data_9CNS
# 
_entry.id   9CNS 
# 
_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   9CNS         pdb_00009cns 10.2210/pdb9cns/pdb 
WWPDB D_1000285865 ?            ?                   
EMDB  EMD-45758    ?            ?                   
# 
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                        9CNS 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB 'EM map of HIV-2 CA assembled into an icosahedron via micelle-templating.' EMD-45676 'other EM volume'      
PDB  'Atomic model of HIV-2 CA as assembled into an icosahedral particle.'      4CLJ      unspecified            
EMDB 'HIV-2 CA hexamer; assembled via liposome templating'                      EMD-45758 '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 3 ? ? ? 
;HIV-2 GL-AN capsid protein with C-terminal Gly-Ser-Ser linker to hexahistidine tag following proteolytic cleavage of the N-terminal Met.
;
2 non-polymer syn 'INOSITOL HEXAKISPHOSPHATE' 660.035   2 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        CA 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;PVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINDEAADW
DAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEP
FQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLMGSSHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINDEAADW
DAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEP
FQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLMGSSHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_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 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   240 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 gag-pol 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    GL-AN 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Human immunodeficiency virus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     11709 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                     ?                                                                      
'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                    ?                                                                      
'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ?                                                                      
'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ?                                                                      
'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                    ?                                                                      
'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ?                                                                      
'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ?                                                                      
'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                     ?                                                                      
'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                   ?                                                                      
'C6 H10 N3 O2 1' 156.162 
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 1 1   PRO 1   1   ?   ?   ?   B . n 
B 1 2   VAL 2   2   ?   ?   ?   B . n 
B 1 3   GLN 3   3   ?   ?   ?   B . n 
B 1 4   GLN 4   4   ?   ?   ?   B . n 
B 1 5   THR 5   5   ?   ?   ?   B . n 
B 1 6   GLY 6   6   ?   ?   ?   B . n 
B 1 7   GLY 7   7   ?   ?   ?   B . n 
B 1 8   GLY 8   8   ?   ?   ?   B . n 
B 1 9   ASN 9   9   ?   ?   ?   B . n 
B 1 10  TYR 10  10  ?   ?   ?   B . n 
B 1 11  ILE 11  11  ?   ?   ?   B . n 
B 1 12  HIS 12  12  ?   ?   ?   B . n 
B 1 13  VAL 13  13  ?   ?   ?   B . n 
B 1 14  PRO 14  14  ?   ?   ?   B . n 
B 1 15  LEU 15  15  ?   ?   ?   B . n 
B 1 16  SER 16  16  ?   ?   ?   B . n 
B 1 17  PRO 17  17  ?   ?   ?   B . n 
B 1 18  ARG 18  18  ?   ?   ?   B . n 
B 1 19  THR 19  19  ?   ?   ?   B . n 
B 1 20  LEU 20  20  ?   ?   ?   B . n 
B 1 21  ASN 21  21  ?   ?   ?   B . n 
B 1 22  ALA 22  22  ?   ?   ?   B . n 
B 1 23  TRP 23  23  ?   ?   ?   B . n 
B 1 24  VAL 24  24  ?   ?   ?   B . n 
B 1 25  LYS 25  25  ?   ?   ?   B . n 
B 1 26  LEU 26  26  ?   ?   ?   B . n 
B 1 27  VAL 27  27  ?   ?   ?   B . n 
B 1 28  GLU 28  28  ?   ?   ?   B . n 
B 1 29  ASP 29  29  ?   ?   ?   B . n 
B 1 30  LYS 30  30  ?   ?   ?   B . n 
B 1 31  LYS 31  31  ?   ?   ?   B . n 
B 1 32  PHE 32  32  ?   ?   ?   B . n 
B 1 33  GLY 33  33  ?   ?   ?   B . n 
B 1 34  ALA 34  34  ?   ?   ?   B . n 
B 1 35  GLU 35  35  ?   ?   ?   B . n 
B 1 36  VAL 36  36  ?   ?   ?   B . n 
B 1 37  VAL 37  37  ?   ?   ?   B . n 
B 1 38  PRO 38  38  ?   ?   ?   B . n 
B 1 39  GLY 39  39  ?   ?   ?   B . n 
B 1 40  PHE 40  40  ?   ?   ?   B . n 
B 1 41  GLN 41  41  ?   ?   ?   B . n 
B 1 42  ALA 42  42  ?   ?   ?   B . n 
B 1 43  LEU 43  43  ?   ?   ?   B . n 
B 1 44  SER 44  44  ?   ?   ?   B . n 
B 1 45  GLU 45  45  ?   ?   ?   B . n 
B 1 46  GLY 46  46  ?   ?   ?   B . n 
B 1 47  CYS 47  47  ?   ?   ?   B . n 
B 1 48  THR 48  48  ?   ?   ?   B . n 
B 1 49  PRO 49  49  ?   ?   ?   B . n 
B 1 50  TYR 50  50  ?   ?   ?   B . n 
B 1 51  ASP 51  51  ?   ?   ?   B . n 
B 1 52  ILE 52  52  ?   ?   ?   B . n 
B 1 53  ASN 53  53  ?   ?   ?   B . n 
B 1 54  GLN 54  54  ?   ?   ?   B . n 
B 1 55  MET 55  55  ?   ?   ?   B . n 
B 1 56  LEU 56  56  ?   ?   ?   B . n 
B 1 57  ASN 57  57  ?   ?   ?   B . n 
B 1 58  CYS 58  58  ?   ?   ?   B . n 
B 1 59  VAL 59  59  ?   ?   ?   B . n 
B 1 60  GLY 60  60  ?   ?   ?   B . n 
B 1 61  ASP 61  61  ?   ?   ?   B . n 
B 1 62  HIS 62  62  ?   ?   ?   B . n 
B 1 63  GLN 63  63  ?   ?   ?   B . n 
B 1 64  ALA 64  64  ?   ?   ?   B . n 
B 1 65  ALA 65  65  ?   ?   ?   B . n 
B 1 66  MET 66  66  ?   ?   ?   B . n 
B 1 67  GLN 67  67  ?   ?   ?   B . n 
B 1 68  ILE 68  68  ?   ?   ?   B . n 
B 1 69  ILE 69  69  ?   ?   ?   B . n 
B 1 70  ARG 70  70  ?   ?   ?   B . n 
B 1 71  GLU 71  71  ?   ?   ?   B . n 
B 1 72  ILE 72  72  ?   ?   ?   B . n 
B 1 73  ILE 73  73  ?   ?   ?   B . n 
B 1 74  ASN 74  74  ?   ?   ?   B . n 
B 1 75  ASP 75  75  ?   ?   ?   B . n 
B 1 76  GLU 76  76  ?   ?   ?   B . n 
B 1 77  ALA 77  77  ?   ?   ?   B . n 
B 1 78  ALA 78  78  ?   ?   ?   B . n 
B 1 79  ASP 79  79  ?   ?   ?   B . n 
B 1 80  TRP 80  80  ?   ?   ?   B . n 
B 1 81  ASP 81  81  ?   ?   ?   B . n 
B 1 82  ALA 82  82  ?   ?   ?   B . n 
B 1 83  GLN 83  83  ?   ?   ?   B . n 
B 1 84  HIS 84  84  ?   ?   ?   B . n 
B 1 85  PRO 85  85  ?   ?   ?   B . n 
B 1 86  ILE 86  86  ?   ?   ?   B . n 
B 1 87  PRO 87  87  ?   ?   ?   B . n 
B 1 88  GLY 88  88  ?   ?   ?   B . n 
B 1 89  PRO 89  89  ?   ?   ?   B . n 
B 1 90  LEU 90  90  ?   ?   ?   B . n 
B 1 91  PRO 91  91  ?   ?   ?   B . n 
B 1 92  ALA 92  92  ?   ?   ?   B . n 
B 1 93  GLY 93  93  ?   ?   ?   B . n 
B 1 94  GLN 94  94  ?   ?   ?   B . n 
B 1 95  LEU 95  95  ?   ?   ?   B . n 
B 1 96  ARG 96  96  ?   ?   ?   B . n 
B 1 97  ASP 97  97  ?   ?   ?   B . n 
B 1 98  PRO 98  98  ?   ?   ?   B . n 
B 1 99  ARG 99  99  ?   ?   ?   B . n 
B 1 100 GLY 100 100 ?   ?   ?   B . n 
B 1 101 SER 101 101 ?   ?   ?   B . n 
B 1 102 ASP 102 102 ?   ?   ?   B . n 
B 1 103 ILE 103 103 ?   ?   ?   B . n 
B 1 104 ALA 104 104 ?   ?   ?   B . n 
B 1 105 GLY 105 105 ?   ?   ?   B . n 
B 1 106 THR 106 106 ?   ?   ?   B . n 
B 1 107 THR 107 107 ?   ?   ?   B . n 
B 1 108 SER 108 108 ?   ?   ?   B . n 
B 1 109 THR 109 109 ?   ?   ?   B . n 
B 1 110 VAL 110 110 ?   ?   ?   B . n 
B 1 111 GLU 111 111 ?   ?   ?   B . n 
B 1 112 GLU 112 112 ?   ?   ?   B . n 
B 1 113 GLN 113 113 ?   ?   ?   B . n 
B 1 114 ILE 114 114 ?   ?   ?   B . n 
B 1 115 GLN 115 115 ?   ?   ?   B . n 
B 1 116 TRP 116 116 ?   ?   ?   B . n 
B 1 117 MET 117 117 ?   ?   ?   B . n 
B 1 118 TYR 118 118 ?   ?   ?   B . n 
B 1 119 ARG 119 119 ?   ?   ?   B . n 
B 1 120 PRO 120 120 ?   ?   ?   B . n 
B 1 121 GLN 121 121 ?   ?   ?   B . n 
B 1 122 ASN 122 122 ?   ?   ?   B . n 
B 1 123 PRO 123 123 ?   ?   ?   B . n 
B 1 124 VAL 124 124 ?   ?   ?   B . n 
B 1 125 PRO 125 125 ?   ?   ?   B . n 
B 1 126 VAL 126 126 ?   ?   ?   B . n 
B 1 127 GLY 127 127 ?   ?   ?   B . n 
B 1 128 ASN 128 128 ?   ?   ?   B . n 
B 1 129 ILE 129 129 ?   ?   ?   B . n 
B 1 130 TYR 130 130 ?   ?   ?   B . n 
B 1 131 ARG 131 131 ?   ?   ?   B . n 
B 1 132 ARG 132 132 ?   ?   ?   B . n 
B 1 133 TRP 133 133 ?   ?   ?   B . n 
B 1 134 ILE 134 134 ?   ?   ?   B . n 
B 1 135 GLN 135 135 ?   ?   ?   B . n 
B 1 136 ILE 136 136 ?   ?   ?   B . n 
B 1 137 GLY 137 137 ?   ?   ?   B . n 
B 1 138 LEU 138 138 ?   ?   ?   B . n 
B 1 139 GLN 139 139 ?   ?   ?   B . n 
B 1 140 LYS 140 140 ?   ?   ?   B . n 
B 1 141 CYS 141 141 ?   ?   ?   B . n 
B 1 142 VAL 142 142 ?   ?   ?   B . n 
B 1 143 ARG 143 143 ?   ?   ?   B . n 
B 1 144 MET 144 144 ?   ?   ?   B . n 
B 1 145 TYR 145 145 ?   ?   ?   B . n 
B 1 146 ASN 146 146 ?   ?   ?   B . n 
B 1 147 PRO 147 147 ?   ?   ?   B . n 
B 1 148 THR 148 148 148 THR THR B . n 
B 1 149 ASN 149 149 149 ASN ASN B . n 
B 1 150 ILE 150 150 150 ILE ILE B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ASP 152 152 152 ASP ASP B . n 
B 1 153 VAL 153 153 153 VAL VAL B . n 
B 1 154 LYS 154 154 154 LYS LYS B . n 
B 1 155 GLN 155 155 155 GLN GLN B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 PRO 157 157 157 PRO PRO B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 GLU 159 159 159 GLU GLU B . n 
B 1 160 PRO 160 160 160 PRO PRO B . n 
B 1 161 PHE 161 161 161 PHE PHE B . n 
B 1 162 GLN 162 162 162 GLN GLN B . n 
B 1 163 SER 163 163 163 SER SER B . n 
B 1 164 TYR 164 164 164 TYR TYR B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 ASP 166 166 166 ASP ASP B . n 
B 1 167 ARG 167 167 167 ARG ARG B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 LYS 170 170 170 LYS LYS B . n 
B 1 171 SER 171 171 171 SER SER B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 ARG 173 173 173 ARG ARG B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 GLU 175 175 175 GLU GLU B . n 
B 1 176 GLN 176 176 176 GLN GLN B . n 
B 1 177 THR 177 177 177 THR THR B . n 
B 1 178 ASP 178 178 178 ASP ASP B . n 
B 1 179 PRO 179 179 179 PRO PRO B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 VAL 181 181 181 VAL VAL B . n 
B 1 182 LYS 182 182 182 LYS LYS B . n 
B 1 183 ASN 183 183 183 ASN ASN B . n 
B 1 184 TRP 184 184 184 TRP TRP B . n 
B 1 185 MET 185 185 185 MET MET B . n 
B 1 186 THR 186 186 186 THR THR B . n 
B 1 187 GLN 187 187 187 GLN GLN B . n 
B 1 188 THR 188 188 188 THR THR B . n 
B 1 189 LEU 189 189 189 LEU LEU B . n 
B 1 190 LEU 190 190 190 LEU LEU B . n 
B 1 191 ILE 191 191 191 ILE ILE B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ASN 193 193 193 ASN ASN B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 ASN 195 195 195 ASN ASN B . n 
B 1 196 PRO 196 196 196 PRO PRO B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 CYS 198 198 198 CYS CYS B . n 
B 1 199 LYS 199 199 199 LYS LYS B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 LEU 202 202 202 LEU LEU B . n 
B 1 203 LYS 203 203 203 LYS LYS B . n 
B 1 204 GLY 204 204 204 GLY GLY B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 GLY 206 206 206 GLY GLY B . n 
B 1 207 MET 207 207 207 MET MET B . n 
B 1 208 ASN 208 208 208 ASN ASN B . n 
B 1 209 PRO 209 209 209 PRO PRO B . n 
B 1 210 THR 210 210 210 THR THR B . n 
B 1 211 LEU 211 211 211 LEU LEU B . n 
B 1 212 GLU 212 212 212 GLU GLU B . n 
B 1 213 GLU 213 213 213 GLU GLU B . n 
B 1 214 MET 214 214 214 MET MET B . n 
B 1 215 LEU 215 215 215 LEU LEU B . n 
B 1 216 THR 216 216 216 THR THR B . n 
B 1 217 ALA 217 217 217 ALA ALA B . n 
B 1 218 CYS 218 218 218 CYS CYS B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLY 220 220 220 GLY GLY B . n 
B 1 221 VAL 221 221 221 VAL VAL B . n 
B 1 222 GLY 222 222 ?   ?   ?   B . n 
B 1 223 GLY 223 223 ?   ?   ?   B . n 
B 1 224 PRO 224 224 ?   ?   ?   B . n 
B 1 225 GLY 225 225 ?   ?   ?   B . n 
B 1 226 GLN 226 226 ?   ?   ?   B . n 
B 1 227 LYS 227 227 ?   ?   ?   B . n 
B 1 228 ALA 228 228 ?   ?   ?   B . n 
B 1 229 ARG 229 229 ?   ?   ?   B . n 
B 1 230 LEU 230 230 ?   ?   ?   B . n 
B 1 231 MET 231 231 ?   ?   ?   B . n 
B 1 232 GLY 232 232 ?   ?   ?   B . n 
B 1 233 SER 233 233 ?   ?   ?   B . n 
B 1 234 SER 234 234 ?   ?   ?   B . n 
B 1 235 HIS 235 235 ?   ?   ?   B . n 
B 1 236 HIS 236 236 ?   ?   ?   B . n 
B 1 237 HIS 237 237 ?   ?   ?   B . n 
B 1 238 HIS 238 238 ?   ?   ?   B . n 
B 1 239 HIS 239 239 ?   ?   ?   B . n 
B 1 240 HIS 240 240 ?   ?   ?   B . n 
C 1 1   PRO 1   1   ?   ?   ?   C . n 
C 1 2   VAL 2   2   ?   ?   ?   C . n 
C 1 3   GLN 3   3   ?   ?   ?   C . n 
C 1 4   GLN 4   4   ?   ?   ?   C . n 
C 1 5   THR 5   5   ?   ?   ?   C . n 
C 1 6   GLY 6   6   ?   ?   ?   C . n 
C 1 7   GLY 7   7   ?   ?   ?   C . n 
C 1 8   GLY 8   8   ?   ?   ?   C . n 
C 1 9   ASN 9   9   ?   ?   ?   C . n 
C 1 10  TYR 10  10  ?   ?   ?   C . n 
C 1 11  ILE 11  11  ?   ?   ?   C . n 
C 1 12  HIS 12  12  ?   ?   ?   C . n 
C 1 13  VAL 13  13  ?   ?   ?   C . n 
C 1 14  PRO 14  14  ?   ?   ?   C . n 
C 1 15  LEU 15  15  ?   ?   ?   C . n 
C 1 16  SER 16  16  ?   ?   ?   C . n 
C 1 17  PRO 17  17  ?   ?   ?   C . n 
C 1 18  ARG 18  18  ?   ?   ?   C . n 
C 1 19  THR 19  19  ?   ?   ?   C . n 
C 1 20  LEU 20  20  ?   ?   ?   C . n 
C 1 21  ASN 21  21  ?   ?   ?   C . n 
C 1 22  ALA 22  22  ?   ?   ?   C . n 
C 1 23  TRP 23  23  ?   ?   ?   C . n 
C 1 24  VAL 24  24  ?   ?   ?   C . n 
C 1 25  LYS 25  25  ?   ?   ?   C . n 
C 1 26  LEU 26  26  ?   ?   ?   C . n 
C 1 27  VAL 27  27  ?   ?   ?   C . n 
C 1 28  GLU 28  28  ?   ?   ?   C . n 
C 1 29  ASP 29  29  ?   ?   ?   C . n 
C 1 30  LYS 30  30  ?   ?   ?   C . n 
C 1 31  LYS 31  31  ?   ?   ?   C . n 
C 1 32  PHE 32  32  ?   ?   ?   C . n 
C 1 33  GLY 33  33  ?   ?   ?   C . n 
C 1 34  ALA 34  34  ?   ?   ?   C . n 
C 1 35  GLU 35  35  ?   ?   ?   C . n 
C 1 36  VAL 36  36  ?   ?   ?   C . n 
C 1 37  VAL 37  37  ?   ?   ?   C . n 
C 1 38  PRO 38  38  ?   ?   ?   C . n 
C 1 39  GLY 39  39  ?   ?   ?   C . n 
C 1 40  PHE 40  40  ?   ?   ?   C . n 
C 1 41  GLN 41  41  ?   ?   ?   C . n 
C 1 42  ALA 42  42  ?   ?   ?   C . n 
C 1 43  LEU 43  43  ?   ?   ?   C . n 
C 1 44  SER 44  44  ?   ?   ?   C . n 
C 1 45  GLU 45  45  ?   ?   ?   C . n 
C 1 46  GLY 46  46  ?   ?   ?   C . n 
C 1 47  CYS 47  47  ?   ?   ?   C . n 
C 1 48  THR 48  48  ?   ?   ?   C . n 
C 1 49  PRO 49  49  ?   ?   ?   C . n 
C 1 50  TYR 50  50  ?   ?   ?   C . n 
C 1 51  ASP 51  51  ?   ?   ?   C . n 
C 1 52  ILE 52  52  ?   ?   ?   C . n 
C 1 53  ASN 53  53  ?   ?   ?   C . n 
C 1 54  GLN 54  54  ?   ?   ?   C . n 
C 1 55  MET 55  55  ?   ?   ?   C . n 
C 1 56  LEU 56  56  ?   ?   ?   C . n 
C 1 57  ASN 57  57  ?   ?   ?   C . n 
C 1 58  CYS 58  58  ?   ?   ?   C . n 
C 1 59  VAL 59  59  ?   ?   ?   C . n 
C 1 60  GLY 60  60  ?   ?   ?   C . n 
C 1 61  ASP 61  61  ?   ?   ?   C . n 
C 1 62  HIS 62  62  ?   ?   ?   C . n 
C 1 63  GLN 63  63  ?   ?   ?   C . n 
C 1 64  ALA 64  64  ?   ?   ?   C . n 
C 1 65  ALA 65  65  ?   ?   ?   C . n 
C 1 66  MET 66  66  ?   ?   ?   C . n 
C 1 67  GLN 67  67  ?   ?   ?   C . n 
C 1 68  ILE 68  68  ?   ?   ?   C . n 
C 1 69  ILE 69  69  ?   ?   ?   C . n 
C 1 70  ARG 70  70  ?   ?   ?   C . n 
C 1 71  GLU 71  71  ?   ?   ?   C . n 
C 1 72  ILE 72  72  ?   ?   ?   C . n 
C 1 73  ILE 73  73  ?   ?   ?   C . n 
C 1 74  ASN 74  74  ?   ?   ?   C . n 
C 1 75  ASP 75  75  ?   ?   ?   C . n 
C 1 76  GLU 76  76  ?   ?   ?   C . n 
C 1 77  ALA 77  77  ?   ?   ?   C . n 
C 1 78  ALA 78  78  ?   ?   ?   C . n 
C 1 79  ASP 79  79  ?   ?   ?   C . n 
C 1 80  TRP 80  80  ?   ?   ?   C . n 
C 1 81  ASP 81  81  ?   ?   ?   C . n 
C 1 82  ALA 82  82  ?   ?   ?   C . n 
C 1 83  GLN 83  83  ?   ?   ?   C . n 
C 1 84  HIS 84  84  ?   ?   ?   C . n 
C 1 85  PRO 85  85  ?   ?   ?   C . n 
C 1 86  ILE 86  86  ?   ?   ?   C . n 
C 1 87  PRO 87  87  ?   ?   ?   C . n 
C 1 88  GLY 88  88  ?   ?   ?   C . n 
C 1 89  PRO 89  89  ?   ?   ?   C . n 
C 1 90  LEU 90  90  ?   ?   ?   C . n 
C 1 91  PRO 91  91  ?   ?   ?   C . n 
C 1 92  ALA 92  92  ?   ?   ?   C . n 
C 1 93  GLY 93  93  ?   ?   ?   C . n 
C 1 94  GLN 94  94  ?   ?   ?   C . n 
C 1 95  LEU 95  95  ?   ?   ?   C . n 
C 1 96  ARG 96  96  ?   ?   ?   C . n 
C 1 97  ASP 97  97  ?   ?   ?   C . n 
C 1 98  PRO 98  98  ?   ?   ?   C . n 
C 1 99  ARG 99  99  ?   ?   ?   C . n 
C 1 100 GLY 100 100 ?   ?   ?   C . n 
C 1 101 SER 101 101 ?   ?   ?   C . n 
C 1 102 ASP 102 102 ?   ?   ?   C . n 
C 1 103 ILE 103 103 ?   ?   ?   C . n 
C 1 104 ALA 104 104 ?   ?   ?   C . n 
C 1 105 GLY 105 105 ?   ?   ?   C . n 
C 1 106 THR 106 106 ?   ?   ?   C . n 
C 1 107 THR 107 107 ?   ?   ?   C . n 
C 1 108 SER 108 108 ?   ?   ?   C . n 
C 1 109 THR 109 109 ?   ?   ?   C . n 
C 1 110 VAL 110 110 ?   ?   ?   C . n 
C 1 111 GLU 111 111 ?   ?   ?   C . n 
C 1 112 GLU 112 112 ?   ?   ?   C . n 
C 1 113 GLN 113 113 ?   ?   ?   C . n 
C 1 114 ILE 114 114 ?   ?   ?   C . n 
C 1 115 GLN 115 115 ?   ?   ?   C . n 
C 1 116 TRP 116 116 ?   ?   ?   C . n 
C 1 117 MET 117 117 ?   ?   ?   C . n 
C 1 118 TYR 118 118 ?   ?   ?   C . n 
C 1 119 ARG 119 119 ?   ?   ?   C . n 
C 1 120 PRO 120 120 ?   ?   ?   C . n 
C 1 121 GLN 121 121 ?   ?   ?   C . n 
C 1 122 ASN 122 122 ?   ?   ?   C . n 
C 1 123 PRO 123 123 ?   ?   ?   C . n 
C 1 124 VAL 124 124 ?   ?   ?   C . n 
C 1 125 PRO 125 125 ?   ?   ?   C . n 
C 1 126 VAL 126 126 ?   ?   ?   C . n 
C 1 127 GLY 127 127 ?   ?   ?   C . n 
C 1 128 ASN 128 128 ?   ?   ?   C . n 
C 1 129 ILE 129 129 ?   ?   ?   C . n 
C 1 130 TYR 130 130 ?   ?   ?   C . n 
C 1 131 ARG 131 131 ?   ?   ?   C . n 
C 1 132 ARG 132 132 ?   ?   ?   C . n 
C 1 133 TRP 133 133 ?   ?   ?   C . n 
C 1 134 ILE 134 134 ?   ?   ?   C . n 
C 1 135 GLN 135 135 ?   ?   ?   C . n 
C 1 136 ILE 136 136 ?   ?   ?   C . n 
C 1 137 GLY 137 137 ?   ?   ?   C . n 
C 1 138 LEU 138 138 ?   ?   ?   C . n 
C 1 139 GLN 139 139 ?   ?   ?   C . n 
C 1 140 LYS 140 140 ?   ?   ?   C . n 
C 1 141 CYS 141 141 ?   ?   ?   C . n 
C 1 142 VAL 142 142 ?   ?   ?   C . n 
C 1 143 ARG 143 143 ?   ?   ?   C . n 
C 1 144 MET 144 144 ?   ?   ?   C . n 
C 1 145 TYR 145 145 ?   ?   ?   C . n 
C 1 146 ASN 146 146 ?   ?   ?   C . n 
C 1 147 PRO 147 147 ?   ?   ?   C . n 
C 1 148 THR 148 148 148 THR THR C . n 
C 1 149 ASN 149 149 149 ASN ASN C . n 
C 1 150 ILE 150 150 150 ILE ILE C . n 
C 1 151 LEU 151 151 151 LEU LEU C . n 
C 1 152 ASP 152 152 152 ASP ASP C . n 
C 1 153 VAL 153 153 153 VAL VAL C . n 
C 1 154 LYS 154 154 154 LYS LYS C . n 
C 1 155 GLN 155 155 155 GLN GLN C . n 
C 1 156 GLY 156 156 156 GLY GLY C . n 
C 1 157 PRO 157 157 157 PRO PRO C . n 
C 1 158 LYS 158 158 158 LYS LYS C . n 
C 1 159 GLU 159 159 159 GLU GLU C . n 
C 1 160 PRO 160 160 160 PRO PRO C . n 
C 1 161 PHE 161 161 161 PHE PHE C . n 
C 1 162 GLN 162 162 162 GLN GLN C . n 
C 1 163 SER 163 163 163 SER SER C . n 
C 1 164 TYR 164 164 164 TYR TYR C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 ASP 166 166 166 ASP ASP C . n 
C 1 167 ARG 167 167 167 ARG ARG C . n 
C 1 168 PHE 168 168 168 PHE PHE C . n 
C 1 169 TYR 169 169 169 TYR TYR C . n 
C 1 170 LYS 170 170 170 LYS LYS C . n 
C 1 171 SER 171 171 171 SER SER C . n 
C 1 172 LEU 172 172 172 LEU LEU C . n 
C 1 173 ARG 173 173 173 ARG ARG C . n 
C 1 174 ALA 174 174 174 ALA ALA C . n 
C 1 175 GLU 175 175 175 GLU GLU C . n 
C 1 176 GLN 176 176 176 GLN GLN C . n 
C 1 177 THR 177 177 177 THR THR C . n 
C 1 178 ASP 178 178 178 ASP ASP C . n 
C 1 179 PRO 179 179 179 PRO PRO C . n 
C 1 180 ALA 180 180 180 ALA ALA C . n 
C 1 181 VAL 181 181 181 VAL VAL C . n 
C 1 182 LYS 182 182 182 LYS LYS C . n 
C 1 183 ASN 183 183 183 ASN ASN C . n 
C 1 184 TRP 184 184 184 TRP TRP C . n 
C 1 185 MET 185 185 185 MET MET C . n 
C 1 186 THR 186 186 186 THR THR C . n 
C 1 187 GLN 187 187 187 GLN GLN C . n 
C 1 188 THR 188 188 188 THR THR C . n 
C 1 189 LEU 189 189 189 LEU LEU C . n 
C 1 190 LEU 190 190 190 LEU LEU C . n 
C 1 191 ILE 191 191 191 ILE ILE C . n 
C 1 192 GLN 192 192 192 GLN GLN C . n 
C 1 193 ASN 193 193 193 ASN ASN C . n 
C 1 194 ALA 194 194 194 ALA ALA C . n 
C 1 195 ASN 195 195 195 ASN ASN C . n 
C 1 196 PRO 196 196 196 PRO PRO C . n 
C 1 197 ASP 197 197 197 ASP ASP C . n 
C 1 198 CYS 198 198 198 CYS CYS C . n 
C 1 199 LYS 199 199 199 LYS LYS C . n 
C 1 200 LEU 200 200 200 LEU LEU C . n 
C 1 201 VAL 201 201 201 VAL VAL C . n 
C 1 202 LEU 202 202 202 LEU LEU C . n 
C 1 203 LYS 203 203 203 LYS LYS C . n 
C 1 204 GLY 204 204 204 GLY GLY C . n 
C 1 205 LEU 205 205 205 LEU LEU C . n 
C 1 206 GLY 206 206 206 GLY GLY C . n 
C 1 207 MET 207 207 207 MET MET C . n 
C 1 208 ASN 208 208 208 ASN ASN C . n 
C 1 209 PRO 209 209 209 PRO PRO C . n 
C 1 210 THR 210 210 210 THR THR C . n 
C 1 211 LEU 211 211 211 LEU LEU C . n 
C 1 212 GLU 212 212 212 GLU GLU C . n 
C 1 213 GLU 213 213 213 GLU GLU C . n 
C 1 214 MET 214 214 214 MET MET C . n 
C 1 215 LEU 215 215 215 LEU LEU C . n 
C 1 216 THR 216 216 216 THR THR C . n 
C 1 217 ALA 217 217 217 ALA ALA C . n 
C 1 218 CYS 218 218 218 CYS CYS C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 GLY 220 220 220 GLY GLY C . n 
C 1 221 VAL 221 221 221 VAL VAL C . n 
C 1 222 GLY 222 222 ?   ?   ?   C . n 
C 1 223 GLY 223 223 ?   ?   ?   C . n 
C 1 224 PRO 224 224 ?   ?   ?   C . n 
C 1 225 GLY 225 225 ?   ?   ?   C . n 
C 1 226 GLN 226 226 ?   ?   ?   C . n 
C 1 227 LYS 227 227 ?   ?   ?   C . n 
C 1 228 ALA 228 228 ?   ?   ?   C . n 
C 1 229 ARG 229 229 ?   ?   ?   C . n 
C 1 230 LEU 230 230 ?   ?   ?   C . n 
C 1 231 MET 231 231 ?   ?   ?   C . n 
C 1 232 GLY 232 232 ?   ?   ?   C . n 
C 1 233 SER 233 233 ?   ?   ?   C . n 
C 1 234 SER 234 234 ?   ?   ?   C . n 
C 1 235 HIS 235 235 ?   ?   ?   C . n 
C 1 236 HIS 236 236 ?   ?   ?   C . n 
C 1 237 HIS 237 237 ?   ?   ?   C . n 
C 1 238 HIS 238 238 ?   ?   ?   C . n 
C 1 239 HIS 239 239 ?   ?   ?   C . n 
C 1 240 HIS 240 240 ?   ?   ?   C . 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 
D 2 IHP 1 301 301 IHP IHP A . 
E 2 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                   9CNS 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9CNS 
_struct.title                        'HIV-2 CA hexamer; assembled via 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        9CNS 
_struct_keywords.text            'HIV-2, Capsid, IP6, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POL_HV2G1 
_struct_ref.pdbx_db_accession          P18042 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINDEAADW
DAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEP
FQSYVDRFYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLM
;
_struct_ref.pdbx_align_begin           136 
# 
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 9CNS A 1 ? 231 ? P18042 136 ? 366 ? 1 231 
2 1 9CNS B 1 ? 231 ? P18042 136 ? 366 ? 1 231 
3 1 9CNS C 1 ? 231 ? P18042 136 ? 366 ? 1 231 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CNS GLY A 232 ? UNP P18042 ? ? 'expression tag' 232 1  
1 9CNS SER A 233 ? UNP P18042 ? ? 'expression tag' 233 2  
1 9CNS SER A 234 ? UNP P18042 ? ? 'expression tag' 234 3  
1 9CNS HIS A 235 ? UNP P18042 ? ? 'expression tag' 235 4  
1 9CNS HIS A 236 ? UNP P18042 ? ? 'expression tag' 236 5  
1 9CNS HIS A 237 ? UNP P18042 ? ? 'expression tag' 237 6  
1 9CNS HIS A 238 ? UNP P18042 ? ? 'expression tag' 238 7  
1 9CNS HIS A 239 ? UNP P18042 ? ? 'expression tag' 239 8  
1 9CNS HIS A 240 ? UNP P18042 ? ? 'expression tag' 240 9  
2 9CNS GLY B 232 ? UNP P18042 ? ? 'expression tag' 232 10 
2 9CNS SER B 233 ? UNP P18042 ? ? 'expression tag' 233 11 
2 9CNS SER B 234 ? UNP P18042 ? ? 'expression tag' 234 12 
2 9CNS HIS B 235 ? UNP P18042 ? ? 'expression tag' 235 13 
2 9CNS HIS B 236 ? UNP P18042 ? ? 'expression tag' 236 14 
2 9CNS HIS B 237 ? UNP P18042 ? ? 'expression tag' 237 15 
2 9CNS HIS B 238 ? UNP P18042 ? ? 'expression tag' 238 16 
2 9CNS HIS B 239 ? UNP P18042 ? ? 'expression tag' 239 17 
2 9CNS HIS B 240 ? UNP P18042 ? ? 'expression tag' 240 18 
3 9CNS GLY C 232 ? UNP P18042 ? ? 'expression tag' 232 19 
3 9CNS SER C 233 ? UNP P18042 ? ? 'expression tag' 233 20 
3 9CNS SER C 234 ? UNP P18042 ? ? 'expression tag' 234 21 
3 9CNS HIS C 235 ? UNP P18042 ? ? 'expression tag' 235 22 
3 9CNS HIS C 236 ? UNP P18042 ? ? 'expression tag' 236 23 
3 9CNS HIS C 237 ? UNP P18042 ? ? 'expression tag' 237 24 
3 9CNS HIS C 238 ? UNP P18042 ? ? 'expression tag' 238 25 
3 9CNS HIS C 239 ? UNP P18042 ? ? 'expression tag' 239 26 
3 9CNS HIS C 240 ? UNP P18042 ? ? 'expression tag' 240 27 
# 
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' ? octadecameric 18 
2 'point asymmetric unit'   ? trimeric      3  
# 
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,E 
2 1       A,B,C,D,E 
# 
_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                'not applicable' 
# 
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 -82.68080 -0.86600000 0.50000000  0.00000000 308.56850 
0.00000000 0.00000000 1.00000000 0.00000 
3 'point symmetry operation' ?     ?     -0.50000000 0.86600000  0.00000000 143.20670 -0.86600000 -0.50000000 0.00000000 534.45660 
0.00000000 0.00000000 1.00000000 0.00000 
4 'point symmetry operation' ?     ?     -1.00000000 0.00000000  0.00000000 451.77540 0.00000000  -1.00000000 0.00000000 451.77660 
0.00000000 0.00000000 1.00000000 0.00000 
5 'point symmetry operation' ?     ?     -0.50000000 -0.86600000 0.00000000 534.45700 0.86600000  -0.50000000 0.00000000 143.20830 
0.00000000 0.00000000 1.00000000 0.00000 
6 'point symmetry operation' ?     ?     0.50000000  -0.86600000 0.00000000 308.57010 0.86600000  0.50000000  0.00000000 -82.68040 
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 SER A 16  ? GLU A 28  ? SER A 16  GLU A 28  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 THR A 109 ? ARG A 119 ? THR A 109 ARG A 119 1 ? 11 
HELX_P HELX_P7  AA7 GLY A 127 ? TYR A 145 ? GLY A 127 TYR A 145 1 ? 19 
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 ? GLU A 175 ? PRO A 160 GLU A 175 1 ? 16 
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 ? LEU A 205 ? ASN A 195 LEU A 205 1 ? 11 
HELX_P HELX_P12 AB3 THR A 210 ? CYS A 218 ? THR A 210 CYS A 218 1 ? 9  
HELX_P HELX_P13 AB4 PRO B 160 ? ARG B 167 ? PRO B 160 ARG B 167 1 ? 8  
HELX_P HELX_P14 AB5 PHE B 168 ? GLU B 175 ? PHE B 168 GLU B 175 1 ? 8  
HELX_P HELX_P15 AB6 ASP B 178 ? THR B 188 ? ASP B 178 THR B 188 1 ? 11 
HELX_P HELX_P16 AB7 THR B 188 ? ASN B 193 ? THR B 188 ASN B 193 1 ? 6  
HELX_P HELX_P17 AB8 ASN B 195 ? GLY B 206 ? ASN B 195 GLY B 206 1 ? 12 
HELX_P HELX_P18 AB9 THR B 210 ? CYS B 218 ? THR B 210 CYS B 218 1 ? 9  
HELX_P HELX_P19 AC1 TYR C 164 ? GLN C 176 ? TYR C 164 GLN C 176 1 ? 13 
HELX_P HELX_P20 AC2 ASP C 178 ? ASN C 193 ? ASP C 178 ASN C 193 1 ? 16 
HELX_P HELX_P21 AC3 ASN C 195 ? GLY C 206 ? ASN C 195 GLY C 206 1 ? 12 
HELX_P HELX_P22 AC4 THR C 210 ? CYS C 218 ? THR C 210 CYS C 218 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_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 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_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 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 198 SG ? ? ? 1_555 A CYS 218 SG ? ? A CYS 198 A CYS 218 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
disulf2 disulf ? ? B CYS 198 SG ? ? ? 1_555 B CYS 218 SG ? ? B CYS 198 B CYS 218 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
disulf3 disulf ? ? C CYS 198 SG ? ? ? 1_555 C CYS 218 SG ? ? C CYS 198 C CYS 218 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 198 ? CYS A 218 ? CYS A 198 ? 1_555 CYS A 218 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 198 ? CYS B 218 ? CYS B 198 ? 1_555 CYS B 218 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS C 198 ? CYS C 218 ? CYS C 198 ? 1_555 CYS C 218 ? 1_555 SG SG . . . None '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  ? GLN A 3  ? VAL A 2  GLN A 3  
AA1 2 ILE A 11 ? HIS A 12 ? ILE A 11 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                   9CNS 
_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 ASN A 122 ? ? -152.16 78.10   
2 1 PRO A 160 ? ? -78.12  -165.24 
3 1 THR A 188 ? ? -130.48 -61.00  
4 1 PRO A 209 ? ? -59.64  171.25  
5 1 THR B 188 ? ? -128.35 -56.24  
6 1 ASN B 208 ? ? 22.58   65.72   
7 1 PRO C 160 ? ? -74.35  -166.73 
8 1 THR C 188 ? ? -125.33 -62.19  
# 
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  ? ? 0.126 'SIDE CHAIN' 
2 1 ARG A 70  ? ? 0.099 'SIDE CHAIN' 
3 1 ARG A 131 ? ? 0.116 'SIDE CHAIN' 
4 1 ARG A 143 ? ? 0.094 'SIDE CHAIN' 
5 1 ARG A 167 ? ? 0.081 'SIDE CHAIN' 
# 
_pdbx_point_symmetry.entry_id             9CNS 
_pdbx_point_symmetry.Schoenflies_symbol   C 
_pdbx_point_symmetry.circular_symmetry    1 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9CNS 
_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.
;
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'FLEXIBLE FIT' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  . 
_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   ? 
# 
_em_3d_reconstruction.entry_id                    9CNS 
_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                  3.25 
_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               603473 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       'The mixed buffer of storage buffer for the protein and lipid components with IP6 supplemented.' 
_em_buffer.pH            7 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'HIV-2 capsid protein assembled into a lattice via liposome templating.' 
_em_entity_assembly.details              
;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.
