.00 ? 151 LEU A N   1 
ATOM   1178 C CA  . LEU A 1 151 ? 128.022 73.422  93.924  1.00 30.00 ? 151 LEU A CA  1 
ATOM   1179 C C   . LEU A 1 151 ? 127.580 73.918  92.548  1.00 30.00 ? 151 LEU A C   1 
ATOM   1180 O O   . LEU A 1 151 ? 128.468 74.250  91.746  1.00 30.00 ? 151 LEU A O   1 
ATOM   1181 C CB  . LEU A 1 151 ? 128.186 71.902  93.922  1.00 30.00 ? 151 LEU A CB  1 
ATOM   1182 C CG  . LEU A 1 151 ? 128.575 71.266  95.254  1.00 30.00 ? 151 LEU A CG  1 
ATOM   1183 C CD1 . LEU A 1 151 ? 129.086 69.855  95.040  1.00 30.00 ? 151 LEU A CD1 1 
ATOM   1184 C CD2 . LEU A 1 151 ? 129.615 72.093  95.989  1.00 30.00 ? 151 LEU A CD2 1 
ATOM   1185 N N   . ASP A 1 152 ? 126.273 73.963  92.286  1.00 30.00 ? 152 ASP A N   1 
ATOM   1186 C CA  . ASP A 1 152 ? 125.725 74.352  90.960  1.00 30.00 ? 152 ASP A CA  1 
ATOM   1187 C C   . ASP A 1 152 ? 125.343 75.831  90.964  1.00 30.00 ? 152 ASP A C   1 
ATOM   1188 O O   . ASP A 1 152 ? 124.937 76.326  89.895  1.00 30.00 ? 152 ASP A O   1 
ATOM   1189 C CB  . ASP A 1 152 ? 124.510 73.501  90.622  1.00 30.00 ? 152 ASP A CB  1 
ATOM   1190 C CG  . ASP A 1 152 ? 124.805 72.012  90.596  1.00 30.00 ? 152 ASP A CG  1 
ATOM   1191 O OD1 . ASP A 1 152 ? 125.970 71.641  90.840  1.00 30.00 ? 152 ASP A OD1 1 
ATOM   1192 O OD2 . ASP A 1 152 ? 123.866 71.236  90.332  1.00 30.00 ? 152 ASP A OD2 1 
ATOM   1193 N N   . VAL A 1 153 ? 125.466 76.509  92.104  1.00 30.00 ? 153 VAL A N   1 
ATOM   1194 C CA  . VAL A 1 153 ? 125.219 77.975  92.174  1.00 30.00 ? 153 VAL A CA  1 
ATOM   1195 C C   . VAL A 1 153 ? 126.502 78.609  91.657  1.00 30.00 ? 153 VAL A C   1 
ATOM   1196 O O   . VAL A 1 153 ? 127.497 78.568  92.397  1.00 30.00 ? 153 VAL A O   1 
ATOM   1197 C CB  . VAL A 1 153 ? 124.872 78.447  93.594  1.00 30.00 ? 153 VAL A CB  1 
ATOM   1198 C CG1 . VAL A 1 153 ? 125.081 79.940  93.778  1.00 30.00 ? 153 VAL A CG1 1 
ATOM   1199 C CG2 . VAL A 1 153 ? 123.458 78.060  93.984  1.00 30.00 ? 153 VAL A CG2 1 
ATOM   1200 N N   . LYS A 1 154 ? 126.503 79.086  90.413  1.00 30.00 ? 154 LYS A N   1 
ATOM   1201 C CA  . LYS A 1 154 ? 127.721 79.635  89.770  1.00 30.00 ? 154 LYS A CA  1 
ATOM   1202 C C   . LYS A 1 154 ? 127.386 80.978  89.126  1.00 30.00 ? 154 LYS A C   1 
ATOM   1203 O O   . LYS A 1 154 ? 126.261 81.114  88.609  1.00 30.00 ? 154 LYS A O   1 
ATOM   1204 C CB  . LYS A 1 154 ? 128.212 78.638  88.725  1.00 30.00 ? 154 LYS A CB  1 
ATOM   1205 C CG  . LYS A 1 154 ? 128.319 77.200  89.209  1.00 30.00 ? 154 LYS A CG  1 
ATOM   1206 C CD  . LYS A 1 154 ? 129.294 76.391  88.397  1.00 30.00 ? 154 LYS A CD  1 
ATOM   1207 C CE  . LYS A 1 154 ? 129.567 75.031  88.996  1.00 30.00 ? 154 LYS A CE  1 
ATOM   1208 N NZ  . LYS A 1 154 ? 130.524 74.260  88.172  1.00 30.00 ? 154 LYS A NZ  1 
ATOM   1209 N N   . GLN A 1 155 ? 128.332 81.917  89.125  1.00 30.00 ? 155 GLN A N   1 
ATOM   1210 C CA  . GLN A 1 155 ? 128.094 83.262  88.546  1.00 30.00 ? 155 GLN A CA  1 
ATOM   1211 C C   . GLN A 1 155 ? 127.783 83.104  87.061  1.00 30.00 ? 155 GLN A C   1 
ATOM   1212 O O   . GLN A 1 155 ? 128.546 82.394  86.377  1.00 30.00 ? 155 GLN A O   1 
ATOM   1213 C CB  . GLN A 1 155 ? 129.306 84.176  88.716  1.00 30.00 ? 155 GLN A CB  1 
ATOM   1214 C CG  . GLN A 1 155 ? 129.015 85.616  88.324  1.00 30.00 ? 155 GLN A CG  1 
ATOM   1215 C CD  . GLN A 1 155 ? 130.103 86.570  88.747  1.00 30.00 ? 155 GLN A CD  1 
ATOM   1216 O OE1 . GLN A 1 155 ? 131.105 86.180  89.342  1.00 30.00 ? 155 GLN A OE1 1 
ATOM   1217 N NE2 . GLN A 1 155 ? 129.903 87.842  88.449  1.00 30.00 ? 155 GLN A NE2 1 
ATOM   1218 N N   . GLY A 1 156 ? 126.709 83.731  86.583  1.00 30.00 ? 156 GLY A N   1 
ATOM   1219 C CA  . GLY A 1 156 ? 126.376 83.734  85.148  1.00 30.00 ? 156 GLY A CA  1 
ATOM   1220 C C   . GLY A 1 156 ? 127.171 84.828  84.464  1.00 30.00 ? 156 GLY A C   1 
ATOM   1221 O O   . GLY A 1 156 ? 127.512 85.799  85.155  1.00 30.00 ? 156 GLY A O   1 
ATOM   1222 N N   . PRO A 1 157 ? 127.501 84.723  83.158  1.00 30.00 ? 157 PRO A N   1 
ATOM   1223 C CA  . PRO A 1 157 ? 128.366 85.708  82.494  1.00 30.00 ? 157 PRO A CA  1 
ATOM   1224 C C   . PRO A 1 157 ? 127.970 87.168  82.745  1.00 30.00 ? 157 PRO A C   1 
ATOM   1225 O O   . PRO A 1 157 ? 128.864 87.972  82.937  1.00 30.00 ? 157 PRO A O   1 
ATOM   1226 C CB  . PRO A 1 157 ? 128.152 85.396  81.012  1.00 30.00 ? 157 PRO A CB  1 
ATOM   1227 C CG  . PRO A 1 157 ? 127.869 83.915  80.992  1.00 30.00 ? 157 PRO A CG  1 
ATOM   1228 C CD  . PRO A 1 157 ? 127.056 83.671  82.244  1.00 30.00 ? 157 PRO A CD  1 
ATOM   1229 N N   . LYS A 1 158 ? 126.674 87.487  82.716  1.00 30.00 ? 158 LYS A N   1 
ATOM   1230 C CA  . LYS A 1 158 ? 126.154 88.861  82.938  1.00 30.00 ? 158 LYS A CA  1 
ATOM   1231 C C   . LYS A 1 158 ? 125.592 88.969  84.355  1.00 30.00 ? 158 LYS A C   1 
ATOM   1232 O O   . LYS A 1 158 ? 125.329 90.107  84.789  1.00 30.00 ? 158 LYS A O   1 
ATOM   1233 C CB  . LYS A 1 158 ? 125.077 89.188  81.905  1.00 30.00 ? 158 LYS A CB  1 
ATOM   1234 C CG  . LYS A 1 158 ? 125.484 88.954  80.456  1.00 30.00 ? 158 LYS A CG  1 
ATOM   1235 C CD  . LYS A 1 158 ? 126.802 89.592  80.069  1.00 30.00 ? 158 LYS A CD  1 
ATOM   1236 C CE  . LYS A 1 158 ? 126.845 91.084  80.318  1.00 30.00 ? 158 LYS A CE  1 
ATOM   1237 N NZ  . LYS A 1 158 ? 128.142 91.664  79.903  1.00 30.00 ? 158 LYS A NZ  1 
ATOM   1238 N N   . GLU A 1 159 ? 125.362 87.843  85.038  1.00 30.00 ? 159 GLU A N   1 
ATOM   1239 C CA  . GLU A 1 159 ? 124.925 87.882  86.456  1.00 30.00 ? 159 GLU A CA  1 
ATOM   1240 C C   . GLU A 1 159 ? 126.019 88.605  87.234  1.00 30.00 ? 159 GLU A C   1 
ATOM   1241 O O   . GLU A 1 159 ? 127.192 88.381  86.904  1.00 30.00 ? 159 GLU A O   1 
ATOM   1242 C CB  . GLU A 1 159 ? 124.746 86.500  87.077  1.00 30.00 ? 159 GLU A CB  1 
ATOM   1243 C CG  . GLU A 1 159 ? 124.216 86.562  88.498  1.00 30.00 ? 159 GLU A CG  1 
ATOM   1244 C CD  . GLU A 1 159 ? 123.979 85.228  89.179  1.00 30.00 ? 159 GLU A CD  1 
ATOM   1245 O OE1 . GLU A 1 159 ? 124.224 84.184  88.549  1.00 30.00 ? 159 GLU A OE1 1 
ATOM   1246 O OE2 . GLU A 1 159 ? 123.551 85.241  90.346  1.00 30.00 ? 159 GLU A OE2 1 
ATOM   1247 N N   . PRO A 1 160 ? 125.704 89.473  88.215  1.00 30.00 ? 160 PRO A N   1 
ATOM   1248 C CA  . PRO A 1 160 ? 126.729 90.098  89.041  1.00 30.00 ? 160 PRO A CA  1 
ATOM   1249 C C   . PRO A 1 160 ? 127.258 89.146  90.119  1.00 30.00 ? 160 PRO A C   1 
ATOM   1250 O O   . PRO A 1 160 ? 126.586 88.177  90.419  1.00 30.00 ? 160 PRO A O   1 
ATOM   1251 C CB  . PRO A 1 160 ? 126.022 91.281  89.708  1.00 30.00 ? 160 PRO A CB  1 
ATOM   1252 C CG  . PRO A 1 160 ? 124.673 91.366  89.029  1.00 30.00 ? 160 PRO A CG  1 
ATOM   1253 C CD  . PRO A 1 160 ? 124.376 89.959  88.566  1.00 30.00 ? 160 PRO A CD  1 
ATOM   1254 N N   . PHE A 1 161 ? 128.424 89.443  90.684  1.00 30.00 ? 161 PHE A N   1 
ATOM   1255 C CA  . PHE A 1 161 ? 129.069 88.611  91.727  1.00 30.00 ? 161 PHE A CA  1 
ATOM   1256 C C   . PHE A 1 161 ? 128.216 88.513  92.987  1.00 30.00 ? 161 PHE A C   1 
ATOM   1257 O O   . PHE A 1 161 ? 128.058 87.398  93.503  1.00 30.00 ? 161 PHE A O   1 
ATOM   1258 C CB  . PHE A 1 161 ? 130.378 89.284  92.116  1.00 30.00 ? 161 PHE A CB  1 
ATOM   1259 C CG  . PHE A 1 161 ? 131.182 88.583  93.176  1.00 30.00 ? 161 PHE A CG  1 
ATOM   1260 C CD1 . PHE A 1 161 ? 131.628 87.288  92.989  1.00 30.00 ? 161 PHE A CD1 1 
ATOM   1261 C CD2 . PHE A 1 161 ? 131.521 89.235  94.347  1.00 30.00 ? 161 PHE A CD2 1 
ATOM   1262 C CE1 . PHE A 1 161 ? 132.379 86.653  93.964  1.00 30.00 ? 161 PHE A CE1 1 