;
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9CNS 
_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              9CNS 
_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                9CNS 
_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              9CNS 
_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 VAL 2   ? B VAL 2   
22  1 Y 1 B GLN 3   ? B GLN 3   
23  1 Y 1 B GLN 4   ? B GLN 4   
24  1 Y 1 B THR 5   ? B THR 5   
25  1 Y 1 B GLY 6   ? B GLY 6   
26  1 Y 1 B GLY 7   ? B GLY 7   
27  1 Y 1 B GLY 8   ? B GLY 8   
28  1 Y 1 B ASN 9   ? B ASN 9   
29  1 Y 1 B TYR 10  ? B TYR 10  
30  1 Y 1 B ILE 11  ? B ILE 11  
31  1 Y 1 B HIS 12  ? B HIS 12  
32  1 Y 1 B VAL 13  ? B VAL 13  
33  1 Y 1 B PRO 14  ? B PRO 14  
34  1 Y 1 B LEU 15  ? B LEU 15  
35  1 Y 1 B SER 16  ? B SER 16  
36  1 Y 1 B PRO 17  ? B PRO 17  
37  1 Y 1 B ARG 18  ? B ARG 18  
38  1 Y 1 B THR 19  ? B THR 19  
39  1 Y 1 B LEU 20  ? B LEU 20  
40  1 Y 1 B ASN 21  ? B ASN 21  
41  1 Y 1 B ALA 22  ? B ALA 22  
42  1 Y 1 B TRP 23  ? B TRP 23  
43  1 Y 1 B VAL 24  ? B VAL 24  
44  1 Y 1 B LYS 25  ? B LYS 25  
45  1 Y 1 B LEU 26  ? B LEU 26  
46  1 Y 1 B VAL 27  ? B VAL 27  
47  1 Y 1 B GLU 28  ? B GLU 28  
48  1 Y 1 B ASP 29  ? B ASP 29  
49  1 Y 1 B LYS 30  ? B LYS 30  
50  1 Y 1 B LYS 31  ? B LYS 31  
51  1 Y 1 B PHE 32  ? B PHE 32  
52  1 Y 1 B GLY 33  ? B GLY 33  
53  1 Y 1 B ALA 34  ? B ALA 34  
54  1 Y 1 B GLU 35  ? B GLU 35  
55  1 Y 1 B VAL 36  ? B VAL 36  
56  1 Y 1 B VAL 37  ? B VAL 37  
57  1 Y 1 B PRO 38  ? B PRO 38  
58  1 Y 1 B GLY 39  ? B GLY 39  
59  1 Y 1 B PHE 40  ? B PHE 40  
60  1 Y 1 B GLN 41  ? B GLN 41  
61  1 Y 1 B ALA 42  ? B ALA 42  
62  1 Y 1 B LEU 43  ? B LEU 43  
63  1 Y 1 B SER 44  ? B SER 44  
64  1 Y 1 B GLU 45  ? B GLU 45  
65  1 Y 1 B GLY 46  ? B GLY 46  
66  1 Y 1 B CYS 47  ? B CYS 47  
67  1 Y 1 B THR 48  ? B THR 48  
68  1 Y 1 B PRO 49  ? B PRO 49  
69  1 Y 1 B TYR 50  ? B TYR 50  
70  1 Y 1 B ASP 51  ? B ASP 51  
71  1 Y 1 B ILE 52  ? B ILE 52  
72  1 Y 1 B ASN 53  ? B ASN 53  
73  1 Y 1 B GLN 54  ? B GLN 54  
74  1 Y 1 B MET 55  ? B MET 55  
75  1 Y 1 B LEU 56  ? B LEU 56  
76  1 Y 1 B ASN 57  ? B ASN 57  
77  1 Y 1 B CYS 58  ? B CYS 58  
78  1 Y 1 B VAL 59  ? B VAL 59  
79  1 Y 1 B GLY 60  ? B GLY 60  
80  1 Y 1 B ASP 61  ? B ASP 61  
81  1 Y 1 B HIS 62  ? B HIS 62  
82  1 Y 1 B GLN 63  ? B GLN 63  
83  1 Y 1 B ALA 64  ? B ALA 64  
84  1 Y 1 B ALA 65  ? B ALA 65  
85  1 Y 1 B MET 66  ? B MET 66  
86  1 Y 1 B GLN 67  ? B GLN 67  
87  1 Y 1 B ILE 68  ? B ILE 68  
88  1 Y 1 B ILE 69  ? B ILE 69  
89  1 Y 1 B ARG 70  ? B ARG 70  
90  1 Y 1 B GLU 71  ? B GLU 71  
91  1 Y 1 B ILE 72  ? B ILE 72  
92  1 Y 1 B ILE 73  ? B ILE 73  
93  1 Y 1 B ASN 74  ? B ASN 74  
94  1 Y 1 B ASP 75  ? B ASP 75  
95  1 Y 1 B GLU 76  ? B GLU 76  
96  1 Y 1 B ALA 77  ? B ALA 77  
97  1 Y 1 B ALA 78  ? B ALA 78  
98  1 Y 1 B ASP 79  ? B ASP 79  
99  1 Y 1 B TRP 80  ? B TRP 80  
100 1 Y 1 B ASP 81  ? B ASP 81  
101 1 Y 1 B ALA 82  ? B ALA 82  
102 1 Y 1 B GLN 83  ? B GLN 83  
103 1 Y 1 B HIS 84  ? B HIS 84  
104 1 Y 1 B PRO 85  ? B PRO 85  
105 1 Y 1 B ILE 86  ? B ILE 86  
106 1 Y 1 B PRO 87  ? B PRO 87  
107 1 Y 1 B GLY 88  ? B GLY 88  
108 1 Y 1 B PRO 89  ? B PRO 89  
109 1 Y 1 B LEU 90  ? B LEU 90  
110 1 Y 1 B PRO 91  ? B PRO 91  
111 1 Y 1 B ALA 92  ? B ALA 92  
112 1 Y 1 B GLY 93  ? B GLY 93  
113 1 Y 1 B GLN 94  ? B GLN 94  
114 1 Y 1 B LEU 95  ? B LEU 95  
115 1 Y 1 B ARG 96  ? B ARG 96  
116 1 Y 1 B ASP 97  ? B ASP 97  
117 1 Y 1 B PRO 98  ? B PRO 98  
118 1 Y 1 B ARG 99  ? B ARG 99  
119 1 Y 1 B GLY 100 ? B GLY 100 
120 1 Y 1 B SER 101 ? B SER 101 
121 1 Y 1 B ASP 102 ? B ASP 102 
122 1 Y 1 B ILE 103 ? B ILE 103 
123 1 Y 1 B ALA 104 ? B ALA 104 
124 1 Y 1 B GLY 105 ? B GLY 105 
125 1 Y 1 B THR 106 ? B THR 106 
126 1 Y 1 B THR 107 ? B THR 107 
127 1 Y 1 B SER 108 ? B SER 108 
128 1 Y 1 B THR 109 ? B THR 109 
129 1 Y 1 B VAL 110 ? B VAL 110 
130 1 Y 1 B GLU 111 ? B GLU 111 
131 1 Y 1 B GLU 112 ? B GLU 112 
132 1 Y 1 B GLN 113 ? B GLN 113 
133 1 Y 1 B ILE 114 ? B ILE 114 
134 1 Y 1 B GLN 115 ? B GLN 115 
135 1 Y 1 B TRP 116 ? B TRP 116 
136 1 Y 1 B MET 117 ? B MET 117 
137 1 Y 1 B TYR 118 ? B TYR 118 
138 1 Y 1 B ARG 119 ? B ARG 119 
139 1 Y 1 B PRO 120 ? B PRO 120 
140 1 Y 1 B GLN 121 ? B GLN 121 
141 1 Y 1 B ASN 122 ? B ASN 122 
142 1 Y 1 B PRO 123 ? B PRO 123 
143 1 Y 1 B VAL 124 ? B VAL 124 
144 1 Y 1 B PRO 125 ? B PRO 125 
145 1 Y 1 B VAL 126 ? B VAL 126 
146 1 Y 1 B GLY 127 ? B GLY 127 
147 1 Y 1 B ASN 128 ? B ASN 128 
148 1 Y 1 B ILE 129 ? B ILE 129 
149 1 Y 1 B TYR 130 ? B TYR 130 
150 1 Y 1 B ARG 131 ? B ARG 131 
151 1 Y 1 B ARG 132 ? B ARG 132 
152 1 Y 1 B TRP 133 ? B TRP 133 
153 1 Y 1 B ILE 134 ? B ILE 134 
154 1 Y 1 B GLN 135 ? B GLN 135 
155 1 Y 1 B ILE 136 ? B ILE 136 
156 1 Y 1 B GLY 137 ? B GLY 137 
157 1 Y 1 B LEU 138 ? B LEU 138 
158 1 Y 1 B GLN 139 ? B GLN 139 
159 1 Y 1 B LYS 140 ? B LYS 140 
160 1 Y 1 B CYS 141 ? B CYS 141 
161 1 Y 1 B VAL 142 ? B VAL 142 
162 1 Y 1 B ARG 143 ? B ARG 143 
163 1 Y 1 B MET 144 ? B MET 144 
164 1 Y 1 B TYR 145 ? B TYR 145 
165 1 Y 1 B ASN 146 ? B ASN 146 
166 1 Y 1 B PRO 147 ? B PRO 147 
167 1 Y 1 B GLY 222 ? B GLY 222 
168 1 Y 1 B GLY 223 ? B GLY 223 
169 1 Y 1 B PRO 224 ? B PRO 224 
170 1 Y 1 B GLY 225 ? B GLY 225 
171 1 Y 1 B GLN 226 ? B GLN 226 
172 1 Y 1 B LYS 227 ? B LYS 227 
173 1 Y 1 B ALA 228 ? B ALA 228 
174 1 Y 1 B ARG 229 ? B ARG 229 
175 1 Y 1 B LEU 230 ? B LEU 230 
176 1 Y 1 B MET 231 ? B MET 231 
177 1 Y 1 B GLY 232 ? B GLY 232 
178 1 Y 1 B SER 233 ? B SER 233 
179 1 Y 1 B SER 234 ? B SER 234 
180 1 Y 1 B HIS 235 ? B HIS 235 
181 1 Y 1 B HIS 236 ? B HIS 236 
182 1 Y 1 B HIS 237 ? B HIS 237 
183 1 Y 1 B HIS 238 ? B HIS 238 
184 1 Y 1 B HIS 239 ? B HIS 239 
185 1 Y 1 B HIS 240 ? B HIS 240 
186 1 Y 1 C PRO 1   ? C PRO 1   
187 1 Y 1 C VAL 2   ? C VAL 2   
188 1 Y 1 C GLN 3   ? C GLN 3   
189 1 Y 1 C GLN 4   ? C GLN 4   
190 1 Y 1 C THR 5   ? C THR 5   
191 1 Y 1 C GLY 6   ? C GLY 6   
192 1 Y 1 C GLY 7   ? C GLY 7   
193 1 Y 1 C GLY 8   ? C GLY 8   
194 1 Y 1 C ASN 9   ? C ASN 9   
195 1 Y 1 C TYR 10  ? C TYR 10  
196 1 Y 1 C ILE 11  ? C ILE 11  
197 1 Y 1 C HIS 12  ? C HIS 12  
198 1 Y 1 C VAL 13  ? C VAL 13  
199 1 Y 1 C PRO 14  ? C PRO 14  
200 1 Y 1 C LEU 15  ? C LEU 15  
201 1 Y 1 C SER 16  ? C SER 16  
202 1 Y 1 C PRO 17  ? C PRO 17  
203 1 Y 1 C ARG 18  ? C ARG 18  
204 1 Y 1 C THR 19  ? C THR 19  
205 1 Y 1 C LEU 20  ? C LEU 20  
206 1 Y 1 C ASN 21  ? C ASN 21  
207 1 Y 1 C ALA 22  ? C ALA 22  
208 1 Y 1 C TRP 23  ? C TRP 23  
209 1 Y 1 C VAL 24  ? C VAL 24  
210 1 Y 1 C LYS 25  ? C LYS 25  
211 1 Y 1 C LEU 26  ? C LEU 26  
212 1 Y 1 C VAL 27  ? C VAL 27  
213 1 Y 1 C GLU 28  ? C GLU 28  
214 1 Y 1 C ASP 29  ? C ASP 29  
215 1 Y 1 C LYS 30  ? C LYS 30  
216 1 Y 1 C LYS 31  ? C LYS 31  
217 1 Y 1 C PHE 32  ? C PHE 32  
218 1 Y 1 C GLY 33  ? C GLY 33  
219 1 Y 1 C ALA 34  ? C ALA 34  
220 1 Y 1 C GLU 35  ? C GLU 35  
221 1 Y 1 C VAL 36  ? C VAL 36  
222 1 Y 1 C VAL 37  ? C VAL 37  
223 1 Y 1 C PRO 38  ? C PRO 38  
224 1 Y 1 C GLY 39  ? C GLY 39  
225 1 Y 1 C PHE 40  ? C PHE 40  
226 1 Y 1 C GLN 41  ? C GLN 41  
227 1 Y 1 C ALA 42  ? C ALA 42  
228 1 Y 1 C LEU 43  ? C LEU 43  
229 1 Y 1 C SER 44  ? C SER 44  
230 1 Y 1 C GLU 45  ? C GLU 45  
231 1 Y 1 C GLY 46  ? C GLY 46  
232 1 Y 1 C CYS 47  ? C CYS 47  
233 1 Y 1 C THR 48  ? C THR 48  
234 1 Y 1 C PRO 49  ? C PRO 49  
235 1 Y 1 C TYR 50  ? C TYR 50  
236 1 Y 1 C ASP 51  ? C ASP 51  
237 1 Y 1 C ILE 52  ? C ILE 52  
238 1 Y 1 C ASN 53  ? C ASN 53  
239 1 Y 1 C GLN 54  ? C GLN 54  
240 1 Y 1 C MET 55  ? C MET 55  
241 1 Y 1 C LEU 56  ? C LEU 56  
242 1 Y 1 C ASN 57  ? C ASN 57  
243 1 Y 1 C CYS 58  ? C CYS 58  
244 1 Y 1 C VAL 59  ? C VAL 59  
245 1 Y 1 C GLY 60  ? C GLY 60  
246 1 Y 1 C ASP 61  ? C ASP 61  
247 1 Y 1 C HIS 62  ? C HIS 62  
248 1 Y 1 C GLN 63  ? C GLN 63  
249 1 Y 1 C ALA 64  ? C ALA 64  
250 1 Y 1 C ALA 65  ? C ALA 65  
251 1 Y 1 C MET 66  ? C MET 66  
252 1 Y 1 C GLN 67  ? C GLN 67  
253 1 Y 1 C ILE 68  ? C ILE 68  
254 1 Y 1 C ILE 69  ? C ILE 69  
255 1 Y 1 C ARG 70  ? C ARG 70  
256 1 Y 1 C GLU 71  ? C GLU 71  
257 1 Y 1 C ILE 72  ? C ILE 72  
258 1 Y 1 C ILE 73  ? C ILE 73  
259 1 Y 1 C ASN 74  ? C ASN 74  
260 1 Y 1 C ASP 75  ? C ASP 75  
261 1 Y 1 C GLU 76  ? C GLU 76  
262 1 Y 1 C ALA 77  ? C ALA 77  
263 1 Y 1 C ALA 78  ? C ALA 78  
264 1 Y 1 C ASP 79  ? C ASP 79  
265 1 Y 1 C TRP 80  ? C TRP 80  
266 1 Y 1 C ASP 81  ? C ASP 81  
267 1 Y 1 C ALA 82  ? C ALA 82  
268 1 Y 1 C GLN 83  ? C GLN 83  
269 1 Y 1 C HIS 84  ? C HIS 84  
270 1 Y 1 C PRO 85  ? C PRO 85  
271 1 Y 1 C ILE 86  ? C ILE 86  
272 1 Y 1 C PRO 87  ? C PRO 87  
273 1 Y 1 C GLY 88  ? C GLY 88  
274 1 Y 1 C PRO 89  ? C PRO 89  
275 1 Y 1 C LEU 90  ? C LEU 90  
276 1 Y 1 C PRO 91  ? C PRO 91  
277 1 Y 1 C ALA 92  ? C ALA 92  
278 1 Y 1 C GLY 93  ? C GLY 93  
279 1 Y 1 C GLN 94  ? C GLN 94  
280 1 Y 1 C LEU 95  ? C LEU 95  
281 1 Y 1 C ARG 96  ? C ARG 96  
282 1 Y 1 C ASP 97  ? C ASP 97  
283 1 Y 1 C PRO 98  ? C PRO 98  
284 1 Y 1 C ARG 99  ? C ARG 99  
285 1 Y 1 C GLY 100 ? C GLY 100 
286 1 Y 1 C SER 101 ? C SER 101 
287 1 Y 1 C ASP 102 ? C ASP 102 
288 1 Y 1 C ILE 103 ? C ILE 103 
289 1 Y 1 C ALA 104 ? C ALA 104 
290 1 Y 1 C GLY 105 ? C GLY 105 
291 1 Y 1 C THR 106 ? C THR 106 
292 1 Y 1 C THR 107 ? C THR 107 
293 1 Y 1 C SER 108 ? C SER 108 
294 1 Y 1 C THR 109 ? C THR 109 
295 1 Y 1 C VAL 110 ? C VAL 110 
296 1 Y 1 C GLU 111 ? C GLU 111 
297 1 Y 1 C GLU 112 ? C GLU 112 
298 1 Y 1 C GLN 113 ? C GLN 113 
299 1 Y 1 C ILE 114 ? C ILE 114 
300 1 Y 1 C GLN 115 ? C GLN 115 
301 1 Y 1 C TRP 116 ? C TRP 116 
302 1 Y 1 C MET 117 ? C MET 117 
303 1 Y 1 C TYR 118 ? C TYR 118 
304 1 Y 1 C ARG 119 ? C ARG 119 
305 1 Y 1 C PRO 120 ? C PRO 120 
306 1 Y 1 C GLN 121 ? C GLN 121 
307 1 Y 1 C ASN 122 ? C ASN 122 
308 1 Y 1 C PRO 123 ? C PRO 123 
309 1 Y 1 C VAL 124 ? C VAL 124 
310 1 Y 1 C PRO 125 ? C PRO 125 
311 1 Y 1 C VAL 126 ? C VAL 126 
312 1 Y 1 C GLY 127 ? C GLY 127 
313 1 Y 1 C ASN 128 ? C ASN 128 
314 1 Y 1 C ILE 129 ? C ILE 129 
315 1 Y 1 C TYR 130 ? C TYR 130 
316 1 Y 1 C ARG 131 ? C ARG 131 
317 1 Y 1 C ARG 132 ? C ARG 132 
318 1 Y 1 C TRP 133 ? C TRP 133 
319 1 Y 1 C ILE 134 ? C ILE 134 
320 1 Y 1 C GLN 135 ? C GLN 135 
321 1 Y 1 C ILE 136 ? C ILE 136 
322 1 Y 1 C GLY 137 ? C GLY 137 
323 1 Y 1 C LEU 138 ? C LEU 138 
324 1 Y 1 C GLN 139 ? C GLN 139 
325 1 Y 1 C LYS 140 ? C LYS 140 
326 1 Y 1 C CYS 141 ? C CYS 141 
327 1 Y 1 C VAL 142 ? C VAL 142 
328 1 Y 1 C ARG 143 ? C ARG 143 
329 1 Y 1 C MET 144 ? C MET 144 
330 1 Y 1 C TYR 145 ? C TYR 145 
331 1 Y 1 C ASN 146 ? C ASN 146 
332 1 Y 1 C PRO 147 ? C PRO 147 
333 1 Y 1 C GLY 222 ? C GLY 222 
334 1 Y 1 C GLY 223 ? C GLY 223 
335 1 Y 1 C PRO 224 ? C PRO 224 
336 1 Y 1 C GLY 225 ? C GLY 225 
337 1 Y 1 C GLN 226 ? C GLN 226 
338 1 Y 1 C LYS 227 ? C LYS 227 
339 1 Y 1 C ALA 228 ? C ALA 228 
340 1 Y 1 C ARG 229 ? C ARG 229 
341 1 Y 1 C LEU 230 ? C LEU 230 
342 1 Y 1 C MET 231 ? C MET 231 
343 1 Y 1 C GLY 232 ? C GLY 232 
344 1 Y 1 C SER 233 ? C SER 233 
345 1 Y 1 C SER 234 ? C SER 234 
346 1 Y 1 C HIS 235 ? C HIS 235 
347 1 Y 1 C HIS 236 ? C HIS 236 
348 1 Y 1 C HIS 237 ? C HIS 237 
349 1 Y 1 C HIS 238 ? C HIS 238 
350 1 Y 1 C HIS 239 ? C HIS 239 
351 1 Y 1 C HIS 240 ? C HIS 240 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
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           9CNS 
_em_admin.last_update        2025-03-05 
_em_admin.map_release_date   2025-03-05 
_em_admin.title              'HIV-2 CA hexamer; assembled via 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 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          11709 
_em_entity_assembly_naturalsource.organism             'Human immunodeficiency virus 2' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               GL-AN 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          469008 
_em_entity_assembly_recombinant.organism             'Escherichia coli BL21(DE3)' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    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   13209858 
_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.

Sample was well-distributed on the grid, mostly monodisperse. Perhaps slightly more particles on carbon versus in the hole.
;
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' T32GM008283 1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' U54AI170791 2 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' P50AI150481 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8CKW 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CNS 
_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   ? 222.496 208.534 185.981 1.00 30.00 ? 1   PRO A N   1 
ATOM   2    C CA  . PRO A 1 1   ? 221.625 209.289 185.076 1.00 30.00 ? 1   PRO A CA  1 
ATOM   3    C C   . PRO A 1 1   ? 222.090 209.241 183.615 1.00 30.00 ? 1   PRO A C   1 
ATOM   4    O O   . PRO A 1 1   ? 223.145 208.701 183.357 1.00 30.00 ? 1   PRO A O   1 
ATOM   5    C CB  . PRO A 1 1   ? 221.801 210.719 185.584 1.00 30.00 ? 1   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 1   ? 221.836 210.561 187.065 1.00 30.00 ? 1   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 1   ? 222.576 209.258 187.259 1.00 30.00 ? 1   PRO A CD  1 
ATOM   8    N N   . VAL A 1 2   ? 221.305 209.796 182.685 1.00 30.00 ? 2   VAL A N   1 
ATOM   9    C CA  . VAL A 1 2   ? 221.642 209.759 181.231 1.00 30.00 ? 2   VAL A CA  1 
ATOM   10   C C   . VAL A 1 2   ? 221.556 211.155 180.615 1.00 30.00 ? 2   VAL A C   1 
ATOM   11   O O   . VAL A 1 2   ? 220.487 211.762 180.728 1.00 30.00 ? 2   VAL A O   1 
ATOM   12   C CB  . VAL A 1 2   ? 220.729 208.786 180.469 1.00 30.00 ? 2   VAL A CB  1 
ATOM   13   C CG1 . VAL A 1 2   ? 221.207 208.607 179.037 1.00 30.00 ? 2   VAL A CG1 1 
ATOM   14   C CG2 . VAL A 1 2   ? 220.630 207.443 181.164 1.00 30.00 ? 2   VAL A CG2 1 
ATOM   15   N N   . GLN A 1 3   ? 222.626 211.637 179.981 1.00 30.00 ? 3   GLN A N   1 
ATOM   16   C CA  . GLN A 1 3   ? 222.643 212.934 179.254 1.00 30.00 ? 3   GLN A CA  1 
ATOM   17   C C   . GLN A 1 3   ? 222.922 212.651 177.782 1.00 30.00 ? 3   GLN A C   1 
ATOM   18   O O   . GLN A 1 3   ? 223.914 211.968 177.524 1.00 30.00 ? 3   GLN A O   1 
ATOM   19   C CB  . GLN A 1 3   ? 223.748 213.846 179.774 1.00 30.00 ? 3   GLN A CB  1 
ATOM   20   C CG  . GLN A 1 3   ? 223.919 215.124 178.969 1.00 30.00 ? 3   GLN A CG  1 
ATOM   21   C CD  . GLN A 1 3   ? 222.639 215.915 178.873 1.00 30.00 ? 3   GLN A CD  1 
ATOM   22   O OE1 . GLN A 1 3   ? 222.098 216.130 177.791 1.00 30.00 ? 3   GLN A OE1 1 
ATOM   23   N NE2 . GLN A 1 3   ? 222.131 216.342 180.017 1.00 30.00 ? 3   GLN A NE2 1 
ATOM   24   N N   . GLN A 1 4   ? 222.102 213.157 176.861 1.00 30.00 ? 4   GLN A N   1 
ATOM   25   C CA  . GLN A 1 4   ? 222.264 212.900 175.406 1.00 30.00 ? 4   GLN A CA  1 
ATOM   26   C C   . GLN A 1 4   ? 223.207 213.961 174.850 1.00 30.00 ? 4   GLN A C   1 
ATOM   27   O O   . GLN A 1 4   ? 223.380 214.981 175.532 1.00 30.00 ? 4   GLN A O   1 
ATOM   28   C CB  . GLN A 1 4   ? 220.923 212.932 174.679 1.00 30.00 ? 4   GLN A CB  1 
ATOM   29   C CG  . GLN A 1 4   ? 220.326 214.322 174.529 1.00 30.00 ? 4   GLN A CG  1 
ATOM   30   C CD  . GLN A 1 4   ? 219.008 214.279 173.797 1.00 30.00 ? 4   GLN A CD  1 
ATOM   31   O OE1 . GLN A 1 4   ? 218.057 213.631 174.228 1.00 30.00 ? 4   GLN A OE1 1 
ATOM   32   N NE2 . GLN A 1 4   ? 218.946 214.969 172.671 1.00 30.00 ? 4   GLN A NE2 1 
ATOM   33   N N   . THR A 1 5   ? 223.798 213.733 173.678 1.00 30.00 ? 5   THR A N   1 
ATOM   34   C CA  . THR A 1 5   ? 224.780 214.670 173.072 1.00 30.00 ? 5   THR A CA  1 
ATOM   35   C C   . THR A 1 5   ? 224.424 214.907 171.602 1.00 30.00 ? 5   THR A C   1 
ATOM   36   O O   . THR A 1 5   ? 223.763 214.025 171.018 1.00 30.00 ? 5   THR A O   1 
ATOM   37   C CB  . THR A 1 5   ? 226.196 214.121 173.273 1.00 30.00 ? 5   THR A CB  1 
ATOM   38   O OG1 . THR A 1 5   ? 226.267 212.853 172.624 1.00 30.00 ? 5   THR A OG1 1 
ATOM   39   C CG2 . THR A 1 5   ? 226.566 213.960 174.730 1.00 30.00 ? 5   THR A CG2 1 
ATOM   40   N N   . GLY A 1 6   ? 224.846 216.039 171.028 1.00 30.00 ? 6   GLY A N   1 
ATOM   41   C CA  . GLY A 1 6   ? 224.578 216.373 169.614 1.00 30.00 ? 6   GLY A CA  1 
ATOM   42   C C   . GLY A 1 6   ? 225.774 216.010 168.758 1.00 30.00 ? 6   GLY A C   1 
ATOM   43   O O   . GLY A 1 6   ? 226.844 216.611 168.975 1.00 30.00 ? 6   GLY A O   1 
ATOM   44   N N   . GLY A 1 7   ? 225.618 215.061 167.830 1.00 30.00 ? 7   GLY A N   1 
ATOM   45   C CA  . GLY A 1 7   ? 226.739 214.554 167.016 1.00 30.00 ? 7   GLY A CA  1 
ATOM   46   C C   . GLY A 1 7   ? 227.372 213.369 167.719 1.00 30.00 ? 7   GLY A C   1 
ATOM   47   O O   . GLY A 1 7   ? 228.307 212.782 167.141 1.00 30.00 ? 7   GLY A O   1 
ATOM   48   N N   . GLY A 1 8   ? 226.890 213.032 168.921 1.00 30.00 ? 8   GLY A N   1 
ATOM   49   C CA  . GLY A 1 8   ? 227.403 211.905 169.724 1.00 30.00 ? 8   GLY A CA  1 
ATOM   50   C C   . GLY A 1 8   ? 226.257 211.077 170.273 1.00 30.00 ? 8   GLY A C   1 
ATOM   51   O O   . GLY A 1 8   ? 225.103 211.534 170.154 1.00 30.00 ? 8   GLY A O   1 
ATOM   52   N N   . ASN A 1 9   ? 226.544 209.907 170.847 1.00 30.00 ? 9   ASN A N   1 
ATOM   53   C CA  . ASN A 1 9   ? 225.510 209.001 171.411 1.00 30.00 ? 9   ASN A CA  1 
ATOM   54   C C   . ASN A 1 9   ? 225.191 209.393 172.852 1.00 30.00 ? 9   ASN A C   1 
ATOM   55   O O   . ASN A 1 9   ? 225.952 210.201 173.420 1.00 30.00 ? 9   ASN A O   1 
ATOM   56   C CB  . ASN A 1 9   ? 225.963 207.542 171.405 1.00 30.00 ? 9   ASN A CB  1 
ATOM   57   C CG  . ASN A 1 9   ? 226.267 207.020 170.019 1.00 30.00 ? 9   ASN A CG  1 
ATOM   58   O OD1 . ASN A 1 9   ? 227.153 207.531 169.337 1.00 30.00 ? 9   ASN A OD1 1 
ATOM   59   N ND2 . ASN A 1 9   ? 225.545 205.995 169.599 1.00 30.00 ? 9   ASN A ND2 1 
ATOM   60   N N   . TYR A 1 10  ? 224.129 208.831 173.434 1.00 30.00 ? 10  TYR A N   1 
ATOM   61   C CA  . TYR A 1 10  ? 223.768 209.076 174.852 1.00 30.00 ? 10  TYR A CA  1 
ATOM   62   C C   . TYR A 1 10  ? 224.957 208.722 175.740 1.00 30.00 ? 10  TYR A C   1 
ATOM   63   O O   . TYR A 1 10  ? 225.659 207.743 175.415 1.00 30.00 ? 10  TYR A O   1 
ATOM   64   C CB  . TYR A 1 10  ? 222.626 208.182 175.324 1.00 30.00 ? 10  TYR A CB  1 
ATOM   65   C CG  . TYR A 1 10  ? 221.250 208.475 174.791 1.00 30.00 ? 10  TYR A CG  1 
ATOM   66   C CD1 . TYR A 1 10  ? 220.640 209.694 175.014 1.00 30.00 ? 10  TYR A CD1 1 
ATOM   67   C CD2 . TYR A 1 10  ? 220.530 207.503 174.120 1.00 30.00 ? 10  TYR A CD2 1 
ATOM   68   C CE1 . TYR A 1 10  ? 219.362 209.956 174.552 1.00 30.00 ? 10  TYR A CE1 1 
ATOM   69   C CE2 . TYR A 1 10  ? 219.252 207.746 173.650 1.00 30.00 ? 10  TYR A CE2 1 
ATOM   70   C CZ  . TYR A 1 10  ? 218.665 208.978 173.867 1.00 30.00 ? 10  TYR A CZ  1 
ATOM   71   O OH  . TYR A 1 10  ? 217.399 209.222 173.400 1.00 30.00 ? 10  TYR A OH  1 
ATOM   72   N N   . ILE A 1 11  ? 225.181 209.455 176.823 1.00 30.00 ? 11  ILE A N   1 
ATOM   73   C CA  . ILE A 1 11  ? 226.287 209.145 177.770 1.00 30.00 ? 11  ILE A CA  1 
ATOM   74   C C   . ILE A 1 11  ? 225.684 208.951 179.158 1.00 30.00 ? 11  ILE A C   1 
ATOM   75   O O   . ILE A 1 11  ? 224.506 209.296 179.325 1.00 30.00 ? 11  ILE A O   1 
ATOM   76   C CB  . ILE A 1 11  ? 227.363 210.248 177.727 1.00 30.00 ? 11  ILE A CB  1 
ATOM   77   C CG1 . ILE A 1 11  ? 228.567 209.907 178.608 1.00 30.00 ? 11  ILE A CG1 1 
ATOM   78   C CG2 . ILE A 1 11  ? 226.784 211.611 178.074 1.00 30.00 ? 11  ILE A CG2 1 
ATOM   79   C CD1 . ILE A 1 11  ? 229.778 210.764 178.348 1.00 30.00 ? 11  ILE A CD1 1 
ATOM   80   N N   . HIS A 1 12  ? 226.434 208.365 180.087 1.00 30.00 ? 12  HIS A N   1 
ATOM   81   C CA  . HIS A 1 12  ? 225.977 208.223 181.488 1.00 30.00 ? 12  HIS A CA  1 
ATOM   82   C C   . HIS A 1 12  ? 226.626 209.303 182.331 1.00 30.00 ? 12  HIS A C   1 
ATOM   83   O O   . HIS A 1 12  ? 227.850 209.230 182.583 1.00 30.00 ? 12  HIS A O   1 
ATOM   84   C CB  . HIS A 1 12  ? 226.444 206.922 182.124 1.00 30.00 ? 12  HIS A CB  1 
ATOM   85   C CG  . HIS A 1 12  ? 226.365 206.851 183.613 1.00 30.00 ? 12  HIS A CG  1 
ATOM   86   N ND1 . HIS A 1 12  ? 227.503 206.751 184.380 1.00 30.00 ? 12  HIS A ND1 1 
ATOM   87   C CD2 . HIS A 1 12  ? 225.351 206.875 184.477 1.00 30.00 ? 12  HIS A CD2 1 
ATOM   88   C CE1 . HIS A 1 12  ? 227.171 206.705 185.659 1.00 30.00 ? 12  HIS A CE1 1 
ATOM   89   N NE2 . HIS A 1 12  ? 225.868 206.774 185.739 1.00 30.00 ? 12  HIS A NE2 1 
ATOM   90   N N   . VAL A 1 13  ? 225.844 210.288 182.739 1.00 30.00 ? 13  VAL A N   1 
ATOM   91   C CA  . VAL A 1 13  ? 226.356 211.305 183.684 1.00 30.00 ? 13  VAL A CA  1 
ATOM   92   C C   . VAL A 1 13  ? 226.298 210.602 185.031 1.00 30.00 ? 13  VAL A C   1 
ATOM   93   O O   . VAL A 1 13  ? 225.521 209.668 185.141 1.00 30.00 ? 13  VAL A O   1 
ATOM   94   C CB  . VAL A 1 13  ? 225.491 212.566 183.648 1.00 30.00 ? 13  VAL A CB  1 
ATOM   95   C CG1 . VAL A 1 13  ? 225.787 213.533 184.778 1.00 30.00 ? 13  VAL A CG1 1 
ATOM   96   C CG2 . VAL A 1 13  ? 225.618 213.266 182.312 1.00 30.00 ? 13  VAL A CG2 1 
ATOM   97   N N   . PRO A 1 14  ? 227.148 210.921 186.014 1.00 30.00 ? 14  PRO A N   1 
ATOM   98   C CA  . PRO A 1 14  ? 227.017 210.312 187.330 1.00 30.00 ? 14  PRO A CA  1 
ATOM   99   C C   . PRO A 1 14  ? 225.911 210.869 188.225 1.00 30.00 ? 14  PRO A C   1 
ATOM   100  O O   . PRO A 1 14  ? 225.324 211.867 187.854 1.00 30.00 ? 14  PRO A O   1 
ATOM   101  C CB  . PRO A 1 14  ? 228.324 210.750 187.977 1.00 30.00 ? 14  PRO A CB  1 
ATOM   102  C CG  . PRO A 1 14  ? 228.629 212.059 187.336 1.00 30.00 ? 14  PRO A CG  1 
ATOM   103  C CD  . PRO A 1 14  ? 228.322 211.778 185.890 1.00 30.00 ? 14  PRO A CD  1 
ATOM   104  N N   . LEU A 1 15  ? 225.653 210.232 189.370 1.00 30.00 ? 15  LEU A N   1 
ATOM   105  C CA  . LEU A 1 15  ? 224.710 210.804 190.360 1.00 30.00 ? 15  LEU A CA  1 
ATOM   106  C C   . LEU A 1 15  ? 225.517 211.859 191.100 1.00 30.00 ? 15  LEU A C   1 
ATOM   107  O O   . LEU A 1 15  ? 226.758 211.820 190.981 1.00 30.00 ? 15  LEU A O   1 
ATOM   108  C CB  . LEU A 1 15  ? 224.202 209.746 191.337 1.00 30.00 ? 15  LEU A CB  1 
ATOM   109  C CG  . LEU A 1 15  ? 222.951 210.115 192.131 1.00 30.00 ? 15  LEU A CG  1 
ATOM   110  C CD1 . LEU A 1 15  ? 221.803 210.527 191.222 1.00 30.00 ? 15  LEU A CD1 1 
ATOM   111  C CD2 . LEU A 1 15  ? 222.500 208.949 192.980 1.00 30.00 ? 15  LEU A CD2 1 
ATOM   112  N N   . SER A 1 16  ? 224.865 212.743 191.844 1.00 30.00 ? 16  SER A N   1 
ATOM   113  C CA  . SER A 1 16  ? 225.573 213.860 192.505 1.00 30.00 ? 16  SER A CA  1 
ATOM   114  C C   . SER A 1 16  ? 225.650 213.650 194.014 1.00 30.00 ? 16  SER A C   1 
ATOM   115  O O   . SER A 1 16  ? 224.666 213.189 194.605 1.00 30.00 ? 16  SER A O   1 
ATOM   116  C CB  . SER A 1 16  ? 224.913 215.137 192.199 1.00 30.00 ? 16  SER A CB  1 
ATOM   117  O OG  . SER A 1 16  ? 223.577 215.129 192.660 1.00 30.00 ? 16  SER A OG  1 
ATOM   118  N N   . PRO A 1 17  ? 226.774 214.033 194.644 1.00 30.00 ? 17  PRO A N   1 
ATOM   119  C CA  . PRO A 1 17  ? 226.962 213.869 196.084 1.00 30.00 ? 17  PRO A CA  1 
ATOM   120  C C   . PRO A 1 17  ? 225.850 214.424 196.975 1.00 30.00 ? 17  PRO A C   1 
ATOM   121  O O   . PRO A 1 17  ? 225.456 213.724 197.863 1.00 30.00 ? 17  PRO A O   1 
ATOM   122  C CB  . PRO A 1 17  ? 228.167 214.782 196.302 1.00 30.00 ? 17  PRO A CB  1 
ATOM   123  C CG  . PRO A 1 17  ? 228.962 214.648 195.056 1.00 30.00 ? 17  PRO A CG  1 
ATOM   124  C CD  . PRO A 1 17  ? 227.901 214.695 193.994 1.00 30.00 ? 17  PRO A CD  1 
ATOM   125  N N   . ARG A 1 18  ? 225.468 215.687 196.768 1.00 30.00 ? 18  ARG A N   1 
ATOM   126  C CA  . ARG A 1 18  ? 224.397 216.361 197.539 1.00 30.00 ? 18  ARG A CA  1 
ATOM   127  C C   . ARG A 1 18  ? 223.163 215.478 197.644 1.00 30.00 ? 18  ARG A C   1 
ATOM   128  O O   . ARG A 1 18  ? 222.575 215.441 198.730 1.00 30.00 ? 18  ARG A O   1 
ATOM   129  C CB  . ARG A 1 18  ? 223.930 217.599 196.784 1.00 30.00 ? 18  ARG A CB  1 
ATOM   130  C CG  . ARG A 1 18  ? 224.970 218.695 196.627 1.00 30.00 ? 18  ARG A CG  1 
ATOM   131  C CD  . ARG A 1 18  ? 224.325 219.937 196.047 1.00 30.00 ? 18  ARG A CD  1 
ATOM   132  N NE  . ARG A 1 18  ? 225.273 221.016 195.808 1.00 30.00 ? 18  ARG A NE  1 
ATOM   133  C CZ  . ARG A 1 18  ? 225.521 221.568 194.624 1.00 30.00 ? 18  ARG A CZ  1 
ATOM   134  N NH1 . ARG A 1 18  ? 225.954 222.814 194.560 1.00 30.00 ? 18  ARG A NH1 1 
ATOM   135  N NH2 . ARG A 1 18  ? 225.326 220.887 193.506 1.00 30.00 ? 18  ARG A NH2 1 
ATOM   136  N N   . THR A 1 19  ? 222.752 214.863 196.539 1.00 30.00 ? 19  THR A N   1 
ATOM   137  C CA  . THR A 1 19  ? 221.538 214.022 196.454 1.00 30.00 ? 19  THR A CA  1 
ATOM   138  C C   . THR A 1 19  ? 221.734 212.712 197.204 1.00 30.00 ? 19  THR A C   1 
ATOM   139  O O   . THR A 1 19  ? 220.783 212.272 197.862 1.00 30.00 ? 19  THR A O   1 
ATOM   140  C CB  . THR A 1 19  ? 221.296 213.753 194.978 1.00 30.00 ? 19  THR A CB  1 
ATOM   141  O OG1 . THR A 1 19  ? 221.066 215.019 194.368 1.00 30.00 ? 19  THR A OG1 1 
ATOM   142  C CG2 . THR A 1 19  ? 220.133 212.830 194.710 1.00 30.00 ? 19  THR A CG2 1 
ATOM   143  N N   . LEU A 1 20  ? 222.898 212.090 197.053 1.00 30.00 ? 20  LEU A N   1 
ATOM   144  C CA  . LEU A 1 20  ? 223.241 210.857 197.797 1.00 30.00 ? 20  LEU A CA  1 
ATOM   145  C C   . LEU A 1 20  ? 223.126 211.149 199.287 1.00 30.00 ? 20  LEU A C   1 
ATOM   146  O O   . LEU A 1 20  ? 222.665 210.264 200.019 1.00 30.00 ? 20  LEU A O   1 
ATOM   147  C CB  . LEU A 1 20  ? 224.689 210.515 197.471 1.00 30.00 ? 20  LEU A CB  1 
ATOM   148  C CG  . LEU A 1 20  ? 224.949 209.527 196.344 1.00 30.00 ? 20  LEU A CG  1 
ATOM   149  C CD1 . LEU A 1 20  ? 224.735 210.160 194.991 1.00 30.00 ? 20  LEU A CD1 1 
ATOM   150  C CD2 . LEU A 1 20  ? 226.367 209.009 196.434 1.00 30.00 ? 20  LEU A CD2 1 
ATOM   151  N N   . ASN A 1 21  ? 223.512 212.354 199.705 1.00 30.00 ? 21  ASN A N   1 
ATOM   152  C CA  . ASN A 1 21  ? 223.547 212.756 201.131 1.00 30.00 ? 21  ASN A CA  1 
ATOM   153  C C   . ASN A 1 21  ? 222.174 213.121 201.669 1.00 30.00 ? 21  ASN A C   1 
ATOM   154  O O   . ASN A 1 21  ? 221.954 212.921 202.870 1.00 30.00 ? 21  ASN A O   1 
ATOM   155  C CB  . ASN A 1 21  ? 224.341 214.040 201.278 1.00 30.00 ? 21  ASN A CB  1 
ATOM   156  C CG  . ASN A 1 21  ? 225.787 213.889 200.876 1.00 30.00 ? 21  ASN A CG  1 
ATOM   157  O OD1 . ASN A 1 21  ? 226.232 212.795 200.547 1.00 30.00 ? 21  ASN A OD1 1 
ATOM   158  N ND2 . ASN A 1 21  ? 226.531 214.980 200.921 1.00 30.00 ? 21  ASN A ND2 1 
ATOM   159  N N   . ALA A 1 22  ? 221.319 213.695 200.833 1.00 30.00 ? 22  ALA A N   1 
ATOM   160  C CA  . ALA A 1 22  ? 219.973 214.138 201.233 1.00 30.00 ? 22  ALA A CA  1 
ATOM   161  C C   . ALA A 1 22  ? 219.102 212.923 201.510 1.00 30.00 ? 22  ALA A C   1 
ATOM   162  O O   . ALA A 1 22  ? 218.369 212.937 202.514 1.00 30.00 ? 22  ALA A O   1 
ATOM   163  C CB  . ALA A 1 22  ? 219.436 214.913 200.095 1.00 30.00 ? 22  ALA A CB  1 
ATOM   164  N N   . TRP A 1 23  ? 219.174 211.924 200.640 1.00 30.00 ? 23  TRP A N   1 
ATOM   165  C CA  . TRP A 1 23  ? 218.439 210.653 200.814 1.00 30.00 ? 23  TRP A CA  1 
ATOM   166  C C   . TRP A 1 23  ? 218.868 210.036 202.136 1.00 30.00 ? 23  TRP A C   1 