ATOM   1263 C CE2 . PHE A 1 161 ? 132.277 88.601  95.318  1.00 30.00 ? 161 PHE A CE2 1 
ATOM   1264 C CZ  . PHE A 1 161 ? 132.703 87.310  95.125  1.00 30.00 ? 161 PHE A CZ  1 
ATOM   1265 N N   . GLN A 1 162 ? 127.669 89.633  93.456  1.00 30.00 ? 162 GLN A N   1 
ATOM   1266 C CA  . GLN A 1 162 ? 126.899 89.682  94.724  1.00 30.00 ? 162 GLN A CA  1 
ATOM   1267 C C   . GLN A 1 162 ? 125.661 88.794  94.634  1.00 30.00 ? 162 GLN A C   1 
ATOM   1268 O O   . GLN A 1 162 ? 125.359 88.125  95.630  1.00 30.00 ? 162 GLN A O   1 
ATOM   1269 C CB  . GLN A 1 162 ? 126.481 91.123  94.979  1.00 30.00 ? 162 GLN A CB  1 
ATOM   1270 C CG  . GLN A 1 162 ? 125.738 91.333  96.284  1.00 30.00 ? 162 GLN A CG  1 
ATOM   1271 C CD  . GLN A 1 162 ? 125.532 92.803  96.540  1.00 30.00 ? 162 GLN A CD  1 
ATOM   1272 O OE1 . GLN A 1 162 ? 124.935 93.512  95.735  1.00 30.00 ? 162 GLN A OE1 1 
ATOM   1273 N NE2 . GLN A 1 162 ? 126.048 93.276  97.661  1.00 30.00 ? 162 GLN A NE2 1 
ATOM   1274 N N   . SER A 1 163 ? 124.957 88.811  93.505  1.00 30.00 ? 163 SER A N   1 
ATOM   1275 C CA  . SER A 1 163 ? 123.737 87.996  93.296  1.00 30.00 ? 163 SER A CA  1 
ATOM   1276 C C   . SER A 1 163 ? 124.114 86.518  93.326  1.00 30.00 ? 163 SER A C   1 
ATOM   1277 O O   . SER A 1 163 ? 123.413 85.744  94.005  1.00 30.00 ? 163 SER A O   1 
ATOM   1278 C CB  . SER A 1 163 ? 123.121 88.366  91.999  1.00 30.00 ? 163 SER A CB  1 
ATOM   1279 O OG  . SER A 1 163 ? 122.835 89.754  91.967  1.00 30.00 ? 163 SER A OG  1 
ATOM   1280 N N   . TYR A 1 164 ? 125.198 86.151  92.648  1.00 30.00 ? 164 TYR A N   1 
ATOM   1281 C CA  . TYR A 1 164 ? 125.724 84.766  92.640  1.00 30.00 ? 164 TYR A CA  1 
ATOM   1282 C C   . TYR A 1 164 ? 126.046 84.380  94.075  1.00 30.00 ? 164 TYR A C   1 
ATOM   1283 O O   . TYR A 1 164 ? 125.730 83.248  94.494  1.00 30.00 ? 164 TYR A O   1 
ATOM   1284 C CB  . TYR A 1 164 ? 126.973 84.754  91.765  1.00 30.00 ? 164 TYR A CB  1 
ATOM   1285 C CG  . TYR A 1 164 ? 128.064 83.789  92.133  1.00 30.00 ? 164 TYR A CG  1 
ATOM   1286 C CD1 . TYR A 1 164 ? 127.859 82.425  92.126  1.00 30.00 ? 164 TYR A CD1 1 
ATOM   1287 C CD2 . TYR A 1 164 ? 129.324 84.257  92.453  1.00 30.00 ? 164 TYR A CD2 1 
ATOM   1288 C CE1 . TYR A 1 164 ? 128.880 81.549  92.445  1.00 30.00 ? 164 TYR A CE1 1 
ATOM   1289 C CE2 . TYR A 1 164 ? 130.355 83.395  92.772  1.00 30.00 ? 164 TYR A CE2 1 
ATOM   1290 C CZ  . TYR A 1 164 ? 130.131 82.033  92.763  1.00 30.00 ? 164 TYR A CZ  1 
ATOM   1291 O OH  . TYR A 1 164 ? 131.128 81.150  93.070  1.00 30.00 ? 164 TYR A OH  1 
ATOM   1292 N N   . VAL A 1 165 ? 126.639 85.314  94.809  1.00 30.00 ? 165 VAL A N   1 
ATOM   1293 C CA  . VAL A 1 165 ? 127.034 85.081  96.221  1.00 30.00 ? 165 VAL A CA  1 
ATOM   1294 C C   . VAL A 1 165 ? 125.801 84.923  97.103  1.00 30.00 ? 165 VAL A C   1 
ATOM   1295 O O   . VAL A 1 165 ? 125.816 84.055  97.990  1.00 30.00 ? 165 VAL A O   1 
ATOM   1296 C CB  . VAL A 1 165 ? 127.899 86.246  96.741  1.00 30.00 ? 165 VAL A CB  1 
ATOM   1297 C CG1 . VAL A 1 165 ? 128.024 86.234  98.254  1.00 30.00 ? 165 VAL A CG1 1 
ATOM   1298 C CG2 . VAL A 1 165 ? 129.279 86.275  96.111  1.00 30.00 ? 165 VAL A CG2 1 
ATOM   1299 N N   . ASP A 1 166 ? 124.786 85.751  96.885  1.00 30.00 ? 166 ASP A N   1 
ATOM   1300 C CA  . ASP A 1 166 ? 123.564 85.711  97.711  1.00 30.00 ? 166 ASP A CA  1 
ATOM   1301 C C   . ASP A 1 166 ? 123.005 84.300  97.613  1.00 30.00 ? 166 ASP A C   1 
ATOM   1302 O O   . ASP A 1 166 ? 122.706 83.707  98.664  1.00 30.00 ? 166 ASP A O   1 
ATOM   1303 C CB  . ASP A 1 166 ? 122.534 86.715  97.219  1.00 30.00 ? 166 ASP A CB  1 
ATOM   1304 C CG  . ASP A 1 166 ? 122.880 88.163  97.506  1.00 30.00 ? 166 ASP A CG  1 
ATOM   1305 O OD1 . ASP A 1 166 ? 123.943 88.403  98.097  1.00 30.00 ? 166 ASP A OD1 1 
ATOM   1306 O OD2 . ASP A 1 166 ? 122.073 89.037  97.143  1.00 30.00 ? 166 ASP A OD2 1 
ATOM   1307 N N   . ARG A 1 167 ? 122.948 83.757  96.406  1.00 30.00 ? 167 ARG A N   1 
ATOM   1308 C CA  . ARG A 1 167 ? 122.421 82.395  96.169  1.00 30.00 ? 167 ARG A CA  1 
ATOM   1309 C C   . ARG A 1 167 ? 123.311 81.369  96.862  1.00 30.00 ? 167 ARG A C   1 
ATOM   1310 O O   . ARG A 1 167 ? 122.763 80.448  97.493  1.00 30.00 ? 167 ARG A O   1 
ATOM   1311 C CB  . ARG A 1 167 ? 122.454 82.161  94.666  1.00 30.00 ? 167 ARG A CB  1 
ATOM   1312 C CG  . ARG A 1 167 ? 121.566 83.099  93.862  1.00 30.00 ? 167 ARG A CG  1 
ATOM   1313 C CD  . ARG A 1 167 ? 122.044 83.266  92.432  1.00 30.00 ? 167 ARG A CD  1 
ATOM   1314 N NE  . ARG A 1 167 ? 122.049 82.017  91.684  1.00 30.00 ? 167 ARG A NE  1 
ATOM   1315 C CZ  . ARG A 1 167 ? 123.114 81.472  91.104  1.00 30.00 ? 167 ARG A CZ  1 
ATOM   1316 N NH1 . ARG A 1 167 ? 124.158 82.205  90.766  1.00 30.00 ? 167 ARG A NH1 1 
ATOM   1317 N NH2 . ARG A 1 167 ? 123.119 80.181  90.830  1.00 30.00 ? 167 ARG A NH2 1 
ATOM   1318 N N   . PHE A 1 168 ? 124.629 81.533  96.767  1.00 30.00 ? 168 PHE A N   1 
ATOM   1319 C CA  . PHE A 1 168 ? 125.617 80.576  97.321  1.00 30.00 ? 168 PHE A CA  1 
ATOM   1320 C C   . PHE A 1 168 ? 125.487 80.471  98.838  1.00 30.00 ? 168 PHE A C   1 
ATOM   1321 O O   . PHE A 1 168 ? 125.409 79.336  99.346  1.00 30.00 ? 168 PHE A O   1 
ATOM   1322 C CB  . PHE A 1 168 ? 126.997 81.081  96.907  1.00 30.00 ? 168 PHE A CB  1 
ATOM   1323 C CG  . PHE A 1 168 ? 128.179 80.263  97.350  1.00 30.00 ? 168 PHE A CG  1 
ATOM   1324 C CD1 . PHE A 1 168 ? 128.537 80.174  98.684  1.00 30.00 ? 168 PHE A CD1 1 
ATOM   1325 C CD2 . PHE A 1 168 ? 128.924 79.561  96.422  1.00 30.00 ? 168 PHE A CD2 1 
ATOM   1326 C CE1 . PHE A 1 168 ? 129.632 79.423  99.073  1.00 30.00 ? 168 PHE A CE1 1 
ATOM   1327 C CE2 . PHE A 1 168 ? 130.010 78.800  96.815  1.00 30.00 ? 168 PHE A CE2 1 
ATOM   1328 C CZ  . PHE A 1 168 ? 130.361 78.732  98.139  1.00 30.00 ? 168 PHE A CZ  1 
ATOM   1329 N N   . TYR A 1 169 ? 125.436 81.604  99.536  1.00 30.00 ? 169 TYR A N   1 
ATOM   1330 C CA  . TYR A 1 169 ? 125.368 81.635  101.019 1.00 30.00 ? 169 TYR A CA  1 
ATOM   1331 C C   . TYR A 1 169 ? 123.990 81.154  101.475 1.00 30.00 ? 169 TYR A C   1 
ATOM   1332 O O   . TYR A 1 169 ? 123.910 80.469  102.513 1.00 30.00 ? 169 TYR A O   1 
ATOM   1333 C CB  . TYR A 1 169 ? 125.731 83.032  101.519 1.00 30.00 ? 169 TYR A CB  1 
ATOM   1334 C CG  . TYR A 1 169 ? 127.215 83.243  101.631 1.00 30.00 ? 169 TYR A CG  1 
ATOM   1335 C CD1 . TYR A 1 169 ? 128.022 83.269  100.511 1.00 30.00 ? 169 TYR A CD1 1 
ATOM   1336 C CD2 . TYR A 1 169 ? 127.826 83.292  102.868 1.00 30.00 ? 169 TYR A CD2 1 
ATOM   1337 C CE1 . TYR A 1 169 ? 129.392 83.419  100.615 1.00 30.00 ? 169 TYR A CE1 1 
ATOM   1338 C CE2 . TYR A 1 169 ? 129.195 83.429  102.992 1.00 30.00 ? 169 TYR A CE2 1 
ATOM   1339 C CZ  . TYR A 1 169 ? 129.981 83.497  101.861 1.00 30.00 ? 169 TYR A CZ  1 
ATOM   1340 O OH  . TYR A 1 169 ? 131.337 83.636  101.988 1.00 30.00 ? 169 TYR A OH  1 
ATOM   1341 N N   . LYS A 1 170 ? 122.937 81.497  100.735 1.00 30.00 ? 170 LYS A N   1 
ATOM   1342 C CA  . LYS A 1 170 ? 121.558 81.050  101.051 1.00 30.00 ? 170 LYS A CA  1 
ATOM   1343 C C   . LYS A 1 170 ? 121.499 79.530  100.988 1.00 30.00 ? 170 LYS A C   1 
ATOM   1344 O O   . LYS A 1 170 ? 120.917 78.916  101.900 1.00 30.00 ? 170 LYS A O   1 
ATOM   1345 C CB  . LYS A 1 170 ? 120.597 81.615  100.013 1.00 30.00 ? 170 LYS A CB  1 
ATOM   1346 C CG  . LYS A 1 170 ? 119.141 81.245  100.223 1.00 30.00 ? 170 LYS A CG  1 
ATOM   1347 C CD  . LYS A 1 170 ? 118.190 82.189  99.536  1.00 30.00 ? 170 LYS A CD  1 
ATOM   1348 C CE  . LYS A 1 170 ? 118.389 82.256  98.040  1.00 30.00 ? 170 LYS A CE  1 