ATOM   167  O O   . TRP A 1 23  ? 217.987 209.615 202.905 1.00 30.00 ? 23  TRP A O   1 
ATOM   168  C CB  . TRP A 1 23  ? 218.828 209.760 199.648 1.00 30.00 ? 23  TRP A CB  1 
ATOM   169  C CG  . TRP A 1 23  ? 218.485 208.329 199.834 1.00 30.00 ? 23  TRP A CG  1 
ATOM   170  C CD1 . TRP A 1 23  ? 219.331 207.266 199.831 1.00 30.00 ? 23  TRP A CD1 1 
ATOM   171  C CD2 . TRP A 1 23  ? 217.175 207.815 200.073 1.00 30.00 ? 23  TRP A CD2 1 
ATOM   172  N NE1 . TRP A 1 23  ? 218.628 206.115 200.048 1.00 30.00 ? 23  TRP A NE1 1 
ATOM   173  C CE2 . TRP A 1 23  ? 217.303 206.423 200.204 1.00 30.00 ? 23  TRP A CE2 1 
ATOM   174  C CE3 . TRP A 1 23  ? 215.919 208.403 200.192 1.00 30.00 ? 23  TRP A CE3 1 
ATOM   175  C CZ2 . TRP A 1 23  ? 216.208 205.606 200.450 1.00 30.00 ? 23  TRP A CZ2 1 
ATOM   176  C CZ3 . TRP A 1 23  ? 214.839 207.595 200.434 1.00 30.00 ? 23  TRP A CZ3 1 
ATOM   177  C CH2 . TRP A 1 23  ? 214.985 206.218 200.564 1.00 30.00 ? 23  TRP A CH2 1 
ATOM   178  N N   . VAL A 1 24  ? 220.170 210.036 202.394 1.00 30.00 ? 24  VAL A N   1 
ATOM   179  C CA  . VAL A 1 24  ? 220.771 209.491 203.639 1.00 30.00 ? 24  VAL A CA  1 
ATOM   180  C C   . VAL A 1 24  ? 220.283 210.287 204.843 1.00 30.00 ? 24  VAL A C   1 
ATOM   181  O O   . VAL A 1 24  ? 220.161 209.698 205.931 1.00 30.00 ? 24  VAL A O   1 
ATOM   182  C CB  . VAL A 1 24  ? 222.291 209.620 203.495 1.00 30.00 ? 24  VAL A CB  1 
ATOM   183  C CG1 . VAL A 1 24  ? 223.010 209.552 204.825 1.00 30.00 ? 24  VAL A CG1 1 
ATOM   184  C CG2 . VAL A 1 24  ? 222.852 208.588 202.538 1.00 30.00 ? 24  VAL A CG2 1 
ATOM   185  N N   . LYS A 1 25  ? 220.054 211.581 204.664 1.00 30.00 ? 25  LYS A N   1 
ATOM   186  C CA  . LYS A 1 25  ? 219.686 212.492 205.772 1.00 30.00 ? 25  LYS A CA  1 
ATOM   187  C C   . LYS A 1 25  ? 218.165 212.586 205.895 1.00 30.00 ? 25  LYS A C   1 
ATOM   188  O O   . LYS A 1 25  ? 217.696 213.279 206.812 1.00 30.00 ? 25  LYS A O   1 
ATOM   189  C CB  . LYS A 1 25  ? 220.367 213.806 205.413 1.00 30.00 ? 25  LYS A CB  1 
ATOM   190  C CG  . LYS A 1 25  ? 220.372 214.869 206.496 1.00 30.00 ? 25  LYS A CG  1 
ATOM   191  C CD  . LYS A 1 25  ? 221.299 216.017 206.181 1.00 30.00 ? 25  LYS A CD  1 
ATOM   192  C CE  . LYS A 1 25  ? 220.962 216.712 204.880 1.00 30.00 ? 25  LYS A CE  1 
ATOM   193  N NZ  . LYS A 1 25  ? 221.832 217.889 204.652 1.00 30.00 ? 25  LYS A NZ  1 
ATOM   194  N N   . LEU A 1 26  ? 217.424 211.925 205.008 1.00 30.00 ? 26  LEU A N   1 
ATOM   195  C CA  . LEU A 1 26  ? 215.940 211.889 205.036 1.00 30.00 ? 26  LEU A CA  1 
ATOM   196  C C   . LEU A 1 26  ? 215.510 210.553 205.632 1.00 30.00 ? 26  LEU A C   1 
ATOM   197  O O   . LEU A 1 26  ? 214.312 210.391 205.919 1.00 30.00 ? 26  LEU A O   1 
ATOM   198  C CB  . LEU A 1 26  ? 215.487 212.024 203.586 1.00 30.00 ? 26  LEU A CB  1 
ATOM   199  C CG  . LEU A 1 26  ? 214.008 211.854 203.279 1.00 30.00 ? 26  LEU A CG  1 
ATOM   200  C CD1 . LEU A 1 26  ? 213.214 213.014 203.839 1.00 30.00 ? 26  LEU A CD1 1 
ATOM   201  C CD2 . LEU A 1 26  ? 213.801 211.742 201.783 1.00 30.00 ? 26  LEU A CD2 1 
ATOM   202  N N   . VAL A 1 27  ? 216.461 209.645 205.826 1.00 30.00 ? 27  VAL A N   1 
ATOM   203  C CA  . VAL A 1 27  ? 216.179 208.274 206.333 1.00 30.00 ? 27  VAL A CA  1 
ATOM   204  C C   . VAL A 1 27  ? 216.751 208.109 207.735 1.00 30.00 ? 27  VAL A C   1 
ATOM   205  O O   . VAL A 1 27  ? 216.206 207.287 208.498 1.00 30.00 ? 27  VAL A O   1 
ATOM   206  C CB  . VAL A 1 27  ? 216.817 207.257 205.382 1.00 30.00 ? 27  VAL A CB  1 
ATOM   207  C CG1 . VAL A 1 27  ? 216.159 207.278 204.020 1.00 30.00 ? 27  VAL A CG1 1 
ATOM   208  C CG2 . VAL A 1 27  ? 218.315 207.410 205.254 1.00 30.00 ? 27  VAL A CG2 1 
ATOM   209  N N   . GLU A 1 28  ? 217.800 208.860 208.056 1.00 30.00 ? 28  GLU A N   1 
ATOM   210  C CA  . GLU A 1 28  ? 218.494 208.758 209.360 1.00 30.00 ? 28  GLU A CA  1 
ATOM   211  C C   . GLU A 1 28  ? 217.940 209.803 210.313 1.00 30.00 ? 28  GLU A C   1 
ATOM   212  O O   . GLU A 1 28  ? 218.383 209.808 211.475 1.00 30.00 ? 28  GLU A O   1 
ATOM   213  C CB  . GLU A 1 28  ? 219.968 209.057 209.150 1.00 30.00 ? 28  GLU A CB  1 
ATOM   214  C CG  . GLU A 1 28  ? 220.696 207.946 208.424 1.00 30.00 ? 28  GLU A CG  1 
ATOM   215  C CD  . GLU A 1 28  ? 222.154 208.243 208.132 1.00 30.00 ? 28  GLU A CD  1 
ATOM   216  O OE1 . GLU A 1 28  ? 222.611 209.343 208.489 1.00 30.00 ? 28  GLU A OE1 1 
ATOM   217  O OE2 . GLU A 1 28  ? 222.828 207.369 207.560 1.00 30.00 ? 28  GLU A OE2 1 
ATOM   218  N N   . ASP A 1 29  ? 217.062 210.678 209.824 1.00 30.00 ? 29  ASP A N   1 
ATOM   219  C CA  . ASP A 1 29  ? 216.506 211.785 210.634 1.00 30.00 ? 29  ASP A CA  1 
ATOM   220  C C   . ASP A 1 29  ? 214.999 211.617 210.756 1.00 30.00 ? 29  ASP A C   1 
ATOM   221  O O   . ASP A 1 29  ? 214.466 211.846 211.859 1.00 30.00 ? 29  ASP A O   1 
ATOM   222  C CB  . ASP A 1 29  ? 216.802 213.103 209.938 1.00 30.00 ? 29  ASP A CB  1 
ATOM   223  C CG  . ASP A 1 29  ? 218.279 213.333 209.685 1.00 30.00 ? 29  ASP A CG  1 
ATOM   224  O OD1 . ASP A 1 29  ? 219.078 212.439 210.019 1.00 30.00 ? 29  ASP A OD1 1 
ATOM   225  O OD2 . ASP A 1 29  ? 218.615 214.407 209.158 1.00 30.00 ? 29  ASP A OD2 1 
ATOM   226  N N   . LYS A 1 30  ? 214.352 211.223 209.664 1.00 30.00 ? 30  LYS A N   1 
ATOM   227  C CA  . LYS A 1 30  ? 212.885 211.032 209.633 1.00 30.00 ? 30  LYS A CA  1 
ATOM   228  C C   . LYS A 1 30  ? 212.597 209.586 210.024 1.00 30.00 ? 30  LYS A C   1 
ATOM   229  O O   . LYS A 1 30  ? 211.405 209.228 210.099 1.00 30.00 ? 30  LYS A O   1 
ATOM   230  C CB  . LYS A 1 30  ? 212.372 211.354 208.234 1.00 30.00 ? 30  LYS A CB  1 
ATOM   231  C CG  . LYS A 1 30  ? 212.858 212.669 207.649 1.00 30.00 ? 30  LYS A CG  1 
ATOM   232  C CD  . LYS A 1 30  ? 212.605 213.858 208.523 1.00 30.00 ? 30  LYS A CD  1 
ATOM   233  C CE  . LYS A 1 30  ? 212.904 215.153 207.803 1.00 30.00 ? 30  LYS A CE  1 
ATOM   234  N NZ  . LYS A 1 30  ? 212.602 216.327 208.653 1.00 30.00 ? 30  LYS A NZ  1 
ATOM   235  N N   . LYS A 1 31  ? 213.643 208.791 210.271 1.00 30.00 ? 31  LYS A N   1 
ATOM   236  C CA  . LYS A 1 31  ? 213.486 207.375 210.686 1.00 30.00 ? 31  LYS A CA  1 
ATOM   237  C C   . LYS A 1 31  ? 212.485 206.708 209.747 1.00 30.00 ? 31  LYS A C   1 
ATOM   238  O O   . LYS A 1 31  ? 211.447 206.220 210.239 1.00 30.00 ? 31  LYS A O   1 
ATOM   239  C CB  . LYS A 1 31  ? 213.031 207.344 212.145 1.00 30.00 ? 31  LYS A CB  1 
ATOM   240  C CG  . LYS A 1 31  ? 213.914 208.133 213.100 1.00 30.00 ? 31  LYS A CG  1 
ATOM   241  C CD  . LYS A 1 31  ? 215.375 207.749 213.028 1.00 30.00 ? 31  LYS A CD  1 
ATOM   242  C CE  . LYS A 1 31  ? 216.235 208.487 214.031 1.00 30.00 ? 31  LYS A CE  1 
ATOM   243  N NZ  . LYS A 1 31  ? 216.228 209.949 213.791 1.00 30.00 ? 31  LYS A NZ  1 
ATOM   244  N N   . PHE A 1 32  ? 212.782 206.684 208.447 1.00 30.00 ? 32  PHE A N   1 
ATOM   245  C CA  . PHE A 1 32  ? 211.874 206.107 207.423 1.00 30.00 ? 32  PHE A CA  1 
ATOM   246  C C   . PHE A 1 32  ? 210.476 206.701 207.593 1.00 30.00 ? 32  PHE A C   1 
ATOM   247  O O   . PHE A 1 32  ? 209.500 205.930 207.650 1.00 30.00 ? 32  PHE A O   1 
ATOM   248  C CB  . PHE A 1 32  ? 211.873 204.577 207.477 1.00 30.00 ? 32  PHE A CB  1 
ATOM   249  C CG  . PHE A 1 32  ? 213.022 203.953 206.740 1.00 30.00 ? 32  PHE A CG  1 
ATOM   250  C CD1 . PHE A 1 32  ? 214.324 204.172 207.144 1.00 30.00 ? 32  PHE A CD1 1 
ATOM   251  C CD2 . PHE A 1 32  ? 212.796 203.199 205.604 1.00 30.00 ? 32  PHE A CD2 1 
ATOM   252  C CE1 . PHE A 1 32  ? 215.379 203.610 206.450 1.00 30.00 ? 32  PHE A CE1 1 
ATOM   253  C CE2 . PHE A 1 32  ? 213.854 202.645 204.906 1.00 30.00 ? 32  PHE A CE2 1 
ATOM   254  C CZ  . PHE A 1 32  ? 215.142 202.851 205.332 1.00 30.00 ? 32  PHE A CZ  1 
ATOM   255  N N   . GLY A 1 33  ? 210.362 208.030 207.622 1.00 30.00 ? 33  GLY A N   1 
ATOM   256  C CA  . GLY A 1 33  ? 209.032 208.664 207.622 1.00 30.00 ? 33  GLY A CA  1 
ATOM   257  C C   . GLY A 1 33  ? 208.416 208.394 206.263 1.00 30.00 ? 33  GLY A C   1 
ATOM   258  O O   . GLY A 1 33  ? 209.192 208.169 205.337 1.00 30.00 ? 33  GLY A O   1 
ATOM   259  N N   . ALA A 1 34  ? 207.095 208.420 206.118 1.00 30.00 ? 34  ALA A N   1 
ATOM   260  C CA  . ALA A 1 34  ? 206.406 208.084 204.851 1.00 30.00 ? 34  ALA A CA  1 
ATOM   261  C C   . ALA A 1 34  ? 206.947 208.934 203.710 1.00 30.00 ? 34  ALA A C   1 
ATOM   262  O O   . ALA A 1 34  ? 207.070 208.413 202.589 1.00 30.00 ? 34  ALA A O   1 
ATOM   263  C CB  . ALA A 1 34  ? 204.968 208.390 205.014 1.00 30.00 ? 34  ALA A CB  1 
ATOM   264  N N   . GLU A 1 35  ? 207.231 210.196 203.993 1.00 30.00 ? 35  GLU A N   1 
ATOM   265  C CA  . GLU A 1 35  ? 207.760 211.164 203.006 1.00 30.00 ? 35  GLU A CA  1 
ATOM   266  C C   . GLU A 1 35  ? 209.038 210.659 202.356 1.00 30.00 ? 35  GLU A C   1 
ATOM   267  O O   . GLU A 1 35  ? 209.427 211.195 201.303 1.00 30.00 ? 35  GLU A O   1 
ATOM   268  C CB  . GLU A 1 35  ? 208.119 212.403 203.793 1.00 30.00 ? 35  GLU A CB  1 
ATOM   269  C CG  . GLU A 1 35  ? 209.117 212.160 204.905 1.00 30.00 ? 35  GLU A CG  1 
ATOM   270  C CD  . GLU A 1 35  ? 209.081 213.196 206.014 1.00 30.00 ? 35  GLU A CD  1 
ATOM   271  O OE1 . GLU A 1 35  ? 208.266 214.130 205.929 1.00 30.00 ? 35  GLU A OE1 1 
ATOM   272  O OE2 . GLU A 1 35  ? 209.860 213.054 206.971 1.00 30.00 ? 35  GLU A OE2 1 
ATOM   273  N N   . VAL A 1 36  ? 209.712 209.728 203.010 1.00 30.00 ? 36  VAL A N   1 
ATOM   274  C CA  . VAL A 1 36  ? 210.955 209.134 202.468 1.00 30.00 ? 36  VAL A CA  1 
ATOM   275  C C   . VAL A 1 36  ? 210.650 208.580 201.079 1.00 30.00 ? 36  VAL A C   1 
ATOM   276  O O   . VAL A 1 36  ? 211.552 208.606 200.232 1.00 30.00 ? 36  VAL A O   1 
ATOM   277  C CB  . VAL A 1 36  ? 211.456 208.031 203.397 1.00 30.00 ? 36  VAL A CB  1 
ATOM   278  C CG1 . VAL A 1 36  ? 210.595 206.789 203.302 1.00 30.00 ? 36  VAL A CG1 1 
ATOM   279  C CG2 . VAL A 1 36  ? 212.890 207.667 203.098 1.00 30.00 ? 36  VAL A CG2 1 
ATOM   280  N N   . VAL A 1 37  ? 209.438 208.071 200.867 1.00 30.00 ? 37  VAL A N   1 
ATOM   281  C CA  . VAL A 1 37  ? 209.037 207.435 199.582 1.00 30.00 ? 37  VAL A CA  1 
ATOM   282  C C   . VAL A 1 37  ? 209.101 208.437 198.427 1.00 30.00 ? 37  VAL A C   1 
ATOM   283  O O   . VAL A 1 37  ? 209.736 208.109 197.413 1.00 30.00 ? 37  VAL A O   1 
ATOM   284  C CB  . VAL A 1 37  ? 207.615 206.876 199.739 1.00 30.00 ? 37  VAL A CB  1 
ATOM   285  C CG1 . VAL A 1 37  ? 207.041 206.403 198.420 1.00 30.00 ? 37  VAL A CG1 1 
ATOM   286  C CG2 . VAL A 1 37  ? 207.563 205.763 200.765 1.00 30.00 ? 37  VAL A CG2 1 
ATOM   287  N N   . PRO A 1 38  ? 208.436 209.611 198.493 1.00 30.00 ? 38  PRO A N   1 
ATOM   288  C CA  . PRO A 1 38  ? 208.572 210.628 197.449 1.00 30.00 ? 38  PRO A CA  1 
ATOM   289  C C   . PRO A 1 38  ? 209.943 211.310 197.388 1.00 30.00 ? 38  PRO A C   1 
ATOM   290  O O   . PRO A 1 38  ? 210.404 211.505 196.304 1.00 30.00 ? 38  PRO A O   1 
ATOM   291  C CB  . PRO A 1 38  ? 207.531 211.693 197.799 1.00 30.00 ? 38  PRO A CB  1 
ATOM   292  C CG  . PRO A 1 38  ? 207.137 211.427 199.216 1.00 30.00 ? 38  PRO A CG  1 
ATOM   293  C CD  . PRO A 1 38  ? 207.366 209.950 199.422 1.00 30.00 ? 38  PRO A CD  1 
ATOM   294  N N   . GLY A 1 39  ? 210.524 211.710 198.522 1.00 30.00 ? 39  GLY A N   1 
ATOM   295  C CA  . GLY A 1 39  ? 211.887 212.275 198.522 1.00 30.00 ? 39  GLY A CA  1 
ATOM   296  C C   . GLY A 1 39  ? 212.762 211.454 197.596 1.00 30.00 ? 39  GLY A C   1 
ATOM   297  O O   . GLY A 1 39  ? 213.427 212.061 196.761 1.00 30.00 ? 39  GLY A O   1 
ATOM   298  N N   . PHE A 1 40  ? 212.721 210.126 197.701 1.00 30.00 ? 40  PHE A N   1 
ATOM   299  C CA  . PHE A 1 40  ? 213.509 209.165 196.898 1.00 30.00 ? 40  PHE A CA  1 
ATOM   300  C C   . PHE A 1 40  ? 213.249 209.348 195.413 1.00 30.00 ? 40  PHE A C   1 
ATOM   301  O O   . PHE A 1 40  ? 214.211 209.536 194.659 1.00 30.00 ? 40  PHE A O   1 
ATOM   302  C CB  . PHE A 1 40  ? 212.999 207.759 197.180 1.00 30.00 ? 40  PHE A CB  1 
ATOM   303  C CG  . PHE A 1 40  ? 213.559 206.667 196.315 1.00 30.00 ? 40  PHE A CG  1 
ATOM   304  C CD1 . PHE A 1 40  ? 214.907 206.369 196.324 1.00 30.00 ? 40  PHE A CD1 1 
ATOM   305  C CD2 . PHE A 1 40  ? 212.725 205.935 195.495 1.00 30.00 ? 40  PHE A CD2 1 
ATOM   306  C CE1 . PHE A 1 40  ? 215.409 205.353 195.532 1.00 30.00 ? 40  PHE A CE1 1 
ATOM   307  C CE2 . PHE A 1 40  ? 213.230 204.922 194.700 1.00 30.00 ? 40  PHE A CE2 1 
ATOM   308  C CZ  . PHE A 1 40  ? 214.570 204.633 194.722 1.00 30.00 ? 40  PHE A CZ  1 
ATOM   309  N N   . GLN A 1 41  ? 211.985 209.260 195.004 1.00 30.00 ? 41  GLN A N   1 
ATOM   310  C CA  . GLN A 1 41  ? 211.570 209.438 193.594 1.00 30.00 ? 41  GLN A CA  1 
ATOM   311  C C   . GLN A 1 41  ? 212.121 210.743 193.031 1.00 30.00 ? 41  GLN A C   1 
ATOM   312  O O   . GLN A 1 41  ? 212.839 210.695 192.034 1.00 30.00 ? 41  GLN A O   1 
ATOM   313  C CB  . GLN A 1 41  ? 210.052 209.493 193.580 1.00 30.00 ? 41  GLN A CB  1 
ATOM   314  C CG  . GLN A 1 41  ? 209.449 209.628 192.199 1.00 30.00 ? 41  GLN A CG  1 
ATOM   315  C CD  . GLN A 1 41  ? 207.946 209.561 192.276 1.00 30.00 ? 41  GLN A CD  1 
ATOM   316  O OE1 . GLN A 1 41  ? 207.370 209.370 193.343 1.00 30.00 ? 41  GLN A OE1 1 
ATOM   317  N NE2 . GLN A 1 41  ? 207.299 209.702 191.132 1.00 30.00 ? 41  GLN A NE2 1 
ATOM   318  N N   . ALA A 1 42  ? 211.812 211.869 193.661 1.00 30.00 ? 42  ALA A N   1 
ATOM   319  C CA  . ALA A 1 42  ? 212.225 213.201 193.180 1.00 30.00 ? 42  ALA A CA  1 
ATOM   320  C C   . ALA A 1 42  ? 213.740 213.274 193.051 1.00 30.00 ? 42  ALA A C   1 
ATOM   321  O O   . ALA A 1 42  ? 214.225 213.761 192.012 1.00 30.00 ? 42  ALA A O   1 
ATOM   322  C CB  . ALA A 1 42  ? 211.770 214.179 194.198 1.00 30.00 ? 42  ALA A CB  1 
ATOM   323  N N   . LEU A 1 43  ? 214.449 212.787 194.063 1.00 30.00 ? 43  LEU A N   1 
ATOM   324  C CA  . LEU A 1 43  ? 215.930 212.774 194.080 1.00 30.00 ? 43  LEU A CA  1 
ATOM   325  C C   . LEU A 1 43  ? 216.417 211.833 192.983 1.00 30.00 ? 43  LEU A C   1 
ATOM   326  O O   . LEU A 1 43  ? 217.594 211.961 192.590 1.00 30.00 ? 43  LEU A O   1 
ATOM   327  C CB  . LEU A 1 43  ? 216.339 212.267 195.463 1.00 30.00 ? 43  LEU A CB  1 
ATOM   328  C CG  . LEU A 1 43  ? 216.163 213.243 196.621 1.00 30.00 ? 43  LEU A CG  1 
ATOM   329  C CD1 . LEU A 1 43  ? 216.431 212.550 197.940 1.00 30.00 ? 43  LEU A CD1 1 
ATOM   330  C CD2 . LEU A 1 43  ? 217.087 214.432 196.473 1.00 30.00 ? 43  LEU A CD2 1 
ATOM   331  N N   . SER A 1 44  ? 215.558 210.928 192.512 1.00 30.00 ? 44  SER A N   1 
ATOM   332  C CA  . SER A 1 44  ? 215.920 209.876 191.531 1.00 30.00 ? 44  SER A CA  1 
ATOM   333  C C   . SER A 1 44  ? 215.155 209.955 190.210 1.00 30.00 ? 44  SER A C   1 
ATOM   334  O O   . SER A 1 44  ? 215.083 208.914 189.530 1.00 30.00 ? 44  SER A O   1 
ATOM   335  C CB  . SER A 1 44  ? 215.620 208.586 192.157 1.00 30.00 ? 44  SER A CB  1 
ATOM   336  O OG  . SER A 1 44  ? 216.303 208.474 193.390 1.00 30.00 ? 44  SER A OG  1 
ATOM   337  N N   . GLU A 1 45  ? 214.584 211.101 189.856 1.00 30.00 ? 45  GLU A N   1 
ATOM   338  C CA  . GLU A 1 45  ? 213.764 211.181 188.622 1.00 30.00 ? 45  GLU A CA  1 
ATOM   339  C C   . GLU A 1 45  ? 214.734 211.359 187.458 1.00 30.00 ? 45  GLU A C   1 
ATOM   340  O O   . GLU A 1 45  ? 215.032 212.519 187.109 1.00 30.00 ? 45  GLU A O   1 
ATOM   341  C CB  . GLU A 1 45  ? 212.732 212.296 188.723 1.00 30.00 ? 45  GLU A CB  1 
ATOM   342  C CG  . GLU A 1 45  ? 211.365 211.810 189.150 1.00 30.00 ? 45  GLU A CG  1 
ATOM   343  C CD  . GLU A 1 45  ? 210.283 212.874 189.177 1.00 30.00 ? 45  GLU A CD  1 
ATOM   344  O OE1 . GLU A 1 45  ? 210.601 214.041 188.887 1.00 30.00 ? 45  GLU A OE1 1 
ATOM   345  O OE2 . GLU A 1 45  ? 209.118 212.527 189.467 1.00 30.00 ? 45  GLU A OE2 1 
ATOM   346  N N   . GLY A 1 46  ? 215.219 210.246 186.906 1.00 30.00 ? 46  GLY A N   1 
ATOM   347  C CA  . GLY A 1 46  ? 216.207 210.268 185.814 1.00 30.00 ? 46  GLY A CA  1 
ATOM   348  C C   . GLY A 1 46  ? 217.508 209.614 186.240 1.00 30.00 ? 46  GLY A C   1 
ATOM   349  O O   . GLY A 1 46  ? 218.515 209.876 185.560 1.00 30.00 ? 46  GLY A O   1 
ATOM   350  N N   . CYS A 1 47  ? 217.516 208.807 187.314 1.00 30.00 ? 47  CYS A N   1 
ATOM   351  C CA  . CYS A 1 47  ? 218.721 208.062 187.722 1.00 30.00 ? 47  CYS A CA  1 
ATOM   352  C C   . CYS A 1 47  ? 218.598 206.643 187.201 1.00 30.00 ? 47  CYS A C   1 
ATOM   353  O O   . CYS A 1 47  ? 217.571 205.995 187.486 1.00 30.00 ? 47  CYS A O   1 
ATOM   354  C CB  . CYS A 1 47  ? 218.834 207.996 189.228 1.00 30.00 ? 47  CYS A CB  1 
ATOM   355  S SG  . CYS A 1 47  ? 219.146 209.615 189.971 1.00 30.00 ? 47  CYS A SG  1 
ATOM   356  N N   . THR A 1 48  ? 219.606 206.181 186.478 1.00 30.00 ? 48  THR A N   1 
ATOM   357  C CA  . THR A 1 48  ? 219.610 204.781 186.018 1.00 30.00 ? 48  THR A CA  1 
ATOM   358  C C   . THR A 1 48  ? 219.787 203.935 187.271 1.00 30.00 ? 48  THR A C   1 
ATOM   359  O O   . THR A 1 48  ? 220.255 204.465 188.288 1.00 30.00 ? 48  THR A O   1 
ATOM   360  C CB  . THR A 1 48  ? 220.719 204.503 185.012 1.00 30.00 ? 48  THR A CB  1 
ATOM   361  O OG1 . THR A 1 48  ? 221.946 204.725 185.698 1.00 30.00 ? 48  THR A OG1 1 
ATOM   362  C CG2 . THR A 1 48  ? 220.653 205.383 183.787 1.00 30.00 ? 48  THR A CG2 1 
ATOM   363  N N   . PRO A 1 49  ? 219.397 202.657 187.242 1.00 30.00 ? 49  PRO A N   1 
ATOM   364  C CA  . PRO A 1 49  ? 219.455 201.821 188.431 1.00 30.00 ? 49  PRO A CA  1 
ATOM   365  C C   . PRO A 1 49  ? 220.791 201.743 189.172 1.00 30.00 ? 49  PRO A C   1 
ATOM   366  O O   . PRO A 1 49  ? 220.737 201.803 190.346 1.00 30.00 ? 49  PRO A O   1 
ATOM   367  C CB  . PRO A 1 49  ? 219.250 200.451 187.818 1.00 30.00 ? 49  PRO A CB  1 
ATOM   368  C CG  . PRO A 1 49  ? 218.365 200.697 186.652 1.00 30.00 ? 49  PRO A CG  1 
ATOM   369  C CD  . PRO A 1 49  ? 218.909 201.967 186.060 1.00 30.00 ? 49  PRO A CD  1 
ATOM   370  N N   . TYR A 1 50  ? 221.912 201.517 188.487 1.00 30.00 ? 50  TYR A N   1 
ATOM   371  C CA  . TYR A 1 50  ? 223.265 201.440 189.092 1.00 30.00 ? 50  TYR A CA  1 
ATOM   372  C C   . TYR A 1 50  ? 223.405 202.513 190.161 1.00 30.00 ? 50  TYR A C   1 
ATOM   373  O O   . TYR A 1 50  ? 223.973 202.228 191.228 1.00 30.00 ? 50  TYR A O   1 
ATOM   374  C CB  . TYR A 1 50  ? 224.261 201.659 187.962 1.00 30.00 ? 50  TYR A CB  1 
ATOM   375  C CG  . TYR A 1 50  ? 225.655 202.095 188.295 1.00 30.00 ? 50  TYR A CG  1 
ATOM   376  C CD1 . TYR A 1 50  ? 226.470 201.362 189.130 1.00 30.00 ? 50  TYR A CD1 1 
ATOM   377  C CD2 . TYR A 1 50  ? 226.190 203.196 187.662 1.00 30.00 ? 50  TYR A CD2 1 
ATOM   378  C CE1 . TYR A 1 50  ? 227.771 201.758 189.386 1.00 30.00 ? 50  TYR A CE1 1 
ATOM   379  C CE2 . TYR A 1 50  ? 227.487 203.603 187.899 1.00 30.00 ? 50  TYR A CE2 1 
ATOM   380  C CZ  . TYR A 1 50  ? 228.278 202.885 188.769 1.00 30.00 ? 50  TYR A CZ  1 
ATOM   381  O OH  . TYR A 1 50  ? 229.556 203.310 188.994 1.00 30.00 ? 50  TYR A OH  1 
ATOM   382  N N   . ASP A 1 51  ? 222.918 203.710 189.863 1.00 30.00 ? 51  ASP A N   1 
ATOM   383  C CA  . ASP A 1 51  ? 222.984 204.867 190.780 1.00 30.00 ? 51  ASP A CA  1 
ATOM   384  C C   . ASP A 1 51  ? 222.004 204.735 191.935 1.00 30.00 ? 51  ASP A C   1 
ATOM   385  O O   . ASP A 1 51  ? 222.395 205.054 193.060 1.00 30.00 ? 51  ASP A O   1 
ATOM   386  C CB  . ASP A 1 51  ? 222.576 206.079 189.975 1.00 30.00 ? 51  ASP A CB  1 
ATOM   387  C CG  . ASP A 1 51  ? 223.600 206.437 188.924 1.00 30.00 ? 51  ASP A CG  1 
ATOM   388  O OD1 . ASP A 1 51  ? 224.700 206.866 189.297 1.00 30.00 ? 51  ASP A OD1 1 
ATOM   389  O OD2 . ASP A 1 51  ? 223.320 206.185 187.759 1.00 30.00 ? 51  ASP A OD2 1 
ATOM   390  N N   . ILE A 1 52  ? 220.758 204.372 191.646 1.00 30.00 ? 52  ILE A N   1 
ATOM   391  C CA  . ILE A 1 52  ? 219.726 204.159 192.697 1.00 30.00 ? 52  ILE A CA  1 
ATOM   392  C C   . ILE A 1 52  ? 220.310 203.182 193.710 1.00 30.00 ? 52  ILE A C   1 
ATOM   393  O O   . ILE A 1 52  ? 220.068 203.373 194.906 1.00 30.00 ? 52  ILE A O   1 
ATOM   394  C CB  . ILE A 1 52  ? 218.433 203.603 192.084 1.00 30.00 ? 52  ILE A CB  1 
ATOM   395  C CG1 . ILE A 1 52  ? 217.799 204.583 191.100 1.00 30.00 ? 52  ILE A CG1 1 
ATOM   396  C CG2 . ILE A 1 52  ? 217.455 203.194 193.167 1.00 30.00 ? 52  ILE A CG2 1 
ATOM   397  C CD1 . ILE A 1 52  ? 216.659 204.003 190.319 1.00 30.00 ? 52  ILE A CD1 1 
ATOM   398  N N   . ASN A 1 53  ? 221.042 202.171 193.243 1.00 30.00 ? 53  ASN A N   1 
ATOM   399  C CA  . ASN A 1 53  ? 221.600 201.118 194.118 1.00 30.00 ? 53  ASN A CA  1 
ATOM   400  C C   . ASN A 1 53  ? 222.724 201.702 194.963 1.00 30.00 ? 53  ASN A C   1 
ATOM   401  O O   . ASN A 1 53  ? 222.813 201.313 196.123 1.00 30.00 ? 53  ASN A O   1 
ATOM   402  C CB  . ASN A 1 53  ? 222.211 199.980 193.319 1.00 30.00 ? 53  ASN A CB  1 
ATOM   403  C CG  . ASN A 1 53  ? 221.237 199.229 192.451 1.00 30.00 ? 53  ASN A CG  1 
ATOM   404  O OD1 . ASN A 1 53  ? 220.068 199.578 192.378 1.00 30.00 ? 53  ASN A OD1 1 
ATOM   405  N ND2 . ASN A 1 53  ? 221.724 198.209 191.772 1.00 30.00 ? 53  ASN A ND2 1 
ATOM   406  N N   . GLN A 1 54  ? 223.568 202.559 194.387 1.00 30.00 ? 54  GLN A N   1 
ATOM   407  C CA  . GLN A 1 54  ? 224.703 203.197 195.101 1.00 30.00 ? 54  GLN A CA  1 
ATOM   408  C C   . GLN A 1 54  ? 224.180 204.048 196.251 1.00 30.00 ? 54  GLN A C   1 
ATOM   409  O O   . GLN A 1 54  ? 224.844 204.075 197.290 1.00 30.00 ? 54  GLN A O   1 
ATOM   410  C CB  . GLN A 1 54  ? 225.480 204.115 194.169 1.00 30.00 ? 54  GLN A CB  1 
ATOM   411  C CG  . GLN A 1 54  ? 226.497 203.394 193.315 1.00 30.00 ? 54  GLN A CG  1 
ATOM   412  C CD  . GLN A 1 54  ? 227.254 204.367 192.451 1.00 30.00 ? 54  GLN A CD  1 
ATOM   413  O OE1 . GLN A 1 54  ? 226.986 205.565 192.448 1.00 30.00 ? 54  GLN A OE1 1 
ATOM   414  N NE2 . GLN A 1 54  ? 228.209 203.847 191.703 1.00 30.00 ? 54  GLN A NE2 1 
ATOM   415  N N   . MET A 1 55  ? 223.071 204.751 196.041 1.00 30.00 ? 55  MET A N   1 
ATOM   416  C CA  . MET A 1 55  ? 222.447 205.622 197.064 1.00 30.00 ? 55  MET A CA  1 
ATOM   417  C C   . MET A 1 55  ? 221.969 204.788 198.243 1.00 30.00 ? 55  MET A C   1 
ATOM   418  O O   . MET A 1 55  ? 222.358 205.090 199.387 1.00 30.00 ? 55  MET A O   1 
ATOM   419  C CB  . MET A 1 55  ? 221.175 206.214 196.482 1.00 30.00 ? 55  MET A CB  1 
ATOM   420  C CG  . MET A 1 55  ? 221.343 207.416 195.616 1.00 30.00 ? 55  MET A CG  1 
ATOM   421  S SD  . MET A 1 55  ? 219.765 207.801 194.813 1.00 30.00 ? 55  MET A SD  1 
ATOM   422  C CE  . MET A 1 55  ? 218.939 208.711 196.113 1.00 30.00 ? 55  MET A CE  1 
ATOM   423  N N   . LEU A 1 56  ? 221.124 203.798 197.961 1.00 30.00 ? 56  LEU A N   1 
ATOM   424  C CA  . LEU A 1 56  ? 220.512 202.945 199.005 1.00 30.00 ? 56  LEU A CA  1 
ATOM   425  C C   . LEU A 1 56  ? 221.628 202.259 199.777 1.00 30.00 ? 56  LEU A C   1 
ATOM   426  O O   . LEU A 1 56  ? 221.476 202.065 200.998 1.00 30.00 ? 56  LEU A O   1 
ATOM   427  C CB  . LEU A 1 56  ? 219.671 201.911 198.262 1.00 30.00 ? 56  LEU A CB  1 
ATOM   428  C CG  . LEU A 1 56  ? 218.427 202.418 197.548 1.00 30.00 ? 56  LEU A CG  1 
ATOM   429  C CD1 . LEU A 1 56  ? 217.751 201.278 196.816 1.00 30.00 ? 56  LEU A CD1 1 
ATOM   430  C CD2 . LEU A 1 56  ? 217.463 203.060 198.524 1.00 30.00 ? 56  LEU A CD2 1 
ATOM   431  N N   . ASN A 1 57  ? 222.747 201.989 199.113 1.00 30.00 ? 57  ASN A N   1 
ATOM   432  C CA  . ASN A 1 57  ? 223.863 201.232 199.723 1.00 30.00 ? 57  ASN A CA  1 
ATOM   433  C C   . ASN A 1 57  ? 224.714 202.104 200.644 1.00 30.00 ? 57  ASN A C   1 
ATOM   434  O O   . ASN A 1 57  ? 225.265 201.557 201.615 1.00 30.00 ? 57  ASN A O   1 
ATOM   435  C CB  . ASN A 1 57  ? 224.739 200.659 198.626 1.00 30.00 ? 57  ASN A CB  1 
ATOM   436  C CG  . ASN A 1 57  ? 224.095 199.513 197.887 1.00 30.00 ? 57  ASN A CG  1 
ATOM   437  O OD1 . ASN A 1 57  ? 222.982 199.116 198.205 1.00 30.00 ? 57  ASN A OD1 1 
ATOM   438  N ND2 . ASN A 1 57  ? 224.794 198.973 196.905 1.00 30.00 ? 57  ASN A ND2 1 
ATOM   439  N N   . CYS A 1 58  ? 224.816 203.402 200.368 1.00 30.00 ? 58  CYS A N   1 
ATOM   440  C CA  . CYS A 1 58  ? 225.594 204.347 201.208 1.00 30.00 ? 58  CYS A CA  1 
ATOM   441  C C   . CYS A 1 58  ? 225.016 204.361 202.617 1.00 30.00 ? 58  CYS A C   1 
ATOM   442  O O   . CYS A 1 58  ? 225.762 204.651 203.562 1.00 30.00 ? 58  CYS A O   1 
ATOM   443  C CB  . CYS A 1 58  ? 225.506 205.759 200.672 1.00 30.00 ? 58  CYS A CB  1 
ATOM   444  S SG  . CYS A 1 58  ? 226.334 205.957 199.081 1.00 30.00 ? 58  CYS A SG  1 
ATOM   445  N N   . VAL A 1 59  ? 223.721 204.094 202.738 1.00 30.00 ? 59  VAL A N   1 
ATOM   446  C CA  . VAL A 1 59  ? 223.053 204.062 204.062 1.00 30.00 ? 59  VAL A CA  1 
ATOM   447  C C   . VAL A 1 59  ? 223.406 202.720 204.694 1.00 30.00 ? 59  VAL A C   1 
ATOM   448  O O   . VAL A 1 59  ? 222.959 201.686 204.156 1.00 30.00 ? 59  VAL A O   1 
ATOM   449  C CB  . VAL A 1 59  ? 221.536 204.216 203.913 1.00 30.00 ? 59  VAL A CB  1 
ATOM   450  C CG1 . VAL A 1 59  ? 220.855 204.307 205.264 1.00 30.00 ? 59  VAL A CG1 1 
ATOM   451  C CG2 . VAL A 1 59  ? 221.146 205.401 203.054 1.00 30.00 ? 59  VAL A CG2 1 
ATOM   452  N N   . GLY A 1 60  ? 224.175 202.736 205.780 1.00 30.00 ? 60  GLY A N   1 
ATOM   453  C CA  . GLY A 1 60  ? 224.622 201.501 206.445 1.00 30.00 ? 60  GLY A CA  1 
ATOM   454  C C   . GLY A 1 60  ? 223.865 201.247 207.719 1.00 30.00 ? 60  GLY A C   1 
ATOM   455  O O   . GLY A 1 60  ? 224.225 200.295 208.440 1.00 30.00 ? 60  GLY A O   1 
ATOM   456  N N   . ASP A 1 61  ? 222.852 202.061 207.973 1.00 30.00 ? 61  ASP A N   1 
ATOM   457  C CA  . ASP A 1 61  ? 222.038 201.963 209.200 1.00 30.00 ? 61  ASP A CA  1 
ATOM   458  C C   . ASP A 1 61  ? 220.622 201.642 208.748 1.00 30.00 ? 61  ASP A C   1 
ATOM   459  O O   . ASP A 1 61  ? 220.382 201.723 207.528 1.00 30.00 ? 61  ASP A O   1 
ATOM   460  C CB  . ASP A 1 61  ? 222.124 203.271 209.966 1.00 30.00 ? 61  ASP A CB  1 
ATOM   461  C CG  . ASP A 1 61  ? 223.537 203.671 210.332 1.00 30.00 ? 61  ASP A CG  1 
ATOM   462  O OD1 . ASP A 1 61  ? 224.462 202.933 209.967 1.00 30.00 ? 61  ASP A OD1 1 
ATOM   463  O OD2 . ASP A 1 61  ? 223.693 204.712 210.991 1.00 30.00 ? 61  ASP A OD2 1 
ATOM   464  N N   . HIS A 1 62  ? 219.747 201.234 209.664 1.00 30.00 ? 62  HIS A N   1 
ATOM   465  C CA  . HIS A 1 62  ? 218.392 200.822 209.247 1.00 30.00 ? 62  HIS A CA  1 
ATOM   466  C C   . HIS A 1 62  ? 218.612 199.752 208.187 1.00 30.00 ? 62  HIS A C   1 
ATOM   467  O O   . HIS A 1 62  ? 217.821 199.690 207.227 1.00 30.00 ? 62  HIS A O   1 
ATOM   468  C CB  . HIS A 1 62  ? 217.665 202.012 208.629 1.00 30.00 ? 62  HIS A CB  1 
ATOM   469  C CG  . HIS A 1 62  ? 217.606 203.239 209.467 1.00 30.00 ? 62  HIS A CG  1 
ATOM   470  N ND1 . HIS A 1 62  ? 216.401 203.756 209.884 1.00 30.00 ? 62  HIS A ND1 1 
ATOM   471  C CD2 . HIS A 1 62  ? 218.544 204.046 209.963 1.00 30.00 ? 62  HIS A CD2 1 
ATOM   472  C CE1 . HIS A 1 62  ? 216.617 204.841 210.610 1.00 30.00 ? 62  HIS A CE1 1 
ATOM   473  N NE2 . HIS A 1 62  ? 217.912 205.037 210.670 1.00 30.00 ? 62  HIS A NE2 1 
ATOM   474  N N   . GLN A 1 63  ? 219.627 198.911 208.371 1.00 30.00 ? 63  GLN A N   1 
ATOM   475  C CA  . GLN A 1 63  ? 220.041 197.937 207.331 1.00 30.00 ? 63  GLN A CA  1 
ATOM   476  C C   . GLN A 1 63  ? 219.078 196.751 207.291 1.00 30.00 ? 63  GLN A C   1 