ATOM   1349 N NZ  . LYS A 1 170 ? 117.410 83.176  97.420  1.00 30.00 ? 170 LYS A NZ  1 
ATOM   1350 N N   . SER A 1 171 ? 122.057 78.949  99.932  1.00 30.00 ? 171 SER A N   1 
ATOM   1351 C CA  . SER A 1 171 ? 122.081 77.483  99.734  1.00 30.00 ? 171 SER A CA  1 
ATOM   1352 C C   . SER A 1 171 ? 122.922 76.835  100.828 1.00 30.00 ? 171 SER A C   1 
ATOM   1353 O O   . SER A 1 171 ? 122.550 75.754  101.286 1.00 30.00 ? 171 SER A O   1 
ATOM   1354 C CB  . SER A 1 171 ? 122.639 77.190  98.399  1.00 30.00 ? 171 SER A CB  1 
ATOM   1355 O OG  . SER A 1 171 ? 121.832 77.767  97.388  1.00 30.00 ? 171 SER A OG  1 
ATOM   1356 N N   . LEU A 1 172 ? 124.054 77.444  101.176 1.00 30.00 ? 172 LEU A N   1 
ATOM   1357 C CA  . LEU A 1 172 ? 124.939 76.935  102.251 1.00 30.00 ? 172 LEU A CA  1 
ATOM   1358 C C   . LEU A 1 172 ? 124.102 76.762  103.521 1.00 30.00 ? 172 LEU A C   1 
ATOM   1359 O O   . LEU A 1 172 ? 124.238 75.707  104.170 1.00 30.00 ? 172 LEU A O   1 
ATOM   1360 C CB  . LEU A 1 172 ? 126.061 77.955  102.434 1.00 30.00 ? 172 LEU A CB  1 
ATOM   1361 C CG  . LEU A 1 172 ? 127.241 77.513  103.293 1.00 30.00 ? 172 LEU A CG  1 
ATOM   1362 C CD1 . LEU A 1 172 ? 128.175 76.606  102.515 1.00 30.00 ? 172 LEU A CD1 1 
ATOM   1363 C CD2 . LEU A 1 172 ? 127.996 78.716  103.821 1.00 30.00 ? 172 LEU A CD2 1 
ATOM   1364 N N   . ARG A 1 173 ? 123.238 77.733  103.837 1.00 30.00 ? 173 ARG A N   1 
ATOM   1365 C CA  . ARG A 1 173 ? 122.335 77.664  105.015 1.00 30.00 ? 173 ARG A CA  1 
ATOM   1366 C C   . ARG A 1 173 ? 121.339 76.522  104.872 1.00 30.00 ? 173 ARG A C   1 
ATOM   1367 O O   . ARG A 1 173 ? 121.286 75.699  105.791 1.00 30.00 ? 173 ARG A O   1 
ATOM   1368 C CB  . ARG A 1 173 ? 121.439 78.898  105.114 1.00 30.00 ? 173 ARG A CB  1 
ATOM   1369 C CG  . ARG A 1 173 ? 122.093 80.143  105.682 1.00 30.00 ? 173 ARG A CG  1 
ATOM   1370 C CD  . ARG A 1 173 ? 121.094 81.282  105.719 1.00 30.00 ? 173 ARG A CD  1 
ATOM   1371 N NE  . ARG A 1 173 ? 119.971 81.050  106.617 1.00 30.00 ? 173 ARG A NE  1 
ATOM   1372 C CZ  . ARG A 1 173 ? 118.971 81.901  106.807 1.00 30.00 ? 173 ARG A CZ  1 
ATOM   1373 N NH1 . ARG A 1 173 ? 118.531 82.650  105.814 1.00 30.00 ? 173 ARG A NH1 1 
ATOM   1374 N NH2 . ARG A 1 173 ? 118.391 81.982  107.990 1.00 30.00 ? 173 ARG A NH2 1 
ATOM   1375 N N   . ALA A 1 174 ? 120.566 76.498  103.787 1.00 30.00 ? 174 ALA A N   1 
ATOM   1376 C CA  . ALA A 1 174 ? 119.487 75.513  103.550 1.00 30.00 ? 174 ALA A CA  1 
ATOM   1377 C C   . ALA A 1 174 ? 120.011 74.083  103.430 1.00 30.00 ? 174 ALA A C   1 
ATOM   1378 O O   . ALA A 1 174 ? 119.352 73.172  103.967 1.00 30.00 ? 174 ALA A O   1 
ATOM   1379 C CB  . ALA A 1 174 ? 118.825 75.917  102.280 1.00 30.00 ? 174 ALA A CB  1 
ATOM   1380 N N   . GLU A 1 175 ? 121.076 73.873  102.655 1.00 30.00 ? 175 GLU A N   1 
ATOM   1381 C CA  . GLU A 1 175 ? 121.716 72.541  102.516 1.00 30.00 ? 175 GLU A CA  1 
ATOM   1382 C C   . GLU A 1 175 ? 122.204 72.140  103.901 1.00 30.00 ? 175 GLU A C   1 
ATOM   1383 O O   . GLU A 1 175 ? 122.350 70.927  104.149 1.00 30.00 ? 175 GLU A O   1 
ATOM   1384 C CB  . GLU A 1 175 ? 122.884 72.612  101.541 1.00 30.00 ? 175 GLU A CB  1 
ATOM   1385 C CG  . GLU A 1 175 ? 122.462 72.871  100.107 1.00 30.00 ? 175 GLU A CG  1 
ATOM   1386 C CD  . GLU A 1 175 ? 121.635 71.759  99.488  1.00 30.00 ? 175 GLU A CD  1 
ATOM   1387 O OE1 . GLU A 1 175 ? 122.152 70.632  99.380  1.00 30.00 ? 175 GLU A OE1 1 
ATOM   1388 O OE2 . GLU A 1 175 ? 120.469 72.019  99.139  1.00 30.00 ? 175 GLU A OE2 1 
ATOM   1389 N N   . GLN A 1 176 ? 122.446 73.130  104.760 1.00 30.00 ? 176 GLN A N   1 
ATOM   1390 C CA  . GLN A 1 176 ? 122.870 72.882  106.159 1.00 30.00 ? 176 GLN A CA  1 
ATOM   1391 C C   . GLN A 1 176 ? 124.095 71.975  106.151 1.00 30.00 ? 176 GLN A C   1 
ATOM   1392 O O   . GLN A 1 176 ? 124.048 70.921  106.806 1.00 30.00 ? 176 GLN A O   1 
ATOM   1393 C CB  . GLN A 1 176 ? 121.716 72.284  106.955 1.00 30.00 ? 176 GLN A CB  1 
ATOM   1394 C CG  . GLN A 1 176 ? 120.525 73.213  107.080 1.00 30.00 ? 176 GLN A CG  1 
ATOM   1395 C CD  . GLN A 1 176 ? 119.299 72.478  107.543 1.00 30.00 ? 176 GLN A CD  1 
ATOM   1396 O OE1 . GLN A 1 176 ? 119.296 71.837  108.589 1.00 30.00 ? 176 GLN A OE1 1 
ATOM   1397 N NE2 . GLN A 1 176 ? 118.257 72.545  106.733 1.00 30.00 ? 176 GLN A NE2 1 
ATOM   1398 N N   . THR A 1 177 ? 125.125 72.336  105.393 1.00 30.00 ? 177 THR A N   1 
ATOM   1399 C CA  . THR A 1 177 ? 126.401 71.581  105.363 1.00 30.00 ? 177 THR A CA  1 
ATOM   1400 C C   . THR A 1 177 ? 127.118 71.846  106.687 1.00 30.00 ? 177 THR A C   1 
ATOM   1401 O O   . THR A 1 177 ? 126.804 72.868  107.313 1.00 30.00 ? 177 THR A O   1 
ATOM   1402 C CB  . THR A 1 177 ? 127.227 72.009  104.151 1.00 30.00 ? 177 THR A CB  1 
ATOM   1403 O OG1 . THR A 1 177 ? 126.385 71.946  103.000 1.00 30.00 ? 177 THR A OG1 1 
ATOM   1404 C CG2 . THR A 1 177 ? 128.453 71.152  103.936 1.00 30.00 ? 177 THR A CG2 1 
ATOM   1405 N N   . ASP A 1 178 ? 128.034 70.974  107.108 1.00 30.00 ? 178 ASP A N   1 
ATOM   1406 C CA  . ASP A 1 178 ? 128.721 71.121  108.416 1.00 30.00 ? 178 ASP A CA  1 
ATOM   1407 C C   . ASP A 1 178 ? 129.513 72.426  108.398 1.00 30.00 ? 178 ASP A C   1 
ATOM   1408 O O   . ASP A 1 178 ? 130.037 72.757  107.333 1.00 30.00 ? 178 ASP A O   1 
ATOM   1409 C CB  . ASP A 1 178 ? 129.656 69.955  108.718 1.00 30.00 ? 178 ASP A CB  1 
ATOM   1410 C CG  . ASP A 1 178 ? 128.955 68.612  108.813 1.00 30.00 ? 178 ASP A CG  1 
ATOM   1411 O OD1 . ASP A 1 178 ? 127.719 68.583  108.656 1.00 30.00 ? 178 ASP A OD1 1 
ATOM   1412 O OD2 . ASP A 1 178 ? 129.654 67.605  109.032 1.00 30.00 ? 178 ASP A OD2 1 
ATOM   1413 N N   . PRO A 1 179 ? 129.684 73.133  109.535 1.00 30.00 ? 179 PRO A N   1 
ATOM   1414 C CA  . PRO A 1 179 ? 130.330 74.455  109.545 1.00 30.00 ? 179 PRO A CA  1 
ATOM   1415 C C   . PRO A 1 179 ? 131.760 74.463  108.992 1.00 30.00 ? 179 PRO A C   1 
ATOM   1416 O O   . PRO A 1 179 ? 132.118 75.437  108.366 1.00 30.00 ? 179 PRO A O   1 
ATOM   1417 C CB  . PRO A 1 179 ? 130.384 74.799  111.039 1.00 30.00 ? 179 PRO A CB  1 
ATOM   1418 C CG  . PRO A 1 179 ? 129.251 74.009  111.641 1.00 30.00 ? 179 PRO A CG  1 
ATOM   1419 C CD  . PRO A 1 179 ? 129.265 72.711  110.869 1.00 30.00 ? 179 PRO A CD  1 
ATOM   1420 N N   . ALA A 1 180 ? 132.550 73.426  109.267 1.00 30.00 ? 180 ALA A N   1 
ATOM   1421 C CA  . ALA A 1 180 ? 133.937 73.307  108.763 1.00 30.00 ? 180 ALA A CA  1 
ATOM   1422 C C   . ALA A 1 180 ? 133.920 73.232  107.236 1.00 30.00 ? 180 ALA A C   1 
ATOM   1423 O O   . ALA A 1 180 ? 134.809 73.841  106.611 1.00 30.00 ? 180 ALA A O   1 
ATOM   1424 C CB  . ALA A 1 180 ? 134.574 72.082  109.347 1.00 30.00 ? 180 ALA A CB  1 
ATOM   1425 N N   . VAL A 1 181 ? 132.948 72.521  106.661 1.00 30.00 ? 181 VAL A N   1 
ATOM   1426 C CA  . VAL A 1 181 ? 132.838 72.338  105.185 1.00 30.00 ? 181 VAL A CA  1 
ATOM   1427 C C   . VAL A 1 181 ? 132.308 73.634  104.581 1.00 30.00 ? 181 VAL A C   1 
ATOM   1428 O O   . VAL A 1 181 ? 132.576 73.863  103.396 1.00 30.00 ? 181 VAL A O   1 
ATOM   1429 C CB  . VAL A 1 181 ? 131.903 71.165  104.854 1.00 30.00 ? 181 VAL A CB  1 
ATOM   1430 C CG1 . VAL A 1 181 ? 131.711 70.984  103.360 1.00 30.00 ? 181 VAL A CG1 1 
ATOM   1431 C CG2 . VAL A 1 181 ? 132.380 69.872  105.490 1.00 30.00 ? 181 VAL A CG2 1 
ATOM   1432 N N   . LYS A 1 182 ? 131.558 74.426  105.344 1.00 30.00 ? 182 LYS A N   1 
ATOM   1433 C CA  . LYS A 1 182 ? 131.016 75.731  104.901 1.00 30.00 ? 182 LYS A CA  1 
ATOM   1434 C C   . LYS A 1 182 ? 132.181 76.698  104.706 1.00 30.00 ? 182 LYS A C   1 
ATOM   1435 O O   . LYS A 1 182 ? 132.117 77.476  103.759 1.00 30.00 ? 182 LYS A O   1 
ATOM   1436 C CB  . LYS A 1 182 ? 129.984 76.228  105.912 1.00 30.00 ? 182 LYS A CB  1 
ATOM   1437 C CG  . LYS A 1 182 ? 128.713 75.394  105.959 1.00 30.00 ? 182 LYS A CG  1 
ATOM   1438 C CD  . LYS A 1 182 ? 127.757 75.782  107.057 1.00 30.00 ? 182 LYS A CD  1 
ATOM   1439 C CE  . LYS A 1 182 ? 127.255 77.204  106.944 1.00 30.00 ? 182 LYS A CE  1 
ATOM   1440 N NZ  . LYS A 1 182 ? 126.293 77.515  108.026 1.00 30.00 ? 182 LYS A NZ  1 
ATOM   1441 N N   . ASN A 1 183 ? 133.197 76.644  105.564 1.00 30.00 ? 183 ASN A N   1 
ATOM   1442 C CA  . ASN A 1 183 ? 134.397 77.511  105.445 1.00 30.00 ? 183 ASN A CA  1 
ATOM   1443 C C   . ASN A 1 183 ? 135.178 77.142  104.183 1.00 30.00 ? 183 ASN A C   1 
ATOM   1444 O O   . ASN A 1 183 ? 135.680 78.064  103.524 1.00 30.00 ? 183 ASN A O   1 
ATOM   1445 C CB  . ASN A 1 183 ? 135.296 77.392  106.671 1.00 30.00 ? 183 ASN A CB  1 
ATOM   1446 C CG  . ASN A 1 183 ? 134.618 77.848  107.944 1.00 30.00 ? 183 ASN A CG  1 
ATOM   1447 O OD1 . ASN A 1 183 ? 133.470 78.283  107.924 1.00 30.00 ? 183 ASN A OD1 1 
ATOM   1448 N ND2 . ASN A 1 183 ? 135.327 77.758  109.056 1.00 30.00 ? 183 ASN A ND2 1 
ATOM   1449 N N   . TRP A 1 184 ? 135.264 75.856  103.839 1.00 30.00 ? 184 TRP A N   1 
ATOM   1450 C CA  . TRP A 1 184 ? 136.007 75.398  102.638 1.00 30.00 ? 184 TRP A CA  1 
ATOM   1451 C C   . TRP A 1 184 ? 135.286 75.893  101.386 1.00 30.00 ? 184 TRP A C   1 
ATOM   1452 O O   . TRP A 1 184 ? 135.960 76.459  100.507 1.00 30.00 ? 184 TRP A O   1 
ATOM   1453 C CB  . TRP A 1 184 ? 136.156 73.874  102.635 1.00 30.00 ? 184 TRP A CB  1 
ATOM   1454 C CG  . TRP A 1 184 ? 136.741 73.334  101.368 1.00 30.00 ? 184 TRP A CG  1 
ATOM   1455 C CD1 . TRP A 1 184 ? 138.026 72.921  101.176 1.00 30.00 ? 184 TRP A CD1 1 
ATOM   1456 C CD2 . TRP A 1 184 ? 136.048 73.064  100.136 1.00 30.00 ? 184 TRP A CD2 1 
ATOM   1457 N NE1 . TRP A 1 184 ? 138.195 72.471  99.896  1.00 30.00 ? 184 TRP A NE1 1 
ATOM   1458 C CE2 . TRP A 1 184 ? 136.998 72.539  99.236  1.00 30.00 ? 184 TRP A CE2 1 
ATOM   1459 C CE3 . TRP A 1 184 ? 134.732 73.231  99.696  1.00 30.00 ? 184 TRP A CE3 1 
ATOM   1460 C CZ2 . TRP A 1 184 ? 136.670 72.184  97.930  1.00 30.00 ? 184 TRP A CZ2 1 
ATOM   1461 C CZ3 . TRP A 1 184 ? 134.408 72.884  98.405  1.00 30.00 ? 184 TRP A CZ3 1 
ATOM   1462 C CH2 . TRP A 1 184 ? 135.366 72.366  97.536  1.00 30.00 ? 184 TRP A CH2 1 
ATOM   1463 N N   . MET A 1 185 ? 133.968 75.715  101.323 1.00 30.00 ? 185 MET A N   1 
ATOM   1464 C CA  . MET A 1 185 ? 133.159 76.105  100.141 1.00 30.00 ? 185 MET A CA  1 
ATOM   1465 C C   . MET A 1 185 ? 133.270 77.610  99.926  1.00 30.00 ? 185 MET A C   1 
ATOM   1466 O O   . MET A 1 185 ? 133.537 78.024  98.783  1.00 30.00 ? 185 MET A O   1 
ATOM   1467 C CB  . MET A 1 185 ? 131.694 75.764  100.396 1.00 30.00 ? 185 MET A CB  1 
ATOM   1468 C CG  . MET A 1 185 ? 131.305 74.390  99.925  1.00 30.00 ? 185 MET A CG  1 
ATOM   1469 S SD  . MET A 1 185 ? 129.688 73.913  100.557 1.00 30.00 ? 185 MET A SD  1 
ATOM   1470 C CE  . MET A 1 185 ? 129.824 72.130  100.480 1.00 30.00 ? 185 MET A CE  1 
ATOM   1471 N N   . THR A 1 186 ? 133.137 78.392  100.993 1.00 30.00 ? 186 THR A N   1 
ATOM   1472 C CA  . THR A 1 186 ? 133.145 79.871  100.896 1.00 30.00 ? 186 THR A CA  1 
ATOM   1473 C C   . THR A 1 186 ? 134.496 80.348  100.369 1.00 30.00 ? 186 THR A C   1 
ATOM   1474 O O   . THR A 1 186 ? 134.488 81.287  99.562  1.00 30.00 ? 186 THR A O   1 
ATOM   1475 C CB  . THR A 1 186 ? 132.812 80.502  102.249 1.00 30.00 ? 186 THR A CB  1 
ATOM   1476 O OG1 . THR A 1 186 ? 133.630 79.878  103.236 1.00 30.00 ? 186 THR A OG1 1 
ATOM   1477 C CG2 . THR A 1 186 ? 131.352 80.356  102.614 1.00 30.00 ? 186 THR A CG2 1 
ATOM   1478 N N   . GLN A 1 187 ? 135.599 79.712  100.759 1.00 30.00 ? 187 GLN A N   1 
ATOM   1479 C CA  . GLN A 1 187 ? 136.961 80.187  100.400 1.00 30.00 ? 187 GLN A CA  1 
ATOM   1480 C C   . GLN A 1 187 ? 137.486 79.546  99.114  1.00 30.00 ? 187 GLN A C   1 
ATOM   1481 O O   . GLN A 1 187 ? 138.513 80.046  98.613  1.00 30.00 ? 187 GLN A O   1 
ATOM   1482 C CB  . GLN A 1 187 ? 137.893 79.834  101.553 1.00 30.00 ? 187 GLN A CB  1 
ATOM   1483 C CG  . GLN A 1 187 ? 137.519 80.516  102.859 1.00 30.00 ? 187 GLN A CG  1 
ATOM   1484 C CD  . GLN A 1 187 ? 138.316 79.989  104.026 1.00 30.00 ? 187 GLN A CD  1 
ATOM   1485 O OE1 . GLN A 1 187 ? 139.166 79.114  103.881 1.00 30.00 ? 187 GLN A OE1 1 
ATOM   1486 N NE2 . GLN A 1 187 ? 138.040 80.524  105.203 1.00 30.00 ? 187 GLN A NE2 1 
ATOM   1487 N N   . THR A 1 188 ? 136.833 78.506  98.589  1.00 30.00 ? 188 THR A N   1 
ATOM   1488 C CA  . THR A 1 188 ? 137.339 77.748  97.412  1.00 30.00 ? 188 THR A CA  1 
ATOM   1489 C C   . THR A 1 188 ? 136.318 77.663  96.281  1.00 30.00 ? 188 THR A C   1 
ATOM   1490 O O   . THR A 1 188 ? 136.635 78.146  95.177  1.00 30.00 ? 188 THR A O   1 
ATOM   1491 C CB  . THR A 1 188 ? 137.676 76.318  97.832  1.00 30.00 ? 188 THR A CB  1 
ATOM   1492 O OG1 . THR A 1 188 ? 138.584 76.391  98.931  1.00 30.00 ? 188 THR A OG1 1 
ATOM   1493 C CG2 . THR A 1 188 ? 138.276 75.497  96.713  1.00 30.00 ? 188 THR A CG2 1 
ATOM   1494 N N   . LEU A 1 189 ? 135.146 77.087  96.542  1.00 30.00 ? 189 LEU A N   1 
ATOM   1495 C CA  . LEU A 1 189 ? 134.103 76.862  95.509  1.00 30.00 ? 189 LEU A CA  1 
ATOM   1496 C C   . LEU A 1 189 ? 133.653 78.204  94.938  1.00 30.00 ? 189 LEU A C   1 
ATOM   1497 O O   . LEU A 1 189 ? 133.153 78.217  93.799  1.00 30.00 ? 189 LEU A O   1 
ATOM   1498 C CB  . LEU A 1 189 ? 132.939 76.135  96.183  1.00 30.00 ? 189 LEU A CB  1 
ATOM   1499 C CG  . LEU A 1 189 ? 131.772 75.742  95.282  1.00 30.00 ? 189 LEU A CG  1 
ATOM   1500 C CD1 . LEU A 1 189 ? 132.161 74.607  94.355  1.00 30.00 ? 189 LEU A CD1 1 
ATOM   1501 C CD2 . LEU A 1 189 ? 130.568 75.352  96.120  1.00 30.00 ? 189 LEU A CD2 1 
ATOM   1502 N N   . LEU A 1 190 ? 133.814 79.287  95.695  1.00 30.00 ? 190 LEU A N   1 
ATOM   1503 C CA  . LEU A 1 190 ? 133.313 80.618  95.276  1.00 30.00 ? 190 LEU A CA  1 
ATOM   1504 C C   . LEU A 1 190 ? 134.292 81.341  94.362  1.00 30.00 ? 190 LEU A C   1 
ATOM   1505 O O   . LEU A 1 190 ? 133.874 82.260  93.639  1.00 30.00 ? 190 LEU A O   1 
ATOM   1506 C CB  . LEU A 1 190 ? 133.057 81.430  96.546  1.00 30.00 ? 190 LEU A CB  1 
ATOM   1507 C CG  . LEU A 1 190 ? 132.288 82.736  96.367  1.00 30.00 ? 190 LEU A CG  1 
ATOM   1508 C CD1 . LEU A 1 190 ? 130.818 82.474  96.099  1.00 30.00 ? 190 LEU A CD1 1 
ATOM   1509 C CD2 . LEU A 1 190 ? 132.439 83.612  97.596  1.00 30.00 ? 190 LEU A CD2 1 
ATOM   1510 N N   . ILE A 1 191 ? 135.568 81.034  94.469  1.00 30.00 ? 191 ILE A N   1 
ATOM   1511 C CA  . ILE A 1 191 ? 136.536 81.588  93.494  1.00 30.00 ? 191 ILE A CA  1 
ATOM   1512 C C   . ILE A 1 191 ? 136.376 80.666  92.289  1.00 30.00 ? 191 ILE A C   1 
ATOM   1513 O O   . ILE A 1 191 ? 136.407 81.174  91.164  1.00 30.00 ? 191 ILE A O   1 
ATOM   1514 C CB  . ILE A 1 191 ? 137.943 81.618  94.109  1.00 30.00 ? 191 ILE A CB  1 
ATOM   1515 C CG1 . ILE A 1 191 ? 137.931 82.347  95.456  1.00 30.00 ? 191 ILE A CG1 1 
ATOM   1516 C CG2 . ILE A 1 191 ? 138.942 82.223  93.134  1.00 30.00 ? 191 ILE A CG2 1 
ATOM   1517 C CD1 . ILE A 1 191 ? 139.265 82.396  96.154  1.00 30.00 ? 191 ILE A CD1 1 
ATOM   1518 N N   . GLN A 1 192 ? 136.052 79.394  92.535  1.00 30.00 ? 192 GLN A N   1 
ATOM   1519 C CA  . GLN A 1 192 ? 135.947 78.356  91.478  1.00 30.00 ? 192 GLN A CA  1 