ATOM   477  O O   . GLN A 1 63  ? 219.104 196.049 206.278 1.00 30.00 ? 63  GLN A O   1 
ATOM   478  C CB  . GLN A 1 63  ? 221.473 197.541 207.651 1.00 30.00 ? 63  GLN A CB  1 
ATOM   479  C CG  . GLN A 1 63  ? 222.215 196.894 206.502 1.00 30.00 ? 63  GLN A CG  1 
ATOM   480  C CD  . GLN A 1 63  ? 222.281 197.836 205.331 1.00 30.00 ? 63  GLN A CD  1 
ATOM   481  O OE1 . GLN A 1 63  ? 222.692 198.985 205.466 1.00 30.00 ? 63  GLN A OE1 1 
ATOM   482  N NE2 . GLN A 1 63  ? 221.803 197.376 204.189 1.00 30.00 ? 63  GLN A NE2 1 
ATOM   483  N N   . ALA A 1 64  ? 218.326 196.482 208.351 1.00 30.00 ? 64  ALA A N   1 
ATOM   484  C CA  . ALA A 1 64  ? 217.257 195.462 208.378 1.00 30.00 ? 64  ALA A CA  1 
ATOM   485  C C   . ALA A 1 64  ? 216.191 195.809 207.351 1.00 30.00 ? 64  ALA A C   1 
ATOM   486  O O   . ALA A 1 64  ? 215.775 194.916 206.598 1.00 30.00 ? 64  ALA A O   1 
ATOM   487  C CB  . ALA A 1 64  ? 216.621 195.469 209.719 1.00 30.00 ? 64  ALA A CB  1 
ATOM   488  N N   . ALA A 1 65  ? 215.763 197.063 207.337 1.00 30.00 ? 65  ALA A N   1 
ATOM   489  C CA  . ALA A 1 65  ? 214.717 197.545 206.419 1.00 30.00 ? 65  ALA A CA  1 
ATOM   490  C C   . ALA A 1 65  ? 215.209 197.458 204.983 1.00 30.00 ? 65  ALA A C   1 
ATOM   491  O O   . ALA A 1 65  ? 214.411 197.119 204.096 1.00 30.00 ? 65  ALA A O   1 
ATOM   492  C CB  . ALA A 1 65  ? 214.439 198.957 206.772 1.00 30.00 ? 65  ALA A CB  1 
ATOM   493  N N   . MET A 1 66  ? 216.476 197.799 204.768 1.00 30.00 ? 66  MET A N   1 
ATOM   494  C CA  . MET A 1 66  ? 217.051 197.781 203.406 1.00 30.00 ? 66  MET A CA  1 
ATOM   495  C C   . MET A 1 66  ? 217.047 196.323 202.943 1.00 30.00 ? 66  MET A C   1 
ATOM   496  O O   . MET A 1 66  ? 216.752 196.088 201.765 1.00 30.00 ? 66  MET A O   1 
ATOM   497  C CB  . MET A 1 66  ? 218.469 198.340 203.380 1.00 30.00 ? 66  MET A CB  1 
ATOM   498  C CG  . MET A 1 66  ? 218.616 199.718 203.963 1.00 30.00 ? 66  MET A CG  1 
ATOM   499  S SD  . MET A 1 66  ? 217.835 200.984 202.975 1.00 30.00 ? 66  MET A SD  1 
ATOM   500  C CE  . MET A 1 66  ? 218.919 202.366 203.319 1.00 30.00 ? 66  MET A CE  1 
ATOM   501  N N   . GLN A 1 67  ? 217.328 195.374 203.831 1.00 30.00 ? 67  GLN A N   1 
ATOM   502  C CA  . GLN A 1 67  ? 217.277 193.929 203.495 1.00 30.00 ? 67  GLN A CA  1 
ATOM   503  C C   . GLN A 1 67  ? 215.845 193.556 203.119 1.00 30.00 ? 67  GLN A C   1 
ATOM   504  O O   . GLN A 1 67  ? 215.674 192.793 202.158 1.00 30.00 ? 67  GLN A O   1 
ATOM   505  C CB  . GLN A 1 67  ? 217.732 193.118 204.697 1.00 30.00 ? 67  GLN A CB  1 
ATOM   506  C CG  . GLN A 1 67  ? 217.558 191.615 204.572 1.00 30.00 ? 67  GLN A CG  1 
ATOM   507  C CD  . GLN A 1 67  ? 218.246 191.056 203.354 1.00 30.00 ? 67  GLN A CD  1 
ATOM   508  O OE1 . GLN A 1 67  ? 219.430 191.285 203.129 1.00 30.00 ? 67  GLN A OE1 1 
ATOM   509  N NE2 . GLN A 1 67  ? 217.492 190.344 202.537 1.00 30.00 ? 67  GLN A NE2 1 
ATOM   510  N N   . ILE A 1 68  ? 214.860 194.079 203.848 1.00 30.00 ? 68  ILE A N   1 
ATOM   511  C CA  . ILE A 1 68  ? 213.425 193.811 203.551 1.00 30.00 ? 68  ILE A CA  1 
ATOM   512  C C   . ILE A 1 68  ? 213.142 194.313 202.141 1.00 30.00 ? 68  ILE A C   1 
ATOM   513  O O   . ILE A 1 68  ? 212.475 193.595 201.405 1.00 30.00 ? 68  ILE A O   1 
ATOM   514  C CB  . ILE A 1 68  ? 212.500 194.510 204.557 1.00 30.00 ? 68  ILE A CB  1 
ATOM   515  C CG1 . ILE A 1 68  ? 212.661 193.947 205.966 1.00 30.00 ? 68  ILE A CG1 1 
ATOM   516  C CG2 . ILE A 1 68  ? 211.056 194.435 204.095 1.00 30.00 ? 68  ILE A CG2 1 
ATOM   517  C CD1 . ILE A 1 68  ? 211.939 194.737 207.022 1.00 30.00 ? 68  ILE A CD1 1 
ATOM   518  N N   . ILE A 1 69  ? 213.639 195.499 201.795 1.00 30.00 ? 69  ILE A N   1 
ATOM   519  C CA  . ILE A 1 69  ? 213.431 196.090 200.444 1.00 30.00 ? 69  ILE A CA  1 
ATOM   520  C C   . ILE A 1 69  ? 214.074 195.156 199.425 1.00 30.00 ? 69  ILE A C   1 
ATOM   521  O O   . ILE A 1 69  ? 213.485 194.992 198.361 1.00 30.00 ? 69  ILE A O   1 
ATOM   522  C CB  . ILE A 1 69  ? 214.031 197.502 200.354 1.00 30.00 ? 69  ILE A CB  1 
ATOM   523  C CG1 . ILE A 1 69  ? 213.285 198.496 201.239 1.00 30.00 ? 69  ILE A CG1 1 
ATOM   524  C CG2 . ILE A 1 69  ? 214.078 197.977 198.915 1.00 30.00 ? 69  ILE A CG2 1 
ATOM   525  C CD1 . ILE A 1 69  ? 214.040 199.774 201.472 1.00 30.00 ? 69  ILE A CD1 1 
ATOM   526  N N   . ARG A 1 70  ? 215.235 194.583 199.745 1.00 30.00 ? 70  ARG A N   1 
ATOM   527  C CA  . ARG A 1 70  ? 215.966 193.703 198.800 1.00 30.00 ? 70  ARG A CA  1 
ATOM   528  C C   . ARG A 1 70  ? 215.146 192.436 198.586 1.00 30.00 ? 70  ARG A C   1 
ATOM   529  O O   . ARG A 1 70  ? 215.077 191.978 197.436 1.00 30.00 ? 70  ARG A O   1 
ATOM   530  C CB  . ARG A 1 70  ? 217.359 193.365 199.319 1.00 30.00 ? 70  ARG A CB  1 
ATOM   531  C CG  . ARG A 1 70  ? 218.310 194.548 199.319 1.00 30.00 ? 70  ARG A CG  1 
ATOM   532  C CD  . ARG A 1 70  ? 219.461 194.315 200.267 1.00 30.00 ? 70  ARG A CD  1 
ATOM   533  N NE  . ARG A 1 70  ? 220.295 195.498 200.396 1.00 30.00 ? 70  ARG A NE  1 
ATOM   534  C CZ  . ARG A 1 70  ? 221.340 195.600 201.207 1.00 30.00 ? 70  ARG A CZ  1 
ATOM   535  N NH1 . ARG A 1 70  ? 222.259 196.520 200.979 1.00 30.00 ? 70  ARG A NH1 1 
ATOM   536  N NH2 . ARG A 1 70  ? 221.469 194.788 202.244 1.00 30.00 ? 70  ARG A NH2 1 
ATOM   537  N N   . GLU A 1 71  ? 214.546 191.897 199.641 1.00 30.00 ? 71  GLU A N   1 
ATOM   538  C CA  . GLU A 1 71  ? 213.677 190.704 199.530 1.00 30.00 ? 71  GLU A CA  1 
ATOM   539  C C   . GLU A 1 71  ? 212.501 191.023 198.616 1.00 30.00 ? 71  GLU A C   1 
ATOM   540  O O   . GLU A 1 71  ? 212.147 190.154 197.814 1.00 30.00 ? 71  GLU A O   1 
ATOM   541  C CB  . GLU A 1 71  ? 213.099 190.350 200.889 1.00 30.00 ? 71  GLU A CB  1 
ATOM   542  C CG  . GLU A 1 71  ? 214.123 189.842 201.876 1.00 30.00 ? 71  GLU A CG  1 
ATOM   543  C CD  . GLU A 1 71  ? 213.567 189.562 203.260 1.00 30.00 ? 71  GLU A CD  1 
ATOM   544  O OE1 . GLU A 1 71  ? 212.356 189.779 203.467 1.00 30.00 ? 71  GLU A OE1 1 
ATOM   545  O OE2 . GLU A 1 71  ? 214.345 189.121 204.126 1.00 30.00 ? 71  GLU A OE2 1 
ATOM   546  N N   . ILE A 1 72  ? 211.918 192.214 198.745 1.00 30.00 ? 72  ILE A N   1 
ATOM   547  C CA  . ILE A 1 72  ? 210.718 192.634 197.967 1.00 30.00 ? 72  ILE A CA  1 
ATOM   548  C C   . ILE A 1 72  ? 211.085 192.789 196.494 1.00 30.00 ? 72  ILE A C   1 
ATOM   549  O O   . ILE A 1 72  ? 210.249 192.455 195.674 1.00 30.00 ? 72  ILE A O   1 
ATOM   550  C CB  . ILE A 1 72  ? 210.160 193.948 198.535 1.00 30.00 ? 72  ILE A CB  1 
ATOM   551  C CG1 . ILE A 1 72  ? 209.602 193.777 199.949 1.00 30.00 ? 72  ILE A CG1 1 
ATOM   552  C CG2 . ILE A 1 72  ? 209.121 194.549 197.606 1.00 30.00 ? 72  ILE A CG2 1 
ATOM   553  C CD1 . ILE A 1 72  ? 208.410 192.864 200.032 1.00 30.00 ? 72  ILE A CD1 1 
ATOM   554  N N   . ILE A 1 73  ? 212.266 193.313 196.182 1.00 30.00 ? 73  ILE A N   1 
ATOM   555  C CA  . ILE A 1 73  ? 212.711 193.546 194.778 1.00 30.00 ? 73  ILE A CA  1 
ATOM   556  C C   . ILE A 1 73  ? 212.897 192.194 194.098 1.00 30.00 ? 73  ILE A C   1 
ATOM   557  O O   . ILE A 1 73  ? 212.664 192.143 192.888 1.00 30.00 ? 73  ILE A O   1 
ATOM   558  C CB  . ILE A 1 73  ? 214.026 194.336 194.786 1.00 30.00 ? 73  ILE A CB  1 
ATOM   559  C CG1 . ILE A 1 73  ? 213.839 195.759 195.306 1.00 30.00 ? 73  ILE A CG1 1 
ATOM   560  C CG2 . ILE A 1 73  ? 214.670 194.343 193.412 1.00 30.00 ? 73  ILE A CG2 1 
ATOM   561  C CD1 . ILE A 1 73  ? 215.135 196.428 195.677 1.00 30.00 ? 73  ILE A CD1 1 
ATOM   562  N N   . ASN A 1 74  ? 213.329 191.167 194.828 1.00 30.00 ? 74  ASN A N   1 
ATOM   563  C CA  . ASN A 1 74  ? 213.588 189.792 194.336 1.00 30.00 ? 74  ASN A CA  1 
ATOM   564  C C   . ASN A 1 74  ? 212.257 189.076 194.107 1.00 30.00 ? 74  ASN A C   1 
ATOM   565  O O   . ASN A 1 74  ? 212.169 188.277 193.155 1.00 30.00 ? 74  ASN A O   1 
ATOM   566  C CB  . ASN A 1 74  ? 214.431 189.025 195.349 1.00 30.00 ? 74  ASN A CB  1 
ATOM   567  C CG  . ASN A 1 74  ? 215.788 189.644 195.586 1.00 30.00 ? 74  ASN A CG  1 
ATOM   568  O OD1 . ASN A 1 74  ? 216.146 190.629 194.948 1.00 30.00 ? 74  ASN A OD1 1 
ATOM   569  N ND2 . ASN A 1 74  ? 216.555 189.061 196.490 1.00 30.00 ? 74  ASN A ND2 1 
ATOM   570  N N   . ASP A 1 75  ? 211.268 189.324 194.963 1.00 30.00 ? 75  ASP A N   1 
ATOM   571  C CA  . ASP A 1 75  ? 209.928 188.695 194.852 1.00 30.00 ? 75  ASP A CA  1 
ATOM   572  C C   . ASP A 1 75  ? 209.196 189.267 193.641 1.00 30.00 ? 75  ASP A C   1 
ATOM   573  O O   . ASP A 1 75  ? 208.668 188.470 192.835 1.00 30.00 ? 75  ASP A O   1 
ATOM   574  C CB  . ASP A 1 75  ? 209.138 188.961 196.125 1.00 30.00 ? 75  ASP A CB  1 
ATOM   575  C CG  . ASP A 1 75  ? 209.780 188.381 197.368 1.00 30.00 ? 75  ASP A CG  1 
ATOM   576  O OD1 . ASP A 1 75  ? 210.849 187.757 197.235 1.00 30.00 ? 75  ASP A OD1 1 
ATOM   577  O OD2 . ASP A 1 75  ? 209.206 188.562 198.455 1.00 30.00 ? 75  ASP A OD2 1 
ATOM   578  N N   . GLU A 1 76  ? 209.195 190.592 193.498 1.00 30.00 ? 76  GLU A N   1 
ATOM   579  C CA  . GLU A 1 76  ? 208.585 191.263 192.326 1.00 30.00 ? 76  GLU A CA  1 
ATOM   580  C C   . GLU A 1 76  ? 209.358 190.792 191.108 1.00 30.00 ? 76  GLU A C   1 
ATOM   581  O O   . GLU A 1 76  ? 208.746 190.611 190.036 1.00 30.00 ? 76  GLU A O   1 
ATOM   582  C CB  . GLU A 1 76  ? 208.770 192.772 192.378 1.00 30.00 ? 76  GLU A CB  1 
ATOM   583  C CG  . GLU A 1 76  ? 208.180 193.458 193.591 1.00 30.00 ? 76  GLU A CG  1 
ATOM   584  C CD  . GLU A 1 76  ? 206.694 193.739 193.510 1.00 30.00 ? 76  GLU A CD  1 
ATOM   585  O OE1 . GLU A 1 76  ? 206.283 194.446 192.574 1.00 30.00 ? 76  GLU A OE1 1 
ATOM   586  O OE2 . GLU A 1 76  ? 205.960 193.276 194.400 1.00 30.00 ? 76  GLU A OE2 1 
ATOM   587  N N   . ALA A 1 77  ? 210.667 190.613 191.277 1.00 30.00 ? 77  ALA A N   1 
ATOM   588  C CA  . ALA A 1 77  ? 211.543 190.225 190.160 1.00 30.00 ? 77  ALA A CA  1 
ATOM   589  C C   . ALA A 1 77  ? 211.083 188.892 189.573 1.00 30.00 ? 77  ALA A C   1 
ATOM   590  O O   . ALA A 1 77  ? 211.047 188.778 188.330 1.00 30.00 ? 77  ALA A O   1 
ATOM   591  C CB  . ALA A 1 77  ? 212.972 190.126 190.590 1.00 30.00 ? 77  ALA A CB  1 
ATOM   592  N N   . ALA A 1 78  ? 210.724 187.933 190.421 1.00 30.00 ? 78  ALA A N   1 
ATOM   593  C CA  . ALA A 1 78  ? 210.286 186.593 189.981 1.00 30.00 ? 78  ALA A CA  1 
ATOM   594  C C   . ALA A 1 78  ? 209.060 186.735 189.082 1.00 30.00 ? 78  ALA A C   1 
ATOM   595  O O   . ALA A 1 78  ? 208.982 186.011 188.070 1.00 30.00 ? 78  ALA A O   1 
ATOM   596  C CB  . ALA A 1 78  ? 209.966 185.773 191.192 1.00 30.00 ? 78  ALA A CB  1 
ATOM   597  N N   . ASP A 1 79  ? 208.151 187.646 189.428 1.00 30.00 ? 79  ASP A N   1 
ATOM   598  C CA  . ASP A 1 79  ? 206.893 187.849 188.666 1.00 30.00 ? 79  ASP A CA  1 
ATOM   599  C C   . ASP A 1 79  ? 207.211 188.277 187.237 1.00 30.00 ? 79  ASP A C   1 
ATOM   600  O O   . ASP A 1 79  ? 206.617 187.704 186.309 1.00 30.00 ? 79  ASP A O   1 
ATOM   601  C CB  . ASP A 1 79  ? 206.039 188.936 189.308 1.00 30.00 ? 79  ASP A CB  1 
ATOM   602  C CG  . ASP A 1 79  ? 205.713 188.683 190.768 1.00 30.00 ? 79  ASP A CG  1 
ATOM   603  O OD1 . ASP A 1 79  ? 206.169 187.655 191.303 1.00 30.00 ? 79  ASP A OD1 1 
ATOM   604  O OD2 . ASP A 1 79  ? 205.001 189.515 191.356 1.00 30.00 ? 79  ASP A OD2 1 
ATOM   605  N N   . TRP A 1 80  ? 208.131 189.224 187.067 1.00 30.00 ? 80  TRP A N   1 
ATOM   606  C CA  . TRP A 1 80  ? 208.499 189.753 185.729 1.00 30.00 ? 80  TRP A CA  1 
ATOM   607  C C   . TRP A 1 80  ? 209.099 188.633 184.883 1.00 30.00 ? 80  TRP A C   1 
ATOM   608  O O   . TRP A 1 80  ? 208.755 188.552 183.692 1.00 30.00 ? 80  TRP A O   1 
ATOM   609  C CB  . TRP A 1 80  ? 209.462 190.927 185.902 1.00 30.00 ? 80  TRP A CB  1 
ATOM   610  C CG  . TRP A 1 80  ? 210.150 191.379 184.656 1.00 30.00 ? 80  TRP A CG  1 
ATOM   611  C CD1 . TRP A 1 80  ? 211.061 190.690 183.912 1.00 30.00 ? 80  TRP A CD1 1 
ATOM   612  C CD2 . TRP A 1 80  ? 209.954 192.633 183.986 1.00 30.00 ? 80  TRP A CD2 1 
ATOM   613  N NE1 . TRP A 1 80  ? 211.460 191.438 182.840 1.00 30.00 ? 80  TRP A NE1 1 
ATOM   614  C CE2 . TRP A 1 80  ? 210.793 192.632 182.856 1.00 30.00 ? 80  TRP A CE2 1 
ATOM   615  C CE3 . TRP A 1 80  ? 209.158 193.753 184.235 1.00 30.00 ? 80  TRP A CE3 1 
ATOM   616  C CZ2 . TRP A 1 80  ? 210.854 193.709 181.977 1.00 30.00 ? 80  TRP A CZ2 1 
ATOM   617  C CZ3 . TRP A 1 80  ? 209.220 194.817 183.367 1.00 30.00 ? 80  TRP A CZ3 1 
ATOM   618  C CH2 . TRP A 1 80  ? 210.057 194.794 182.254 1.00 30.00 ? 80  TRP A CH2 1 
ATOM   619  N N   . ASP A 1 81  ? 209.948 187.797 185.477 1.00 30.00 ? 81  ASP A N   1 
ATOM   620  C CA  . ASP A 1 81  ? 210.612 186.689 184.747 1.00 30.00 ? 81  ASP A CA  1 
ATOM   621  C C   . ASP A 1 81  ? 209.543 185.709 184.274 1.00 30.00 ? 81  ASP A C   1 
ATOM   622  O O   . ASP A 1 81  ? 209.619 185.277 183.113 1.00 30.00 ? 81  ASP A O   1 
ATOM   623  C CB  . ASP A 1 81  ? 211.617 185.962 185.637 1.00 30.00 ? 81  ASP A CB  1 
ATOM   624  C CG  . ASP A 1 81  ? 212.665 186.867 186.252 1.00 30.00 ? 81  ASP A CG  1 
ATOM   625  O OD1 . ASP A 1 81  ? 212.600 188.081 186.003 1.00 30.00 ? 81  ASP A OD1 1 
ATOM   626  O OD2 . ASP A 1 81  ? 213.538 186.346 186.970 1.00 30.00 ? 81  ASP A OD2 1 
ATOM   627  N N   . ALA A 1 82  ? 208.550 185.419 185.112 1.00 30.00 ? 82  ALA A N   1 
ATOM   628  C CA  . ALA A 1 82  ? 207.472 184.457 184.795 1.00 30.00 ? 82  ALA A CA  1 
ATOM   629  C C   . ALA A 1 82  ? 206.568 185.027 183.705 1.00 30.00 ? 82  ALA A C   1 
ATOM   630  O O   . ALA A 1 82  ? 206.364 184.333 182.690 1.00 30.00 ? 82  ALA A O   1 
ATOM   631  C CB  . ALA A 1 82  ? 206.692 184.207 186.051 1.00 30.00 ? 82  ALA A CB  1 
ATOM   632  N N   . GLN A 1 83  ? 206.117 186.269 183.864 1.00 30.00 ? 83  GLN A N   1 
ATOM   633  C CA  . GLN A 1 83  ? 205.151 186.901 182.932 1.00 30.00 ? 83  GLN A CA  1 
ATOM   634  C C   . GLN A 1 83  ? 205.800 187.215 181.586 1.00 30.00 ? 83  GLN A C   1 
ATOM   635  O O   . GLN A 1 83  ? 205.084 187.133 180.568 1.00 30.00 ? 83  GLN A O   1 
ATOM   636  C CB  . GLN A 1 83  ? 204.660 188.192 183.571 1.00 30.00 ? 83  GLN A CB  1 
ATOM   637  C CG  . GLN A 1 83  ? 203.801 187.955 184.800 1.00 30.00 ? 83  GLN A CG  1 
ATOM   638  C CD  . GLN A 1 83  ? 203.407 189.245 185.471 1.00 30.00 ? 83  GLN A CD  1 
ATOM   639  O OE1 . GLN A 1 83  ? 203.762 190.333 185.024 1.00 30.00 ? 83  GLN A OE1 1 
ATOM   640  N NE2 . GLN A 1 83  ? 202.663 189.129 186.557 1.00 30.00 ? 83  GLN A NE2 1 
ATOM   641  N N   . HIS A 1 84  ? 207.089 187.550 181.577 1.00 30.00 ? 84  HIS A N   1 
ATOM   642  C CA  . HIS A 1 84  ? 207.794 187.945 180.329 1.00 30.00 ? 84  HIS A CA  1 
ATOM   643  C C   . HIS A 1 84  ? 208.667 186.773 179.880 1.00 30.00 ? 84  HIS A C   1 
ATOM   644  O O   . HIS A 1 84  ? 209.598 186.385 180.613 1.00 30.00 ? 84  HIS A O   1 
ATOM   645  C CB  . HIS A 1 84  ? 208.556 189.253 180.542 1.00 30.00 ? 84  HIS A CB  1 
ATOM   646  C CG  . HIS A 1 84  ? 207.657 190.400 180.835 1.00 30.00 ? 84  HIS A CG  1 
ATOM   647  N ND1 . HIS A 1 84  ? 206.818 190.449 181.927 1.00 30.00 ? 84  HIS A ND1 1 
ATOM   648  C CD2 . HIS A 1 84  ? 207.465 191.541 180.169 1.00 30.00 ? 84  HIS A CD2 1 
ATOM   649  C CE1 . HIS A 1 84  ? 206.149 191.590 181.911 1.00 30.00 ? 84  HIS A CE1 1 
ATOM   650  N NE2 . HIS A 1 84  ? 206.525 192.269 180.850 1.00 30.00 ? 84  HIS A NE2 1 
ATOM   651  N N   . PRO A 1 85  ? 208.424 186.203 178.682 1.00 30.00 ? 85  PRO A N   1 
ATOM   652  C CA  . PRO A 1 85  ? 209.144 185.008 178.233 1.00 30.00 ? 85  PRO A CA  1 
ATOM   653  C C   . PRO A 1 85  ? 210.518 185.247 177.599 1.00 30.00 ? 85  PRO A C   1 
ATOM   654  O O   . PRO A 1 85  ? 210.871 186.398 177.412 1.00 30.00 ? 85  PRO A O   1 
ATOM   655  C CB  . PRO A 1 85  ? 208.194 184.493 177.149 1.00 30.00 ? 85  PRO A CB  1 
ATOM   656  C CG  . PRO A 1 85  ? 207.679 185.750 176.506 1.00 30.00 ? 85  PRO A CG  1 
ATOM   657  C CD  . PRO A 1 85  ? 207.471 186.684 177.676 1.00 30.00 ? 85  PRO A CD  1 
ATOM   658  N N   . ILE A 1 86  ? 211.244 184.172 177.282 1.00 30.00 ? 86  ILE A N   1 
ATOM   659  C CA  . ILE A 1 86  ? 212.567 184.262 176.599 1.00 30.00 ? 86  ILE A CA  1 
ATOM   660  C C   . ILE A 1 86  ? 212.285 184.012 175.121 1.00 30.00 ? 86  ILE A C   1 
ATOM   661  O O   . ILE A 1 86  ? 211.727 182.943 174.803 1.00 30.00 ? 86  ILE A O   1 
ATOM   662  C CB  . ILE A 1 86  ? 213.565 183.263 177.210 1.00 30.00 ? 86  ILE A CB  1 
ATOM   663  C CG1 . ILE A 1 86  ? 213.555 183.332 178.739 1.00 30.00 ? 86  ILE A CG1 1 
ATOM   664  C CG2 . ILE A 1 86  ? 214.956 183.478 176.636 1.00 30.00 ? 86  ILE A CG2 1 
ATOM   665  C CD1 . ILE A 1 86  ? 214.483 182.354 179.412 1.00 30.00 ? 86  ILE A CD1 1 
ATOM   666  N N   . PRO A 1 87  ? 212.629 184.941 174.205 1.00 30.00 ? 87  PRO A N   1 
ATOM   667  C CA  . PRO A 1 87  ? 212.304 184.782 172.791 1.00 30.00 ? 87  PRO A CA  1 
ATOM   668  C C   . PRO A 1 87  ? 213.148 183.628 172.242 1.00 30.00 ? 87  PRO A C   1 
ATOM   669  O O   . PRO A 1 87  ? 212.930 183.255 171.107 1.00 30.00 ? 87  PRO A O   1 
ATOM   670  C CB  . PRO A 1 87  ? 212.660 186.125 172.141 1.00 30.00 ? 87  PRO A CB  1 
ATOM   671  C CG  . PRO A 1 87  ? 212.878 187.070 173.304 1.00 30.00 ? 87  PRO A CG  1 
ATOM   672  C CD  . PRO A 1 87  ? 213.347 186.192 174.444 1.00 30.00 ? 87  PRO A CD  1 
ATOM   673  N N   . GLY A 1 88  ? 214.102 183.129 173.030 1.00 30.00 ? 88  GLY A N   1 
ATOM   674  C CA  . GLY A 1 88  ? 214.973 182.007 172.640 1.00 30.00 ? 88  GLY A CA  1 
ATOM   675  C C   . GLY A 1 88  ? 216.386 182.521 172.498 1.00 30.00 ? 88  GLY A C   1 
ATOM   676  O O   . GLY A 1 88  ? 216.611 183.697 172.848 1.00 30.00 ? 88  GLY A O   1 
ATOM   677  N N   . PRO A 1 89  ? 217.359 181.725 172.017 1.00 30.00 ? 89  PRO A N   1 
ATOM   678  C CA  . PRO A 1 89  ? 218.689 182.256 171.780 1.00 30.00 ? 89  PRO A CA  1 
ATOM   679  C C   . PRO A 1 89  ? 218.502 183.525 170.940 1.00 30.00 ? 89  PRO A C   1 
ATOM   680  O O   . PRO A 1 89  ? 217.983 183.413 169.844 1.00 30.00 ? 89  PRO A O   1 
ATOM   681  C CB  . PRO A 1 89  ? 219.426 181.145 171.023 1.00 30.00 ? 89  PRO A CB  1 
ATOM   682  C CG  . PRO A 1 89  ? 218.329 180.194 170.579 1.00 30.00 ? 89  PRO A CG  1 
ATOM   683  C CD  . PRO A 1 89  ? 217.238 180.326 171.621 1.00 30.00 ? 89  PRO A CD  1 
ATOM   684  N N   . LEU A 1 90  ? 218.922 184.681 171.455 1.00 30.00 ? 90  LEU A N   1 
ATOM   685  C CA  . LEU A 1 90  ? 218.800 185.967 170.720 1.00 30.00 ? 90  LEU A CA  1 
ATOM   686  C C   . LEU A 1 90  ? 220.077 186.153 169.901 1.00 30.00 ? 90  LEU A C   1 
ATOM   687  O O   . LEU A 1 90  ? 221.173 186.052 170.486 1.00 30.00 ? 90  LEU A O   1 
ATOM   688  C CB  . LEU A 1 90  ? 218.579 187.108 171.716 1.00 30.00 ? 90  LEU A CB  1 
ATOM   689  C CG  . LEU A 1 90  ? 217.274 187.044 172.509 1.00 30.00 ? 90  LEU A CG  1 
ATOM   690  C CD1 . LEU A 1 90  ? 217.056 188.320 173.301 1.00 30.00 ? 90  LEU A CD1 1 
ATOM   691  C CD2 . LEU A 1 90  ? 216.087 186.788 171.594 1.00 30.00 ? 90  LEU A CD2 1 
ATOM   692  N N   . PRO A 1 91  ? 219.991 186.414 168.580 1.00 30.00 ? 91  PRO A N   1 
ATOM   693  C CA  . PRO A 1 91  ? 221.181 186.497 167.736 1.00 30.00 ? 91  PRO A CA  1 
ATOM   694  C C   . PRO A 1 91  ? 222.228 187.500 168.217 1.00 30.00 ? 91  PRO A C   1 
ATOM   695  O O   . PRO A 1 91  ? 221.838 188.550 168.688 1.00 30.00 ? 91  PRO A O   1 
ATOM   696  C CB  . PRO A 1 91  ? 220.643 187.048 166.410 1.00 30.00 ? 91  PRO A CB  1 
ATOM   697  C CG  . PRO A 1 91  ? 219.210 186.583 166.375 1.00 30.00 ? 91  PRO A CG  1 
ATOM   698  C CD  . PRO A 1 91  ? 218.758 186.614 167.818 1.00 30.00 ? 91  PRO A CD  1 
ATOM   699  N N   . ALA A 1 92  ? 223.487 187.046 168.267 1.00 30.00 ? 92  ALA A N   1 
ATOM   700  C CA  . ALA A 1 92  ? 224.627 187.901 168.644 1.00 30.00 ? 92  ALA A CA  1 
ATOM   701  C C   . ALA A 1 92  ? 224.464 189.215 167.896 1.00 30.00 ? 92  ALA A C   1 
ATOM   702  O O   . ALA A 1 92  ? 224.004 189.176 166.736 1.00 30.00 ? 92  ALA A O   1 
ATOM   703  C CB  . ALA A 1 92  ? 225.922 187.217 168.308 1.00 30.00 ? 92  ALA A CB  1 
ATOM   704  N N   . GLY A 1 93  ? 224.812 190.344 168.521 1.00 30.00 ? 93  GLY A N   1 
ATOM   705  C CA  . GLY A 1 93  ? 224.624 191.680 167.920 1.00 30.00 ? 93  GLY A CA  1 
ATOM   706  C C   . GLY A 1 93  ? 223.412 192.346 168.539 1.00 30.00 ? 93  GLY A C   1 
ATOM   707  O O   . GLY A 1 93  ? 223.234 193.559 168.309 1.00 30.00 ? 93  GLY A O   1 
ATOM   708  N N   . GLN A 1 94  ? 222.610 191.590 169.297 1.00 30.00 ? 94  GLN A N   1 
ATOM   709  C CA  . GLN A 1 94  ? 221.400 192.108 169.985 1.00 30.00 ? 94  GLN A CA  1 
ATOM   710  C C   . GLN A 1 94  ? 221.632 192.049 171.494 1.00 30.00 ? 94  GLN A C   1 
ATOM   711  O O   . GLN A 1 94  ? 222.064 190.983 171.974 1.00 30.00 ? 94  GLN A O   1 
ATOM   712  C CB  . GLN A 1 94  ? 220.172 191.273 169.623 1.00 30.00 ? 94  GLN A CB  1 
ATOM   713  C CG  . GLN A 1 94  ? 218.954 191.579 170.482 1.00 30.00 ? 94  GLN A CG  1 
ATOM   714  C CD  . GLN A 1 94  ? 217.697 190.938 169.948 1.00 30.00 ? 94  GLN A CD  1 
ATOM   715  O OE1 . GLN A 1 94  ? 217.613 189.722 169.793 1.00 30.00 ? 94  GLN A OE1 1 
ATOM   716  N NE2 . GLN A 1 94  ? 216.705 191.761 169.652 1.00 30.00 ? 94  GLN A NE2 1 
ATOM   717  N N   . LEU A 1 95  ? 221.349 193.136 172.212 1.00 30.00 ? 95  LEU A N   1 
ATOM   718  C CA  . LEU A 1 95  ? 221.475 193.154 173.691 1.00 30.00 ? 95  LEU A CA  1 
ATOM   719  C C   . LEU A 1 95  ? 220.369 192.261 174.254 1.00 30.00 ? 95  LEU A C   1 
ATOM   720  O O   . LEU A 1 95  ? 219.226 192.374 173.767 1.00 30.00 ? 95  LEU A O   1 
ATOM   721  C CB  . LEU A 1 95  ? 221.366 194.596 174.194 1.00 30.00 ? 95  LEU A CB  1 
ATOM   722  C CG  . LEU A 1 95  ? 221.460 194.778 175.707 1.00 30.00 ? 95  LEU A CG  1 
ATOM   723  C CD1 . LEU A 1 95  ? 222.787 194.275 176.248 1.00 30.00 ? 95  LEU A CD1 1 
ATOM   724  C CD2 . LEU A 1 95  ? 221.270 196.240 176.076 1.00 30.00 ? 95  LEU A CD2 1 
ATOM   725  N N   . ARG A 1 96  ? 220.680 191.424 175.243 1.00 30.00 ? 96  ARG A N   1 
ATOM   726  C CA  . ARG A 1 96  ? 219.700 190.457 175.802 1.00 30.00 ? 96  ARG A CA  1 
ATOM   727  C C   . ARG A 1 96  ? 218.446 191.213 176.228 1.00 30.00 ? 96  ARG A C   1 
ATOM   728  O O   . ARG A 1 96  ? 218.588 192.295 176.809 1.00 30.00 ? 96  ARG A O   1 
ATOM   729  C CB  . ARG A 1 96  ? 220.281 189.720 177.008 1.00 30.00 ? 96  ARG A CB  1 
ATOM   730  C CG  . ARG A 1 96  ? 220.638 190.605 178.193 1.00 30.00 ? 96  ARG A CG  1 
ATOM   731  C CD  . ARG A 1 96  ? 221.246 189.777 179.306 1.00 30.00 ? 96  ARG A CD  1 
ATOM   732  N NE  . ARG A 1 96  ? 221.653 190.582 180.446 1.00 30.00 ? 96  ARG A NE  1 
ATOM   733  C CZ  . ARG A 1 96  ? 222.566 191.547 180.412 1.00 30.00 ? 96  ARG A CZ  1 
ATOM   734  N NH1 . ARG A 1 96  ? 223.382 191.672 179.381 1.00 30.00 ? 96  ARG A NH1 1 
ATOM   735  N NH2 . ARG A 1 96  ? 222.682 192.370 181.438 1.00 30.00 ? 96  ARG A NH2 1 
ATOM   736  N N   . ASP A 1 97  ? 217.266 190.657 175.975 1.00 30.00 ? 97  ASP A N   1 
ATOM   737  C CA  . ASP A 1 97  ? 216.008 191.300 176.422 1.00 30.00 ? 97  ASP A CA  1 
ATOM   738  C C   . ASP A 1 97  ? 216.068 191.422 177.945 1.00 30.00 ? 97  ASP A C   1 
ATOM   739  O O   . ASP A 1 97  ? 216.542 190.470 178.598 1.00 30.00 ? 97  ASP A O   1 
ATOM   740  C CB  . ASP A 1 97  ? 214.777 190.548 175.927 1.00 30.00 ? 97  ASP A CB  1 
ATOM   741  C CG  . ASP A 1 97  ? 214.396 190.921 174.507 1.00 30.00 ? 97  ASP A CG  1 
ATOM   742  O OD1 . ASP A 1 97  ? 214.128 192.115 174.270 1.00 30.00 ? 97  ASP A OD1 1 
ATOM   743  O OD2 . ASP A 1 97  ? 214.366 190.020 173.652 1.00 30.00 ? 97  ASP A OD2 1 
ATOM   744  N N   . PRO A 1 98  ? 215.609 192.542 178.538 1.00 30.00 ? 98  PRO A N   1 
ATOM   745  C CA  . PRO A 1 98  ? 215.749 192.761 179.980 1.00 30.00 ? 98  PRO A CA  1 
ATOM   746  C C   . PRO A 1 98  ? 215.069 191.771 180.927 1.00 30.00 ? 98  PRO A C   1 
ATOM   747  O O   . PRO A 1 98  ? 214.010 191.287 180.575 1.00 30.00 ? 98  PRO A O   1 
ATOM   748  C CB  . PRO A 1 98  ? 214.997 194.074 180.206 1.00 30.00 ? 98  PRO A CB  1 
ATOM   749  C CG  . PRO A 1 98  ? 215.063 194.781 178.880 1.00 30.00 ? 98  PRO A CG  1 
ATOM   750  C CD  . PRO A 1 98  ? 214.966 193.669 177.861 1.00 30.00 ? 98  PRO A CD  1 
ATOM   751  N N   . ARG A 1 99  ? 215.682 191.504 182.081 1.00 30.00 ? 99  ARG A N   1 
ATOM   752  C CA  . ARG A 1 99  ? 215.100 190.635 183.137 1.00 30.00 ? 99  ARG A CA  1 
ATOM   753  C C   . ARG A 1 99  ? 215.016 191.485 184.407 1.00 30.00 ? 99  ARG A C   1 
ATOM   754  O O   . ARG A 1 99  ? 215.531 192.607 184.358 1.00 30.00 ? 99  ARG A O   1 
ATOM   755  C CB  . ARG A 1 99  ? 215.970 189.399 183.355 1.00 30.00 ? 99  ARG A CB  1 
ATOM   756  C CG  . ARG A 1 99  ? 216.349 188.661 182.078 1.00 30.00 ? 99  ARG A CG  1 
ATOM   757  C CD  . ARG A 1 99  ? 215.161 188.151 181.286 1.00 30.00 ? 99  ARG A CD  1 
ATOM   758  N NE  . ARG A 1 99  ? 214.357 187.188 182.025 1.00 30.00 ? 99  ARG A NE  1 
ATOM   759  C CZ  . ARG A 1 99  ? 213.257 186.599 181.566 1.00 30.00 ? 99  ARG A CZ  1 
ATOM   760  N NH1 . ARG A 1 99  ? 212.626 185.718 182.320 1.00 30.00 ? 99  ARG A NH1 1 
ATOM   761  N NH2 . ARG A 1 99  ? 212.785 186.883 180.363 1.00 30.00 ? 99  ARG A NH2 1 
ATOM   762  N N   . GLY A 1 100 ? 214.413 191.001 185.495 1.00 30.00 ? 100 GLY A N   1 
ATOM   763  C CA  . GLY A 1 100 ? 214.236 191.748 186.757 1.00 30.00 ? 100 GLY A CA  1 
ATOM   764  C C   . GLY A 1 100 ? 215.568 192.138 187.376 1.00 30.00 ? 100 GLY A C   1 
ATOM   765  O O   . GLY A 1 100 ? 215.620 193.211 188.004 1.00 30.00 ? 100 GLY A O   1 
ATOM   766  N N   . SER A 1 101 ? 216.650 191.401 187.120 1.00 30.00 ? 101 SER A N   1 
ATOM   767  C CA  . SER A 1 101 ? 217.976 191.672 187.738 1.00 30.00 ? 101 SER A CA  1 
ATOM   768  C C   . SER A 1 101 ? 218.727 192.746 186.950 1.00 30.00 ? 101 SER A C   1 
ATOM   769  O O   . SER A 1 101 ? 219.430 193.550 187.586 1.00 30.00 ? 101 SER A O   1 
ATOM   770  C CB  . SER A 1 101 ? 218.786 190.430 187.799 1.00 30.00 ? 101 SER A CB  1 
ATOM   771  O OG  . SER A 1 101 ? 219.105 189.987 186.492 1.00 30.00 ? 101 SER A OG  1 
ATOM   772  N N   . ASP A 1 102 ? 218.616 192.746 185.621 1.00 30.00 ? 102 ASP A N   1 
ATOM   773  C CA  . ASP A 1 102 ? 219.249 193.786 184.772 1.00 30.00 ? 102 ASP A CA  1 
ATOM   774  C C   . ASP A 1 102 ? 218.560 195.105 185.098 1.00 30.00 ? 102 ASP A C   1 
ATOM   775  O O   . ASP A 1 102 ? 219.241 196.148 185.086 1.00 30.00 ? 102 ASP A O   1 
ATOM   776  C CB  . ASP A 1 102 ? 219.095 193.502 183.283 1.00 30.00 ? 102 ASP A CB  1 
ATOM   777  C CG  . ASP A 1 102 ? 219.451 192.093 182.851 1.00 30.00 ? 102 ASP A CG  1 
ATOM   778  O OD1 . ASP A 1 102 ? 219.867 191.298 183.713 1.00 30.00 ? 102 ASP A OD1 1 
ATOM   779  O OD2 . ASP A 1 102 ? 219.278 191.797 181.654 1.00 30.00 ? 102 ASP A OD2 1 
ATOM   780  N N   . ILE A 1 103 ? 217.243 195.061 185.294 1.00 30.00 ? 103 ILE A N   1 
ATOM   781  C CA  . ILE A 1 103 ? 216.447 196.254 185.689 1.00 30.00 ? 103 ILE A CA  1 
ATOM   782  C C   . ILE A 1 103 ? 217.105 196.882 186.915 1.00 30.00 ? 103 ILE A C   1 
ATOM   783  O O   . ILE A 1 103 ? 217.091 198.117 187.012 1.00 30.00 ? 103 ILE A O   1 
ATOM   784  C CB  . ILE A 1 103 ? 214.997 195.815 185.945 1.00 30.00 ? 103 ILE A CB  1 
ATOM   785  C CG1 . ILE A 1 103 ? 214.243 195.650 184.625 1.00 30.00 ? 103 ILE A CG1 1 
ATOM   786  C CG2 . ILE A 1 103 ? 214.283 196.779 186.875 1.00 30.00 ? 103 ILE A CG2 1 
ATOM   787  C CD1 . ILE A 1 103 ? 212.858 195.079 184.773 1.00 30.00 ? 103 ILE A CD1 1 
ATOM   788  N N   . ALA A 1 104 ? 217.607 196.063 187.837 1.00 30.00 ? 104 ALA A N   1 
ATOM   789  C CA  . ALA A 1 104 ? 218.302 196.535 189.055 1.00 30.00 ? 104 ALA A CA  1 
ATOM   790  C C   . ALA A 1 104 ? 219.686 197.071 188.691 1.00 30.00 ? 104 ALA A C   1 
ATOM   791  O O   . ALA A 1 104 ? 220.155 197.989 189.388 1.00 30.00 ? 104 ALA A O   1 
ATOM   792  C CB  . ALA A 1 104 ? 218.405 195.395 190.020 1.00 30.00 ? 104 ALA A CB  1 
ATOM   793  N N   . GLY A 1 105 ? 220.337 196.485 187.682 1.00 30.00 ? 105 GLY A N   1 
ATOM   794  C CA  . GLY A 1 105 ? 221.691 196.890 187.257 1.00 30.00 ? 105 GLY A CA  1 
ATOM   795  C C   . GLY A 1 105 ? 222.744 196.050 187.950 1.00 30.00 ? 105 GLY A C   1 
ATOM   796  O O   . GLY A 1 105 ? 223.936 196.375 187.804 1.00 30.00 ? 105 GLY A O   1 
ATOM   797  N N   . THR A 1 106 ? 222.331 195.019 188.689 1.00 30.00 ? 106 THR A N   1 
ATOM   798  C CA  . THR A 1 106 ? 223.245 194.099 189.410 1.00 30.00 ? 106 THR A CA  1 
ATOM   799  C C   . THR A 1 106 ? 224.142 193.353 188.429 1.00 30.00 ? 106 THR A C   1 
ATOM   800  O O   . THR A 1 106 ? 225.356 193.632 188.418 1.00 30.00 ? 106 THR A O   1 
ATOM   801  C CB  . THR A 1 106 ? 222.440 193.030 190.150 1.00 30.00 ? 106 THR A CB  1 
ATOM   802  O OG1 . THR A 1 106 ? 221.511 193.702 190.996 1.00 30.00 ? 106 THR A OG1 1 
ATOM   803  C CG2 . THR A 1 106 ? 223.296 192.089 190.968 1.00 30.00 ? 106 THR A CG2 1 
ATOM   804  N N   . THR A 1 107 ? 223.568 192.449 187.640 1.00 30.00 ? 107 THR A N   1 
ATOM   805  C CA  . THR A 1 107 ? 224.296 191.601 186.666 1.00 30.00 ? 107 THR A CA  1 
ATOM   806  C C   . THR A 1 107 ? 224.552 192.412 185.403 1.00 30.00 ? 107 THR A C   1 
ATOM   807  O O   . THR A 1 107 ? 225.508 192.080 184.675 1.00 30.00 ? 107 THR A O   1 
ATOM   808  C CB  . THR A 1 107 ? 223.457 190.372 186.316 1.00 30.00 ? 107 THR A CB  1 
ATOM   809  O OG1 . THR A 1 107 ? 224.240 189.516 185.486 1.00 30.00 ? 107 THR A OG1 1 
ATOM   810  C CG2 . THR A 1 107 ? 222.167 190.706 185.600 1.00 30.00 ? 107 THR A CG2 1 
ATOM   811  N N   . SER A 1 108 ? 223.738 193.436 185.164 1.00 30.00 ? 108 SER A N   1 
ATOM   812  C CA  . SER A 1 108 ? 223.834 194.278 183.951 1.00 30.00 ? 108 SER A CA  1 
ATOM   813  C C   . SER A 1 108 ? 224.770 195.456 184.197 1.00 30.00 ? 108 SER A C   1 
ATOM   814  O O   . SER A 1 108 ? 225.129 195.682 185.369 1.00 30.00 ? 108 SER A O   1 
ATOM   815  C CB  . SER A 1 108 ? 222.484 194.770 183.569 1.00 30.00 ? 108 SER A CB  1 
ATOM   816  O OG  . SER A 1 108 ? 222.550 195.551 182.389 1.00 30.00 ? 108 SER A OG  1 
ATOM   817  N N   . THR A 1 109 ? 225.056 196.225 183.150 1.00 30.00 ? 109 THR A N   1 
ATOM   818  C CA  . THR A 1 109 ? 225.879 197.448 183.262 1.00 30.00 ? 109 THR A CA  1 
ATOM   819  C C   . THR A 1 109 ? 225.003 198.644 182.905 1.00 30.00 ? 109 THR A C   1 
ATOM   820  O O   . THR A 1 109 ? 223.995 198.445 182.201 1.00 30.00 ? 109 THR A O   1 
ATOM   821  C CB  . THR A 1 109 ? 227.091 197.388 182.339 1.00 30.00 ? 109 THR A CB  1 
ATOM   822  O OG1 . THR A 1 109 ? 227.921 198.497 182.676 1.00 30.00 ? 109 THR A OG1 1 
ATOM   823  C CG2 . THR A 1 109 ? 226.733 197.449 180.873 1.00 30.00 ? 109 THR A CG2 1 
ATOM   824  N N   . VAL A 1 110 ? 225.388 199.833 183.345 1.00 30.00 ? 110 VAL A N   1 
ATOM   825  C CA  . VAL A 1 110 ? 224.612 201.077 183.096 1.00 30.00 ? 110 VAL A CA  1 
ATOM   826  C C   . VAL A 1 110 ? 224.405 201.267 181.598 1.00 30.00 ? 110 VAL A C   1 
ATOM   827  O O   . VAL A 1 110 ? 223.297 201.641 181.212 1.00 30.00 ? 110 VAL A O   1 
ATOM   828  C CB  . VAL A 1 110 ? 225.378 202.275 183.664 1.00 30.00 ? 110 VAL A CB  1 
ATOM   829  C CG1 . VAL A 1 110 ? 226.785 202.390 183.100 1.00 30.00 ? 110 VAL A CG1 1 
ATOM   830  C CG2 . VAL A 1 110 ? 224.622 203.571 183.443 1.00 30.00 ? 110 VAL A CG2 1 
ATOM   831  N N   . GLU A 1 111 ? 225.423 200.996 180.791 1.00 30.00 ? 111 GLU A N   1 
ATOM   832  C CA  . GLU A 1 111 ? 225.370 201.240 179.330 1.00 30.00 ? 111 GLU A CA  1 
ATOM   833  C C   . GLU A 1 111 ? 224.251 200.411 178.716 1.00 30.00 ? 111 GLU A C   1 
ATOM   834  O O   . GLU A 1 111 ? 223.604 200.919 177.794 1.00 30.00 ? 111 GLU A O   1 
ATOM   835  C CB  . GLU A 1 111 ? 226.689 200.804 178.718 1.00 30.00 ? 111 GLU A CB  1 
ATOM   836  C CG  . GLU A 1 111 ? 227.891 201.506 179.313 1.00 30.00 ? 111 GLU A CG  1 
ATOM   837  C CD  . GLU A 1 111 ? 229.226 200.932 178.878 1.00 30.00 ? 111 GLU A CD  1 
ATOM   838  O OE1 . GLU A 1 111 ? 229.225 199.969 178.088 1.00 30.00 ? 111 GLU A OE1 1 
ATOM   839  O OE2 . GLU A 1 111 ? 230.262 201.442 179.343 1.00 30.00 ? 111 GLU A OE2 1 
ATOM   840  N N   . GLU A 1 112 ? 224.093 199.170 179.165 1.00 30.00 ? 112 GLU A N   1 
ATOM   841  C CA  . GLU A 1 112 ? 223.027 198.258 178.686 1.00 30.00 ? 112 GLU A CA  1 
ATOM   842  C C   . GLU A 1 112 ? 221.681 198.709 179.241 1.00 30.00 ? 112 GLU A C   1 
ATOM   843  O O   . GLU A 1 112 ? 220.678 198.524 178.546 1.00 30.00 ? 112 GLU A O   1 
ATOM   844  C CB  . GLU A 1 112 ? 223.352 196.859 179.177 1.00 30.00 ? 112 GLU A CB  1 
ATOM   845  C CG  . GLU A 1 112 ? 224.527 196.244 178.457 1.00 30.00 ? 112 GLU A CG  1 
ATOM   846  C CD  . GLU A 1 112 ? 225.027 194.961 179.090 1.00 30.00 ? 112 GLU A CD  1 
ATOM   847  O OE1 . GLU A 1 112 ? 224.510 194.600 180.157 1.00 30.00 ? 112 GLU A OE1 1 
ATOM   848  O OE2 . GLU A 1 112 ? 225.914 194.320 178.503 1.00 30.00 ? 112 GLU A OE2 1 
ATOM   849  N N   . GLN A 1 113 ? 221.664 199.207 180.474 1.00 30.00 ? 113 GLN A N   1 
ATOM   850  C CA  . GLN A 1 113 ? 220.430 199.717 181.122 1.00 30.00 ? 113 GLN A CA  1 
ATOM   851  C C   . GLN A 1 113 ? 219.978 200.976 180.383 1.00 30.00 ? 113 GLN A C   1 
ATOM   852  O O   . GLN A 1 113 ? 218.762 201.190 180.311 1.00 30.00 ? 113 GLN A O   1 
ATOM   853  C CB  . GLN A 1 113 ? 220.722 199.978 182.593 1.00 30.00 ? 113 GLN A CB  1 
ATOM   854  C CG  . GLN A 1 113 ? 220.955 198.709 183.392 1.00 30.00 ? 113 GLN A CG  1 
ATOM   855  C CD  . GLN A 1 113 ? 221.725 198.992 184.654 1.00 30.00 ? 113 GLN A CD  1 
ATOM   856  O OE1 . GLN A 1 113 ? 221.311 199.785 185.492 1.00 30.00 ? 113 GLN A OE1 1 
ATOM   857  N NE2 . GLN A 1 113 ? 222.866 198.343 184.795 1.00 30.00 ? 113 GLN A NE2 1 
ATOM   858  N N   . ILE A 1 114 ? 220.917 201.778 179.875 1.00 30.00 ? 114 ILE A N   1 
ATOM   859  C CA  . ILE A 1 114 ? 220.601 203.003 179.085 1.00 30.00 ? 114 ILE A CA  1 
ATOM   860  C C   . ILE A 1 114 ? 220.131 202.542 177.710 1.00 30.00 ? 114 ILE A C   1 
ATOM   861  O O   . ILE A 1 114 ? 219.213 203.171 177.167 1.00 30.00 ? 114 ILE A O   1 
ATOM   862  C CB  . ILE A 1 114 ? 221.836 203.914 178.958 1.00 30.00 ? 114 ILE A CB  1 
ATOM   863  C CG1 . ILE A 1 114 ? 222.247 204.500 180.309 1.00 30.00 ? 114 ILE A CG1 1 
ATOM   864  C CG2 . ILE A 1 114 ? 221.596 205.014 177.938 1.00 30.00 ? 114 ILE A CG2 1 
ATOM   865  C CD1 . ILE A 1 114 ? 223.512 205.322 180.278 1.00 30.00 ? 114 ILE A CD1 1 
ATOM   866  N N   . GLN A 1 115 ? 220.736 201.484 177.173 1.00 30.00 ? 115 GLN A N   1 
ATOM   867  C CA  . GLN A 1 115 ? 220.426 200.983 175.810 1.00 30.00 ? 115 GLN A CA  1 
ATOM   868  C C   . GLN A 1 115 ? 218.962 200.552 175.744 1.00 30.00 ? 115 GLN A C   1 
ATOM   869  O O   . GLN A 1 115 ? 218.291 200.965 174.793 1.00 30.00 ? 115 GLN A O   1 
ATOM   870  C CB  . GLN A 1 115 ? 221.340 199.809 175.471 1.00 30.00 ? 115 GLN A CB  1 
ATOM   871  C CG  . GLN A 1 115 ? 221.018 199.131 174.151 1.00 30.00 ? 115 GLN A CG  1 
ATOM   872  C CD  . GLN A 1 115 ? 221.038 200.104 173.000 1.00 30.00 ? 115 GLN A CD  1 
ATOM   873  O OE1 . GLN A 1 115 ? 220.040 200.301 172.310 1.00 30.00 ? 115 GLN A OE1 1 
ATOM   874  N NE2 . GLN A 1 115 ? 222.185 200.727 172.786 1.00 30.00 ? 115 GLN A NE2 1 
ATOM   875  N N   . TRP A 1 116 ? 218.484 199.777 176.718 1.00 30.00 ? 116 TRP A N   1 
ATOM   876  C CA  . TRP A 1 116 ? 217.065 199.344 176.773 1.00 30.00 ? 116 TRP A CA  1 
ATOM   877  C C   . TRP A 1 116 ? 216.187 200.551 177.066 1.00 30.00 ? 116 TRP A C   1 
ATOM   878  O O   . TRP A 1 116 ? 215.164 200.712 176.388 1.00 30.00 ? 116 TRP A O   1 
ATOM   879  C CB  . TRP A 1 116 ? 216.850 198.299 177.862 1.00 30.00 ? 116 TRP A CB  1 
ATOM   880  C CG  . TRP A 1 116 ? 217.645 197.050 177.694 1.00 30.00 ? 116 TRP A CG  1 
ATOM   881  C CD1 . TRP A 1 116 ? 217.705 196.265 176.586 1.00 30.00 ? 116 TRP A CD1 1 
ATOM   882  C CD2 . TRP A 1 116 ? 218.405 196.380 178.709 1.00 30.00 ? 116 TRP A CD2 1 
ATOM   883  N NE1 . TRP A 1 116 ? 218.499 195.180 176.823 1.00 30.00 ? 116 TRP A NE1 1 
ATOM   884  C CE2 . TRP A 1 116 ? 218.940 195.219 178.119 1.00 30.00 ? 116 TRP A CE2 1 
ATOM   885  C CE3 . TRP A 1 116 ? 218.698 196.658 180.045 1.00 30.00 ? 116 TRP A CE3 1 
ATOM   886  C CZ2 . TRP A 1 116 ? 219.761 194.342 178.824 1.00 30.00 ? 116 TRP A CZ2 1 
ATOM   887  C CZ3 . TRP A 1 116 ? 219.508 195.791 180.740 1.00 30.00 ? 116 TRP A CZ3 1 
ATOM   888  C CH2 . TRP A 1 116 ? 220.031 194.649 180.136 1.00 30.00 ? 116 TRP A CH2 1 
ATOM   889  N N   . MET A 1 117 ? 216.616 201.402 177.990 1.00 30.00 ? 117 MET A N   1 
ATOM   890  C CA  . MET A 1 117 ? 215.824 202.572 178.439 1.00 30.00 ? 117 MET A CA  1 
ATOM   891  C C   . MET A 1 117 ? 215.568 203.488 177.239 1.00 30.00 ? 117 MET A C   1 
ATOM   892  O O   . MET A 1 117 ? 214.577 204.243 177.297 1.00 30.00 ? 117 MET A O   1 
ATOM   893  C CB  . MET A 1 117 ? 216.614 203.264 179.554 1.00 30.00 ? 117 MET A CB  1 
ATOM   894  C CG  . MET A 1 117 ? 216.113 204.620 179.982 1.00 30.00 ? 117 MET A CG  1 
ATOM   895  S SD  . MET A 1 117 ? 217.053 205.290 181.391 1.00 30.00 ? 117 MET A SD  1 
ATOM   896  C CE  . MET A 1 117 ? 217.442 203.819 182.339 1.00 30.00 ? 117 MET A CE  1 
ATOM   897  N N   . TYR A 1 118 ? 216.406 203.426 176.197 1.00 30.00 ? 118 TYR A N   1 
ATOM   898  C CA  . TYR A 1 118 ? 216.278 204.289 174.993 1.00 30.00 ? 118 TYR A CA  1 
ATOM   899  C C   . TYR A 1 118 ? 216.238 203.507 173.670 1.00 30.00 ? 118 TYR A C   1 
ATOM   900  O O   . TYR A 1 118 ? 216.154 204.190 172.631 1.00 30.00 ? 118 TYR A O   1 
ATOM   901  C CB  . TYR A 1 118 ? 217.446 205.273 174.987 1.00 30.00 ? 118 TYR A CB  1 
ATOM   902  C CG  . TYR A 1 118 ? 217.373 206.312 176.074 1.00 30.00 ? 118 TYR A CG  1 
ATOM   903  C CD1 . TYR A 1 118 ? 216.371 207.265 176.082 1.00 30.00 ? 118 TYR A CD1 1 
ATOM   904  C CD2 . TYR A 1 118 ? 218.264 206.302 177.130 1.00 30.00 ? 118 TYR A CD2 1 
ATOM   905  C CE1 . TYR A 1 118 ? 216.287 208.216 177.083 1.00 30.00 ? 118 TYR A CE1 1 
ATOM   906  C CE2 . TYR A 1 118 ? 218.187 207.238 178.146 1.00 30.00 ? 118 TYR A CE2 1 
ATOM   907  C CZ  . TYR A 1 118 ? 217.198 208.201 178.121 1.00 30.00 ? 118 TYR A CZ  1 
ATOM   908  O OH  . TYR A 1 118 ? 217.125 209.130 179.127 1.00 30.00 ? 118 TYR A OH  1 
ATOM   909  N N   . ARG A 1 119 ? 216.270 202.168 173.655 1.00 30.00 ? 119 ARG A N   1 
ATOM   910  C CA  . ARG A 1 119 ? 216.345 201.436 172.357 1.00 30.00 ? 119 ARG A CA  1 
ATOM   911  C C   . ARG A 1 119 ? 215.125 201.851 171.533 1.00 30.00 ? 119 ARG A C   1 
ATOM   912  O O   . ARG A 1 119 ? 214.010 201.831 172.083 1.00 30.00 ? 119 ARG A O   1 
ATOM   913  C CB  . ARG A 1 119 ? 216.436 199.911 172.493 1.00 30.00 ? 119 ARG A CB  1 
ATOM   914  C CG  . ARG A 1 119 ? 215.287 199.220 173.208 1.00 30.00 ? 119 ARG A CG  1 
ATOM   915  C CD  . ARG A 1 119 ? 215.650 197.754 173.313 1.00 30.00 ? 119 ARG A CD  1 
ATOM   916  N NE  . ARG A 1 119 ? 214.717 196.961 174.096 1.00 30.00 ? 119 ARG A NE  1 
ATOM   917  C CZ  . ARG A 1 119 ? 214.834 195.656 174.321 1.00 30.00 ? 119 ARG A CZ  1 
ATOM   918  N NH1 . ARG A 1 119 ? 213.835 194.991 174.870 1.00 30.00 ? 119 ARG A NH1 1 
ATOM   919  N NH2 . ARG A 1 119 ? 215.937 195.008 173.989 1.00 30.00 ? 119 ARG A NH2 1 
ATOM   920  N N   . PRO A 1 120 ? 215.281 202.235 170.249 1.00 30.00 ? 120 PRO A N   1 
ATOM   921  C CA  . PRO A 1 120 ? 214.157 202.741 169.465 1.00 30.00 ? 120 PRO A CA  1 
ATOM   922  C C   . PRO A 1 120 ? 213.077 201.689 169.210 1.00 30.00 ? 120 PRO A C   1 
ATOM   923  O O   . PRO A 1 120 ? 211.920 202.033 169.295 1.00 30.00 ? 120 PRO A O   1 
ATOM   924  C CB  . PRO A 1 120 ? 214.784 203.133 168.120 1.00 30.00 ? 120 PRO A CB  1 
ATOM   925  C CG  . PRO A 1 120 ? 216.267 203.227 168.396 1.00 30.00 ? 120 PRO A CG  1 
ATOM   926  C CD  . PRO A 1 120 ? 216.517 202.195 169.472 1.00 30.00 ? 120 PRO A CD  1 
ATOM   927  N N   . GLN A 1 121 ? 213.465 200.449 168.921 1.00 30.00 ? 121 GLN A N   1 
ATOM   928  C CA  . GLN A 1 121 ? 212.489 199.396 168.534 1.00 30.00 ? 121 GLN A CA  1 
ATOM   929  C C   . GLN A 1 121 ? 211.455 199.178 169.643 1.00 30.00 ? 121 GLN A C   1 
ATOM   930  O O   . GLN A 1 121 ? 210.260 199.164 169.312 1.00 30.00 ? 121 GLN A O   1 
ATOM   931  C CB  . GLN A 1 121 ? 213.209 198.087 168.195 1.00 30.00 ? 121 GLN A CB  1 
ATOM   932  C CG  . GLN A 1 121 ? 214.215 197.615 169.237 1.00 30.00 ? 121 GLN A CG  1 
ATOM   933  C CD  . GLN A 1 121 ? 214.704 196.213 168.967 1.00 30.00 ? 121 GLN A CD  1 
ATOM   934  O OE1 . GLN A 1 121 ? 215.298 195.931 167.930 1.00 30.00 ? 121 GLN A OE1 1 
ATOM   935  N NE2 . GLN A 1 121 ? 214.461 195.319 169.912 1.00 30.00 ? 121 GLN A NE2 1 
ATOM   936  N N   . ASN A 1 122 ? 211.879 199.020 170.894 1.00 30.00 ? 122 ASN A N   1 
ATOM   937  C CA  . ASN A 1 122 ? 210.962 198.802 172.042 1.00 30.00 ? 122 ASN A CA  1 
ATOM   938  C C   . ASN A 1 122 ? 211.641 199.344 173.298 1.00 30.00 ? 122 ASN A C   1 
ATOM   939  O O   . ASN A 1 122 ? 212.161 198.539 174.082 1.00 30.00 ? 122 ASN A O   1 
ATOM   940  C CB  . ASN A 1 122 ? 210.547 197.336 172.171 1.00 30.00 ? 122 ASN A CB  1 
ATOM   941  C CG  . ASN A 1 122 ? 211.711 196.369 172.224 1.00 30.00 ? 122 ASN A CG  1 
ATOM   942  O OD1 . ASN A 1 122 ? 212.868 196.767 172.139 1.00 30.00 ? 122 ASN A OD1 1 
ATOM   943  N ND2 . ASN A 1 122 ? 211.410 195.089 172.355 1.00 30.00 ? 122 ASN A ND2 1 
ATOM   944  N N   . PRO A 1 123 ? 211.658 200.667 173.537 1.00 30.00 ? 123 PRO A N   1 
ATOM   945  C CA  . PRO A 1 123 ? 212.392 201.184 174.679 1.00 30.00 ? 123 PRO A CA  1 
ATOM   946  C C   . PRO A 1 123 ? 211.813 200.587 175.966 1.00 30.00 ? 123 PRO A C   1 
ATOM   947  O O   . PRO A 1 123 ? 210.630 200.765 176.193 1.00 30.00 ? 123 PRO A O   1 
ATOM   948  C CB  . PRO A 1 123 ? 212.169 202.699 174.591 1.00 30.00 ? 123 PRO A CB  1 
ATOM   949  C CG  . PRO A 1 123 ? 210.923 202.858 173.749 1.00 30.00 ? 123 PRO A CG  1 
ATOM   950  C CD  . PRO A 1 123 ? 210.956 201.698 172.778 1.00 30.00 ? 123 PRO A CD  1 
ATOM   951  N N   . VAL A 1 124 ? 212.639 199.904 176.762 1.00 30.00 ? 124 VAL A N   1 
ATOM   952  C CA  . VAL A 1 124 ? 212.214 199.320 178.067 1.00 30.00 ? 124 VAL A CA  1 
ATOM   953  C C   . VAL A 1 124 ? 212.858 200.165 179.164 1.00 30.00 ? 124 VAL A C   1 
ATOM   954  O O   . VAL A 1 124 ? 214.075 200.016 179.383 1.00 30.00 ? 124 VAL A O   1 
ATOM   955  C CB  . VAL A 1 124 ? 212.630 197.847 178.204 1.00 30.00 ? 124 VAL A CB  1 
ATOM   956  C CG1 . VAL A 1 124 ? 212.199 197.257 179.536 1.00 30.00 ? 124 VAL A CG1 1 
ATOM   957  C CG2 . VAL A 1 124 ? 212.110 197.003 177.056 1.00 30.00 ? 124 VAL A CG2 1 
ATOM   958  N N   . PRO A 1 125 ? 212.100 201.027 179.871 1.00 30.00 ? 125 PRO A N   1 
ATOM   959  C CA  . PRO A 1 125 ? 212.683 201.893 180.882 1.00 30.00 ? 125 PRO A CA  1 
ATOM   960  C C   . PRO A 1 125 ? 213.020 201.044 182.110 1.00 30.00 ? 125 PRO A C   1 
ATOM   961  O O   . PRO A 1 125 ? 212.122 200.754 182.873 1.00 30.00 ? 125 PRO A O   1 
ATOM   962  C CB  . PRO A 1 125 ? 211.576 202.913 181.146 1.00 30.00 ? 125 PRO A CB  1 
ATOM   963  C CG  . PRO A 1 125 ? 210.305 202.146 180.891 1.00 30.00 ? 125 PRO A CG  1 
ATOM   964  C CD  . PRO A 1 125 ? 210.651 201.195 179.766 1.00 30.00 ? 125 PRO A CD  1 
ATOM   965  N N   . VAL A 1 126 ? 214.290 200.685 182.288 1.00 30.00 ? 126 VAL A N   1 
ATOM   966  C CA  . VAL A 1 126 ? 214.741 199.821 183.407 1.00 30.00 ? 126 VAL A CA  1 
ATOM   967  C C   . VAL A 1 126 ? 215.077 200.762 184.554 1.00 30.00 ? 126 VAL A C   1 
ATOM   968  O O   . VAL A 1 126 ? 215.617 200.285 185.547 1.00 30.00 ? 126 VAL A O   1 
ATOM   969  C CB  . VAL A 1 126 ? 215.933 198.943 183.004 1.00 30.00 ? 126 VAL A CB  1 
ATOM   970  C CG1 . VAL A 1 126 ? 215.560 197.967 181.903 1.00 30.00 ? 126 VAL A CG1 1 
ATOM   971  C CG2 . VAL A 1 126 ? 217.144 199.765 182.600 1.00 30.00 ? 126 VAL A CG2 1 
ATOM   972  N N   . GLY A 1 127 ? 214.753 202.045 184.418 1.00 30.00 ? 127 GLY A N   1 
ATOM   973  C CA  . GLY A 1 127 ? 215.034 203.044 185.456 1.00 30.00 ? 127 GLY A CA  1 
ATOM   974  C C   . GLY A 1 127 ? 213.843 203.272 186.356 1.00 30.00 ? 127 GLY A C   1 
ATOM   975  O O   . GLY A 1 127 ? 214.072 203.358 187.562 1.00 30.00 ? 127 GLY A O   1 
ATOM   976  N N   . ASN A 1 128 ? 212.623 203.327 185.826 1.00 30.00 ? 128 ASN A N   1 
ATOM   977  C CA  . ASN A 1 128 ? 211.421 203.664 186.634 1.00 30.00 ? 128 ASN A CA  1 
ATOM   978  C C   . ASN A 1 128 ? 210.790 202.406 187.228 1.00 30.00 ? 128 ASN A C   1 
ATOM   979  O O   . ASN A 1 128 ? 210.224 202.506 188.331 1.00 30.00 ? 128 ASN A O   1 
ATOM   980  C CB  . ASN A 1 128 ? 210.389 204.389 185.784 1.00 30.00 ? 128 ASN A CB  1 
ATOM   981  C CG  . ASN A 1 128 ? 210.956 205.623 185.122 1.00 30.00 ? 128 ASN A CG  1 
ATOM   982  O OD1 . ASN A 1 128 ? 211.428 206.534 185.797 1.00 30.00 ? 128 ASN A OD1 1 
ATOM   983  N ND2 . ASN A 1 128 ? 210.930 205.654 183.801 1.00 30.00 ? 128 ASN A ND2 1 
ATOM   984  N N   . ILE A 1 129 ? 210.890 201.274 186.534 1.00 30.00 ? 129 ILE A N   1 
ATOM   985  C CA  . ILE A 1 129 ? 210.288 199.991 186.994 1.00 30.00 ? 129 ILE A CA  1 
ATOM   986  C C   . ILE A 1 129 ? 210.915 199.627 188.333 1.00 30.00 ? 129 ILE A C   1 
ATOM   987  O O   . ILE A 1 129 ? 210.172 199.222 189.243 1.00 30.00 ? 129 ILE A O   1 
ATOM   988  C CB  . ILE A 1 129 ? 210.561 198.882 185.965 1.00 30.00 ? 129 ILE A CB  1 
ATOM   989  C CG1 . ILE A 1 129 ? 209.925 199.187 184.608 1.00 30.00 ? 129 ILE A CG1 1 
ATOM   990  C CG2 . ILE A 1 129 ? 210.118 197.531 186.503 1.00 30.00 ? 129 ILE A CG2 1 
ATOM   991  C CD1 . ILE A 1 129 ? 210.363 198.249 183.512 1.00 30.00 ? 129 ILE A CD1 1 
ATOM   992  N N   . TYR A 1 130 ? 212.230 199.762 188.452 1.00 30.00 ? 130 TYR A N   1 
ATOM   993  C CA  . TYR A 1 130 ? 212.973 199.379 189.672 1.00 30.00 ? 130 TYR A CA  1 
ATOM   994  C C   . TYR A 1 130 ? 212.557 200.225 190.868 1.00 30.00 ? 130 TYR A C   1 
ATOM   995  O O   . TYR A 1 130 ? 212.313 199.636 191.925 1.00 30.00 ? 130 TYR A O   1 
ATOM   996  C CB  . TYR A 1 130 ? 214.449 199.629 189.426 1.00 30.00 ? 130 TYR A CB  1 
ATOM   997  C CG  . TYR A 1 130 ? 215.364 199.163 190.520 1.00 30.00 ? 130 TYR A CG  1 
ATOM   998  C CD1 . TYR A 1 130 ? 215.382 197.841 190.912 1.00 30.00 ? 130 TYR A CD1 1 
ATOM   999  C CD2 . TYR A 1 130 ? 216.235 200.037 191.136 1.00 30.00 ? 130 TYR A CD2 1 
ATOM   1000 C CE1 . TYR A 1 130 ? 216.230 197.399 191.909 1.00 30.00 ? 130 TYR A CE1 1 
ATOM   1001 C CE2 . TYR A 1 130 ? 217.092 199.613 192.133 1.00 30.00 ? 130 TYR A CE2 1 
ATOM   1002 C CZ  . TYR A 1 130 ? 217.089 198.288 192.519 1.00 30.00 ? 130 TYR A CZ  1 
ATOM   1003 O OH  . TYR A 1 130 ? 217.922 197.844 193.507 1.00 30.00 ? 130 TYR A OH  1 
ATOM   1004 N N   . ARG A 1 131 ? 212.563 201.551 190.704 1.00 30.00 ? 131 ARG A N   1 
ATOM   1005 C CA  . ARG A 1 131 ? 212.168 202.516 191.760 1.00 30.00 ? 131 ARG A CA  1 
ATOM   1006 C C   . ARG A 1 131 ? 210.819 202.123 192.337 1.00 30.00 ? 131 ARG A C   1 
ATOM   1007 O O   . ARG A 1 131 ? 210.705 202.165 193.550 1.00 30.00 ? 131 ARG A O   1 
ATOM   1008 C CB  . ARG A 1 131 ? 212.056 203.904 191.141 1.00 30.00 ? 131 ARG A CB  1 
ATOM   1009 C CG  . ARG A 1 131 ? 213.404 204.435 190.681 1.00 30.00 ? 131 ARG A CG  1 
ATOM   1010 C CD  . ARG A 1 131 ? 213.386 205.571 189.686 1.00 30.00 ? 131 ARG A CD  1 
ATOM   1011 N NE  . ARG A 1 131 ? 212.899 206.817 190.242 1.00 30.00 ? 131 ARG A NE  1 
ATOM   1012 C CZ  . ARG A 1 131 ? 211.852 207.487 189.788 1.00 30.00 ? 131 ARG A CZ  1 
ATOM   1013 N NH1 . ARG A 1 131 ? 210.886 206.872 189.133 1.00 30.00 ? 131 ARG A NH1 1 
ATOM   1014 N NH2 . ARG A 1 131 ? 211.762 208.782 190.017 1.00 30.00 ? 131 ARG A NH2 1 
ATOM   1015 N N   . ARG A 1 132 ? 209.834 201.847 191.488 1.00 30.00 ? 132 ARG A N   1 
ATOM   1016 C CA  . ARG A 1 132 ? 208.484 201.409 191.895 1.00 30.00 ? 132 ARG A CA  1 
ATOM   1017 C C   . ARG A 1 132 ? 208.601 200.274 192.907 1.00 30.00 ? 132 ARG A C   1 
ATOM   1018 O O   . ARG A 1 132 ? 207.889 200.323 193.923 1.00 30.00 ? 132 ARG A O   1 
ATOM   1019 C CB  . ARG A 1 132 ? 207.758 200.939 190.646 1.00 30.00 ? 132 ARG A CB  1 
ATOM   1020 C CG  . ARG A 1 132 ? 206.266 200.721 190.820 1.00 30.00 ? 132 ARG A CG  1 
ATOM   1021 C CD  . ARG A 1 132 ? 205.700 200.214 189.513 1.00 30.00 ? 132 ARG A CD  1 
ATOM   1022 N NE  . ARG A 1 132 ? 205.929 201.165 188.434 1.00 30.00 ? 132 ARG A NE  1 
ATOM   1023 C CZ  . ARG A 1 132 ? 205.608 200.970 187.161 1.00 30.00 ? 132 ARG A CZ  1 
ATOM   1024 N NH1 . ARG A 1 132 ? 205.185 199.791 186.743 1.00 30.00 ? 132 ARG A NH1 1 
ATOM   1025 N NH2 . ARG A 1 132 ? 205.743 201.959 186.294 1.00 30.00 ? 132 ARG A NH2 1 
ATOM   1026 N N   . TRP A 1 133 ? 209.455 199.285 192.638 1.00 30.00 ? 133 TRP A N   1 
ATOM   1027 C CA  . TRP A 1 133 ? 209.614 198.104 193.517 1.00 30.00 ? 133 TRP A CA  1 
ATOM   1028 C C   . TRP A 1 133 ? 210.203 198.551 194.851 1.00 30.00 ? 133 TRP A C   1 
ATOM   1029 O O   . TRP A 1 133 ? 209.736 198.066 195.903 1.00 30.00 ? 133 TRP A O   1 
ATOM   1030 C CB  . TRP A 1 133 ? 210.542 197.103 192.852 1.00 30.00 ? 133 TRP A CB  1 
ATOM   1031 C CG  . TRP A 1 133 ? 210.123 196.626 191.497 1.00 30.00 ? 133 TRP A CG  1 
ATOM   1032 C CD1 . TRP A 1 133 ? 208.991 196.945 190.807 1.00 30.00 ? 133 TRP A CD1 1 
ATOM   1033 C CD2 . TRP A 1 133 ? 210.870 195.748 190.641 1.00 30.00 ? 133 TRP A CD2 1 
ATOM   1034 N NE1 . TRP A 1 133 ? 208.979 196.314 189.592 1.00 30.00 ? 133 TRP A NE1 1 
ATOM   1035 C CE2 . TRP A 1 133 ? 210.121 195.572 189.464 1.00 30.00 ? 133 TRP A CE2 1 
ATOM   1036 C CE3 . TRP A 1 133 ? 212.094 195.090 190.760 1.00 30.00 ? 133 TRP A CE3 1 
ATOM   1037 C CZ2 . TRP A 1 133 ? 210.559 194.765 188.419 1.00 30.00 ? 133 TRP A CZ2 1 
ATOM   1038 C CZ3 . TRP A 1 133 ? 212.528 194.291 189.729 1.00 30.00 ? 133 TRP A CZ3 1 
ATOM   1039 C CH2 . TRP A 1 133 ? 211.769 194.134 188.574 1.00 30.00 ? 133 TRP A CH2 1 
ATOM   1040 N N   . ILE A 1 134 ? 211.236 199.392 194.779 1.00 30.00 ? 134 ILE A N   1 
ATOM   1041 C CA  . ILE A 1 134 ? 211.917 199.903 195.995 1.00 30.00 ? 134 ILE A CA  1 
ATOM   1042 C C   . ILE A 1 134 ? 210.851 200.588 196.834 1.00 30.00 ? 134 ILE A C   1 
ATOM   1043 O O   . ILE A 1 134 ? 210.919 200.440 198.039 1.00 30.00 ? 134 ILE A O   1 
ATOM   1044 C CB  . ILE A 1 134 ? 213.023 200.930 195.695 1.00 30.00 ? 134 ILE A CB  1 
ATOM   1045 C CG1 . ILE A 1 134 ? 213.808 200.694 194.408 1.00 30.00 ? 134 ILE A CG1 1 
ATOM   1046 C CG2 . ILE A 1 134 ? 213.970 201.023 196.872 1.00 30.00 ? 134 ILE A CG2 1 
ATOM   1047 C CD1 . ILE A 1 134 ? 214.426 199.338 194.301 1.00 30.00 ? 134 ILE A CD1 1 
ATOM   1048 N N   . GLN A 1 135 ? 209.908 201.288 196.202 1.00 30.00 ? 135 GLN A N   1 
ATOM   1049 C CA  . GLN A 1 135 ? 208.887 202.095 196.919 1.00 30.00 ? 135 GLN A CA  1 
ATOM   1050 C C   . GLN A 1 135 ? 207.907 201.217 197.697 1.00 30.00 ? 135 GLN A C   1 
ATOM   1051 O O   . GLN A 1 135 ? 207.291 201.745 198.614 1.00 30.00 ? 135 GLN A O   1 
ATOM   1052 C CB  . GLN A 1 135 ? 208.129 202.985 195.941 1.00 30.00 ? 135 GLN A CB  1 
ATOM   1053 C CG  . GLN A 1 135 ? 208.934 204.203 195.527 1.00 30.00 ? 135 GLN A CG  1 
ATOM   1054 C CD  . GLN A 1 135 ? 208.142 205.154 194.671 1.00 30.00 ? 135 GLN A CD  1 
ATOM   1055 O OE1 . GLN A 1 135 ? 206.973 204.925 194.376 1.00 30.00 ? 135 GLN A OE1 1 
ATOM   1056 N NE2 . GLN A 1 135 ? 208.775 206.244 194.272 1.00 30.00 ? 135 GLN A NE2 1 
ATOM   1057 N N   . ILE A 1 136 ? 207.761 199.946 197.339 1.00 30.00 ? 136 ILE A N   1 
ATOM   1058 C CA  . ILE A 1 136 ? 206.828 199.017 198.037 1.00 30.00 ? 136 ILE A CA  1 
ATOM   1059 C C   . ILE A 1 136 ? 207.527 198.520 199.301 1.00 30.00 ? 136 ILE A C   1 
ATOM   1060 O O   . ILE A 1 136 ? 206.825 198.319 200.292 1.00 30.00 ? 136 ILE A O   1 
ATOM   1061 C CB  . ILE A 1 136 ? 206.424 197.871 197.099 1.00 30.00 ? 136 ILE A CB  1 
ATOM   1062 C CG1 . ILE A 1 136 ? 205.795 198.401 195.810 1.00 30.00 ? 136 ILE A CG1 1 
ATOM   1063 C CG2 . ILE A 1 136 ? 205.510 196.891 197.811 1.00 30.00 ? 136 ILE A CG2 1 
ATOM   1064 C CD1 . ILE A 1 136 ? 205.624 197.358 194.740 1.00 30.00 ? 136 ILE A CD1 1 
ATOM   1065 N N   . GLY A 1 137 ? 208.844 198.309 199.260 1.00 30.00 ? 137 GLY A N   1 
ATOM   1066 C CA  . GLY A 1 137 ? 209.640 197.917 200.439 1.00 30.00 ? 137 GLY A CA  1 
ATOM   1067 C C   . GLY A 1 137 ? 209.702 199.070 201.421 1.00 30.00 ? 137 GLY A C   1 
ATOM   1068 O O   . GLY A 1 137 ? 209.435 198.831 202.613 1.00 30.00 ? 137 GLY A O   1 
ATOM   1069 N N   . LEU A 1 138 ? 209.956 200.289 200.935 1.00 30.00 ? 138 LEU A N   1 
ATOM   1070 C CA  . LEU A 1 138 ? 209.986 201.507 201.784 1.00 30.00 ? 138 LEU A CA  1 
ATOM   1071 C C   . LEU A 1 138 ? 208.623 201.674 202.446 1.00 30.00 ? 138 LEU A C   1 
ATOM   1072 O O   . LEU A 1 138 ? 208.585 201.940 203.662 1.00 30.00 ? 138 LEU A O   1 
ATOM   1073 C CB  . LEU A 1 138 ? 210.239 202.726 200.895 1.00 30.00 ? 138 LEU A CB  1 
ATOM   1074 C CG  . LEU A 1 138 ? 211.676 203.191 200.720 1.00 30.00 ? 138 LEU A CG  1 
ATOM   1075 C CD1 . LEU A 1 138 ? 212.435 202.271 199.800 1.00 30.00 ? 138 LEU A CD1 1 
ATOM   1076 C CD2 . LEU A 1 138 ? 211.696 204.596 200.162 1.00 30.00 ? 138 LEU A CD2 1 
ATOM   1077 N N   . GLN A 1 139 ? 207.548 201.490 201.681 1.00 30.00 ? 139 GLN A N   1 
ATOM   1078 C CA  . GLN A 1 139 ? 206.171 201.726 202.182 1.00 30.00 ? 139 GLN A CA  1 
ATOM   1079 C C   . GLN A 1 139 ? 205.826 200.729 203.286 1.00 30.00 ? 139 GLN A C   1 
ATOM   1080 O O   . GLN A 1 139 ? 205.246 201.162 204.291 1.00 30.00 ? 139 GLN A O   1 
ATOM   1081 C CB  . GLN A 1 139 ? 205.157 201.650 201.048 1.00 30.00 ? 139 GLN A CB  1 
ATOM   1082 C CG  . GLN A 1 139 ? 205.105 202.917 200.213 1.00 30.00 ? 139 GLN A CG  1 
ATOM   1083 C CD  . GLN A 1 139 ? 204.150 202.799 199.055 1.00 30.00 ? 139 GLN A CD  1 
ATOM   1084 O OE1 . GLN A 1 139 ? 203.498 201.777 198.865 1.00 30.00 ? 139 GLN A OE1 1 
ATOM   1085 N NE2 . GLN A 1 139 ? 204.060 203.858 198.271 1.00 30.00 ? 139 GLN A NE2 1 
ATOM   1086 N N   . LYS A 1 140 ? 206.192 199.463 203.137 1.00 30.00 ? 140 LYS A N   1 
ATOM   1087 C CA  . LYS A 1 140 ? 205.912 198.442 204.171 1.00 30.00 ? 140 LYS A CA  1 
ATOM   1088 C C   . LYS A 1 140 ? 206.582 198.834 205.479 1.00 30.00 ? 140 LYS A C   1 
ATOM   1089 O O   . LYS A 1 140 ? 205.941 198.696 206.525 1.00 30.00 ? 140 LYS A O   1 
ATOM   1090 C CB  . LYS A 1 140 ? 206.526 197.109 203.785 1.00 30.00 ? 140 LYS A CB  1 
ATOM   1091 C CG  . LYS A 1 140 ? 205.851 196.377 202.639 1.00 30.00 ? 140 LYS A CG  1 
ATOM   1092 C CD  . LYS A 1 140 ? 206.710 195.265 202.083 1.00 30.00 ? 140 LYS A CD  1 
ATOM   1093 C CE  . LYS A 1 140 ? 207.275 194.356 203.152 1.00 30.00 ? 140 LYS A CE  1 
ATOM   1094 N NZ  . LYS A 1 140 ? 206.199 193.741 203.957 1.00 30.00 ? 140 LYS A NZ  1 
ATOM   1095 N N   . CYS A 1 141 ? 207.828 199.294 205.417 1.00 30.00 ? 141 CYS A N   1 
ATOM   1096 C CA  . CYS A 1 141 ? 208.607 199.679 206.618 1.00 30.00 ? 141 CYS A CA  1 