ATOM   1520 C C   . GLN A 1 192 ? 134.725 78.504  90.568  1.00 30.00 ? 192 GLN A C   1 
ATOM   1521 O O   . GLN A 1 192 ? 134.911 78.346  89.349  1.00 30.00 ? 192 GLN A O   1 
ATOM   1522 C CB  . GLN A 1 192 ? 135.872 76.996  92.166  1.00 30.00 ? 192 GLN A CB  1 
ATOM   1523 C CG  . GLN A 1 192 ? 135.939 75.822  91.206  1.00 30.00 ? 192 GLN A CG  1 
ATOM   1524 C CD  . GLN A 1 192 ? 137.234 75.822  90.434  1.00 30.00 ? 192 GLN A CD  1 
ATOM   1525 O OE1 . GLN A 1 192 ? 138.318 75.746  91.006  1.00 30.00 ? 192 GLN A OE1 1 
ATOM   1526 N NE2 . GLN A 1 192 ? 137.127 75.924  89.120  1.00 30.00 ? 192 GLN A NE2 1 
ATOM   1527 N N   . ASN A 1 193 ? 133.532 78.785  91.097  1.00 30.00 ? 193 ASN A N   1 
ATOM   1528 C CA  . ASN A 1 193 ? 132.288 78.795  90.278  1.00 30.00 ? 193 ASN A CA  1 
ATOM   1529 C C   . ASN A 1 193 ? 132.034 80.181  89.690  1.00 30.00 ? 193 ASN A C   1 
ATOM   1530 O O   . ASN A 1 193 ? 131.135 80.295  88.837  1.00 30.00 ? 193 ASN A O   1 
ATOM   1531 C CB  . ASN A 1 193 ? 131.063 78.388  91.091  1.00 30.00 ? 193 ASN A CB  1 
ATOM   1532 C CG  . ASN A 1 193 ? 131.146 76.992  91.664  1.00 30.00 ? 193 ASN A CG  1 
ATOM   1533 O OD1 . ASN A 1 193 ? 132.143 76.296  91.488  1.00 30.00 ? 193 ASN A OD1 1 
ATOM   1534 N ND2 . ASN A 1 193 ? 130.099 76.583  92.361  1.00 30.00 ? 193 ASN A ND2 1 
ATOM   1535 N N   . ALA A 1 194 ? 132.803 81.186  90.098  1.00 30.00 ? 194 ALA A N   1 
ATOM   1536 C CA  . ALA A 1 194 ? 132.620 82.577  89.635  1.00 30.00 ? 194 ALA A CA  1 
ATOM   1537 C C   . ALA A 1 194 ? 133.148 82.737  88.211  1.00 30.00 ? 194 ALA A C   1 
ATOM   1538 O O   . ALA A 1 194 ? 134.006 81.921  87.815  1.00 30.00 ? 194 ALA A O   1 
ATOM   1539 C CB  . ALA A 1 194 ? 133.347 83.491  90.571  1.00 30.00 ? 194 ALA A CB  1 
ATOM   1540 N N   . ASN A 1 195 ? 132.654 83.729  87.464  1.00 30.00 ? 195 ASN A N   1 
ATOM   1541 C CA  . ASN A 1 195 ? 133.165 84.036  86.102  1.00 30.00 ? 195 ASN A CA  1 
ATOM   1542 C C   . ASN A 1 195 ? 134.691 84.120  86.187  1.00 30.00 ? 195 ASN A C   1 
ATOM   1543 O O   . ASN A 1 195 ? 135.176 84.350  87.283  1.00 30.00 ? 195 ASN A O   1 
ATOM   1544 C CB  . ASN A 1 195 ? 132.592 85.342  85.556  1.00 30.00 ? 195 ASN A CB  1 
ATOM   1545 C CG  . ASN A 1 195 ? 131.093 85.307  85.362  1.00 30.00 ? 195 ASN A CG  1 
ATOM   1546 O OD1 . ASN A 1 195 ? 130.459 84.272  85.551  1.00 30.00 ? 195 ASN A OD1 1 
ATOM   1547 N ND2 . ASN A 1 195 ? 130.524 86.428  84.957  1.00 30.00 ? 195 ASN A ND2 1 
ATOM   1548 N N   . PRO A 1 196 ? 135.449 83.927  85.088  1.00 30.00 ? 196 PRO A N   1 
ATOM   1549 C CA  . PRO A 1 196 ? 136.907 83.929  85.151  1.00 30.00 ? 196 PRO A CA  1 
ATOM   1550 C C   . PRO A 1 196 ? 137.449 85.332  85.445  1.00 30.00 ? 196 PRO A C   1 
ATOM   1551 O O   . PRO A 1 196 ? 138.331 85.443  86.257  1.00 30.00 ? 196 PRO A O   1 
ATOM   1552 C CB  . PRO A 1 196 ? 137.356 83.488  83.753  1.00 30.00 ? 196 PRO A CB  1 
ATOM   1553 C CG  . PRO A 1 196 ? 136.109 82.926  83.106  1.00 30.00 ? 196 PRO A CG  1 
ATOM   1554 C CD  . PRO A 1 196 ? 134.968 83.700  83.727  1.00 30.00 ? 196 PRO A CD  1 
ATOM   1555 N N   . ASP A 1 197 ? 136.902 86.361  84.796  1.00 30.00 ? 197 ASP A N   1 
ATOM   1556 C CA  . ASP A 1 197 ? 137.376 87.759  84.976  1.00 30.00 ? 197 ASP A CA  1 
ATOM   1557 C C   . ASP A 1 197 ? 137.243 88.151  86.448  1.00 30.00 ? 197 ASP A C   1 
ATOM   1558 O O   . ASP A 1 197 ? 138.236 88.652  87.008  1.00 30.00 ? 197 ASP A O   1 
ATOM   1559 C CB  . ASP A 1 197 ? 136.606 88.731  84.079  1.00 30.00 ? 197 ASP A CB  1 
ATOM   1560 C CG  . ASP A 1 197 ? 135.090 88.632  84.141  1.00 30.00 ? 197 ASP A CG  1 
ATOM   1561 O OD1 . ASP A 1 197 ? 134.577 87.764  84.872  1.00 30.00 ? 197 ASP A OD1 1 
ATOM   1562 O OD2 . ASP A 1 197 ? 134.430 89.433  83.453  1.00 30.00 ? 197 ASP A OD2 1 
ATOM   1563 N N   . CYS A 1 198 ? 136.092 87.887  87.065  1.00 30.00 ? 198 CYS A N   1 
ATOM   1564 C CA  . CYS A 1 198 ? 135.837 88.205  88.493  1.00 30.00 ? 198 CYS A CA  1 
ATOM   1565 C C   . CYS A 1 198 ? 136.692 87.274  89.353  1.00 30.00 ? 198 CYS A C   1 
ATOM   1566 O O   . CYS A 1 198 ? 137.200 87.734  90.386  1.00 30.00 ? 198 CYS A O   1 
ATOM   1567 C CB  . CYS A 1 198 ? 134.361 88.040  88.816  1.00 30.00 ? 198 CYS A CB  1 
ATOM   1568 S SG  . CYS A 1 198 ? 133.947 88.511  90.514  1.00 30.00 ? 198 CYS A SG  1 
ATOM   1569 N N   . LYS A 1 199 ? 136.856 86.021  88.929  1.00 30.00 ? 199 LYS A N   1 
ATOM   1570 C CA  . LYS A 1 199 ? 137.679 85.021  89.657  1.00 30.00 ? 199 LYS A CA  1 
ATOM   1571 C C   . LYS A 1 199 ? 139.111 85.546  89.747  1.00 30.00 ? 199 LYS A C   1 
ATOM   1572 O O   . LYS A 1 199 ? 139.702 85.438  90.834  1.00 30.00 ? 199 LYS A O   1 
ATOM   1573 C CB  . LYS A 1 199 ? 137.605 83.688  88.910  1.00 30.00 ? 199 LYS A CB  1 
ATOM   1574 C CG  . LYS A 1 199 ? 138.512 82.580  89.417  1.00 30.00 ? 199 LYS A CG  1 
ATOM   1575 C CD  . LYS A 1 199 ? 138.195 81.254  88.764  1.00 30.00 ? 199 LYS A CD  1 
ATOM   1576 C CE  . LYS A 1 199 ? 138.848 80.071  89.443  1.00 30.00 ? 199 LYS A CE  1 
ATOM   1577 N NZ  . LYS A 1 199 ? 138.362 78.791  88.882  1.00 30.00 ? 199 LYS A NZ  1 
ATOM   1578 N N   . LEU A 1 200 ? 139.631 86.122  88.661  1.00 30.00 ? 200 LEU A N   1 
ATOM   1579 C CA  . LEU A 1 200 ? 141.007 86.680  88.622  1.00 30.00 ? 200 LEU A CA  1 
ATOM   1580 C C   . LEU A 1 200 ? 141.093 87.890  89.553  1.00 30.00 ? 200 LEU A C   1 
ATOM   1581 O O   . LEU A 1 200 ? 142.162 88.083  90.146  1.00 30.00 ? 200 LEU A O   1 
ATOM   1582 C CB  . LEU A 1 200 ? 141.357 87.078  87.187  1.00 30.00 ? 200 LEU A CB  1 
ATOM   1583 C CG  . LEU A 1 200 ? 141.508 85.938  86.179  1.00 30.00 ? 200 LEU A CG  1 
ATOM   1584 C CD1 . LEU A 1 200 ? 142.379 86.372  85.015  1.00 30.00 ? 200 LEU A CD1 1 
ATOM   1585 C CD2 . LEU A 1 200 ? 142.064 84.676  86.822  1.00 30.00 ? 200 LEU A CD2 1 
ATOM   1586 N N   . VAL A 1 201 ? 140.029 88.691  89.647  1.00 30.00 ? 201 VAL A N   1 
ATOM   1587 C CA  . VAL A 1 201 ? 139.995 89.877  90.551  1.00 30.00 ? 201 VAL A CA  1 
ATOM   1588 C C   . VAL A 1 201 ? 140.180 89.381  91.986  1.00 30.00 ? 201 VAL A C   1 
ATOM   1589 O O   . VAL A 1 201 ? 141.025 89.962  92.692  1.00 30.00 ? 201 VAL A O   1 
ATOM   1590 C CB  . VAL A 1 201 ? 138.684 90.668  90.388  1.00 30.00 ? 201 VAL A CB  1 
ATOM   1591 C CG1 . VAL A 1 201 ? 138.468 91.675  91.506  1.00 30.00 ? 201 VAL A CG1 1 
ATOM   1592 C CG2 . VAL A 1 201 ? 138.600 91.349  89.034  1.00 30.00 ? 201 VAL A CG2 1 
ATOM   1593 N N   . LEU A 1 202 ? 139.467 88.321  92.379  1.00 30.00 ? 202 LEU A N   1 
ATOM   1594 C CA  . LEU A 1 202 ? 139.562 87.740  93.746  1.00 30.00 ? 202 LEU A CA  1 
ATOM   1595 C C   . LEU A 1 202 ? 140.960 87.148  93.926  1.00 30.00 ? 202 LEU A C   1 
ATOM   1596 O O   . LEU A 1 202 ? 141.531 87.290  95.027  1.00 30.00 ? 202 LEU A O   1 
ATOM   1597 C CB  . LEU A 1 202 ? 138.491 86.658  93.909  1.00 30.00 ? 202 LEU A CB  1 
ATOM   1598 C CG  . LEU A 1 202 ? 137.048 87.077  93.624  1.00 30.00 ? 202 LEU A CG  1 
ATOM   1599 C CD1 . LEU A 1 202 ? 136.073 86.114  94.276  1.00 30.00 ? 202 LEU A CD1 1 
ATOM   1600 C CD2 . LEU A 1 202 ? 136.764 88.503  94.072  1.00 30.00 ? 202 LEU A CD2 1 
ATOM   1601 N N   . LYS A 1 203 ? 141.489 86.499  92.889  1.00 30.00 ? 203 LYS A N   1 
ATOM   1602 C CA  . LYS A 1 203 ? 142.842 85.886  92.919  1.00 30.00 ? 203 LYS A CA  1 
ATOM   1603 C C   . LYS A 1 203 ? 143.894 86.987  93.050  1.00 30.00 ? 203 LYS A C   1 
ATOM   1604 O O   . LYS A 1 203 ? 144.889 86.762  93.766  1.00 30.00 ? 203 LYS A O   1 
ATOM   1605 C CB  . LYS A 1 203 ? 143.029 85.055  91.652  1.00 30.00 ? 203 LYS A CB  1 