ATOM   1097 C C   . CYS A 1 141 ? 207.910 200.814 207.350 1.00 30.00 ? 141 CYS A C   1 
ATOM   1098 O O   . CYS A 1 141 ? 207.802 200.750 208.584 1.00 30.00 ? 141 CYS A O   1 
ATOM   1099 C CB  . CYS A 1 141 ? 209.947 200.240 206.205 1.00 30.00 ? 141 CYS A CB  1 
ATOM   1100 S SG  . CYS A 1 141 ? 210.859 199.192 205.054 1.00 30.00 ? 141 CYS A SG  1 
ATOM   1101 N N   . VAL A 1 142 ? 207.448 201.808 206.600 1.00 30.00 ? 142 VAL A N   1 
ATOM   1102 C CA  . VAL A 1 142 ? 206.727 202.964 207.184 1.00 30.00 ? 142 VAL A CA  1 
ATOM   1103 C C   . VAL A 1 142 ? 205.541 202.391 207.944 1.00 30.00 ? 142 VAL A C   1 
ATOM   1104 O O   . VAL A 1 142 ? 205.270 202.856 209.068 1.00 30.00 ? 142 VAL A O   1 
ATOM   1105 C CB  . VAL A 1 142 ? 206.257 203.891 206.060 1.00 30.00 ? 142 VAL A CB  1 
ATOM   1106 C CG1 . VAL A 1 142 ? 205.220 204.886 206.537 1.00 30.00 ? 142 VAL A CG1 1 
ATOM   1107 C CG2 . VAL A 1 142 ? 207.411 204.604 205.381 1.00 30.00 ? 142 VAL A CG2 1 
ATOM   1108 N N   . ARG A 1 143 ? 204.899 201.380 207.363 1.00 30.00 ? 143 ARG A N   1 
ATOM   1109 C CA  . ARG A 1 143 ? 203.709 200.758 207.978 1.00 30.00 ? 143 ARG A CA  1 
ATOM   1110 C C   . ARG A 1 143 ? 204.170 199.940 209.172 1.00 30.00 ? 143 ARG A C   1 
ATOM   1111 O O   . ARG A 1 143 ? 203.409 199.854 210.132 1.00 30.00 ? 143 ARG A O   1 
ATOM   1112 C CB  . ARG A 1 143 ? 202.979 199.856 206.990 1.00 30.00 ? 143 ARG A CB  1 
ATOM   1113 C CG  . ARG A 1 143 ? 201.600 199.439 207.470 1.00 30.00 ? 143 ARG A CG  1 
ATOM   1114 C CD  . ARG A 1 143 ? 200.832 198.753 206.368 1.00 30.00 ? 143 ARG A CD  1 
ATOM   1115 N NE  . ARG A 1 143 ? 201.569 197.594 205.900 1.00 30.00 ? 143 ARG A NE  1 
ATOM   1116 C CZ  . ARG A 1 143 ? 202.040 197.440 204.670 1.00 30.00 ? 143 ARG A CZ  1 
ATOM   1117 N NH1 . ARG A 1 143 ? 202.243 198.488 203.893 1.00 30.00 ? 143 ARG A NH1 1 
ATOM   1118 N NH2 . ARG A 1 143 ? 202.356 196.233 204.238 1.00 30.00 ? 143 ARG A NH2 1 
ATOM   1119 N N   . MET A 1 144 ? 205.366 199.371 209.120 1.00 30.00 ? 144 MET A N   1 
ATOM   1120 C CA  . MET A 1 144 ? 205.924 198.586 210.244 1.00 30.00 ? 144 MET A CA  1 
ATOM   1121 C C   . MET A 1 144 ? 206.367 199.548 211.346 1.00 30.00 ? 144 MET A C   1 
ATOM   1122 O O   . MET A 1 144 ? 206.593 199.066 212.474 1.00 30.00 ? 144 MET A O   1 
ATOM   1123 C CB  . MET A 1 144 ? 207.120 197.773 209.761 1.00 30.00 ? 144 MET A CB  1 
ATOM   1124 C CG  . MET A 1 144 ? 206.726 196.553 208.964 1.00 30.00 ? 144 MET A CG  1 
ATOM   1125 S SD  . MET A 1 144 ? 208.087 195.409 208.632 1.00 30.00 ? 144 MET A SD  1 
ATOM   1126 C CE  . MET A 1 144 ? 209.525 196.457 208.843 1.00 30.00 ? 144 MET A CE  1 
ATOM   1127 N N   . TYR A 1 145 ? 206.484 200.846 211.044 1.00 30.00 ? 145 TYR A N   1 
ATOM   1128 C CA  . TYR A 1 145 ? 206.958 201.867 212.013 1.00 30.00 ? 145 TYR A CA  1 
ATOM   1129 C C   . TYR A 1 145 ? 205.907 202.940 212.315 1.00 30.00 ? 145 TYR A C   1 
ATOM   1130 O O   . TYR A 1 145 ? 206.333 204.064 212.624 1.00 30.00 ? 145 TYR A O   1 
ATOM   1131 C CB  . TYR A 1 145 ? 208.186 202.603 211.487 1.00 30.00 ? 145 TYR A CB  1 
ATOM   1132 C CG  . TYR A 1 145 ? 209.395 201.773 211.149 1.00 30.00 ? 145 TYR A CG  1 
ATOM   1133 C CD1 . TYR A 1 145 ? 209.979 200.942 212.084 1.00 30.00 ? 145 TYR A CD1 1 
ATOM   1134 C CD2 . TYR A 1 145 ? 210.023 201.910 209.926 1.00 30.00 ? 145 TYR A CD2 1 
ATOM   1135 C CE1 . TYR A 1 145 ? 211.116 200.210 211.788 1.00 30.00 ? 145 TYR A CE1 1 
ATOM   1136 C CE2 . TYR A 1 145 ? 211.159 201.188 209.612 1.00 30.00 ? 145 TYR A CE2 1 
ATOM   1137 C CZ  . TYR A 1 145 ? 211.709 200.334 210.547 1.00 30.00 ? 145 TYR A CZ  1 
ATOM   1138 O OH  . TYR A 1 145 ? 212.836 199.621 210.237 1.00 30.00 ? 145 TYR A OH  1 
ATOM   1139 N N   . ASN A 1 146 ? 204.605 202.674 212.181 1.00 30.00 ? 146 ASN A N   1 
ATOM   1140 C CA  . ASN A 1 146 ? 203.575 203.644 212.641 1.00 30.00 ? 146 ASN A CA  1 
ATOM   1141 C C   . ASN A 1 146 ? 203.431 203.289 214.122 1.00 30.00 ? 146 ASN A C   1 
ATOM   1142 O O   . ASN A 1 146 ? 202.708 202.327 214.437 1.00 30.00 ? 146 ASN A O   1 
ATOM   1143 C CB  . ASN A 1 146 ? 202.280 203.676 211.816 1.00 30.00 ? 146 ASN A CB  1 
ATOM   1144 C CG  . ASN A 1 146 ? 201.718 202.323 211.436 1.00 30.00 ? 146 ASN A CG  1 
ATOM   1145 O OD1 . ASN A 1 146 ? 201.411 201.496 212.289 1.00 30.00 ? 146 ASN A OD1 1 
ATOM   1146 N ND2 . ASN A 1 146 ? 201.557 202.097 210.144 1.00 30.00 ? 146 ASN A ND2 1 
ATOM   1147 N N   . PRO A 1 147 ? 204.098 204.011 215.047 1.00 30.00 ? 147 PRO A N   1 
ATOM   1148 C CA  . PRO A 1 147 ? 204.116 203.619 216.457 1.00 30.00 ? 147 PRO A CA  1 
ATOM   1149 C C   . PRO A 1 147 ? 202.691 203.492 216.989 1.00 30.00 ? 147 PRO A C   1 
ATOM   1150 O O   . PRO A 1 147 ? 202.459 202.621 217.807 1.00 30.00 ? 147 PRO A O   1 
ATOM   1151 C CB  . PRO A 1 147 ? 204.848 204.782 217.136 1.00 30.00 ? 147 PRO A CB  1 
ATOM   1152 C CG  . PRO A 1 147 ? 204.663 205.935 216.193 1.00 30.00 ? 147 PRO A CG  1 
ATOM   1153 C CD  . PRO A 1 147 ? 204.782 205.287 214.836 1.00 30.00 ? 147 PRO A CD  1 
ATOM   1154 N N   . THR A 1 148 ? 201.789 204.348 216.517 1.00 30.00 ? 148 THR A N   1 
ATOM   1155 C CA  . THR A 1 148 ? 200.372 204.346 216.948 1.00 30.00 ? 148 THR A CA  1 
ATOM   1156 C C   . THR A 1 148 ? 199.485 203.907 215.787 1.00 30.00 ? 148 THR A C   1 
ATOM   1157 O O   . THR A 1 148 ? 199.638 204.481 214.689 1.00 30.00 ? 148 THR A O   1 
ATOM   1158 C CB  . THR A 1 148 ? 199.968 205.743 217.416 1.00 30.00 ? 148 THR A CB  1 
ATOM   1159 O OG1 . THR A 1 148 ? 200.079 206.642 216.314 1.00 30.00 ? 148 THR A OG1 1 
ATOM   1160 C CG2 . THR A 1 148 ? 200.822 206.250 218.555 1.00 30.00 ? 148 THR A CG2 1 
ATOM   1161 N N   . ASN A 1 149 ? 198.611 202.926 216.005 1.00 30.00 ? 149 ASN A N   1 
ATOM   1162 C CA  . ASN A 1 149 ? 197.630 202.529 214.965 1.00 30.00 ? 149 ASN A CA  1 
ATOM   1163 C C   . ASN A 1 149 ? 196.503 203.566 215.086 1.00 30.00 ? 149 ASN A C   1 
ATOM   1164 O O   . ASN A 1 149 ? 196.345 204.102 216.200 1.00 30.00 ? 149 ASN A O   1 
ATOM   1165 C CB  . ASN A 1 149 ? 197.200 201.074 215.089 1.00 30.00 ? 149 ASN A CB  1 
ATOM   1166 C CG  . ASN A 1 149 ? 198.367 200.117 215.010 1.00 30.00 ? 149 ASN A CG  1 
ATOM   1167 O OD1 . ASN A 1 149 ? 199.510 200.538 214.854 1.00 30.00 ? 149 ASN A OD1 1 
ATOM   1168 N ND2 . ASN A 1 149 ? 198.088 198.828 215.114 1.00 30.00 ? 149 ASN A ND2 1 
ATOM   1169 N N   . ILE A 1 150 ? 195.786 203.901 214.009 1.00 30.00 ? 150 ILE A N   1 
ATOM   1170 C CA  . ILE A 1 150 ? 194.745 204.982 214.019 1.00 30.00 ? 150 ILE A CA  1 
ATOM   1171 C C   . ILE A 1 150 ? 193.643 204.703 215.043 1.00 30.00 ? 150 ILE A C   1 
ATOM   1172 O O   . ILE A 1 150 ? 193.018 205.682 215.499 1.00 30.00 ? 150 ILE A O   1 
ATOM   1173 C CB  . ILE A 1 150 ? 194.130 205.181 212.621 1.00 30.00 ? 150 ILE A CB  1 
ATOM   1174 C CG1 . ILE A 1 150 ? 193.574 203.894 212.011 1.00 30.00 ? 150 ILE A CG1 1 
ATOM   1175 C CG2 . ILE A 1 150 ? 195.136 205.838 211.694 1.00 30.00 ? 150 ILE A CG2 1 
ATOM   1176 C CD1 . ILE A 1 150 ? 192.128 203.657 212.311 1.00 30.00 ? 150 ILE A CD1 1 
ATOM   1177 N N   . LEU A 1 151 ? 193.395 203.440 215.382 1.00 30.00 ? 151 LEU A N   1 
ATOM   1178 C CA  . LEU A 1 151 ? 192.318 203.053 216.329 1.00 30.00 ? 151 LEU A CA  1 
ATOM   1179 C C   . LEU A 1 151 ? 192.769 203.366 217.754 1.00 30.00 ? 151 LEU A C   1 
ATOM   1180 O O   . LEU A 1 151 ? 191.928 203.263 218.668 1.00 30.00 ? 151 LEU A O   1 
ATOM   1181 C CB  . LEU A 1 151 ? 192.053 201.558 216.160 1.00 30.00 ? 151 LEU A CB  1 
ATOM   1182 C CG  . LEU A 1 151 ? 191.368 201.137 214.865 1.00 30.00 ? 151 LEU A CG  1 
ATOM   1183 C CD1 . LEU A 1 151 ? 191.104 199.645 214.866 1.00 30.00 ? 151 LEU A CD1 1 
ATOM   1184 C CD2 . LEU A 1 151 ? 190.069 201.893 214.681 1.00 30.00 ? 151 LEU A CD2 1 
ATOM   1185 N N   . ASP A 1 152 ? 194.041 203.719 217.935 1.00 30.00 ? 152 ASP A N   1 
ATOM   1186 C CA  . ASP A 1 152 ? 194.621 204.026 219.264 1.00 30.00 ? 152 ASP A CA  1 
ATOM   1187 C C   . ASP A 1 152 ? 194.937 205.513 219.383 1.00 30.00 ? 152 ASP A C   1 
ATOM   1188 O O   . ASP A 1 152 ? 195.320 205.938 220.490 1.00 30.00 ? 152 ASP A O   1 
ATOM   1189 C CB  . ASP A 1 152 ? 195.913 203.252 219.454 1.00 30.00 ? 152 ASP A CB  1 
ATOM   1190 C CG  . ASP A 1 152 ? 195.718 201.752 219.502 1.00 30.00 ? 152 ASP A CG  1 
ATOM   1191 O OD1 . ASP A 1 152 ? 194.996 201.295 220.401 1.00 30.00 ? 152 ASP A OD1 1 
ATOM   1192 O OD2 . ASP A 1 152 ? 196.296 201.059 218.650 1.00 30.00 ? 152 ASP A OD2 1 
ATOM   1193 N N   . VAL A 1 153 ? 194.825 206.268 218.290 1.00 30.00 ? 153 VAL A N   1 
ATOM   1194 C CA  . VAL A 1 153 ? 195.063 207.735 218.311 1.00 30.00 ? 153 VAL A CA  1 
ATOM   1195 C C   . VAL A 1 153 ? 193.785 208.324 218.891 1.00 30.00 ? 153 VAL A C   1 
ATOM   1196 O O   . VAL A 1 153 ? 192.731 208.157 218.244 1.00 30.00 ? 153 VAL A O   1 
ATOM   1197 C CB  . VAL A 1 153 ? 195.372 208.282 216.912 1.00 30.00 ? 153 VAL A CB  1 
ATOM   1198 C CG1 . VAL A 1 153 ? 195.589 209.785 216.934 1.00 30.00 ? 153 VAL A CG1 1 
ATOM   1199 C CG2 . VAL A 1 153 ? 196.563 207.581 216.281 1.00 30.00 ? 153 VAL A CG2 1 
ATOM   1200 N N   . LYS A 1 154 ? 193.852 208.917 220.078 1.00 30.00 ? 154 LYS A N   1 
ATOM   1201 C CA  . LYS A 1 154 ? 192.644 209.441 220.756 1.00 30.00 ? 154 LYS A CA  1 
ATOM   1202 C C   . LYS A 1 154 ? 192.983 210.789 221.378 1.00 30.00 ? 154 LYS A C   1 
ATOM   1203 O O   . LYS A 1 154 ? 194.079 211.282 221.104 1.00 30.00 ? 154 LYS A O   1 
ATOM   1204 C CB  . LYS A 1 154 ? 192.186 208.434 221.805 1.00 30.00 ? 154 LYS A CB  1 
ATOM   1205 C CG  . LYS A 1 154 ? 192.169 206.988 221.332 1.00 30.00 ? 154 LYS A CG  1 
ATOM   1206 C CD  . LYS A 1 154 ? 191.642 206.013 222.342 1.00 30.00 ? 154 LYS A CD  1 
ATOM   1207 C CE  . LYS A 1 154 ? 191.637 204.601 221.802 1.00 30.00 ? 154 LYS A CE  1 
ATOM   1208 N NZ  . LYS A 1 154 ? 191.187 203.629 222.823 1.00 30.00 ? 154 LYS A NZ  1 
ATOM   1209 N N   . GLN A 1 155 ? 192.097 211.334 222.207 1.00 30.00 ? 155 GLN A N   1 
ATOM   1210 C CA  . GLN A 1 155 ? 192.297 212.672 222.814 1.00 30.00 ? 155 GLN A CA  1 
ATOM   1211 C C   . GLN A 1 155 ? 192.324 212.529 224.335 1.00 30.00 ? 155 GLN A C   1 
ATOM   1212 O O   . GLN A 1 155 ? 191.407 211.879 224.874 1.00 30.00 ? 155 GLN A O   1 
ATOM   1213 C CB  . GLN A 1 155 ? 191.181 213.573 222.298 1.00 30.00 ? 155 GLN A CB  1 
ATOM   1214 C CG  . GLN A 1 155 ? 191.413 215.057 222.512 1.00 30.00 ? 155 GLN A CG  1 
ATOM   1215 C CD  . GLN A 1 155 ? 190.366 215.867 221.788 1.00 30.00 ? 155 GLN A CD  1 
ATOM   1216 O OE1 . GLN A 1 155 ? 189.492 215.324 221.119 1.00 30.00 ? 155 GLN A OE1 1 
ATOM   1217 N NE2 . GLN A 1 155 ? 190.441 217.180 221.911 1.00 30.00 ? 155 GLN A NE2 1 
ATOM   1218 N N   . GLY A 1 156 ? 193.339 213.091 224.995 1.00 30.00 ? 156 GLY A N   1 
ATOM   1219 C CA  . GLY A 1 156 ? 193.457 213.068 226.465 1.00 30.00 ? 156 GLY A CA  1 
ATOM   1220 C C   . GLY A 1 156 ? 192.851 214.336 227.030 1.00 30.00 ? 156 GLY A C   1 
ATOM   1221 O O   . GLY A 1 156 ? 192.399 215.159 226.222 1.00 30.00 ? 156 GLY A O   1 
ATOM   1222 N N   . PRO A 1 157 ? 192.808 214.552 228.361 1.00 30.00 ? 157 PRO A N   1 
ATOM   1223 C CA  . PRO A 1 157 ? 192.121 215.720 228.904 1.00 30.00 ? 157 PRO A CA  1 
ATOM   1224 C C   . PRO A 1 157 ? 192.655 217.036 228.334 1.00 30.00 ? 157 PRO A C   1 
ATOM   1225 O O   . PRO A 1 157 ? 191.845 217.917 228.106 1.00 30.00 ? 157 PRO A O   1 
ATOM   1226 C CB  . PRO A 1 157 ? 192.463 215.672 230.398 1.00 30.00 ? 157 PRO A CB  1 
ATOM   1227 C CG  . PRO A 1 157 ? 192.748 214.213 230.669 1.00 30.00 ? 157 PRO A CG  1 
ATOM   1228 C CD  . PRO A 1 157 ? 193.391 213.703 229.397 1.00 30.00 ? 157 PRO A CD  1 
ATOM   1229 N N   . LYS A 1 158 ? 193.966 217.140 228.107 1.00 30.00 ? 158 LYS A N   1 
ATOM   1230 C CA  . LYS A 1 158 ? 194.601 218.410 227.661 1.00 30.00 ? 158 LYS A CA  1 
ATOM   1231 C C   . LYS A 1 158 ? 195.081 218.314 226.210 1.00 30.00 ? 158 LYS A C   1 
ATOM   1232 O O   . LYS A 1 158 ? 195.848 219.210 225.806 1.00 30.00 ? 158 LYS A O   1 
ATOM   1233 C CB  . LYS A 1 158 ? 195.758 218.732 228.607 1.00 30.00 ? 158 LYS A CB  1 
ATOM   1234 C CG  . LYS A 1 158 ? 195.473 218.467 230.080 1.00 30.00 ? 158 LYS A CG  1 
ATOM   1235 C CD  . LYS A 1 158 ? 194.236 219.161 230.608 1.00 30.00 ? 158 LYS A CD  1 
ATOM   1236 C CE  . LYS A 1 158 ? 193.893 218.745 232.020 1.00 30.00 ? 158 LYS A CE  1 
ATOM   1237 N NZ  . LYS A 1 158 ? 192.603 219.326 232.457 1.00 30.00 ? 158 LYS A NZ  1 
ATOM   1238 N N   . GLU A 1 159 ? 194.652 217.301 225.448 1.00 30.00 ? 159 GLU A N   1 
ATOM   1239 C CA  . GLU A 1 159 ? 194.995 217.200 224.003 1.00 30.00 ? 159 GLU A CA  1 
ATOM   1240 C C   . GLU A 1 159 ? 193.875 217.870 223.209 1.00 30.00 ? 159 GLU A C   1 
ATOM   1241 O O   . GLU A 1 159 ? 192.711 217.503 223.434 1.00 30.00 ? 159 GLU A O   1 
ATOM   1242 C CB  . GLU A 1 159 ? 195.128 215.760 223.513 1.00 30.00 ? 159 GLU A CB  1 
ATOM   1243 C CG  . GLU A 1 159 ? 196.225 214.979 224.207 1.00 30.00 ? 159 GLU A CG  1 
ATOM   1244 C CD  . GLU A 1 159 ? 196.418 213.564 223.688 1.00 30.00 ? 159 GLU A CD  1 
ATOM   1245 O OE1 . GLU A 1 159 ? 195.680 213.167 222.766 1.00 30.00 ? 159 GLU A OE1 1 
ATOM   1246 O OE2 . GLU A 1 159 ? 197.303 212.862 224.213 1.00 30.00 ? 159 GLU A OE2 1 
ATOM   1247 N N   . PRO A 1 160 ? 194.139 218.849 222.321 1.00 30.00 ? 160 PRO A N   1 
ATOM   1248 C CA  . PRO A 1 160 ? 193.076 219.433 221.501 1.00 30.00 ? 160 PRO A CA  1 
ATOM   1249 C C   . PRO A 1 160 ? 192.641 218.585 220.298 1.00 30.00 ? 160 PRO A C   1 
ATOM   1250 O O   . PRO A 1 160 ? 193.001 217.421 220.260 1.00 30.00 ? 160 PRO A O   1 
ATOM   1251 C CB  . PRO A 1 160 ? 193.688 220.742 220.987 1.00 30.00 ? 160 PRO A CB  1 
ATOM   1252 C CG  . PRO A 1 160 ? 194.937 220.941 221.815 1.00 30.00 ? 160 PRO A CG  1 
ATOM   1253 C CD  . PRO A 1 160 ? 195.408 219.542 222.134 1.00 30.00 ? 160 PRO A CD  1 
ATOM   1254 N N   . PHE A 1 161 ? 191.907 219.173 219.350 1.00 30.00 ? 161 PHE A N   1 
ATOM   1255 C CA  . PHE A 1 161 ? 191.345 218.464 218.172 1.00 30.00 ? 161 PHE A CA  1 
ATOM   1256 C C   . PHE A 1 161 ? 192.162 218.733 216.910 1.00 30.00 ? 161 PHE A C   1 
ATOM   1257 O O   . PHE A 1 161 ? 191.868 218.100 215.880 1.00 30.00 ? 161 PHE A O   1 
ATOM   1258 C CB  . PHE A 1 161 ? 189.926 218.980 217.967 1.00 30.00 ? 161 PHE A CB  1 
ATOM   1259 C CG  . PHE A 1 161 ? 189.180 218.379 216.811 1.00 30.00 ? 161 PHE A CG  1 
ATOM   1260 C CD1 . PHE A 1 161 ? 188.915 217.023 216.765 1.00 30.00 ? 161 PHE A CD1 1 
ATOM   1261 C CD2 . PHE A 1 161 ? 188.755 219.177 215.769 1.00 30.00 ? 161 PHE A CD2 1 
ATOM   1262 C CE1 . PHE A 1 161 ? 188.227 216.478 215.696 1.00 30.00 ? 161 PHE A CE1 1 
ATOM   1263 C CE2 . PHE A 1 161 ? 188.069 218.629 214.701 1.00 30.00 ? 161 PHE A CE2 1 
ATOM   1264 C CZ  . PHE A 1 161 ? 187.806 217.282 214.667 1.00 30.00 ? 161 PHE A CZ  1 
ATOM   1265 N N   . GLN A 1 162 ? 193.154 219.619 216.984 1.00 30.00 ? 162 GLN A N   1 
ATOM   1266 C CA  . GLN A 1 162 ? 193.995 220.010 215.823 1.00 30.00 ? 162 GLN A CA  1 
ATOM   1267 C C   . GLN A 1 162 ? 195.245 219.141 215.813 1.00 30.00 ? 162 GLN A C   1 
ATOM   1268 O O   . GLN A 1 162 ? 195.699 218.768 214.719 1.00 30.00 ? 162 GLN A O   1 
ATOM   1269 C CB  . GLN A 1 162 ? 194.380 221.473 215.991 1.00 30.00 ? 162 GLN A CB  1 
ATOM   1270 C CG  . GLN A 1 162 ? 195.497 221.964 215.086 1.00 30.00 ? 162 GLN A CG  1 
ATOM   1271 C CD  . GLN A 1 162 ? 195.107 221.948 213.632 1.00 30.00 ? 162 GLN A CD  1 
ATOM   1272 O OE1 . GLN A 1 162 ? 194.132 222.577 213.229 1.00 30.00 ? 162 GLN A OE1 1 
ATOM   1273 N NE2 . GLN A 1 162 ? 195.871 221.222 212.835 1.00 30.00 ? 162 GLN A NE2 1 
ATOM   1274 N N   . SER A 1 163 ? 195.815 218.887 216.986 1.00 30.00 ? 163 SER A N   1 
ATOM   1275 C CA  . SER A 1 163 ? 197.011 218.026 217.131 1.00 30.00 ? 163 SER A CA  1 
ATOM   1276 C C   . SER A 1 163 ? 196.595 216.573 216.948 1.00 30.00 ? 163 SER A C   1 
ATOM   1277 O O   . SER A 1 163 ? 197.334 215.820 216.295 1.00 30.00 ? 163 SER A O   1 
ATOM   1278 C CB  . SER A 1 163 ? 197.609 218.234 218.463 1.00 30.00 ? 163 SER A CB  1 
ATOM   1279 O OG  . SER A 1 163 ? 198.638 217.288 218.696 1.00 30.00 ? 163 SER A OG  1 
ATOM   1280 N N   . TYR A 1 164 ? 195.451 216.202 217.508 1.00 30.00 ? 164 TYR A N   1 
ATOM   1281 C CA  . TYR A 1 164 ? 194.915 214.827 217.419 1.00 30.00 ? 164 TYR A CA  1 
ATOM   1282 C C   . TYR A 1 164 ? 194.614 214.460 215.971 1.00 30.00 ? 164 TYR A C   1 
ATOM   1283 O O   . TYR A 1 164 ? 194.963 213.339 215.553 1.00 30.00 ? 164 TYR A O   1 
ATOM   1284 C CB  . TYR A 1 164 ? 193.630 214.782 218.231 1.00 30.00 ? 164 TYR A CB  1 
ATOM   1285 C CG  . TYR A 1 164 ? 192.670 213.707 217.824 1.00 30.00 ? 164 TYR A CG  1 
ATOM   1286 C CD1 . TYR A 1 164 ? 193.042 212.380 217.852 1.00 30.00 ? 164 TYR A CD1 1 
ATOM   1287 C CD2 . TYR A 1 164 ? 191.389 214.021 217.421 1.00 30.00 ? 164 TYR A CD2 1 
ATOM   1288 C CE1 . TYR A 1 164 ? 192.164 211.384 217.473 1.00 30.00 ? 164 TYR A CE1 1 
ATOM   1289 C CE2 . TYR A 1 164 ? 190.494 213.038 217.048 1.00 30.00 ? 164 TYR A CE2 1 
ATOM   1290 C CZ  . TYR A 1 164 ? 190.886 211.714 217.074 1.00 30.00 ? 164 TYR A CZ  1 
ATOM   1291 O OH  . TYR A 1 164 ? 190.039 210.703 216.714 1.00 30.00 ? 164 TYR A OH  1 
ATOM   1292 N N   . VAL A 1 165 ? 193.957 215.364 215.245 1.00 30.00 ? 165 VAL A N   1 
ATOM   1293 C CA  . VAL A 1 165 ? 193.565 215.113 213.832 1.00 30.00 ? 165 VAL A CA  1 
ATOM   1294 C C   . VAL A 1 165 ? 194.857 215.004 213.027 1.00 30.00 ? 165 VAL A C   1 
ATOM   1295 O O   . VAL A 1 165 ? 194.890 214.206 212.075 1.00 30.00 ? 165 VAL A O   1 
ATOM   1296 C CB  . VAL A 1 165 ? 192.632 216.219 213.307 1.00 30.00 ? 165 VAL A CB  1 
ATOM   1297 C CG1 . VAL A 1 165 ? 193.292 217.572 213.207 1.00 30.00 ? 165 VAL A CG1 1 
ATOM   1298 C CG2 . VAL A 1 165 ? 192.023 215.854 211.973 1.00 30.00 ? 165 VAL A CG2 1 
ATOM   1299 N N   . ASP A 1 166 ? 195.887 215.762 213.411 1.00 30.00 ? 166 ASP A N   1 
ATOM   1300 C CA  . ASP A 1 166 ? 197.201 215.677 212.735 1.00 30.00 ? 166 ASP A CA  1 
ATOM   1301 C C   . ASP A 1 166 ? 197.804 214.302 212.980 1.00 30.00 ? 166 ASP A C   1 
ATOM   1302 O O   . ASP A 1 166 ? 198.250 213.684 212.009 1.00 30.00 ? 166 ASP A O   1 
ATOM   1303 C CB  . ASP A 1 166 ? 198.189 216.718 213.227 1.00 30.00 ? 166 ASP A CB  1 
ATOM   1304 C CG  . ASP A 1 166 ? 197.893 218.129 212.759 1.00 30.00 ? 166 ASP A CG  1 
ATOM   1305 O OD1 . ASP A 1 166 ? 196.898 218.306 212.043 1.00 30.00 ? 166 ASP A OD1 1 
ATOM   1306 O OD2 . ASP A 1 166 ? 198.672 219.037 213.104 1.00 30.00 ? 166 ASP A OD2 1 
ATOM   1307 N N   . ARG A 1 167 ? 197.797 213.830 214.221 1.00 30.00 ? 167 ARG A N   1 
ATOM   1308 C CA  . ARG A 1 167 ? 198.370 212.511 214.581 1.00 30.00 ? 167 ARG A CA  1 
ATOM   1309 C C   . ARG A 1 167 ? 197.571 211.410 213.885 1.00 30.00 ? 167 ARG A C   1 
ATOM   1310 O O   . ARG A 1 167 ? 198.187 210.393 213.522 1.00 30.00 ? 167 ARG A O   1 
ATOM   1311 C CB  . ARG A 1 167 ? 198.306 212.369 216.097 1.00 30.00 ? 167 ARG A CB  1 
ATOM   1312 C CG  . ARG A 1 167 ? 199.252 213.290 216.848 1.00 30.00 ? 167 ARG A CG  1 
ATOM   1313 C CD  . ARG A 1 167 ? 198.789 213.504 218.272 1.00 30.00 ? 167 ARG A CD  1 
ATOM   1314 N NE  . ARG A 1 167 ? 198.565 212.247 218.973 1.00 30.00 ? 167 ARG A NE  1 
ATOM   1315 C CZ  . ARG A 1 167 ? 197.413 211.865 219.512 1.00 30.00 ? 167 ARG A CZ  1 
ATOM   1316 N NH1 . ARG A 1 167 ? 196.457 212.740 219.768 1.00 30.00 ? 167 ARG A NH1 1 
ATOM   1317 N NH2 . ARG A 1 167 ? 197.231 210.597 219.834 1.00 30.00 ? 167 ARG A NH2 1 
ATOM   1318 N N   . PHE A 1 168 ? 196.263 211.596 213.700 1.00 30.00 ? 168 PHE A N   1 
ATOM   1319 C CA  . PHE A 1 168 ? 195.359 210.608 213.064 1.00 30.00 ? 168 PHE A CA  1 
ATOM   1320 C C   . PHE A 1 168 ? 195.641 210.466 211.571 1.00 30.00 ? 168 PHE A C   1 
ATOM   1321 O O   . PHE A 1 168 ? 195.927 209.338 211.128 1.00 30.00 ? 168 PHE A O   1 
ATOM   1322 C CB  . PHE A 1 168 ? 193.938 211.119 213.267 1.00 30.00 ? 168 PHE A CB  1 
ATOM   1323 C CG  . PHE A 1 168 ? 192.830 210.374 212.581 1.00 30.00 ? 168 PHE A CG  1 
ATOM   1324 C CD1 . PHE A 1 168 ? 192.625 209.030 212.815 1.00 30.00 ? 168 PHE A CD1 1 
ATOM   1325 C CD2 . PHE A 1 168 ? 191.947 211.041 211.756 1.00 30.00 ? 168 PHE A CD2 1 
ATOM   1326 C CE1 . PHE A 1 168 ? 191.589 208.358 212.191 1.00 30.00 ? 168 PHE A CE1 1 
ATOM   1327 C CE2 . PHE A 1 168 ? 190.907 210.370 211.141 1.00 30.00 ? 168 PHE A CE2 1 
ATOM   1328 C CZ  . PHE A 1 168 ? 190.731 209.029 211.358 1.00 30.00 ? 168 PHE A CZ  1 
ATOM   1329 N N   . TYR A 1 169 ? 195.564 211.562 210.822 1.00 30.00 ? 169 TYR A N   1 
ATOM   1330 C CA  . TYR A 1 169 ? 195.746 211.569 209.349 1.00 30.00 ? 169 TYR A CA  1 
ATOM   1331 C C   . TYR A 1 169 ? 197.150 211.121 208.943 1.00 30.00 ? 169 TYR A C   1 
ATOM   1332 O O   . TYR A 1 169 ? 197.278 210.400 207.935 1.00 30.00 ? 169 TYR A O   1 
ATOM   1333 C CB  . TYR A 1 169 ? 195.492 212.985 208.851 1.00 30.00 ? 169 TYR A CB  1 
ATOM   1334 C CG  . TYR A 1 169 ? 194.056 213.300 208.545 1.00 30.00 ? 169 TYR A CG  1 
ATOM   1335 C CD1 . TYR A 1 169 ? 193.363 212.587 207.588 1.00 30.00 ? 169 TYR A CD1 1 
ATOM   1336 C CD2 . TYR A 1 169 ? 193.399 214.321 209.193 1.00 30.00 ? 169 TYR A CD2 1 
ATOM   1337 C CE1 . TYR A 1 169 ? 192.045 212.871 207.291 1.00 30.00 ? 169 TYR A CE1 1 
ATOM   1338 C CE2 . TYR A 1 169 ? 192.082 214.623 208.908 1.00 30.00 ? 169 TYR A CE2 1 
ATOM   1339 C CZ  . TYR A 1 169 ? 191.404 213.896 207.954 1.00 30.00 ? 169 TYR A CZ  1 
ATOM   1340 O OH  . TYR A 1 169 ? 190.103 214.198 207.673 1.00 30.00 ? 169 TYR A OH  1 
ATOM   1341 N N   . LYS A 1 170 ? 198.173 211.548 209.678 1.00 30.00 ? 170 LYS A N   1 
ATOM   1342 C CA  . LYS A 1 170 ? 199.580 211.178 209.388 1.00 30.00 ? 170 LYS A CA  1 
ATOM   1343 C C   . LYS A 1 170 ? 199.715 209.661 209.435 1.00 30.00 ? 170 LYS A C   1 
ATOM   1344 O O   . LYS A 1 170 ? 200.472 209.104 208.621 1.00 30.00 ? 170 LYS A O   1 
ATOM   1345 C CB  . LYS A 1 170 ? 200.476 211.776 210.465 1.00 30.00 ? 170 LYS A CB  1 
ATOM   1346 C CG  . LYS A 1 170 ? 201.944 211.393 210.388 1.00 30.00 ? 170 LYS A CG  1 
ATOM   1347 C CD  . LYS A 1 170 ? 202.731 211.838 211.591 1.00 30.00 ? 170 LYS A CD  1 
ATOM   1348 C CE  . LYS A 1 170 ? 202.709 213.334 211.798 1.00 30.00 ? 170 LYS A CE  1 
ATOM   1349 N NZ  . LYS A 1 170 ? 203.568 213.725 212.938 1.00 30.00 ? 170 LYS A NZ  1 
ATOM   1350 N N   . SER A 1 171 ? 199.077 209.030 210.411 1.00 30.00 ? 171 SER A N   1 
ATOM   1351 C CA  . SER A 1 171 ? 199.086 207.558 210.562 1.00 30.00 ? 171 SER A CA  1 
ATOM   1352 C C   . SER A 1 171 ? 198.253 206.922 209.456 1.00 30.00 ? 171 SER A C   1 
ATOM   1353 O O   . SER A 1 171 ? 198.718 205.938 208.866 1.00 30.00 ? 171 SER A O   1 
ATOM   1354 C CB  . SER A 1 171 ? 198.514 207.229 211.879 1.00 30.00 ? 171 SER A CB  1 
ATOM   1355 O OG  . SER A 1 171 ? 199.219 207.891 212.910 1.00 30.00 ? 171 SER A OG  1 
ATOM   1356 N N   . LEU A 1 172 ? 197.103 207.511 209.146 1.00 30.00 ? 172 LEU A N   1 
ATOM   1357 C CA  . LEU A 1 172 ? 196.148 206.961 208.154 1.00 30.00 ? 172 LEU A CA  1 
ATOM   1358 C C   . LEU A 1 172 ? 196.852 206.756 206.811 1.00 30.00 ? 172 LEU A C   1 
ATOM   1359 O O   . LEU A 1 172 ? 196.679 205.672 206.224 1.00 30.00 ? 172 LEU A O   1 
ATOM   1360 C CB  . LEU A 1 172 ? 195.033 208.003 208.074 1.00 30.00 ? 172 LEU A CB  1 
ATOM   1361 C CG  . LEU A 1 172 ? 193.835 207.701 207.191 1.00 30.00 ? 172 LEU A CG  1 
ATOM   1362 C CD1 . LEU A 1 172 ? 192.877 206.765 207.891 1.00 30.00 ? 172 LEU A CD1 1 
ATOM   1363 C CD2 . LEU A 1 172 ? 193.132 208.992 206.829 1.00 30.00 ? 172 LEU A CD2 1 
ATOM   1364 N N   . ARG A 1 173 ? 197.634 207.737 206.356 1.00 30.00 ? 173 ARG A N   1 
ATOM   1365 C CA  . ARG A 1 173 ? 198.395 207.638 205.082 1.00 30.00 ? 173 ARG A CA  1 
ATOM   1366 C C   . ARG A 1 173 ? 199.513 206.607 205.212 1.00 30.00 ? 173 ARG A C   1 
ATOM   1367 O O   . ARG A 1 173 ? 199.737 205.865 204.238 1.00 30.00 ? 173 ARG A O   1 
ATOM   1368 C CB  . ARG A 1 173 ? 199.029 208.982 204.720 1.00 30.00 ? 173 ARG A CB  1 
ATOM   1369 C CG  . ARG A 1 173 ? 200.015 209.545 205.728 1.00 30.00 ? 173 ARG A CG  1 
ATOM   1370 C CD  . ARG A 1 173 ? 200.620 210.852 205.264 1.00 30.00 ? 173 ARG A CD  1 
ATOM   1371 N NE  . ARG A 1 173 ? 201.353 210.732 204.013 1.00 30.00 ? 173 ARG A NE  1 
ATOM   1372 C CZ  . ARG A 1 173 ? 201.973 211.732 203.397 1.00 30.00 ? 173 ARG A CZ  1 
ATOM   1373 N NH1 . ARG A 1 173 ? 202.112 212.900 203.991 1.00 30.00 ? 173 ARG A NH1 1 
ATOM   1374 N NH2 . ARG A 1 173 ? 202.474 211.557 202.189 1.00 30.00 ? 173 ARG A NH2 1 
ATOM   1375 N N   . ALA A 1 174 ? 200.188 206.564 206.358 1.00 30.00 ? 174 ALA A N   1 
ATOM   1376 C CA  . ALA A 1 174 ? 201.349 205.679 206.597 1.00 30.00 ? 174 ALA A CA  1 
ATOM   1377 C C   . ALA A 1 174 ? 200.914 204.223 206.736 1.00 30.00 ? 174 ALA A C   1 
ATOM   1378 O O   . ALA A 1 174 ? 201.754 203.333 206.496 1.00 30.00 ? 174 ALA A O   1 
ATOM   1379 C CB  . ALA A 1 174 ? 202.009 206.151 207.840 1.00 30.00 ? 174 ALA A CB  1 
ATOM   1380 N N   . GLU A 1 175 ? 199.668 203.990 207.137 1.00 30.00 ? 175 GLU A N   1 
ATOM   1381 C CA  . GLU A 1 175 ? 199.111 202.620 207.237 1.00 30.00 ? 175 GLU A CA  1 
ATOM   1382 C C   . GLU A 1 175 ? 198.838 202.139 205.817 1.00 30.00 ? 175 GLU A C   1 
ATOM   1383 O O   . GLU A 1 175 ? 198.530 200.943 205.652 1.00 30.00 ? 175 GLU A O   1 
ATOM   1384 C CB  . GLU A 1 175 ? 197.830 202.631 208.058 1.00 30.00 ? 175 GLU A CB  1 
ATOM   1385 C CG  . GLU A 1 175 ? 198.064 202.847 209.537 1.00 30.00 ? 175 GLU A CG  1 
ATOM   1386 C CD  . GLU A 1 175 ? 196.859 202.519 210.397 1.00 30.00 ? 175 GLU A CD  1 
ATOM   1387 O OE1 . GLU A 1 175 ? 195.787 203.073 210.122 1.00 30.00 ? 175 GLU A OE1 1 
ATOM   1388 O OE2 . GLU A 1 175 ? 197.007 201.743 211.359 1.00 30.00 ? 175 GLU A OE2 1 
ATOM   1389 N N   . GLN A 1 176 ? 198.925 203.044 204.842 1.00 30.00 ? 176 GLN A N   1 
ATOM   1390 C CA  . GLN A 1 176 ? 198.699 202.712 203.414 1.00 30.00 ? 176 GLN A CA  1 
ATOM   1391 C C   . GLN A 1 176 ? 197.250 202.250 203.295 1.00 30.00 ? 176 GLN A C   1 
ATOM   1392 O O   . GLN A 1 176 ? 196.995 201.294 202.542 1.00 30.00 ? 176 GLN A O   1 
ATOM   1393 C CB  . GLN A 1 176 ? 199.672 201.635 202.934 1.00 30.00 ? 176 GLN A CB  1 
ATOM   1394 C CG  . GLN A 1 176 ? 201.120 201.819 203.373 1.00 30.00 ? 176 GLN A CG  1 
ATOM   1395 C CD  . GLN A 1 176 ? 201.776 203.056 202.815 1.00 30.00 ? 176 GLN A CD  1 
ATOM   1396 O OE1 . GLN A 1 176 ? 201.895 203.225 201.606 1.00 30.00 ? 176 GLN A OE1 1 
ATOM   1397 N NE2 . GLN A 1 176 ? 202.240 203.919 203.699 1.00 30.00 ? 176 GLN A NE2 1 
ATOM   1398 N N   . THR A 1 177 ? 196.332 202.910 203.999 1.00 30.00 ? 177 THR A N   1 
ATOM   1399 C CA  . THR A 1 177 ? 194.903 202.512 204.030 1.00 30.00 ? 177 THR A CA  1 
ATOM   1400 C C   . THR A 1 177 ? 194.254 202.809 202.677 1.00 30.00 ? 177 THR A C   1 
ATOM   1401 O O   . THR A 1 177 ? 194.839 203.601 201.913 1.00 30.00 ? 177 THR A O   1 
ATOM   1402 C CB  . THR A 1 177 ? 194.177 203.239 205.162 1.00 30.00 ? 177 THR A CB  1 
ATOM   1403 O OG1 . THR A 1 177 ? 192.951 202.548 205.394 1.00 30.00 ? 177 THR A OG1 1 
ATOM   1404 C CG2 . THR A 1 177 ? 193.905 204.697 204.860 1.00 30.00 ? 177 THR A CG2 1 
ATOM   1405 N N   . ASP A 1 178 ? 193.093 202.213 202.400 1.00 30.00 ? 178 ASP A N   1 
ATOM   1406 C CA  . ASP A 1 178 ? 192.387 202.388 201.104 1.00 30.00 ? 178 ASP A CA  1 
ATOM   1407 C C   . ASP A 1 178 ? 191.485 203.615 201.189 1.00 30.00 ? 178 ASP A C   1 
ATOM   1408 O O   . ASP A 1 178 ? 191.346 204.149 202.298 1.00 30.00 ? 178 ASP A O   1 
ATOM   1409 C CB  . ASP A 1 178 ? 191.582 201.144 200.749 1.00 30.00 ? 178 ASP A CB  1 
ATOM   1410 C CG  . ASP A 1 178 ? 192.435 199.895 200.659 1.00 30.00 ? 178 ASP A CG  1 
ATOM   1411 O OD1 . ASP A 1 178 ? 193.368 199.888 199.837 1.00 30.00 ? 178 ASP A OD1 1 
ATOM   1412 O OD2 . ASP A 1 178 ? 192.156 198.945 201.408 1.00 30.00 ? 178 ASP A OD2 1 
ATOM   1413 N N   . PRO A 1 179 ? 190.858 204.070 200.082 1.00 30.00 ? 179 PRO A N   1 
ATOM   1414 C CA  . PRO A 1 179 ? 190.088 205.323 200.091 1.00 30.00 ? 179 PRO A CA  1 
ATOM   1415 C C   . PRO A 1 179 ? 188.725 205.304 200.798 1.00 30.00 ? 179 PRO A C   1 
ATOM   1416 O O   . PRO A 1 179 ? 188.433 206.244 201.504 1.00 30.00 ? 179 PRO A O   1 
ATOM   1417 C CB  . PRO A 1 179 ? 189.798 205.553 198.604 1.00 30.00 ? 179 PRO A CB  1 
ATOM   1418 C CG  . PRO A 1 179 ? 190.790 204.695 197.872 1.00 30.00 ? 179 PRO A CG  1 
ATOM   1419 C CD  . PRO A 1 179 ? 190.904 203.475 198.750 1.00 30.00 ? 179 PRO A CD  1 
ATOM   1420 N N   . ALA A 1 180 ? 187.900 204.282 200.567 1.00 30.00 ? 180 ALA A N   1 
ATOM   1421 C CA  . ALA A 1 180 ? 186.549 204.187 201.163 1.00 30.00 ? 180 ALA A CA  1 
ATOM   1422 C C   . ALA A 1 180 ? 186.681 204.122 202.680 1.00 30.00 ? 180 ALA A C   1 
ATOM   1423 O O   . ALA A 1 180 ? 185.938 204.844 203.377 1.00 30.00 ? 180 ALA A O   1 
ATOM   1424 C CB  . ALA A 1 180 ? 185.871 202.959 200.653 1.00 30.00 ? 180 ALA A CB  1 
ATOM   1425 N N   . VAL A 1 181 ? 187.608 203.301 203.166 1.00 30.00 ? 181 VAL A N   1 
ATOM   1426 C CA  . VAL A 1 181 ? 187.880 203.177 204.622 1.00 30.00 ? 181 VAL A CA  1 
ATOM   1427 C C   . VAL A 1 181 ? 188.344 204.543 205.100 1.00 30.00 ? 181 VAL A C   1 
ATOM   1428 O O   . VAL A 1 181 ? 187.952 204.946 206.205 1.00 30.00 ? 181 VAL A O   1 
ATOM   1429 C CB  . VAL A 1 181 ? 188.965 202.127 204.882 1.00 30.00 ? 181 VAL A CB  1 
ATOM   1430 C CG1 . VAL A 1 181 ? 189.459 202.163 206.315 1.00 30.00 ? 181 VAL A CG1 1 
ATOM   1431 C CG2 . VAL A 1 181 ? 188.498 200.734 204.510 1.00 30.00 ? 181 VAL A CG2 1 
ATOM   1432 N N   . LYS A 1 182 ? 189.137 205.224 204.277 1.00 30.00 ? 182 LYS A N   1 
ATOM   1433 C CA  . LYS A 1 182 ? 189.705 206.538 204.653 1.00 30.00 ? 182 LYS A CA  1 
ATOM   1434 C C   . LYS A 1 182 ? 188.552 207.474 205.010 1.00 30.00 ? 182 LYS A C   1 
ATOM   1435 O O   . LYS A 1 182 ? 188.627 208.091 206.079 1.00 30.00 ? 182 LYS A O   1 
ATOM   1436 C CB  . LYS A 1 182 ? 190.525 207.101 203.498 1.00 30.00 ? 182 LYS A CB  1 
ATOM   1437 C CG  . LYS A 1 182 ? 191.524 208.178 203.871 1.00 30.00 ? 182 LYS A CG  1 
ATOM   1438 C CD  . LYS A 1 182 ? 192.257 208.745 202.679 1.00 30.00 ? 182 LYS A CD  1 
ATOM   1439 C CE  . LYS A 1 182 ? 193.196 209.878 203.037 1.00 30.00 ? 182 LYS A CE  1 
ATOM   1440 N NZ  . LYS A 1 182 ? 192.460 211.063 203.535 1.00 30.00 ? 182 LYS A NZ  1 
ATOM   1441 N N   . ASN A 1 183 ? 187.500 207.516 204.193 1.00 30.00 ? 183 ASN A N   1 
ATOM   1442 C CA  . ASN A 1 183 ? 186.345 208.424 204.412 1.00 30.00 ? 183 ASN A CA  1 
ATOM   1443 C C   . ASN A 1 183 ? 185.560 208.032 205.661 1.00 30.00 ? 183 ASN A C   1 
ATOM   1444 O O   . ASN A 1 183 ? 185.196 208.932 206.429 1.00 30.00 ? 183 ASN A O   1 
ATOM   1445 C CB  . ASN A 1 183 ? 185.382 208.389 203.233 1.00 30.00 ? 183 ASN A CB  1 
ATOM   1446 C CG  . ASN A 1 183 ? 186.057 208.742 201.928 1.00 30.00 ? 183 ASN A CG  1 
ATOM   1447 O OD1 . ASN A 1 183 ? 186.100 207.929 201.009 1.00 30.00 ? 183 ASN A OD1 1 
ATOM   1448 N ND2 . ASN A 1 183 ? 186.603 209.943 201.846 1.00 30.00 ? 183 ASN A ND2 1 
ATOM   1449 N N   . TRP A 1 184 ? 185.288 206.742 205.846 1.00 30.00 ? 184 TRP A N   1 
ATOM   1450 C CA  . TRP A 1 184 ? 184.518 206.254 207.016 1.00 30.00 ? 184 TRP A CA  1 
ATOM   1451 C C   . TRP A 1 184 ? 185.285 206.591 208.286 1.00 30.00 ? 184 TRP A C   1 
ATOM   1452 O O   . TRP A 1 184 ? 184.684 207.170 209.205 1.00 30.00 ? 184 TRP A O   1 
ATOM   1453 C CB  . TRP A 1 184 ? 184.347 204.748 206.930 1.00 30.00 ? 184 TRP A CB  1 
ATOM   1454 C CG  . TRP A 1 184 ? 183.836 204.160 208.202 1.00 30.00 ? 184 TRP A CG  1 
ATOM   1455 C CD1 . TRP A 1 184 ? 182.558 204.162 208.672 1.00 30.00 ? 184 TRP A CD1 1 
ATOM   1456 C CD2 . TRP A 1 184 ? 184.646 203.618 209.249 1.00 30.00 ? 184 TRP A CD2 1 
ATOM   1457 N NE1 . TRP A 1 184 ? 182.509 203.580 209.909 1.00 30.00 ? 184 TRP A NE1 1 
ATOM   1458 C CE2 . TRP A 1 184 ? 183.779 203.247 210.293 1.00 30.00 ? 184 TRP A CE2 1 
ATOM   1459 C CE3 . TRP A 1 184 ? 186.013 203.387 209.388 1.00 30.00 ? 184 TRP A CE3 1 
ATOM   1460 C CZ2 . TRP A 1 184 ? 184.242 202.658 211.464 1.00 30.00 ? 184 TRP A CZ2 1 
ATOM   1461 C CZ3 . TRP A 1 184 ? 186.470 202.804 210.544 1.00 30.00 ? 184 TRP A CZ3 1 
ATOM   1462 C CH2 . TRP A 1 184 ? 185.595 202.441 211.564 1.00 30.00 ? 184 TRP A CH2 1 
ATOM   1463 N N   . MET A 1 185 ? 186.575 206.269 208.307 1.00 30.00 ? 185 MET A N   1 
ATOM   1464 C CA  . MET A 1 185 ? 187.455 206.558 209.461 1.00 30.00 ? 185 MET A CA  1 
ATOM   1465 C C   . MET A 1 185 ? 187.450 208.064 209.660 1.00 30.00 ? 185 MET A C   1 
ATOM   1466 O O   . MET A 1 185 ? 187.350 208.515 210.816 1.00 30.00 ? 185 MET A O   1 
ATOM   1467 C CB  . MET A 1 185 ? 188.881 206.137 209.122 1.00 30.00 ? 185 MET A CB  1 
ATOM   1468 C CG  . MET A 1 185 ? 189.258 204.772 209.613 1.00 30.00 ? 185 MET A CG  1 
ATOM   1469 S SD  . MET A 1 185 ? 190.922 204.349 209.089 1.00 30.00 ? 185 MET A SD  1 
ATOM   1470 C CE  . MET A 1 185 ? 190.884 202.574 209.301 1.00 30.00 ? 185 MET A CE  1 
ATOM   1471 N N   . THR A 1 186 ? 187.513 208.801 208.558 1.00 30.00 ? 186 THR A N   1 
ATOM   1472 C CA  . THR A 1 186 ? 187.588 210.277 208.588 1.00 30.00 ? 186 THR A CA  1 
ATOM   1473 C C   . THR A 1 186 ? 186.319 210.884 209.161 1.00 30.00 ? 186 THR A C   1 
ATOM   1474 O O   . THR A 1 186 ? 186.459 211.868 209.894 1.00 30.00 ? 186 THR A O   1 
ATOM   1475 C CB  . THR A 1 186 ? 187.798 210.848 207.186 1.00 30.00 ? 186 THR A CB  1 
ATOM   1476 O OG1 . THR A 1 186 ? 189.159 210.633 206.823 1.00 30.00 ? 186 THR A OG1 1 
ATOM   1477 C CG2 . THR A 1 186 ? 187.501 212.327 207.084 1.00 30.00 ? 186 THR A CG2 1 
ATOM   1478 N N   . GLN A 1 187 ? 185.142 210.349 208.848 1.00 30.00 ? 187 GLN A N   1 
ATOM   1479 C CA  . GLN A 1 187 ? 183.854 210.960 209.262 1.00 30.00 ? 187 GLN A CA  1 
ATOM   1480 C C   . GLN A 1 187 ? 183.336 210.354 210.561 1.00 30.00 ? 187 GLN A C   1 
ATOM   1481 O O   . GLN A 1 187 ? 182.323 210.875 211.069 1.00 30.00 ? 187 GLN A O   1 
ATOM   1482 C CB  . GLN A 1 187 ? 182.809 210.686 208.186 1.00 30.00 ? 187 GLN A CB  1 
ATOM   1483 C CG  . GLN A 1 187 ? 183.140 211.264 206.818 1.00 30.00 ? 187 GLN A CG  1 
ATOM   1484 C CD  . GLN A 1 187 ? 182.846 212.739 206.707 1.00 30.00 ? 187 GLN A CD  1 
ATOM   1485 O OE1 . GLN A 1 187 ? 181.998 213.158 205.923 1.00 30.00 ? 187 GLN A OE1 1 
ATOM   1486 N NE2 . GLN A 1 187 ? 183.543 213.543 207.493 1.00 30.00 ? 187 GLN A NE2 1 
ATOM   1487 N N   . THR A 1 188 ? 183.986 209.317 211.088 1.00 30.00 ? 188 THR A N   1 
ATOM   1488 C CA  . THR A 1 188 ? 183.463 208.580 212.264 1.00 30.00 ? 188 THR A CA  1 
ATOM   1489 C C   . THR A 1 188 ? 184.488 208.381 213.373 1.00 30.00 ? 188 THR A C   1 
ATOM   1490 O O   . THR A 1 188 ? 184.198 208.824 214.483 1.00 30.00 ? 188 THR A O   1 
ATOM   1491 C CB  . THR A 1 188 ? 183.029 207.189 211.819 1.00 30.00 ? 188 THR A CB  1 
ATOM   1492 O OG1 . THR A 1 188 ? 182.108 207.366 210.744 1.00 30.00 ? 188 THR A OG1 1 
ATOM   1493 C CG2 . THR A 1 188 ? 182.401 206.374 212.926 1.00 30.00 ? 188 THR A CG2 1 
ATOM   1494 N N   . LEU A 1 189 ? 185.592 207.688 213.097 1.00 30.00 ? 189 LEU A N   1 
ATOM   1495 C CA  . LEU A 1 189 ? 186.601 207.342 214.130 1.00 30.00 ? 189 LEU A CA  1 
ATOM   1496 C C   . LEU A 1 189 ? 187.258 208.618 214.651 1.00 30.00 ? 189 LEU A C   1 
ATOM   1497 O O   . LEU A 1 189 ? 187.761 208.592 215.776 1.00 30.00 ? 189 LEU A O   1 
ATOM   1498 C CB  . LEU A 1 189 ? 187.627 206.403 213.499 1.00 30.00 ? 189 LEU A CB  1 
ATOM   1499 C CG  . LEU A 1 189 ? 188.670 205.828 214.448 1.00 30.00 ? 189 LEU A CG  1 
ATOM   1500 C CD1 . LEU A 1 189 ? 188.070 204.735 215.309 1.00 30.00 ? 189 LEU A CD1 1 
ATOM   1501 C CD2 . LEU A 1 189 ? 189.849 205.300 213.668 1.00 30.00 ? 189 LEU A CD2 1 
ATOM   1502 N N   . LEU A 1 190 ? 187.308 209.674 213.844 1.00 30.00 ? 190 LEU A N   1 
ATOM   1503 C CA  . LEU A 1 190 ? 187.849 210.978 214.300 1.00 30.00 ? 190 LEU A CA  1 
ATOM   1504 C C   . LEU A 1 190 ? 187.020 211.479 215.480 1.00 30.00 ? 190 LEU A C   1 
ATOM   1505 O O   . LEU A 1 190 ? 187.584 212.085 216.402 1.00 30.00 ? 190 LEU A O   1 
ATOM   1506 C CB  . LEU A 1 190 ? 187.758 211.980 213.158 1.00 30.00 ? 190 LEU A CB  1 
ATOM   1507 C CG  . LEU A 1 190 ? 188.175 213.407 213.490 1.00 30.00 ? 190 LEU A CG  1 
ATOM   1508 C CD1 . LEU A 1 190 ? 189.637 213.462 213.882 1.00 30.00 ? 190 LEU A CD1 1 
ATOM   1509 C CD2 . LEU A 1 190 ? 187.917 214.317 212.304 1.00 30.00 ? 190 LEU A CD2 1 
ATOM   1510 N N   . ILE A 1 191 ? 185.706 211.312 215.421 1.00 30.00 ? 191 ILE A N   1 
ATOM   1511 C CA  . ILE A 1 191 ? 184.810 211.833 216.494 1.00 30.00 ? 191 ILE A CA  1 
ATOM   1512 C C   . ILE A 1 191 ? 184.797 210.840 217.656 1.00 30.00 ? 191 ILE A C   1 
ATOM   1513 O O   . ILE A 1 191 ? 184.757 211.296 218.814 1.00 30.00 ? 191 ILE A O   1 
ATOM   1514 C CB  . ILE A 1 191 ? 183.405 212.054 215.913 1.00 30.00 ? 191 ILE A CB  1 
ATOM   1515 C CG1 . ILE A 1 191 ? 183.442 213.015 214.725 1.00 30.00 ? 191 ILE A CG1 1 
ATOM   1516 C CG2 . ILE A 1 191 ? 182.437 212.523 216.989 1.00 30.00 ? 191 ILE A CG2 1 
ATOM   1517 C CD1 . ILE A 1 191 ? 182.159 213.074 213.944 1.00 30.00 ? 191 ILE A CD1 1 
ATOM   1518 N N   . GLN A 1 192 ? 184.846 209.540 217.365 1.00 30.00 ? 192 GLN A N   1 
ATOM   1519 C CA  . GLN A 1 192 ? 184.764 208.476 218.397 1.00 30.00 ? 192 GLN A CA  1 
ATOM   1520 C C   . GLN A 1 192 ? 185.955 208.568 219.351 1.00 30.00 ? 192 GLN A C   1 
ATOM   1521 O O   . GLN A 1 192 ? 185.711 208.622 220.569 1.00 30.00 ? 192 GLN A O   1 
ATOM   1522 C CB  . GLN A 1 192 ? 184.720 207.124 217.693 1.00 30.00 ? 192 GLN A CB  1 
ATOM   1523 C CG  . GLN A 1 192 ? 184.772 205.913 218.613 1.00 30.00 ? 192 GLN A CG  1 
ATOM   1524 C CD  . GLN A 1 192 ? 183.533 205.759 219.458 1.00 30.00 ? 192 GLN A CD  1 
ATOM   1525 O OE1 . GLN A 1 192 ? 183.198 206.615 220.271 1.00 30.00 ? 192 GLN A OE1 1 
ATOM   1526 N NE2 . GLN A 1 192 ? 182.847 204.642 219.282 1.00 30.00 ? 192 GLN A NE2 1 
ATOM   1527 N N   . ASN A 1 193 ? 187.184 208.595 218.837 1.00 30.00 ? 193 ASN A N   1 
ATOM   1528 C CA  . ASN A 1 193 ? 188.403 208.615 219.684 1.00 30.00 ? 193 ASN A CA  1 
ATOM   1529 C C   . ASN A 1 193 ? 188.721 210.066 220.030 1.00 30.00 ? 193 ASN A C   1 
ATOM   1530 O O   . ASN A 1 193 ? 189.730 210.582 219.518 1.00 30.00 ? 193 ASN A O   1 
ATOM   1531 C CB  . ASN A 1 193 ? 189.568 207.942 218.970 1.00 30.00 ? 193 ASN A CB  1 
ATOM   1532 C CG  . ASN A 1 193 ? 189.328 206.477 218.686 1.00 30.00 ? 193 ASN A CG  1 
ATOM   1533 O OD1 . ASN A 1 193 ? 188.289 205.932 219.047 1.00 30.00 ? 193 ASN A OD1 1 
ATOM   1534 N ND2 . ASN A 1 193 ? 190.289 205.834 218.047 1.00 30.00 ? 193 ASN A ND2 1 
ATOM   1535 N N   . ALA A 1 194 ? 187.896 210.704 220.857 1.00 30.00 ? 194 ALA A N   1 
ATOM   1536 C CA  . ALA A 1 194 ? 188.050 212.140 221.168 1.00 30.00 ? 194 ALA A CA  1 
ATOM   1537 C C   . ALA A 1 194 ? 187.572 212.465 222.580 1.00 30.00 ? 194 ALA A C   1 
ATOM   1538 O O   . ALA A 1 194 ? 186.920 211.598 223.194 1.00 30.00 ? 194 ALA A O   1 
ATOM   1539 C CB  . ALA A 1 194 ? 187.252 212.909 220.165 1.00 30.00 ? 194 ALA A CB  1 
ATOM   1540 N N   . ASN A 1 195 ? 187.869 213.671 223.068 1.00 30.00 ? 195 ASN A N   1 
ATOM   1541 C CA  . ASN A 1 195 ? 187.362 214.129 224.383 1.00 30.00 ? 195 ASN A CA  1 
ATOM   1542 C C   . ASN A 1 195 ? 185.865 214.387 224.240 1.00 30.00 ? 195 ASN A C   1 
ATOM   1543 O O   . ASN A 1 195 ? 185.464 214.937 223.198 1.00 30.00 ? 195 ASN A O   1 
ATOM   1544 C CB  . ASN A 1 195 ? 188.016 215.416 224.873 1.00 30.00 ? 195 ASN A CB  1 
ATOM   1545 C CG  . ASN A 1 195 ? 189.388 215.228 225.476 1.00 30.00 ? 195 ASN A CG  1 
ATOM   1546 O OD1 . ASN A 1 195 ? 189.888 214.112 225.577 1.00 30.00 ? 195 ASN A OD1 1 
ATOM   1547 N ND2 . ASN A 1 195 ? 189.988 216.326 225.904 1.00 30.00 ? 195 ASN A ND2 1 
ATOM   1548 N N   . PRO A 1 196 ? 185.029 214.045 225.239 1.00 30.00 ? 196 PRO A N   1 
ATOM   1549 C CA  . PRO A 1 196 ? 183.582 214.193 225.106 1.00 30.00 ? 196 PRO A CA  1 
ATOM   1550 C C   . PRO A 1 196 ? 183.135 215.650 224.944 1.00 30.00 ? 196 PRO A C   1 
ATOM   1551 O O   . PRO A 1 196 ? 182.272 215.884 224.138 1.00 30.00 ? 196 PRO A O   1 
ATOM   1552 C CB  . PRO A 1 196 ? 183.039 213.662 226.436 1.00 30.00 ? 196 PRO A CB  1 
ATOM   1553 C CG  . PRO A 1 196 ? 184.161 212.833 227.009 1.00 30.00 ? 196 PRO A CG  1 
ATOM   1554 C CD  . PRO A 1 196 ? 185.419 213.531 226.549 1.00 30.00 ? 196 PRO A CD  1 
ATOM   1555 N N   . ASP A 1 197 ? 183.737 216.586 225.679 1.00 30.00 ? 197 ASP A N   1 
ATOM   1556 C CA  . ASP A 1 197 ? 183.315 218.011 225.650 1.00 30.00 ? 197 ASP A CA  1 
ATOM   1557 C C   . ASP A 1 197 ? 183.431 218.527 224.217 1.00 30.00 ? 197 ASP A C   1 
ATOM   1558 O O   . ASP A 1 197 ? 182.478 219.184 223.757 1.00 30.00 ? 197 ASP A O   1 
ATOM   1559 C CB  . ASP A 1 197 ? 184.151 218.860 226.608 1.00 30.00 ? 197 ASP A CB  1 
ATOM   1560 C CG  . ASP A 1 197 ? 185.624 218.938 226.255 1.00 30.00 ? 197 ASP A CG  1 
ATOM   1561 O OD1 . ASP A 1 197 ? 186.268 217.878 226.217 1.00 30.00 ? 197 ASP A OD1 1 
ATOM   1562 O OD2 . ASP A 1 197 ? 186.109 220.061 226.027 1.00 30.00 ? 197 ASP A OD2 1 
ATOM   1563 N N   . CYS A 1 198 ? 184.536 218.232 223.532 1.00 30.00 ? 198 CYS A N   1 
ATOM   1564 C CA  . CYS A 1 198 ? 184.750 218.633 222.118 1.00 30.00 ? 198 CYS A CA  1 
ATOM   1565 C C   . CYS A 1 198 ? 183.825 217.806 221.225 1.00 30.00 ? 198 CYS A C   1 
ATOM   1566 O O   . CYS A 1 198 ? 183.317 218.364 220.239 1.00 30.00 ? 198 CYS A O   1 
ATOM   1567 C CB  . CYS A 1 198 ? 186.200 218.420 221.715 1.00 30.00 ? 198 CYS A CB  1 
ATOM   1568 S SG  . CYS A 1 198 ? 186.520 218.864 219.991 1.00 30.00 ? 198 CYS A SG  1 
ATOM   1569 N N   . LYS A 1 199 ? 183.601 216.537 221.567 1.00 30.00 ? 199 LYS A N   1 
ATOM   1570 C CA  . LYS A 1 199 ? 182.742 215.616 220.780 1.00 30.00 ? 199 LYS A CA  1 
ATOM   1571 C C   . LYS A 1 199 ? 181.340 216.206 220.667 1.00 30.00 ? 199 LYS A C   1 
ATOM   1572 O O   . LYS A 1 199 ? 180.788 216.192 219.555 1.00 30.00 ? 199 LYS A O   1 
ATOM   1573 C CB  . LYS A 1 199 ? 182.661 214.273 221.503 1.00 30.00 ? 199 LYS A CB  1 
ATOM   1574 C CG  . LYS A 1 199 ? 182.143 213.100 220.691 1.00 30.00 ? 199 LYS A CG  1 
ATOM   1575 C CD  . LYS A 1 199 ? 182.454 211.790 221.369 1.00 30.00 ? 199 LYS A CD  1 
ATOM   1576 C CE  . LYS A 1 199 ? 182.025 210.578 220.575 1.00 30.00 ? 199 LYS A CE  1 
ATOM   1577 N NZ  . LYS A 1 199 ? 182.478 209.327 221.224 1.00 30.00 ? 199 LYS A NZ  1 
ATOM   1578 N N   . LEU A 1 200 ? 180.808 216.743 221.765 1.00 30.00 ? 200 LEU A N   1 
ATOM   1579 C CA  . LEU A 1 200 ? 179.438 217.312 221.794 1.00 30.00 ? 200 LEU A CA  1 
ATOM   1580 C C   . LEU A 1 200 ? 179.373 218.475 220.809 1.00 30.00 ? 200 LEU A C   1 
ATOM   1581 O O   . LEU A 1 200 ? 178.329 218.612 220.157 1.00 30.00 ? 200 LEU A O   1 
ATOM   1582 C CB  . LEU A 1 200 ? 179.133 217.808 223.209 1.00 30.00 ? 200 LEU A CB  1 
ATOM   1583 C CG  . LEU A 1 200 ? 179.245 216.789 224.342 1.00 30.00 ? 200 LEU A CG  1 
ATOM   1584 C CD1 . LEU A 1 200 ? 178.415 217.225 225.534 1.00 30.00 ? 200 LEU A CD1 1 
ATOM   1585 C CD2 . LEU A 1 200 ? 178.847 215.392 223.895 1.00 30.00 ? 200 LEU A CD2 1 
ATOM   1586 N N   . VAL A 1 201 ? 180.424 219.292 220.740 1.00 30.00 ? 201 VAL A N   1 
ATOM   1587 C CA  . VAL A 1 201 ? 180.487 220.488 219.849 1.00 30.00 ? 201 VAL A CA  1 
ATOM   1588 C C   . VAL A 1 201 ? 180.632 220.059 218.386 1.00 30.00 ? 201 VAL A C   1 
ATOM   1589 O O   . VAL A 1 201 ? 179.983 220.692 217.530 1.00 30.00 ? 201 VAL A O   1 
ATOM   1590 C CB  . VAL A 1 201 ? 181.650 221.387 220.295 1.00 30.00 ? 201 VAL A CB  1 
ATOM   1591 C CG1 . VAL A 1 201 ? 181.863 222.562 219.356 1.00 30.00 ? 201 VAL A CG1 1 
ATOM   1592 C CG2 . VAL A 1 201 ? 181.466 221.871 221.720 1.00 30.00 ? 201 VAL A CG2 1 
ATOM   1593 N N   . LEU A 1 202 ? 181.451 219.043 218.100 1.00 30.00 ? 202 LEU A N   1 
ATOM   1594 C CA  . LEU A 1 202 ? 181.632 218.509 216.723 1.00 30.00 ? 202 LEU A CA  1 
ATOM   1595 C C   . LEU A 1 202 ? 180.293 217.943 216.264 1.00 30.00 ? 202 LEU A C   1 
ATOM   1596 O O   . LEU A 1 202 ? 180.015 217.996 215.050 1.00 30.00 ? 202 LEU A O   1 
ATOM   1597 C CB  . LEU A 1 202 ? 182.686 217.401 216.738 1.00 30.00 ? 202 LEU A CB  1 
ATOM   1598 C CG  . LEU A 1 202 ? 184.122 217.830 217.018 1.00 30.00 ? 202 LEU A CG  1 
ATOM   1599 C CD1 . LEU A 1 202 ? 185.029 216.613 217.089 1.00 30.00 ? 202 LEU A CD1 1 
ATOM   1600 C CD2 . LEU A 1 202 ? 184.622 218.799 215.958 1.00 30.00 ? 202 LEU A CD2 1 
ATOM   1601 N N   . LYS A 1 203 ? 179.509 217.411 217.200 1.00 30.00 ? 203 LYS A N   1 
ATOM   1602 C CA  . LYS A 1 203 ? 178.201 216.784 216.893 1.00 30.00 ? 203 LYS A CA  1 
ATOM   1603 C C   . LYS A 1 203 ? 177.138 217.875 216.758 1.00 30.00 ? 203 LYS A C   1 
ATOM   1604 O O   . LYS A 1 203 ? 176.150 217.629 216.040 1.00 30.00 ? 203 LYS A O   1 
ATOM   1605 C CB  . LYS A 1 203 ? 177.907 215.780 218.004 1.00 30.00 ? 203 LYS A CB  1 
ATOM   1606 C CG  . LYS A 1 203 ? 178.733 214.506 217.909 1.00 30.00 ? 203 LYS A CG  1 
ATOM   1607 C CD  . LYS A 1 203 ? 178.477 213.532 219.023 1.00 30.00 ? 203 LYS A CD  1 
ATOM   1608 C CE  . LYS A 1 203 ? 179.155 212.201 218.787 1.00 30.00 ? 203 LYS A CE  1 
ATOM   1609 N NZ  . LYS A 1 203 ? 178.723 211.195 219.782 1.00 30.00 ? 203 LYS A NZ  1 
ATOM   1610 N N   . GLY A 1 204 ? 177.320 219.027 217.405 1.00 30.00 ? 204 GLY A N   1 
ATOM   1611 C CA  . GLY A 1 204 ? 176.410 220.185 217.299 1.00 30.00 ? 204 GLY A CA  1 
ATOM   1612 C C   . GLY A 1 204 ? 176.402 220.753 215.891 1.00 30.00 ? 204 GLY A C   1 
ATOM   1613 O O   . GLY A 1 204 ? 175.399 221.398 215.531 1.00 30.00 ? 204 GLY A O   1 
ATOM   1614 N N   . LEU A 1 205 ? 177.468 220.529 215.116 1.00 30.00 ? 205 LEU A N   1 
ATOM   1615 C CA  . LEU A 1 205 ? 177.599 221.059 213.731 1.00 30.00 ? 205 LEU A CA  1 
ATOM   1616 C C   . LEU A 1 205 ? 176.486 220.493 212.849 1.00 30.00 ? 205 LEU A C   1 
ATOM   1617 O O   . LEU A 1 205 ? 175.967 221.259 212.014 1.00 30.00 ? 205 LEU A O   1 
ATOM   1618 C CB  . LEU A 1 205 ? 178.973 220.662 213.182 1.00 30.00 ? 205 LEU A CB  1 
ATOM   1619 C CG  . LEU A 1 205 ? 180.172 221.126 214.007 1.00 30.00 ? 205 LEU A CG  1 
ATOM   1620 C CD1 . LEU A 1 205 ? 181.461 220.978 213.217 1.00 30.00 ? 205 LEU A CD1 1 
ATOM   1621 C CD2 . LEU A 1 205 ? 179.993 222.559 214.475 1.00 30.00 ? 205 LEU A CD2 1 
ATOM   1622 N N   . GLY A 1 206 ? 176.133 219.217 213.024 1.00 30.00 ? 206 GLY A N   1 
ATOM   1623 C CA  . GLY A 1 206 ? 175.103 218.548 212.207 1.00 30.00 ? 206 GLY A CA  1 
ATOM   1624 C C   . GLY A 1 206 ? 175.577 217.177 211.764 1.00 30.00 ? 206 GLY A C   1 
ATOM   1625 O O   . GLY A 1 206 ? 176.110 216.452 212.628 1.00 30.00 ? 206 GLY A O   1 
ATOM   1626 N N   . MET A 1 207 ? 175.407 216.820 210.485 1.00 30.00 ? 207 MET A N   1 
ATOM   1627 C CA  . MET A 1 207 ? 175.798 215.491 209.951 1.00 30.00 ? 207 MET A CA  1 
ATOM   1628 C C   . MET A 1 207 ? 176.869 215.669 208.877 1.00 30.00 ? 207 MET A C   1 
ATOM   1629 O O   . MET A 1 207 ? 176.850 216.716 208.219 1.00 30.00 ? 207 MET A O   1 
ATOM   1630 C CB  . MET A 1 207 ? 174.591 214.795 209.329 1.00 30.00 ? 207 MET A CB  1 
ATOM   1631 C CG  . MET A 1 207 ? 173.589 214.309 210.353 1.00 30.00 ? 207 MET A CG  1 
ATOM   1632 S SD  . MET A 1 207 ? 174.310 213.184 211.569 1.00 30.00 ? 207 MET A SD  1 
ATOM   1633 C CE  . MET A 1 207 ? 172.860 212.240 212.036 1.00 30.00 ? 207 MET A CE  1 
ATOM   1634 N N   . ASN A 1 208 ? 177.772 214.700 208.728 1.00 30.00 ? 208 ASN A N   1 
ATOM   1635 C CA  . ASN A 1 208 ? 178.876 214.751 207.731 1.00 30.00 ? 208 ASN A CA  1 
ATOM   1636 C C   . ASN A 1 208 ? 179.514 216.143 207.749 1.00 30.00 ? 208 ASN A C   1 
ATOM   1637 O O   . ASN A 1 208 ? 179.558 216.782 206.690 1.00 30.00 ? 208 ASN A O   1 
ATOM   1638 C CB  . ASN A 1 208 ? 178.394 214.295 206.350 1.00 30.00 ? 208 ASN A CB  1 
ATOM   1639 C CG  . ASN A 1 208 ? 177.146 215.002 205.868 1.00 30.00 ? 208 ASN A CG  1 
ATOM   1640 O OD1 . ASN A 1 208 ? 177.162 216.201 205.603 1.00 30.00 ? 208 ASN A OD1 1 
ATOM   1641 N ND2 . ASN A 1 208 ? 176.069 214.252 205.706 1.00 30.00 ? 208 ASN A ND2 1 
ATOM   1642 N N   . PRO A 1 209 ? 180.038 216.633 208.893 1.00 30.00 ? 209 PRO A N   1 
ATOM   1643 C CA  . PRO A 1 209 ? 180.723 217.913 208.907 1.00 30.00 ? 209 PRO A CA  1 
ATOM   1644 C C   . PRO A 1 209 ? 181.924 217.884 207.952 1.00 30.00 ? 209 PRO A C   1 
ATOM   1645 O O   . PRO A 1 209 ? 182.234 216.810 207.494 1.00 30.00 ? 209 PRO A O   1 
ATOM   1646 C CB  . PRO A 1 209 ? 181.196 218.053 210.354 1.00 30.00 ? 209 PRO A CB  1 
ATOM   1647 C CG  . PRO A 1 209 ? 180.266 217.176 211.138 1.00 30.00 ? 209 PRO A CG  1 
ATOM   1648 C CD  . PRO A 1 209 ? 180.029 216.003 210.217 1.00 30.00 ? 209 PRO A CD  1 
ATOM   1649 N N   . THR A 1 210 ? 182.579 219.018 207.689 1.00 30.00 ? 210 THR A N   1 
ATOM   1650 C CA  . THR A 1 210 ? 183.793 219.096 206.839 1.00 30.00 ? 210 THR A CA  1 
ATOM   1651 C C   . THR A 1 210 ? 184.950 219.428 207.777 1.00 30.00 ? 210 THR A C   1 
ATOM   1652 O O   . THR A 1 210 ? 184.667 220.049 208.809 1.00 30.00 ? 210 THR A O   1 
ATOM   1653 C CB  . THR A 1 210 ? 183.597 220.099 205.707 1.00 30.00 ? 210 THR A CB  1 
ATOM   1654 O OG1 . THR A 1 210 ? 184.812 220.111 204.961 1.00 30.00 ? 210 THR A OG1 1 
ATOM   1655 C CG2 . THR A 1 210 ? 183.280 221.498 206.181 1.00 30.00 ? 210 THR A CG2 1 
ATOM   1656 N N   . LEU A 1 211 ? 186.190 219.036 207.473 1.00 30.00 ? 211 LEU A N   1 
ATOM   1657 C CA  . LEU A 1 211 ? 187.311 219.214 208.434 1.00 30.00 ? 211 LEU A CA  1 
ATOM   1658 C C   . LEU A 1 211 ? 187.448 220.706 208.706 1.00 30.00 ? 211 LEU A C   1 
ATOM   1659 O O   . LEU A 1 211 ? 187.849 221.045 209.819 1.00 30.00 ? 211 LEU A O   1 
ATOM   1660 C CB  . LEU A 1 211 ? 188.608 218.599 207.911 1.00 30.00 ? 211 LEU A CB  1 
ATOM   1661 C CG  . LEU A 1 211 ? 189.835 218.799 208.795 1.00 30.00 ? 211 LEU A CG  1 
ATOM   1662 C CD1 . LEU A 1 211 ? 189.684 218.070 210.114 1.00 30.00 ? 211 LEU A CD1 1 
ATOM   1663 C CD2 . LEU A 1 211 ? 191.089 218.328 208.083 1.00 30.00 ? 211 LEU A CD2 1 
ATOM   1664 N N   . GLU A 1 212 ? 187.076 221.568 207.768 1.00 30.00 ? 212 GLU A N   1 
ATOM   1665 C CA  . GLU A 1 212 ? 187.102 223.018 208.051 1.00 30.00 ? 212 GLU A CA  1 
ATOM   1666 C C   . GLU A 1 212 ? 186.168 223.291 209.220 1.00 30.00 ? 212 GLU A C   1 
ATOM   1667 O O   . GLU A 1 212 ? 186.631 223.881 210.206 1.00 30.00 ? 212 GLU A O   1 
ATOM   1668 C CB  . GLU A 1 212 ? 186.606 223.816 206.859 1.00 30.00 ? 212 GLU A CB  1 
ATOM   1669 C CG  . GLU A 1 212 ? 186.597 225.313 207.098 1.00 30.00 ? 212 GLU A CG  1 
ATOM   1670 C CD  . GLU A 1 212 ? 185.791 226.109 206.089 1.00 30.00 ? 212 GLU A CD  1 
ATOM   1671 O OE1 . GLU A 1 212 ? 185.196 225.492 205.186 1.00 30.00 ? 212 GLU A OE1 1 
ATOM   1672 O OE2 . GLU A 1 212 ? 185.776 227.349 206.197 1.00 30.00 ? 212 GLU A OE2 1 
ATOM   1673 N N   . GLU A 1 213 ? 184.933 222.799 209.161 1.00 30.00 ? 213 GLU A N   1 
ATOM   1674 C CA  . GLU A 1 213 ? 183.913 223.093 210.194 1.00 30.00 ? 213 GLU A CA  1 
ATOM   1675 C C   . GLU A 1 213 ? 184.327 222.433 211.493 1.00 30.00 ? 213 GLU A C   1 
ATOM   1676 O O   . GLU A 1 213 ? 184.276 223.088 212.526 1.00 30.00 ? 213 GLU A O   1 
ATOM   1677 C CB  . GLU A 1 213 ? 182.549 222.595 209.746 1.00 30.00 ? 213 GLU A CB  1 
ATOM   1678 C CG  . GLU A 1 213 ? 181.946 223.456 208.658 1.00 30.00 ? 213 GLU A CG  1 
ATOM   1679 C CD  . GLU A 1 213 ? 180.588 223.000 208.154 1.00 30.00 ? 213 GLU A CD  1 
ATOM   1680 O OE1 . GLU A 1 213 ? 180.085 221.976 208.650 1.00 30.00 ? 213 GLU A OE1 1 
ATOM   1681 O OE2 . GLU A 1 213 ? 180.036 223.675 207.266 1.00 30.00 ? 213 GLU A OE2 1 
ATOM   1682 N N   . MET A 1 214 ? 184.773 221.198 211.428 1.00 30.00 ? 214 MET A N   1 
ATOM   1683 C CA  . MET A 1 214 ? 185.104 220.474 212.667 1.00 30.00 ? 214 MET A CA  1 
ATOM   1684 C C   . MET A 1 214 ? 186.211 221.264 213.348 1.00 30.00 ? 214 MET A C   1 
ATOM   1685 O O   . MET A 1 214 ? 186.088 221.514 214.550 1.00 30.00 ? 214 MET A O   1 
ATOM   1686 C CB  . MET A 1 214 ? 185.586 219.060 212.365 1.00 30.00 ? 214 MET A CB  1 
ATOM   1687 C CG  . MET A 1 214 ? 184.497 218.165 211.849 1.00 30.00 ? 214 MET A CG  1 
ATOM   1688 S SD  . MET A 1 214 ? 185.100 216.493 211.591 1.00 30.00 ? 214 MET A SD  1 
ATOM   1689 C CE  . MET A 1 214 ? 184.793 215.811 213.218 1.00 30.00 ? 214 MET A CE  1 
ATOM   1690 N N   . LEU A 1 215 ? 187.208 221.712 212.596 1.00 30.00 ? 215 LEU A N   1 
ATOM   1691 C CA  . LEU A 1 215 ? 188.388 222.389 213.187 1.00 30.00 ? 215 LEU A CA  1 
ATOM   1692 C C   . LEU A 1 215 ? 187.986 223.743 213.754 1.00 30.00 ? 215 LEU A C   1 
ATOM   1693 O O   . LEU A 1 215 ? 188.400 224.033 214.881 1.00 30.00 ? 215 LEU A O   1 
ATOM   1694 C CB  . LEU A 1 215 ? 189.470 222.546 212.122 1.00 30.00 ? 215 LEU A CB  1 
ATOM   1695 C CG  . LEU A 1 215 ? 190.305 221.301 211.839 1.00 30.00 ? 215 LEU A CG  1 
ATOM   1696 C CD1 . LEU A 1 215 ? 191.285 221.558 210.712 1.00 30.00 ? 215 LEU A CD1 1 
ATOM   1697 C CD2 . LEU A 1 215 ? 191.051 220.862 213.085 1.00 30.00 ? 215 LEU A CD2 1 
ATOM   1698 N N   . THR A 1 216 ? 187.205 224.537 213.031 1.00 30.00 ? 216 THR A N   1 
ATOM   1699 C CA  . THR A 1 216 ? 186.860 225.903 213.500 1.00 30.00 ? 216 THR A CA  1 
ATOM   1700 C C   . THR A 1 216 ? 185.990 225.783 214.748 1.00 30.00 ? 216 THR A C   1 
ATOM   1701 O O   . THR A 1 216 ? 186.247 226.516 215.709 1.00 30.00 ? 216 THR A O   1 
ATOM   1702 C CB  . THR A 1 216 ? 186.165 226.734 212.417 1.00 30.00 ? 216 THR A CB  1 
ATOM   1703 O OG1 . THR A 1 216 ? 185.951 228.035 212.959 1.00 30.00 ? 216 THR A OG1 1 
ATOM   1704 C CG2 . THR A 1 216 ? 184.842 226.167 211.954 1.00 30.00 ? 216 THR A CG2 1 
ATOM   1705 N N   . ALA A 1 217 ? 185.015 224.884 214.737 1.00 30.00 ? 217 ALA A N   1 
ATOM   1706 C CA  . ALA A 1 217 ? 184.054 224.730 215.841 1.00 30.00 ? 217 ALA A CA  1 
ATOM   1707 C C   . ALA A 1 217 ? 184.787 224.435 217.136 1.00 30.00 ? 217 ALA A C   1 
ATOM   1708 O O   . ALA A 1 217 ? 184.623 225.212 218.078 1.00 30.00 ? 217 ALA A O   1 
ATOM   1709 C CB  . ALA A 1 217 ? 183.118 223.614 215.519 1.00 30.00 ? 217 ALA A CB  1 
ATOM   1710 N N   . CYS A 1 218 ? 185.573 223.370 217.176 1.00 30.00 ? 218 CYS A N   1 
ATOM   1711 C CA  . CYS A 1 218 ? 186.222 222.948 218.437 1.00 30.00 ? 218 CYS A CA  1 
ATOM   1712 C C   . CYS A 1 218 ? 187.478 223.789 218.615 1.00 30.00 ? 218 CYS A C   1 
ATOM   1713 O O   . CYS A 1 218 ? 188.553 223.209 218.790 1.00 30.00 ? 218 CYS A O   1 
ATOM   1714 C CB  . CYS A 1 218 ? 186.517 221.456 218.428 1.00 30.00 ? 218 CYS A CB  1 
ATOM   1715 S SG  . CYS A 1 218 ? 187.033 220.824 220.045 1.00 30.00 ? 218 CYS A SG  1 