ATOM   1606 C CG  . LYS A 1 203 ? 142.268 83.740  91.651  1.00 30.00 ? 203 LYS A CG  1 
ATOM   1607 C CD  . LYS A 1 203 ? 142.281 83.040  90.320  1.00 30.00 ? 203 LYS A CD  1 
ATOM   1608 C CE  . LYS A 1 203 ? 141.634 81.675  90.378  1.00 30.00 ? 203 LYS A CE  1 
ATOM   1609 N NZ  . LYS A 1 203 ? 142.382 80.738  91.248  1.00 30.00 ? 203 LYS A NZ  1 
ATOM   1610 N N   . GLY A 1 204 ? 143.679 88.131  92.398  1.00 30.00 ? 204 GLY A N   1 
ATOM   1611 C CA  . GLY A 1 204 ? 144.610 89.272  92.461  1.00 30.00 ? 204 GLY A CA  1 
ATOM   1612 C C   . GLY A 1 204 ? 144.712 89.774  93.886  1.00 30.00 ? 204 GLY A C   1 
ATOM   1613 O O   . GLY A 1 204 ? 145.796 90.257  94.264  1.00 30.00 ? 204 GLY A O   1 
ATOM   1614 N N   . LEU A 1 205 ? 143.628 89.655  94.656  1.00 30.00 ? 205 LEU A N   1 
ATOM   1615 C CA  . LEU A 1 205 ? 143.604 90.103  96.072  1.00 30.00 ? 205 LEU A CA  1 
ATOM   1616 C C   . LEU A 1 205 ? 144.646 89.316  96.858  1.00 30.00 ? 205 LEU A C   1 
ATOM   1617 O O   . LEU A 1 205 ? 145.364 89.943  97.661  1.00 30.00 ? 205 LEU A O   1 
ATOM   1618 C CB  . LEU A 1 205 ? 142.219 89.850  96.680  1.00 30.00 ? 205 LEU A CB  1 
ATOM   1619 C CG  . LEU A 1 205 ? 141.011 90.329  95.875  1.00 30.00 ? 205 LEU A CG  1 
ATOM   1620 C CD1 . LEU A 1 205 ? 139.729 90.174  96.673  1.00 30.00 ? 205 LEU A CD1 1 
ATOM   1621 C CD2 . LEU A 1 205 ? 141.177 91.767  95.420  1.00 30.00 ? 205 LEU A CD2 1 
ATOM   1622 N N   . GLY A 1 206 ? 144.723 88.004  96.632  1.00 30.00 ? 206 GLY A N   1 
ATOM   1623 C CA  . GLY A 1 206 ? 145.656 87.135  97.370  1.00 30.00 ? 206 GLY A CA  1 
ATOM   1624 C C   . GLY A 1 206 ? 144.950 85.917  97.927  1.00 30.00 ? 206 GLY A C   1 
ATOM   1625 O O   . GLY A 1 206 ? 144.091 85.374  97.205  1.00 30.00 ? 206 GLY A O   1 
ATOM   1626 N N   . MET A 1 207 ? 145.255 85.524  99.166  1.00 30.00 ? 207 MET A N   1 
ATOM   1627 C CA  . MET A 1 207 ? 144.706 84.289  99.785  1.00 30.00 ? 207 MET A CA  1 
ATOM   1628 C C   . MET A 1 207 ? 143.737 84.630  100.917 1.00 30.00 ? 207 MET A C   1 
ATOM   1629 O O   . MET A 1 207 ? 143.984 85.628  101.616 1.00 30.00 ? 207 MET A O   1 
ATOM   1630 C CB  . MET A 1 207 ? 145.848 83.455  100.368 1.00 30.00 ? 207 MET A CB  1 
ATOM   1631 C CG  . MET A 1 207 ? 146.625 82.666  99.334  1.00 30.00 ? 207 MET A CG  1 
ATOM   1632 S SD  . MET A 1 207 ? 145.652 81.382  98.509  1.00 30.00 ? 207 MET A SD  1 
ATOM   1633 C CE  . MET A 1 207 ? 145.223 82.218  96.984  1.00 30.00 ? 207 MET A CE  1 
ATOM   1634 N N   . ASN A 1 208 ? 142.685 83.828  101.095 1.00 30.00 ? 208 ASN A N   1 
ATOM   1635 C CA  . ASN A 1 208 ? 141.680 84.023  102.173 1.00 30.00 ? 208 ASN A CA  1 
ATOM   1636 C C   . ASN A 1 208 ? 141.120 85.444  102.119 1.00 30.00 ? 208 ASN A C   1 
ATOM   1637 O O   . ASN A 1 208 ? 140.999 86.068  103.185 1.00 30.00 ? 208 ASN A O   1 
ATOM   1638 C CB  . ASN A 1 208 ? 142.270 83.718  103.551 1.00 30.00 ? 208 ASN A CB  1 
ATOM   1639 C CG  . ASN A 1 208 ? 142.736 82.284  103.685 1.00 30.00 ? 208 ASN A CG  1 
ATOM   1640 O OD1 . ASN A 1 208 ? 142.606 81.491  102.756 1.00 30.00 ? 208 ASN A OD1 1 
ATOM   1641 N ND2 . ASN A 1 208 ? 143.268 81.942  104.846 1.00 30.00 ? 208 ASN A ND2 1 
ATOM   1642 N N   . PRO A 1 209 ? 140.743 85.985  100.946 1.00 30.00 ? 209 PRO A N   1 
ATOM   1643 C CA  . PRO A 1 209 ? 140.145 87.305  100.920 1.00 30.00 ? 209 PRO A CA  1 
ATOM   1644 C C   . PRO A 1 209 ? 138.826 87.297  101.702 1.00 30.00 ? 209 PRO A C   1 
ATOM   1645 O O   . PRO A 1 209 ? 138.054 86.396  101.473 1.00 30.00 ? 209 PRO A O   1 
ATOM   1646 C CB  . PRO A 1 209 ? 139.919 87.563  99.428  1.00 30.00 ? 209 PRO A CB  1 
ATOM   1647 C CG  . PRO A 1 209 ? 139.836 86.187  98.819  1.00 30.00 ? 209 PRO A CG  1 
ATOM   1648 C CD  . PRO A 1 209 ? 140.817 85.365  99.624  1.00 30.00 ? 209 PRO A CD  1 
ATOM   1649 N N   . THR A 1 210 ? 138.589 88.274  102.582 1.00 30.00 ? 210 THR A N   1 
ATOM   1650 C CA  . THR A 1 210 ? 137.324 88.390  103.347 1.00 30.00 ? 210 THR A CA  1 
ATOM   1651 C C   . THR A 1 210 ? 136.228 88.738  102.352 1.00 30.00 ? 210 THR A C   1 
ATOM   1652 O O   . THR A 1 210 ? 136.566 89.120  101.224 1.00 30.00 ? 210 THR A O   1 
ATOM   1653 C CB  . THR A 1 210 ? 137.379 89.468  104.428 1.00 30.00 ? 210 THR A CB  1 
ATOM   1654 O OG1 . THR A 1 210 ? 137.496 90.724  103.761 1.00 30.00 ? 210 THR A OG1 1 
ATOM   1655 C CG2 . THR A 1 210 ? 138.521 89.275  105.400 1.00 30.00 ? 210 THR A CG2 1 
ATOM   1656 N N   . LEU A 1 211 ? 134.971 88.573  102.727 1.00 30.00 ? 211 LEU A N   1 
ATOM   1657 C CA  . LEU A 1 211 ? 133.867 88.804  101.773 1.00 30.00 ? 211 LEU A CA  1 
ATOM   1658 C C   . LEU A 1 211 ? 133.746 90.286  101.474 1.00 30.00 ? 211 LEU A C   1 
ATOM   1659 O O   . LEU A 1 211 ? 133.463 90.627  100.335 1.00 30.00 ? 211 LEU A O   1 
ATOM   1660 C CB  . LEU A 1 211 ? 132.570 88.237  102.352 1.00 30.00 ? 211 LEU A CB  1 
ATOM   1661 C CG  . LEU A 1 211 ? 131.340 88.327  101.452 1.00 30.00 ? 211 LEU A CG  1 
ATOM   1662 C CD1 . LEU A 1 211 ? 131.482 87.429  100.236 1.00 30.00 ? 211 LEU A CD1 1 
ATOM   1663 C CD2 . LEU A 1 211 ? 130.093 87.959  102.233 1.00 30.00 ? 211 LEU A CD2 1 
ATOM   1664 N N   . GLU A 1 212 ? 133.972 91.121  102.469 1.00 30.00 ? 212 GLU A N   1 
ATOM   1665 C CA  . GLU A 1 212 ? 133.880 92.580  102.272 1.00 30.00 ? 212 GLU A CA  1 
ATOM   1666 C C   . GLU A 1 212 ? 134.907 92.893  101.194 1.00 30.00 ? 212 GLU A C   1 
ATOM   1667 O O   . GLU A 1 212 ? 134.558 93.587  100.234 1.00 30.00 ? 212 GLU A O   1 
ATOM   1668 C CB  . GLU A 1 212 ? 134.130 93.266  103.610 1.00 30.00 ? 212 GLU A CB  1 
ATOM   1669 C CG  . GLU A 1 212 ? 133.158 92.813  104.687 1.00 30.00 ? 212 GLU A CG  1 
ATOM   1670 C CD  . GLU A 1 212 ? 133.531 93.207  106.103 1.00 30.00 ? 212 GLU A CD  1 
ATOM   1671 O OE1 . GLU A 1 212 ? 133.631 94.413  106.363 1.00 30.00 ? 212 GLU A OE1 1 
ATOM   1672 O OE2 . GLU A 1 212 ? 133.719 92.301  106.938 1.00 30.00 ? 212 GLU A OE2 1 
ATOM   1673 N N   . GLU A 1 213 ? 136.087 92.291  101.291 1.00 30.00 ? 213 GLU A N   1 
ATOM   1674 C CA  . GLU A 1 213 ? 137.185 92.538  100.330 1.00 30.00 ? 213 GLU A CA  1 
ATOM   1675 C C   . GLU A 1 213 ? 136.764 92.055  98.949  1.00 30.00 ? 213 GLU A C   1 
ATOM   1676 O O   . GLU A 1 213 ? 136.889 92.835  97.998  1.00 30.00 ? 213 GLU A O   1 
ATOM   1677 C CB  . GLU A 1 213 ? 138.423 91.799  100.823 1.00 30.00 ? 213 GLU A CB  1 
ATOM   1678 C CG  . GLU A 1 213 ? 139.683 92.096  100.043 1.00 30.00 ? 213 GLU A CG  1 
ATOM   1679 C CD  . GLU A 1 213 ? 140.936 91.570  100.720 1.00 30.00 ? 213 GLU A CD  1 
ATOM   1680 O OE1 . GLU A 1 213 ? 141.207 91.993  101.861 1.00 30.00 ? 213 GLU A OE1 1 
ATOM   1681 O OE2 . GLU A 1 213 ? 141.633 90.732  100.115 1.00 30.00 ? 213 GLU A OE2 1 
ATOM   1682 N N   . MET A 1 214 ? 136.225 90.848  98.851  1.00 30.00 ? 214 MET A N   1 
ATOM   1683 C CA  . MET A 1 214 ? 135.866 90.249  97.544  1.00 30.00 ? 214 MET A CA  1 
ATOM   1684 C C   . MET A 1 214 ? 134.679 90.988  96.954  1.00 30.00 ? 214 MET A C   1 
ATOM   1685 O O   . MET A 1 214 ? 134.719 91.286  95.759  1.00 30.00 ? 214 MET A O   1 
ATOM   1686 C CB  . MET A 1 214 ? 135.482 88.783  97.727  1.00 30.00 ? 214 MET A CB  1 
ATOM   1687 C CG  . MET A 1 214 ? 136.678 87.860  97.827  1.00 30.00 ? 214 MET A CG  1 
ATOM   1688 S SD  . MET A 1 214 ? 136.264 86.118  98.125  1.00 30.00 ? 214 MET A SD  1 
ATOM   1689 C CE  . MET A 1 214 ? 134.934 86.255  99.317  1.00 30.00 ? 214 MET A CE  1 
ATOM   1690 N N   . LEU A 1 215 ? 133.690 91.310  97.768  1.00 30.00 ? 215 LEU A N   1 
ATOM   1691 C CA  . LEU A 1 215 ? 132.435 91.914  97.272  1.00 30.00 ? 215 LEU A CA  1 
ATOM   1692 C C   . LEU A 1 215 ? 132.770 93.312  96.763  1.00 30.00 ? 215 LEU A C   1 
ATOM   1693 O O   . LEU A 1 215 ? 132.195 93.703  95.737  1.00 30.00 ? 215 LEU A O   1 
ATOM   1694 C CB  . LEU A 1 215 ? 131.430 91.900  98.423  1.00 30.00 ? 215 LEU A CB  1 
ATOM   1695 C CG  . LEU A 1 215 ? 129.962 92.054  98.048  1.00 30.00 ? 215 LEU A CG  1 
ATOM   1696 C CD1 . LEU A 1 215 ? 129.467 90.839  97.283  1.00 30.00 ? 215 LEU A CD1 1 
ATOM   1697 C CD2 . LEU A 1 215 ? 129.127 92.255  99.299  1.00 30.00 ? 215 LEU A CD2 1 
ATOM   1698 N N   . THR A 1 216 ? 133.674 94.025  97.433  1.00 30.00 ? 216 THR A N   1 
ATOM   1699 C CA  . THR A 1 216 ? 134.111 95.385  97.021  1.00 30.00 ? 216 THR A CA  1 
ATOM   1700 C C   . THR A 1 216 ? 134.960 95.302  95.760  1.00 30.00 ? 216 THR A C   1 
ATOM   1701 O O   . THR A 1 216 ? 134.736 96.115  94.853  1.00 30.00 ? 216 THR A O   1 
ATOM   1702 C CB  . THR A 1 216 ? 134.947 96.046  98.117  1.00 30.00 ? 216 THR A CB  1 
ATOM   1703 O OG1 . THR A 1 216 ? 134.133 96.165  99.281  1.00 30.00 ? 216 THR A OG1 1 
ATOM   1704 C CG2 . THR A 1 216 ? 135.467 97.412  97.729  1.00 30.00 ? 216 THR A CG2 1 
ATOM   1705 N N   . ALA A 1 217 ? 135.870 94.339  95.690  1.00 30.00 ? 217 ALA A N   1 
ATOM   1706 C CA  . ALA A 1 217 ? 136.836 94.215  94.580  1.00 30.00 ? 217 ALA A CA  1 
ATOM   1707 C C   . ALA A 1 217 ? 136.161 93.920  93.245  1.00 30.00 ? 217 ALA A C   1 
ATOM   1708 O O   . ALA A 1 217 ? 136.594 94.505  92.248  1.00 30.00 ? 217 ALA A O   1 
ATOM   1709 C CB  . ALA A 1 217 ? 137.795 93.119  94.920  1.00 30.00 ? 217 ALA A CB  1 
ATOM   1710 N N   . CYS A 1 218 ? 135.150 93.065  93.213  1.00 30.00 ? 218 CYS A N   1 
ATOM   1711 C CA  . CYS A 1 218 ? 134.527 92.632  91.938  1.00 30.00 ? 218 CYS A CA  1 
ATOM   1712 C C   . CYS A 1 218 ? 133.316 93.517  91.663  1.00 30.00 ? 218 CYS A C   1 
ATOM   1713 O O   . CYS A 1 218 ? 132.521 93.168  90.777  1.00 30.00 ? 218 CYS A O   1 
ATOM   1714 C CB  . CYS A 1 218 ? 134.139 91.161  91.991  1.00 30.00 ? 218 CYS A CB  1 
ATOM   1715 S SG  . CYS A 1 218 ? 133.553 90.502  90.408  1.00 30.00 ? 218 CYS A SG  1 
ATOM   1716 N N   . GLN A 1 219 ? 133.200 94.637  92.371  1.00 30.00 ? 219 GLN A N   1 
ATOM   1717 C CA  . GLN A 1 219 ? 132.092 95.589  92.127  1.00 30.00 ? 219 GLN A CA  1 
ATOM   1718 C C   . GLN A 1 219 ? 132.376 96.293  90.802  1.00 30.00 ? 219 GLN A C   1 
ATOM   1719 O O   . GLN A 1 219 ? 133.378 97.026  90.739  1.00 30.00 ? 219 GLN A O   1 
ATOM   1720 C CB  . GLN A 1 219 ? 131.989 96.582  93.282  1.00 30.00 ? 219 GLN A CB  1 
ATOM   1721 C CG  . GLN A 1 219 ? 130.804 97.526  93.172  1.00 30.00 ? 219 GLN A CG  1 
ATOM   1722 C CD  . GLN A 1 219 ? 130.654 98.390  94.399  1.00 30.00 ? 219 GLN A CD  1 
ATOM   1723 O OE1 . GLN A 1 219 ? 131.427 98.297  95.350  1.00 30.00 ? 219 GLN A OE1 1 
ATOM   1724 N NE2 . GLN A 1 219 ? 129.643 99.243  94.389  1.00 30.00 ? 219 GLN A NE2 1 
ATOM   1725 N N   . GLY A 1 220 ? 131.542 96.067  89.783  1.00 30.00 ? 220 GLY A N   1 
ATOM   1726 C CA  . GLY A 1 220 ? 131.703 96.697  88.458  1.00 30.00 ? 220 GLY A CA  1 
ATOM   1727 C C   . GLY A 1 220 ? 132.508 95.843  87.495  1.00 30.00 ? 220 GLY A C   1 
ATOM   1728 O O   . GLY A 1 220 ? 132.797 96.341  86.394  1.00 30.00 ? 220 GLY A O   1 
ATOM   1729 N N   . VAL A 1 221 ? 132.850 94.607  87.864  1.00 30.00 ? 221 VAL A N   1 
ATOM   1730 C CA  . VAL A 1 221 ? 133.686 93.700  87.022  1.00 30.00 ? 221 VAL A CA  1 
ATOM   1731 C C   . VAL A 1 221 ? 132.759 92.814  86.186  1.00 30.00 ? 221 VAL A C   1 
ATOM   1732 O O   . VAL A 1 221 ? 132.246 93.329  85.178  1.00 30.00 ? 221 VAL A O   1 
ATOM   1733 C CB  . VAL A 1 221 ? 134.632 92.857  87.898  1.00 30.00 ? 221 VAL A CB  1 
ATOM   1734 C CG1 . VAL A 1 221 ? 135.409 91.826  87.093  1.00 30.00 ? 221 VAL A CG1 1 
ATOM   1735 C CG2 . VAL A 1 221 ? 135.578 93.731  88.704  1.00 30.00 ? 221 VAL A CG2 1 
ATOM   1736 N N   . SER B 2 2   ? 89.322  59.296  109.470 1.00 30.00 ? 2   SER B N   1 
ATOM   1737 C CA  . SER B 2 2   ? 89.775  59.765  110.802 1.00 30.00 ? 2   SER B CA  1 
ATOM   1738 C C   . SER B 2 2   ? 89.455  61.254  110.977 1.00 30.00 ? 2   SER B C   1 
ATOM   1739 O O   . SER B 2 2   ? 88.293  61.550  111.299 1.00 30.00 ? 2   SER B O   1 
ATOM   1740 C CB  . SER B 2 2   ? 91.236  59.467  110.973 1.00 30.00 ? 2   SER B CB  1 
ATOM   1741 O OG  . SER B 2 2   ? 91.711  59.950  112.220 1.00 30.00 ? 2   SER B OG  1 
ATOM   1742 N N   . GLY B 2 3   ? 90.418  62.161  110.784 1.00 30.00 ? 3   GLY B N   1 
ATOM   1743 C CA  . GLY B 2 3   ? 90.203  63.608  110.954 1.00 30.00 ? 3   GLY B CA  1 
ATOM   1744 C C   . GLY B 2 3   ? 90.995  64.431  109.964 1.00 30.00 ? 3   GLY B C   1 
ATOM   1745 O O   . GLY B 2 3   ? 91.743  63.830  109.179 1.00 30.00 ? 3   GLY B O   1 
ATOM   1746 N N   . VAL B 2 4   ? 90.851  65.754  110.006 1.00 30.00 ? 4   VAL B N   1 
ATOM   1747 C CA  . VAL B 2 4   ? 91.624  66.691  109.146 1.00 30.00 ? 4   VAL B CA  1 
ATOM   1748 C C   . VAL B 2 4   ? 92.679  67.302  110.063 1.00 30.00 ? 4   VAL B C   1 
ATOM   1749 O O   . VAL B 2 4   ? 93.045  68.455  109.832 1.00 30.00 ? 4   VAL B O   1 
ATOM   1750 C CB  . VAL B 2 4   ? 90.740  67.757  108.477 1.00 30.00 ? 4   VAL B CB  1 
ATOM   1751 C CG1 . VAL B 2 4   ? 89.842  67.143  107.424 1.00 30.00 ? 4   VAL B CG1 1 
ATOM   1752 C CG2 . VAL B 2 4   ? 89.917  68.554  109.474 1.00 30.00 ? 4   VAL B CG2 1 
ATOM   1753 N N   . PHE B 2 5   ? 93.087  66.579  111.106 1.00 30.00 ? 5   PHE B N   1 
ATOM   1754 C CA  . PHE B 2 5   ? 94.134  67.026  112.056 1.00 30.00 ? 5   PHE B CA  1 
ATOM   1755 C C   . PHE B 2 5   ? 95.319  66.068  111.948 1.00 30.00 ? 5   PHE B C   1 
ATOM   1756 O O   . PHE B 2 5   ? 95.344  65.077  112.696 1.00 30.00 ? 5   PHE B O   1 
ATOM   1757 C CB  . PHE B 2 5   ? 93.576  67.063  113.477 1.00 30.00 ? 5   PHE B CB  1 
ATOM   1758 C CG  . PHE B 2 5   ? 92.381  67.959  113.671 1.00 30.00 ? 5   PHE B CG  1 
ATOM   1759 C CD1 . PHE B 2 5   ? 92.455  69.316  113.408 1.00 30.00 ? 5   PHE B CD1 1 
ATOM   1760 C CD2 . PHE B 2 5   ? 91.183  67.442  114.132 1.00 30.00 ? 5   PHE B CD2 1 
ATOM   1761 C CE1 . PHE B 2 5   ? 91.352  70.133  113.596 1.00 30.00 ? 5   PHE B CE1 1 
ATOM   1762 C CE2 . PHE B 2 5   ? 90.082  68.261  114.318 1.00 30.00 ? 5   PHE B CE2 1 
ATOM   1763 C CZ  . PHE B 2 5   ? 90.171  69.604  114.052 1.00 30.00 ? 5   PHE B CZ  1 
ATOM   1764 N N   . THR B 2 6   ? 96.271  66.347  111.055 1.00 30.00 ? 6   THR B N   1 
ATOM   1765 C CA  . THR B 2 6   ? 97.484  65.509  110.860 1.00 30.00 ? 6   THR B CA  1 
ATOM   1766 C C   . THR B 2 6   ? 98.273  65.490  112.167 1.00 30.00 ? 6   THR B C   1 
ATOM   1767 O O   . THR B 2 6   ? 98.791  64.415  112.510 1.00 30.00 ? 6   THR B O   1 
ATOM   1768 C CB  . THR B 2 6   ? 98.340  66.014  109.690 1.00 30.00 ? 6   THR B CB  1 
ATOM   1769 O OG1 . THR B 2 6   ? 99.542  65.244  109.669 1.00 30.00 ? 6   THR B OG1 1 
ATOM   1770 C CG2 . THR B 2 6   ? 98.697  67.481  109.776 1.00 30.00 ? 6   THR B CG2 1 
ATOM   1771 N N   . PHE B 2 7   ? 98.338  66.615  112.878 1.00 30.00 ? 7   PHE B N   1 
ATOM   1772 C CA  . PHE B 2 7   ? 99.106  66.751  114.137 1.00 30.00 ? 7   PHE B CA  1 
ATOM   1773 C C   . PHE B 2 7   ? 98.128  66.795  115.305 1.00 30.00 ? 7   PHE B C   1 
ATOM   1774 O O   . PHE B 2 7   ? 97.024  67.316  115.122 1.00 30.00 ? 7   PHE B O   1 
ATOM   1775 C CB  . PHE B 2 7   ? 99.937  68.031  114.100 1.00 30.00 ? 7   PHE B CB  1 
ATOM   1776 C CG  . PHE B 2 7   ? 100.905 68.118  112.953 1.00 30.00 ? 7   PHE B CG  1 
ATOM   1777 C CD1 . PHE B 2 7   ? 101.955 67.225  112.840 1.00 30.00 ? 7   PHE B CD1 1 
ATOM   1778 C CD2 . PHE B 2 7   ? 100.741 69.072  111.966 1.00 30.00 ? 7   PHE B CD2 1 
ATOM   1779 C CE1 . PHE B 2 7   ? 102.835 67.303  111.775 1.00 30.00 ? 7   PHE B CE1 1 
ATOM   1780 C CE2 . PHE B 2 7   ? 101.613 69.137  110.893 1.00 30.00 ? 7   PHE B CE2 1 
ATOM   1781 C CZ  . PHE B 2 7   ? 102.662 68.258  110.804 1.00 30.00 ? 7   PHE B CZ  1 
ATOM   1782 N N   . GLY B 2 8   ? 98.482  66.208  116.443 1.00 30.00 ? 8   GLY B N   1 
ATOM   1783 C CA  . GLY B 2 8   ? 97.640  66.298  117.648 1.00 30.00 ? 8   GLY B CA  1 
ATOM   1784 C C   . GLY B 2 8   ? 96.604  65.201  117.708 1.00 30.00 ? 8   GLY B C   1 
ATOM   1785 O O   . GLY B 2 8   ? 96.817  64.171  117.048 1.00 30.00 ? 8   GLY B O   1 
ATOM   1786 N N   . ALA B 2 9   ? 95.518  65.413  118.452 1.00 30.00 ? 9   ALA B N   1 
ATOM   1787 C CA  . ALA B 2 9   ? 94.450  64.408  118.631 1.00 30.00 ? 9   ALA B CA  1 
ATOM   1788 C C   . ALA B 2 9   ? 93.466  64.486  117.462 1.00 30.00 ? 9   ALA B C   1 
ATOM   1789 O O   . ALA B 2 9   ? 93.415  63.503  116.698 1.00 30.00 ? 9   ALA B O   1 
ATOM   1790 C CB  . ALA B 2 9   ? 93.758  64.654  119.942 1.00 30.00 ? 9   ALA B CB  1 
HETATM 1791 C C1  . IHP C 3 .   ? 94.910  96.787  118.837 0.17 20.00 ? 301 IHP A C1  1 
HETATM 1792 C C2  . IHP C 3 .   ? 95.276  95.339  119.111 0.17 20.00 ? 301 IHP A C2  1 
HETATM 1793 C C3  . IHP C 3 .   ? 96.792  95.192  119.127 0.17 20.00 ? 301 IHP A C3  1 
HETATM 1794 C C4  . IHP C 3 .   ? 97.460  96.177  120.076 0.17 20.00 ? 301 IHP A C4  1 
HETATM 1795 C C5  . IHP C 3 .   ? 96.960  97.599  119.888 0.17 20.00 ? 301 IHP A C5  1 
HETATM 1796 C C6  . IHP C 3 .   ? 95.452  97.631  119.972 0.17 20.00 ? 301 IHP A C6  1 
HETATM 1797 O O11 . IHP C 3 .   ? 93.457  96.960  118.734 0.17 20.00 ? 301 IHP A O11 1 
HETATM 1798 P P1  . IHP C 3 .   ? 92.301  96.750  119.843 0.17 20.00 ? 301 IHP A P1  1 
HETATM 1799 O O21 . IHP C 3 .   ? 92.102  95.262  120.046 0.17 20.00 ? 301 IHP A O21 1 
HETATM 1800 O O31 . IHP C 3 .   ? 92.729  97.445  121.120 0.17 20.00 ? 301 IHP A O31 1 
HETATM 1801 O O41 . IHP C 3 .   ? 91.081  97.406  119.230 0.17 20.00 ? 301 IHP A O41 1 
HETATM 1802 O O12 . IHP C 3 .   ? 94.731  94.998  120.430 0.17 20.00 ? 301 IHP A O12 1 
HETATM 1803 P P2  . IHP C 3 .   ? 94.448  93.558  121.106 0.17 20.00 ? 301 IHP A P2  1 
HETATM 1804 O O22 . IHP C 3 .   ? 95.746  92.916  121.547 0.17 20.00 ? 301 IHP A O22 1 
HETATM 1805 O O32 . IHP C 3 .   ? 93.733  92.741  120.050 0.17 20.00 ? 301 IHP A O32 1 
HETATM 1806 O O42 . IHP C 3 .   ? 93.546  93.866  122.284 0.17 20.00 ? 301 IHP A O42 1 
HETATM 1807 O O13 . IHP C 3 .   ? 97.147  93.843  119.575 0.17 20.00 ? 301 IHP A O13 1 
HETATM 1808 P P3  . IHP C 3 .   ? 97.050  92.455  118.755 0.17 20.00 ? 301 IHP A P3  1 
HETATM 1809 O O23 . IHP C 3 .   ? 98.121  92.500  117.686 0.17 20.00 ? 301 IHP A O23 1 
HETATM 1810 O O33 . IHP C 3 .   ? 95.660  92.354  118.166 0.17 20.00 ? 301 IHP A O33 1 
HETATM 1811 O O43 . IHP C 3 .   ? 97.312  91.360  119.767 0.17 20.00 ? 301 IHP A O43 1 
HETATM 1812 O O14 . IHP C 3 .   ? 98.904  96.186  119.828 0.17 20.00 ? 301 IHP A O14 1 
HETATM 1813 P P4  . IHP C 3 .   ? 99.924  94.950  119.982 0.17 20.00 ? 301 IHP A P4  1 
HETATM 1814 O O24 . IHP C 3 .   ? 99.894  94.177  118.684 0.17 20.00 ? 301 IHP A O24 1 
HETATM 1815 O O34 . IHP C 3 .   ? 99.430  94.124  121.155 0.17 20.00 ? 301 IHP A O34 1 
HETATM 1816 O O44 . IHP C 3 .   ? 101.283 95.561  120.249 0.17 20.00 ? 301 IHP A O44 1 
HETATM 1817 O O15 . IHP C 3 .   ? 97.480  98.466  120.947 0.17 20.00 ? 301 IHP A O15 1 
HETATM 1818 P P5  . IHP C 3 .   ? 99.034  98.792  121.215 0.17 20.00 ? 301 IHP A P5  1 
HETATM 1819 O O25 . IHP C 3 .   ? 99.654  97.604  121.926 0.17 20.00 ? 301 IHP A O25 1 
HETATM 1820 O O35 . IHP C 3 .   ? 99.039  100.041 122.072 0.17 20.00 ? 301 IHP A O35 1 
HETATM 1821 O O45 . IHP C 3 .   ? 99.649  99.029  119.849 0.17 20.00 ? 301 IHP A O45 1 
HETATM 1822 O O16 . IHP C 3 .   ? 94.970  99.014  119.903 0.17 20.00 ? 301 IHP A O16 1 
HETATM 1823 P P6  . IHP C 3 .   ? 95.021  100.042 118.665 0.17 20.00 ? 301 IHP A P6  1 
HETATM 1824 O O26 . IHP C 3 .   ? 96.446  100.094 118.153 0.17 20.00 ? 301 IHP A O26 1 
HETATM 1825 O O36 . IHP C 3 .   ? 94.037  99.512  117.642 0.17 20.00 ? 301 IHP A O36 1 
HETATM 1826 O O46 . IHP C 3 .   ? 94.583  101.375 119.233 0.17 20.00 ? 301 IHP A O46 1 
HETATM 1827 C C1  . IHP D 3 .   ? 96.555  97.251  107.197 0.17 20.00 ? 302 IHP A C1  1 
HETATM 1828 C C2  . IHP D 3 .   ? 95.119  96.802  107.378 0.17 20.00 ? 302 IHP A C2  1 
HETATM 1829 C C3  . IHP D 3 .   ? 94.987  95.323  107.082 0.17 20.00 ? 302 IHP A C3  1 
HETATM 1830 C C4  . IHP D 3 .   ? 95.881  94.516  108.006 0.17 20.00 ? 302 IHP A C4  1 
HETATM 1831 C C5  . IHP D 3 .   ? 97.329  94.969  107.945 0.17 20.00 ? 302 IHP A C5  1 
HETATM 1832 C C6  . IHP D 3 .   ? 97.492  96.472  108.101 0.17 20.00 ? 302 IHP A C6  1 
HETATM 1833 O O11 . IHP D 3 .   ? 96.623  98.682  107.506 0.17 20.00 ? 302 IHP A O11 1 
HETATM 1834 P P1  . IHP D 3 .   ? 97.945  99.593  107.668 0.17 20.00 ? 302 IHP A P1  1 
HETATM 1835 O O21 . IHP D 3 .   ? 97.452  101.028 107.675 0.17 20.00 ? 302 IHP A O21 1 
HETATM 1836 O O31 . IHP D 3 .   ? 98.590  99.216  108.989 0.17 20.00 ? 302 IHP A O31 1 
HETATM 1837 O O41 . IHP D 3 .   ? 98.842  99.299  106.481 0.17 20.00 ? 302 IHP A O41 1 
HETATM 1838 O O12 . IHP D 3 .   ? 94.693  96.987  108.768 0.17 20.00 ? 302 IHP A O12 1 
HETATM 1839 P P2  . IHP D 3 .   ? 94.617  98.362  109.599 0.17 20.00 ? 302 IHP A P2  1 
HETATM 1840 O O22 . IHP D 3 .   ? 94.146  99.443  108.649 0.17 20.00 ? 302 IHP A O22 1 
HETATM 1841 O O32 . IHP D 3 .   ? 95.980  98.650  110.195 0.17 20.00 ? 302 IHP A O32 1 
HETATM 1842 O O42 . IHP D 3 .   ? 93.584  98.061  110.663 0.17 20.00 ? 302 IHP A O42 1 
HETATM 1843 O O13 . IHP D 3 .   ? 93.600  94.927  107.332 0.17 20.00 ? 302 IHP A O13 1 
HETATM 1844 P P3  . IHP D 3 .   ? 92.318  95.566  106.596 0.17 20.00 ? 302 IHP A P3  1 
HETATM 1845 O O23 . IHP D 3 .   ? 91.146  94.662  106.931 0.17 20.00 ? 302 IHP A O23 1 
HETATM 1846 O O33 . IHP D 3 .   ? 92.644  95.567  105.116 0.17 20.00 ? 302 IHP A O33 1 
HETATM 1847 O O43 . IHP D 3 .   ? 92.121  96.967  107.146 0.17 20.00 ? 302 IHP A O43 1 
HETATM 1848 O O14 . IHP D 3 .   ? 95.834  93.107  107.605 0.17 20.00 ? 302 IHP A O14 1 
HETATM 1849 P P4  . IHP D 3 .   ? 94.545  92.141  107.704 0.17 20.00 ? 302 IHP A P4  1 
HETATM 1850 O O24 . IHP D 3 .   ? 93.624  92.432  106.535 0.17 20.00 ? 302 IHP A O24 1 
HETATM 1851 O O34 . IHP D 3 .   ? 93.898  92.477  109.036 0.17 20.00 ? 302 IHP A O34 1 
HETATM 1852 O O44 . IHP D 3 .   ? 95.081  90.724  107.670 0.17 20.00 ? 302 IHP A O44 1 
HETATM 1853 O O15 . IHP D 3 .   ? 98.063  94.348  109.050 0.17 20.00 ? 302 IHP A O15 1 
HETATM 1854 P P5  . IHP D 3 .   ? 98.219  92.773  109.348 0.17 20.00 ? 302 IHP A P5  1 
HETATM 1855 O O25 . IHP D 3 .   ? 99.370  92.662  110.328 0.17 20.00 ? 302 IHP A O25 1 
HETATM 1856 O O35 . IHP D 3 .   ? 98.519  92.096  108.025 0.17 20.00 ? 302 IHP A O35 1 
HETATM 1857 O O45 . IHP D 3 .   ? 96.917  92.301  109.960 0.17 20.00 ? 302 IHP A O45 1 
HETATM 1858 O O16 . IHP D 3 .   ? 98.863  96.828  107.728 0.17 20.00 ? 302 IHP A O16 1 
HETATM 1859 P P6  . IHP D 3 .   ? 100.221 96.212  108.340 0.17 20.00 ? 302 IHP A P6  1 
HETATM 1860 O O26 . IHP D 3 .   ? 100.062 96.214  109.848 0.17 20.00 ? 302 IHP A O26 1 
HETATM 1861 O O36 . IHP D 3 .   ? 100.403 94.817  107.773 0.17 20.00 ? 302 IHP A O36 1 
HETATM 1862 O O46 . IHP D 3 .   ? 101.316 97.156  107.883 0.17 20.00 ? 302 IHP A O46 1 
# 