ATOM   1716 N N   . GLN A 1 219 ? 187.330 225.108 218.606 1.00 30.00 ? 219 GLN A N   1 
ATOM   1717 C CA  . GLN A 1 219 ? 188.451 226.042 218.852 1.00 30.00 ? 219 GLN A CA  1 
ATOM   1718 C C   . GLN A 1 219 ? 188.314 226.505 220.301 1.00 30.00 ? 219 GLN A C   1 
ATOM   1719 O O   . GLN A 1 219 ? 187.457 227.367 220.552 1.00 30.00 ? 219 GLN A O   1 
ATOM   1720 C CB  . GLN A 1 219 ? 188.368 227.202 217.862 1.00 30.00 ? 219 GLN A CB  1 
ATOM   1721 C CG  . GLN A 1 219 ? 189.291 228.367 218.182 1.00 30.00 ? 219 GLN A CG  1 
ATOM   1722 C CD  . GLN A 1 219 ? 190.733 227.942 218.276 1.00 30.00 ? 219 GLN A CD  1 
ATOM   1723 O OE1 . GLN A 1 219 ? 191.369 228.069 219.318 1.00 30.00 ? 219 GLN A OE1 1 
ATOM   1724 N NE2 . GLN A 1 219 ? 191.257 227.420 217.180 1.00 30.00 ? 219 GLN A NE2 1 
ATOM   1725 N N   . GLY A 1 220 ? 189.093 225.936 221.222 1.00 30.00 ? 220 GLY A N   1 
ATOM   1726 C CA  . GLY A 1 220 ? 189.054 226.313 222.648 1.00 30.00 ? 220 GLY A CA  1 
ATOM   1727 C C   . GLY A 1 220 ? 188.210 225.364 223.482 1.00 30.00 ? 220 GLY A C   1 
ATOM   1728 O O   . GLY A 1 220 ? 188.159 225.568 224.707 1.00 30.00 ? 220 GLY A O   1 
ATOM   1729 N N   . VAL A 1 221 ? 187.594 224.351 222.868 1.00 30.00 ? 221 VAL A N   1 
ATOM   1730 C CA  . VAL A 1 221 ? 186.750 223.352 223.586 1.00 30.00 ? 221 VAL A CA  1 
ATOM   1731 C C   . VAL A 1 221 ? 187.616 222.126 223.879 1.00 30.00 ? 221 VAL A C   1 
ATOM   1732 O O   . VAL A 1 221 ? 188.395 221.756 222.983 1.00 30.00 ? 221 VAL A O   1 
ATOM   1733 C CB  . VAL A 1 221 ? 185.505 222.969 222.767 1.00 30.00 ? 221 VAL A CB  1 
ATOM   1734 C CG1 . VAL A 1 221 ? 184.677 221.903 223.464 1.00 30.00 ? 221 VAL A CG1 1 
ATOM   1735 C CG2 . VAL A 1 221 ? 184.651 224.180 222.439 1.00 30.00 ? 221 VAL A CG2 1 
ATOM   1736 N N   . THR B 1 148 ? 176.214 257.696 219.591 1.00 30.00 ? 148 THR B N   1 
ATOM   1737 C CA  . THR B 1 148 ? 177.367 256.796 219.866 1.00 30.00 ? 148 THR B CA  1 
ATOM   1738 C C   . THR B 1 148 ? 177.980 256.341 218.538 1.00 30.00 ? 148 THR B C   1 
ATOM   1739 O O   . THR B 1 148 ? 177.622 256.939 217.504 1.00 30.00 ? 148 THR B O   1 
ATOM   1740 C CB  . THR B 1 148 ? 176.948 255.581 220.700 1.00 30.00 ? 148 THR B CB  1 
ATOM   1741 O OG1 . THR B 1 148 ? 176.001 254.840 219.931 1.00 30.00 ? 148 THR B OG1 1 
ATOM   1742 C CG2 . THR B 1 148 ? 176.351 255.951 222.039 1.00 30.00 ? 148 THR B CG2 1 
ATOM   1743 N N   . ASN B 1 149 ? 178.864 255.336 218.559 1.00 30.00 ? 149 ASN B N   1 
ATOM   1744 C CA  . ASN B 1 149 ? 179.520 254.807 217.334 1.00 30.00 ? 149 ASN B CA  1 
ATOM   1745 C C   . ASN B 1 149 ? 179.445 253.282 217.295 1.00 30.00 ? 149 ASN B C   1 
ATOM   1746 O O   . ASN B 1 149 ? 179.488 252.696 218.379 1.00 30.00 ? 149 ASN B O   1 
ATOM   1747 C CB  . ASN B 1 149 ? 180.970 255.260 217.232 1.00 30.00 ? 149 ASN B CB  1 
ATOM   1748 C CG  . ASN B 1 149 ? 181.099 256.760 217.090 1.00 30.00 ? 149 ASN B CG  1 
ATOM   1749 O OD1 . ASN B 1 149 ? 181.699 257.418 217.936 1.00 30.00 ? 149 ASN B OD1 1 
ATOM   1750 N ND2 . ASN B 1 149 ? 180.532 257.308 216.029 1.00 30.00 ? 149 ASN B ND2 1 
ATOM   1751 N N   . ILE B 1 150 ? 179.540 252.669 216.117 1.00 30.00 ? 150 ILE B N   1 
ATOM   1752 C CA  . ILE B 1 150 ? 179.340 251.202 215.927 1.00 30.00 ? 150 ILE B CA  1 
ATOM   1753 C C   . ILE B 1 150 ? 180.449 250.346 216.554 1.00 30.00 ? 150 ILE B C   1 
ATOM   1754 O O   . ILE B 1 150 ? 180.166 249.172 216.857 1.00 30.00 ? 150 ILE B O   1 
ATOM   1755 C CB  . ILE B 1 150 ? 179.258 250.958 214.413 1.00 30.00 ? 150 ILE B CB  1 
ATOM   1756 C CG1 . ILE B 1 150 ? 178.403 249.743 214.066 1.00 30.00 ? 150 ILE B CG1 1 
ATOM   1757 C CG2 . ILE B 1 150 ? 180.641 250.872 213.792 1.00 30.00 ? 150 ILE B CG2 1 
ATOM   1758 C CD1 . ILE B 1 150 ? 176.937 250.038 214.120 1.00 30.00 ? 150 ILE B CD1 1 
ATOM   1759 N N   . LEU B 1 151 ? 181.663 250.875 216.718 1.00 30.00 ? 151 LEU B N   1 
ATOM   1760 C CA  . LEU B 1 151 ? 182.799 250.109 217.299 1.00 30.00 ? 151 LEU B CA  1 
ATOM   1761 C C   . LEU B 1 151 ? 182.737 250.266 218.818 1.00 30.00 ? 151 LEU B C   1 
ATOM   1762 O O   . LEU B 1 151 ? 183.619 249.705 219.498 1.00 30.00 ? 151 LEU B O   1 
ATOM   1763 C CB  . LEU B 1 151 ? 184.129 250.617 216.730 1.00 30.00 ? 151 LEU B CB  1 
ATOM   1764 C CG  . LEU B 1 151 ? 184.363 250.399 215.239 1.00 30.00 ? 151 LEU B CG  1 
ATOM   1765 C CD1 . LEU B 1 151 ? 185.835 250.561 214.913 1.00 30.00 ? 151 LEU B CD1 1 
ATOM   1766 C CD2 . LEU B 1 151 ? 183.874 249.033 214.802 1.00 30.00 ? 151 LEU B CD2 1 
ATOM   1767 N N   . ASP B 1 152 ? 181.737 250.992 219.325 1.00 30.00 ? 152 ASP B N   1 
ATOM   1768 C CA  . ASP B 1 152 ? 181.532 251.203 220.780 1.00 30.00 ? 152 ASP B CA  1 
ATOM   1769 C C   . ASP B 1 152 ? 180.199 250.607 221.226 1.00 30.00 ? 152 ASP B C   1 
ATOM   1770 O O   . ASP B 1 152 ? 180.071 250.323 222.431 1.00 30.00 ? 152 ASP B O   1 
ATOM   1771 C CB  . ASP B 1 152 ? 181.502 252.686 221.116 1.00 30.00 ? 152 ASP B CB  1 
ATOM   1772 C CG  . ASP B 1 152 ? 182.831 253.387 220.919 1.00 30.00 ? 152 ASP B CG  1 
ATOM   1773 O OD1 . ASP B 1 152 ? 183.802 252.983 221.583 1.00 30.00 ? 152 ASP B OD1 1 
ATOM   1774 O OD2 . ASP B 1 152 ? 182.877 254.334 220.114 1.00 30.00 ? 152 ASP B OD2 1 
ATOM   1775 N N   . VAL B 1 153 ? 179.227 250.472 220.320 1.00 30.00 ? 153 VAL B N   1 
ATOM   1776 C CA  . VAL B 1 153 ? 177.879 249.919 220.647 1.00 30.00 ? 153 VAL B CA  1 
ATOM   1777 C C   . VAL B 1 153 ? 178.120 248.489 221.118 1.00 30.00 ? 153 VAL B C   1 
ATOM   1778 O O   . VAL B 1 153 ? 178.852 247.761 220.420 1.00 30.00 ? 153 VAL B O   1 
ATOM   1779 C CB  . VAL B 1 153 ? 176.861 249.947 219.490 1.00 30.00 ? 153 VAL B CB  1 
ATOM   1780 C CG1 . VAL B 1 153 ? 176.610 251.350 218.978 1.00 30.00 ? 153 VAL B CG1 1 
ATOM   1781 C CG2 . VAL B 1 153 ? 177.236 249.035 218.339 1.00 30.00 ? 153 VAL B CG2 1 
ATOM   1782 N N   . LYS B 1 154 ? 177.587 248.121 222.283 1.00 30.00 ? 154 LYS B N   1 
ATOM   1783 C CA  . LYS B 1 154 ? 177.779 246.765 222.855 1.00 30.00 ? 154 LYS B CA  1 
ATOM   1784 C C   . LYS B 1 154 ? 176.516 246.354 223.608 1.00 30.00 ? 154 LYS B C   1 
ATOM   1785 O O   . LYS B 1 154 ? 176.014 247.175 224.399 1.00 30.00 ? 154 LYS B O   1 
ATOM   1786 C CB  . LYS B 1 154 ? 179.004 246.763 223.771 1.00 30.00 ? 154 LYS B CB  1 
ATOM   1787 C CG  . LYS B 1 154 ? 180.326 247.020 223.064 1.00 30.00 ? 154 LYS B CG  1 
ATOM   1788 C CD  . LYS B 1 154 ? 181.509 247.134 223.980 1.00 30.00 ? 154 LYS B CD  1 
ATOM   1789 C CE  . LYS B 1 154 ? 182.766 247.512 223.229 1.00 30.00 ? 154 LYS B CE  1 
ATOM   1790 N NZ  . LYS B 1 154 ? 183.927 247.631 224.138 1.00 30.00 ? 154 LYS B NZ  1 
ATOM   1791 N N   . GLN B 1 155 ? 176.035 245.131 223.388 1.00 30.00 ? 155 GLN B N   1 
ATOM   1792 C CA  . GLN B 1 155 ? 174.839 244.606 224.093 1.00 30.00 ? 155 GLN B CA  1 
ATOM   1793 C C   . GLN B 1 155 ? 175.107 244.665 225.597 1.00 30.00 ? 155 GLN B C   1 
ATOM   1794 O O   . GLN B 1 155 ? 176.224 244.289 226.004 1.00 30.00 ? 155 GLN B O   1 
ATOM   1795 C CB  . GLN B 1 155 ? 174.576 243.176 223.629 1.00 30.00 ? 155 GLN B CB  1 
ATOM   1796 C CG  . GLN B 1 155 ? 173.331 242.532 224.217 1.00 30.00 ? 155 GLN B CG  1 
ATOM   1797 C CD  . GLN B 1 155 ? 173.237 241.087 223.793 1.00 30.00 ? 155 GLN B CD  1 
ATOM   1798 O OE1 . GLN B 1 155 ? 174.065 240.592 223.034 1.00 30.00 ? 155 GLN B OE1 1 
ATOM   1799 N NE2 . GLN B 1 155 ? 172.224 240.391 224.276 1.00 30.00 ? 155 GLN B NE2 1 
ATOM   1800 N N   . GLY B 1 156 ? 174.129 245.106 226.389 1.00 30.00 ? 156 GLY B N   1 
ATOM   1801 C CA  . GLY B 1 156 ? 174.262 245.174 227.856 1.00 30.00 ? 156 GLY B CA  1 
ATOM   1802 C C   . GLY B 1 156 ? 174.199 243.776 228.438 1.00 30.00 ? 156 GLY B C   1 
ATOM   1803 O O   . GLY B 1 156 ? 173.683 242.897 227.743 1.00 30.00 ? 156 GLY B O   1 
ATOM   1804 N N   . PRO B 1 157 ? 174.715 243.508 229.656 1.00 30.00 ? 157 PRO B N   1 
ATOM   1805 C CA  . PRO B 1 157 ? 174.760 242.138 230.183 1.00 30.00 ? 157 PRO B CA  1 
ATOM   1806 C C   . PRO B 1 157 ? 173.379 241.484 230.308 1.00 30.00 ? 157 PRO B C   1 
ATOM   1807 O O   . PRO B 1 157 ? 173.279 240.314 229.989 1.00 30.00 ? 157 PRO B O   1 
ATOM   1808 C CB  . PRO B 1 157 ? 175.349 242.310 231.589 1.00 30.00 ? 157 PRO B CB  1 
ATOM   1809 C CG  . PRO B 1 157 ? 176.103 243.616 231.526 1.00 30.00 ? 157 PRO B CG  1 
ATOM   1810 C CD  . PRO B 1 157 ? 175.298 244.479 230.580 1.00 30.00 ? 157 PRO B CD  1 
ATOM   1811 N N   . LYS B 1 158 ? 172.372 242.232 230.774 1.00 30.00 ? 158 LYS B N   1 
ATOM   1812 C CA  . LYS B 1 158 ? 170.984 241.726 230.941 1.00 30.00 ? 158 LYS B CA  1 
ATOM   1813 C C   . LYS B 1 158 ? 170.117 242.374 229.863 1.00 30.00 ? 158 LYS B C   1 
ATOM   1814 O O   . LYS B 1 158 ? 168.890 242.459 230.071 1.00 30.00 ? 158 LYS B O   1 
ATOM   1815 C CB  . LYS B 1 158 ? 170.473 242.051 232.346 1.00 30.00 ? 158 LYS B CB  1 
ATOM   1816 C CG  . LYS B 1 158 ? 171.346 241.541 233.484 1.00 30.00 ? 158 LYS B CG  1 
ATOM   1817 C CD  . LYS B 1 158 ? 171.512 240.041 233.489 1.00 30.00 ? 158 LYS B CD  1 
ATOM   1818 C CE  . LYS B 1 158 ? 172.321 239.546 234.667 1.00 30.00 ? 158 LYS B CE  1 
ATOM   1819 N NZ  . LYS B 1 158 ? 172.447 238.071 234.654 1.00 30.00 ? 158 LYS B NZ  1 
ATOM   1820 N N   . GLU B 1 159 ? 170.728 242.799 228.756 1.00 30.00 ? 159 GLU B N   1 
ATOM   1821 C CA  . GLU B 1 159 ? 170.011 243.434 227.623 1.00 30.00 ? 159 GLU B CA  1 
ATOM   1822 C C   . GLU B 1 159 ? 169.896 242.405 226.504 1.00 30.00 ? 159 GLU B C   1 
ATOM   1823 O O   . GLU B 1 159 ? 170.840 241.612 226.356 1.00 30.00 ? 159 GLU B O   1 
ATOM   1824 C CB  . GLU B 1 159 ? 170.783 244.636 227.089 1.00 30.00 ? 159 GLU B CB  1 
ATOM   1825 C CG  . GLU B 1 159 ? 170.085 245.373 225.958 1.00 30.00 ? 159 GLU B CG  1 
ATOM   1826 C CD  . GLU B 1 159 ? 170.879 246.513 225.344 1.00 30.00 ? 159 GLU B CD  1 
ATOM   1827 O OE1 . GLU B 1 159 ? 172.009 246.759 225.795 1.00 30.00 ? 159 GLU B OE1 1 
ATOM   1828 O OE2 . GLU B 1 159 ? 170.365 247.150 224.412 1.00 30.00 ? 159 GLU B OE2 1 
ATOM   1829 N N   . PRO B 1 160 ? 168.798 242.368 225.725 1.00 30.00 ? 160 PRO B N   1 
ATOM   1830 C CA  . PRO B 1 160 ? 168.712 241.462 224.595 1.00 30.00 ? 160 PRO B CA  1 
ATOM   1831 C C   . PRO B 1 160 ? 169.681 241.880 223.492 1.00 30.00 ? 160 PRO B C   1 
ATOM   1832 O O   . PRO B 1 160 ? 170.057 243.035 223.464 1.00 30.00 ? 160 PRO B O   1 
ATOM   1833 C CB  . PRO B 1 160 ? 167.295 241.641 224.048 1.00 30.00 ? 160 PRO B CB  1 
ATOM   1834 C CG  . PRO B 1 160 ? 166.548 242.356 225.148 1.00 30.00 ? 160 PRO B CG  1 
ATOM   1835 C CD  . PRO B 1 160 ? 167.593 243.180 225.866 1.00 30.00 ? 160 PRO B CD  1 
ATOM   1836 N N   . PHE B 1 161 ? 170.015 240.965 222.587 1.00 30.00 ? 161 PHE B N   1 
ATOM   1837 C CA  . PHE B 1 161 ? 170.878 241.284 221.427 1.00 30.00 ? 161 PHE B CA  1 
ATOM   1838 C C   . PHE B 1 161 ? 169.951 241.911 220.385 1.00 30.00 ? 161 PHE B C   1 
ATOM   1839 O O   . PHE B 1 161 ? 170.460 242.375 219.360 1.00 30.00 ? 161 PHE B O   1 
ATOM   1840 C CB  . PHE B 1 161 ? 171.590 240.021 220.950 1.00 30.00 ? 161 PHE B CB  1 
ATOM   1841 C CG  . PHE B 1 161 ? 171.031 239.467 219.672 1.00 30.00 ? 161 PHE B CG  1 
ATOM   1842 C CD1 . PHE B 1 161 ? 169.711 239.069 219.602 1.00 30.00 ? 161 PHE B CD1 1 
ATOM   1843 C CD2 . PHE B 1 161 ? 171.813 239.390 218.533 1.00 30.00 ? 161 PHE B CD2 1 
ATOM   1844 C CE1 . PHE B 1 161 ? 169.189 238.581 218.420 1.00 30.00 ? 161 PHE B CE1 1 
ATOM   1845 C CE2 . PHE B 1 161 ? 171.288 238.900 217.351 1.00 30.00 ? 161 PHE B CE2 1 
ATOM   1846 C CZ  . PHE B 1 161 ? 169.978 238.494 217.298 1.00 30.00 ? 161 PHE B CZ  1 
ATOM   1847 N N   . GLN B 1 162 ? 168.637 241.893 220.628 1.00 30.00 ? 162 GLN B N   1 
ATOM   1848 C CA  . GLN B 1 162 ? 167.623 242.538 219.756 1.00 30.00 ? 162 GLN B CA  1 
ATOM   1849 C C   . GLN B 1 162 ? 167.657 244.038 220.016 1.00 30.00 ? 162 GLN B C   1 
ATOM   1850 O O   . GLN B 1 162 ? 167.617 244.819 219.055 1.00 30.00 ? 162 GLN B O   1 
ATOM   1851 C CB  . GLN B 1 162 ? 166.246 242.000 220.125 1.00 30.00 ? 162 GLN B CB  1 
ATOM   1852 C CG  . GLN B 1 162 ? 165.080 242.896 219.740 1.00 30.00 ? 162 GLN B CG  1 
ATOM   1853 C CD  . GLN B 1 162 ? 165.031 243.193 218.264 1.00 30.00 ? 162 GLN B CD  1 
ATOM   1854 O OE1 . GLN B 1 162 ? 164.926 242.293 217.436 1.00 30.00 ? 162 GLN B OE1 1 
ATOM   1855 N NE2 . GLN B 1 162 ? 165.102 244.468 217.926 1.00 30.00 ? 162 GLN B NE2 1 
ATOM   1856 N N   . SER B 1 163 ? 167.654 244.439 221.281 1.00 30.00 ? 163 SER B N   1 
ATOM   1857 C CA  . SER B 1 163 ? 167.799 245.869 221.640 1.00 30.00 ? 163 SER B CA  1 
ATOM   1858 C C   . SER B 1 163 ? 169.107 246.358 221.020 1.00 30.00 ? 163 SER B C   1 
ATOM   1859 O O   . SER B 1 163 ? 169.112 247.468 220.453 1.00 30.00 ? 163 SER B O   1 
ATOM   1860 C CB  . SER B 1 163 ? 167.780 246.035 223.129 1.00 30.00 ? 163 SER B CB  1 
ATOM   1861 O OG  . SER B 1 163 ? 167.842 247.406 223.487 1.00 30.00 ? 163 SER B OG  1 
ATOM   1862 N N   . TYR B 1 164 ? 170.154 245.533 221.069 1.00 30.00 ? 164 TYR B N   1 
ATOM   1863 C CA  . TYR B 1 164 ? 171.498 245.875 220.540 1.00 30.00 ? 164 TYR B CA  1 
ATOM   1864 C C   . TYR B 1 164 ? 171.485 246.099 219.025 1.00 30.00 ? 164 TYR B C   1 
ATOM   1865 O O   . TYR B 1 164 ? 172.122 247.073 218.582 1.00 30.00 ? 164 TYR B O   1 
ATOM   1866 C CB  . TYR B 1 164 ? 172.463 244.741 220.877 1.00 30.00 ? 164 TYR B CB  1 
ATOM   1867 C CG  . TYR B 1 164 ? 173.810 244.859 220.226 1.00 30.00 ? 164 TYR B CG  1 
ATOM   1868 C CD1 . TYR B 1 164 ? 174.649 245.917 220.514 1.00 30.00 ? 164 TYR B CD1 1 
ATOM   1869 C CD2 . TYR B 1 164 ? 174.225 243.932 219.289 1.00 30.00 ? 164 TYR B CD2 1 
ATOM   1870 C CE1 . TYR B 1 164 ? 175.885 246.037 219.907 1.00 30.00 ? 164 TYR B CE1 1 
ATOM   1871 C CE2 . TYR B 1 164 ? 175.457 244.038 218.671 1.00 30.00 ? 164 TYR B CE2 1 
ATOM   1872 C CZ  . TYR B 1 164 ? 176.289 245.097 218.979 1.00 30.00 ? 164 TYR B CZ  1 
ATOM   1873 O OH  . TYR B 1 164 ? 177.514 245.217 218.373 1.00 30.00 ? 164 TYR B OH  1 
ATOM   1874 N N   . VAL B 1 165 ? 170.808 245.243 218.252 1.00 30.00 ? 165 VAL B N   1 
ATOM   1875 C CA  . VAL B 1 165 ? 170.799 245.346 216.759 1.00 30.00 ? 165 VAL B CA  1 
ATOM   1876 C C   . VAL B 1 165 ? 170.115 246.661 216.377 1.00 30.00 ? 165 VAL B C   1 
ATOM   1877 O O   . VAL B 1 165 ? 170.557 247.282 215.394 1.00 30.00 ? 165 VAL B O   1 
ATOM   1878 C CB  . VAL B 1 165 ? 170.137 244.145 216.051 1.00 30.00 ? 165 VAL B CB  1 
ATOM   1879 C CG1 . VAL B 1 165 ? 170.989 242.894 216.158 1.00 30.00 ? 165 VAL B CG1 1 
ATOM   1880 C CG2 . VAL B 1 165 ? 168.726 243.860 216.514 1.00 30.00 ? 165 VAL B CG2 1 
ATOM   1881 N N   . ASP B 1 166 ? 169.085 247.070 217.120 1.00 30.00 ? 166 ASP B N   1 
ATOM   1882 C CA  . ASP B 1 166 ? 168.351 248.332 216.844 1.00 30.00 ? 166 ASP B CA  1 
ATOM   1883 C C   . ASP B 1 166 ? 169.239 249.517 217.219 1.00 30.00 ? 166 ASP B C   1 
ATOM   1884 O O   . ASP B 1 166 ? 168.989 250.611 216.688 1.00 30.00 ? 166 ASP B O   1 
ATOM   1885 C CB  . ASP B 1 166 ? 167.015 248.371 217.578 1.00 30.00 ? 166 ASP B CB  1 
ATOM   1886 C CG  . ASP B 1 166 ? 165.971 247.439 216.992 1.00 30.00 ? 166 ASP B CG  1 
ATOM   1887 O OD1 . ASP B 1 166 ? 166.290 246.748 216.003 1.00 30.00 ? 166 ASP B OD1 1 
ATOM   1888 O OD2 . ASP B 1 166 ? 164.843 247.423 217.519 1.00 30.00 ? 166 ASP B OD2 1 
ATOM   1889 N N   . ARG B 1 167 ? 170.231 249.314 218.085 1.00 30.00 ? 167 ARG B N   1 
ATOM   1890 C CA  . ARG B 1 167 ? 171.194 250.372 218.484 1.00 30.00 ? 167 ARG B CA  1 
ATOM   1891 C C   . ARG B 1 167 ? 172.432 250.277 217.594 1.00 30.00 ? 167 ARG B C   1 
ATOM   1892 O O   . ARG B 1 167 ? 173.349 251.098 217.792 1.00 30.00 ? 167 ARG B O   1 
ATOM   1893 C CB  . ARG B 1 167 ? 171.588 250.164 219.944 1.00 30.00 ? 167 ARG B CB  1 
ATOM   1894 C CG  . ARG B 1 167 ? 170.451 250.337 220.936 1.00 30.00 ? 167 ARG B CG  1 
ATOM   1895 C CD  . ARG B 1 167 ? 170.797 249.660 222.244 1.00 30.00 ? 167 ARG B CD  1 
ATOM   1896 N NE  . ARG B 1 167 ? 172.091 250.095 222.752 1.00 30.00 ? 167 ARG B NE  1 
ATOM   1897 C CZ  . ARG B 1 167 ? 173.133 249.304 222.991 1.00 30.00 ? 167 ARG B CZ  1 
ATOM   1898 N NH1 . ARG B 1 167 ? 172.998 247.990 223.047 1.00 30.00 ? 167 ARG B NH1 1 
ATOM   1899 N NH2 . ARG B 1 167 ? 174.319 249.841 223.208 1.00 30.00 ? 167 ARG B NH2 1 
ATOM   1900 N N   . PHE B 1 168 ? 172.459 249.336 216.647 1.00 30.00 ? 168 PHE B N   1 
ATOM   1901 C CA  . PHE B 1 168 ? 173.634 249.077 215.777 1.00 30.00 ? 168 PHE B CA  1 
ATOM   1902 C C   . PHE B 1 168 ? 173.337 249.489 214.336 1.00 30.00 ? 168 PHE B C   1 
ATOM   1903 O O   . PHE B 1 168 ? 174.096 250.315 213.805 1.00 30.00 ? 168 PHE B O   1 
ATOM   1904 C CB  . PHE B 1 168 ? 173.967 247.591 215.891 1.00 30.00 ? 168 PHE B CB  1 
ATOM   1905 C CG  . PHE B 1 168 ? 175.153 247.108 215.100 1.00 30.00 ? 168 PHE B CG  1 
ATOM   1906 C CD1 . PHE B 1 168 ? 175.130 247.057 213.718 1.00 30.00 ? 168 PHE B CD1 1 
ATOM   1907 C CD2 . PHE B 1 168 ? 176.314 246.736 215.752 1.00 30.00 ? 168 PHE B CD2 1 
ATOM   1908 C CE1 . PHE B 1 168 ? 176.231 246.608 213.008 1.00 30.00 ? 168 PHE B CE1 1 
ATOM   1909 C CE2 . PHE B 1 168 ? 177.416 246.294 215.043 1.00 30.00 ? 168 PHE B CE2 1 
ATOM   1910 C CZ  . PHE B 1 168 ? 177.372 246.230 213.672 1.00 30.00 ? 168 PHE B CZ  1 
ATOM   1911 N N   . TYR B 1 169 ? 172.275 248.951 213.732 1.00 30.00 ? 169 TYR B N   1 
ATOM   1912 C CA  . TYR B 1 169 ? 171.874 249.267 212.337 1.00 30.00 ? 169 TYR B CA  1 
ATOM   1913 C C   . TYR B 1 169 ? 171.501 250.747 212.267 1.00 30.00 ? 169 TYR B C   1 
ATOM   1914 O O   . TYR B 1 169 ? 171.715 251.348 211.206 1.00 30.00 ? 169 TYR B O   1 
ATOM   1915 C CB  . TYR B 1 169 ? 170.728 248.356 211.899 1.00 30.00 ? 169 TYR B CB  1 
ATOM   1916 C CG  . TYR B 1 169 ? 171.129 246.917 211.717 1.00 30.00 ? 169 TYR B CG  1 
ATOM   1917 C CD1 . TYR B 1 169 ? 172.086 246.558 210.786 1.00 30.00 ? 169 TYR B CD1 1 
ATOM   1918 C CD2 . TYR B 1 169 ? 170.569 245.918 212.488 1.00 30.00 ? 169 TYR B CD2 1 
ATOM   1919 C CE1 . TYR B 1 169 ? 172.470 245.240 210.617 1.00 30.00 ? 169 TYR B CE1 1 
ATOM   1920 C CE2 . TYR B 1 169 ? 170.941 244.595 212.333 1.00 30.00 ? 169 TYR B CE2 1 
ATOM   1921 C CZ  . TYR B 1 169 ? 171.894 244.256 211.394 1.00 30.00 ? 169 TYR B CZ  1 
ATOM   1922 O OH  . TYR B 1 169 ? 172.254 242.943 211.244 1.00 30.00 ? 169 TYR B OH  1 
ATOM   1923 N N   . LYS B 1 170 ? 170.935 251.297 213.341 1.00 30.00 ? 170 LYS B N   1 
ATOM   1924 C CA  . LYS B 1 170 ? 170.593 252.740 213.428 1.00 30.00 ? 170 LYS B CA  1 
ATOM   1925 C C   . LYS B 1 170 ? 171.880 253.556 213.346 1.00 30.00 ? 170 LYS B C   1 
ATOM   1926 O O   . LYS B 1 170 ? 171.846 254.640 212.732 1.00 30.00 ? 170 LYS B O   1 
ATOM   1927 C CB  . LYS B 1 170 ? 169.893 253.004 214.759 1.00 30.00 ? 170 LYS B CB  1 
ATOM   1928 C CG  . LYS B 1 170 ? 169.483 254.445 215.020 1.00 30.00 ? 170 LYS B CG  1 
ATOM   1929 C CD  . LYS B 1 170 ? 168.938 254.668 216.413 1.00 30.00 ? 170 LYS B CD  1 
ATOM   1930 C CE  . LYS B 1 170 ? 167.670 253.893 216.696 1.00 30.00 ? 170 LYS B CE  1 
ATOM   1931 N NZ  . LYS B 1 170 ? 167.176 254.145 218.069 1.00 30.00 ? 170 LYS B NZ  1 
ATOM   1932 N N   . SER B 1 171 ? 172.964 253.068 213.951 1.00 30.00 ? 171 SER B N   1 
ATOM   1933 C CA  . SER B 1 171 ? 174.270 253.772 213.995 1.00 30.00 ? 171 SER B CA  1 
ATOM   1934 C C   . SER B 1 171 ? 175.144 253.373 212.806 1.00 30.00 ? 171 SER B C   1 
ATOM   1935 O O   . SER B 1 171 ? 176.171 254.027 212.600 1.00 30.00 ? 171 SER B O   1 
ATOM   1936 C CB  . SER B 1 171 ? 174.957 253.445 215.274 1.00 30.00 ? 171 SER B CB  1 
ATOM   1937 O OG  . SER B 1 171 ? 174.212 253.919 216.383 1.00 30.00 ? 171 SER B OG  1 
ATOM   1938 N N   . LEU B 1 172 ? 174.727 252.377 212.028 1.00 30.00 ? 172 LEU B N   1 
ATOM   1939 C CA  . LEU B 1 172 ? 175.483 251.897 210.846 1.00 30.00 ? 172 LEU B CA  1 
ATOM   1940 C C   . LEU B 1 172 ? 175.102 252.804 209.676 1.00 30.00 ? 172 LEU B C   1 
ATOM   1941 O O   . LEU B 1 172 ? 176.021 253.342 209.021 1.00 30.00 ? 172 LEU B O   1 
ATOM   1942 C CB  . LEU B 1 172 ? 175.061 250.442 210.636 1.00 30.00 ? 172 LEU B CB  1 
ATOM   1943 C CG  . LEU B 1 172 ? 175.969 249.546 209.807 1.00 30.00 ? 172 LEU B CG  1 
ATOM   1944 C CD1 . LEU B 1 172 ? 177.279 249.292 210.525 1.00 30.00 ? 172 LEU B CD1 1 
ATOM   1945 C CD2 . LEU B 1 172 ? 175.267 248.229 209.534 1.00 30.00 ? 172 LEU B CD2 1 
ATOM   1946 N N   . ARG B 1 173 ? 173.802 253.020 209.465 1.00 30.00 ? 173 ARG B N   1 
ATOM   1947 C CA  . ARG B 1 173 ? 173.288 253.920 208.398 1.00 30.00 ? 173 ARG B CA  1 
ATOM   1948 C C   . ARG B 1 173 ? 173.729 255.357 208.668 1.00 30.00 ? 173 ARG B C   1 
ATOM   1949 O O   . ARG B 1 173 ? 174.098 256.036 207.696 1.00 30.00 ? 173 ARG B O   1 
ATOM   1950 C CB  . ARG B 1 173 ? 171.760 253.880 208.368 1.00 30.00 ? 173 ARG B CB  1 
ATOM   1951 C CG  . ARG B 1 173 ? 171.090 254.303 209.668 1.00 30.00 ? 173 ARG B CG  1 
ATOM   1952 C CD  . ARG B 1 173 ? 169.589 254.107 209.666 1.00 30.00 ? 173 ARG B CD  1 
ATOM   1953 N NE  . ARG B 1 173 ? 168.918 254.965 208.701 1.00 30.00 ? 173 ARG B NE  1 
ATOM   1954 C CZ  . ARG B 1 173 ? 167.605 255.011 208.502 1.00 30.00 ? 173 ARG B CZ  1 
ATOM   1955 N NH1 . ARG B 1 173 ? 166.779 254.292 209.242 1.00 30.00 ? 173 ARG B NH1 1 
ATOM   1956 N NH2 . ARG B 1 173 ? 167.115 255.794 207.557 1.00 30.00 ? 173 ARG B NH2 1 
ATOM   1957 N N   . ALA B 1 174 ? 173.703 255.801 209.926 1.00 30.00 ? 174 ALA B N   1 
ATOM   1958 C CA  . ALA B 1 174 ? 174.035 257.192 210.310 1.00 30.00 ? 174 ALA B CA  1 
ATOM   1959 C C   . ALA B 1 174 ? 175.486 257.501 209.955 1.00 30.00 ? 174 ALA B C   1 
ATOM   1960 O O   . ALA B 1 174 ? 175.751 258.628 209.497 1.00 30.00 ? 174 ALA B O   1 
ATOM   1961 C CB  . ALA B 1 174 ? 173.816 257.355 211.783 1.00 30.00 ? 174 ALA B CB  1 
ATOM   1962 N N   . GLU B 1 175 ? 176.382 256.526 210.126 1.00 30.00 ? 175 GLU B N   1 
ATOM   1963 C CA  . GLU B 1 175 ? 177.830 256.704 209.849 1.00 30.00 ? 175 GLU B CA  1 
ATOM   1964 C C   . GLU B 1 175 ? 178.067 256.656 208.343 1.00 30.00 ? 175 GLU B C   1 
ATOM   1965 O O   . GLU B 1 175 ? 179.225 256.853 207.927 1.00 30.00 ? 175 GLU B O   1 
ATOM   1966 C CB  . GLU B 1 175 ? 178.619 255.603 210.549 1.00 30.00 ? 175 GLU B CB  1 
ATOM   1967 C CG  . GLU B 1 175 ? 178.759 255.836 212.035 1.00 30.00 ? 175 GLU B CG  1 
ATOM   1968 C CD  . GLU B 1 175 ? 179.522 254.757 212.777 1.00 30.00 ? 175 GLU B CD  1 
ATOM   1969 O OE1 . GLU B 1 175 ? 179.937 253.773 212.136 1.00 30.00 ? 175 GLU B OE1 1 
ATOM   1970 O OE2 . GLU B 1 175 ? 179.720 254.922 213.987 1.00 30.00 ? 175 GLU B OE2 1 
ATOM   1971 N N   . GLN B 1 176 ? 177.019 256.395 207.561 1.00 30.00 ? 176 GLN B N   1 
ATOM   1972 C CA  . GLN B 1 176 ? 177.119 256.348 206.083 1.00 30.00 ? 176 GLN B CA  1 
ATOM   1973 C C   . GLN B 1 176 ? 178.189 255.319 205.730 1.00 30.00 ? 176 GLN B C   1 
ATOM   1974 O O   . GLN B 1 176 ? 178.965 255.574 204.789 1.00 30.00 ? 176 GLN B O   1 
ATOM   1975 C CB  . GLN B 1 176 ? 177.471 257.725 205.523 1.00 30.00 ? 176 GLN B CB  1 
ATOM   1976 C CG  . GLN B 1 176 ? 176.573 258.847 206.022 1.00 30.00 ? 176 GLN B CG  1 
ATOM   1977 C CD  . GLN B 1 176 ? 175.123 258.628 205.670 1.00 30.00 ? 176 GLN B CD  1 
ATOM   1978 O OE1 . GLN B 1 176 ? 174.759 258.508 204.503 1.00 30.00 ? 176 GLN B OE1 1 
ATOM   1979 N NE2 . GLN B 1 176 ? 174.281 258.570 206.687 1.00 30.00 ? 176 GLN B NE2 1 
ATOM   1980 N N   . THR B 1 177 ? 178.226 254.196 206.446 1.00 30.00 ? 177 THR B N   1 
ATOM   1981 C CA  . THR B 1 177 ? 179.239 253.134 206.221 1.00 30.00 ? 177 THR B CA  1 
ATOM   1982 C C   . THR B 1 177 ? 179.065 252.600 204.799 1.00 30.00 ? 177 THR B C   1 
ATOM   1983 O O   . THR B 1 177 ? 177.920 252.618 204.304 1.00 30.00 ? 177 THR B O   1 
ATOM   1984 C CB  . THR B 1 177 ? 179.117 252.019 207.264 1.00 30.00 ? 177 THR B CB  1 
ATOM   1985 O OG1 . THR B 1 177 ? 180.271 251.187 207.140 1.00 30.00 ? 177 THR B OG1 1 
ATOM   1986 C CG2 . THR B 1 177 ? 177.868 251.178 207.111 1.00 30.00 ? 177 THR B CG2 1 
ATOM   1987 N N   . ASP B 1 178 ? 180.147 252.140 204.172 1.00 30.00 ? 178 ASP B N   1 
ATOM   1988 C CA  . ASP B 1 178 ? 180.097 251.601 202.790 1.00 30.00 ? 178 ASP B CA  1 
ATOM   1989 C C   . ASP B 1 178 ? 179.315 250.291 202.828 1.00 30.00 ? 178 ASP B C   1 
ATOM   1990 O O   . ASP B 1 178 ? 179.151 249.759 203.925 1.00 30.00 ? 178 ASP B O   1 
ATOM   1991 C CB  . ASP B 1 178 ? 181.490 251.362 202.219 1.00 30.00 ? 178 ASP B CB  1 
ATOM   1992 C CG  . ASP B 1 178 ? 182.333 252.620 202.139 1.00 30.00 ? 178 ASP B CG  1 
ATOM   1993 O OD1 . ASP B 1 178 ? 181.908 253.564 201.447 1.00 30.00 ? 178 ASP B OD1 1 
ATOM   1994 O OD2 . ASP B 1 178 ? 183.406 252.644 202.772 1.00 30.00 ? 178 ASP B OD2 1 
ATOM   1995 N N   . PRO B 1 179 ? 178.769 249.801 201.697 1.00 30.00 ? 179 PRO B N   1 
ATOM   1996 C CA  . PRO B 1 179 ? 177.966 248.578 201.686 1.00 30.00 ? 179 PRO B CA  1 
ATOM   1997 C C   . PRO B 1 179 ? 178.757 247.321 202.069 1.00 30.00 ? 179 PRO B C   1 
ATOM   1998 O O   . PRO B 1 179 ? 178.216 246.511 202.785 1.00 30.00 ? 179 PRO B O   1 
ATOM   1999 C CB  . PRO B 1 179 ? 177.525 248.448 200.224 1.00 30.00 ? 179 PRO B CB  1 
ATOM   2000 C CG  . PRO B 1 179 ? 177.678 249.835 199.655 1.00 30.00 ? 179 PRO B CG  1 
ATOM   2001 C CD  . PRO B 1 179 ? 178.886 250.395 200.368 1.00 30.00 ? 179 PRO B CD  1 
ATOM   2002 N N   . ALA B 1 180 ? 179.984 247.166 201.564 1.00 30.00 ? 180 ALA B N   1 
ATOM   2003 C CA  . ALA B 1 180 ? 180.845 245.997 201.858 1.00 30.00 ? 180 ALA B CA  1 
ATOM   2004 C C   . ALA B 1 180 ? 181.290 246.044 203.318 1.00 30.00 ? 180 ALA B C   1 
ATOM   2005 O O   . ALA B 1 180 ? 181.329 244.976 203.954 1.00 30.00 ? 180 ALA B O   1 
ATOM   2006 C CB  . ALA B 1 180 ? 182.035 246.005 200.947 1.00 30.00 ? 180 ALA B CB  1 
ATOM   2007 N N   . VAL B 1 181 ? 181.622 247.233 203.818 1.00 30.00 ? 181 VAL B N   1 
ATOM   2008 C CA  . VAL B 1 181 ? 182.057 247.424 205.229 1.00 30.00 ? 181 VAL B CA  1 
ATOM   2009 C C   . VAL B 1 181 ? 180.854 247.101 206.108 1.00 30.00 ? 181 VAL B C   1 
ATOM   2010 O O   . VAL B 1 181 ? 181.066 246.671 207.249 1.00 30.00 ? 181 VAL B O   1 
ATOM   2011 C CB  . VAL B 1 181 ? 182.532 248.868 205.449 1.00 30.00 ? 181 VAL B CB  1 
ATOM   2012 C CG1 . VAL B 1 181 ? 182.911 249.128 206.896 1.00 30.00 ? 181 VAL B CG1 1 
ATOM   2013 C CG2 . VAL B 1 181 ? 183.678 249.236 204.524 1.00 30.00 ? 181 VAL B CG2 1 
ATOM   2014 N N   . LYS B 1 182 ? 179.647 247.339 205.602 1.00 30.00 ? 182 LYS B N   1 
ATOM   2015 C CA  . LYS B 1 182 ? 178.380 247.065 206.316 1.00 30.00 ? 182 LYS B CA  1 
ATOM   2016 C C   . LYS B 1 182 ? 178.241 245.561 206.525 1.00 30.00 ? 182 LYS B C   1 
ATOM   2017 O O   . LYS B 1 182 ? 177.965 245.164 207.661 1.00 30.00 ? 182 LYS B O   1 
ATOM   2018 C CB  . LYS B 1 182 ? 177.202 247.577 205.496 1.00 30.00 ? 182 LYS B CB  1 
ATOM   2019 C CG  . LYS B 1 182 ? 175.955 247.889 206.303 1.00 30.00 ? 182 LYS B CG  1 
ATOM   2020 C CD  . LYS B 1 182 ? 174.815 248.395 205.458 1.00 30.00 ? 182 LYS B CD  1 
ATOM   2021 C CE  . LYS B 1 182 ? 173.559 248.664 206.258 1.00 30.00 ? 182 LYS B CE  1 
ATOM   2022 N NZ  . LYS B 1 182 ? 172.998 247.418 206.829 1.00 30.00 ? 182 LYS B NZ  1 
ATOM   2023 N N   . ASN B 1 183 ? 178.491 244.759 205.492 1.00 30.00 ? 183 ASN B N   1 
ATOM   2024 C CA  . ASN B 1 183 ? 178.312 243.288 205.573 1.00 30.00 ? 183 ASN B CA  1 
ATOM   2025 C C   . ASN B 1 183 ? 179.285 242.702 206.597 1.00 30.00 ? 183 ASN B C   1 
ATOM   2026 O O   . ASN B 1 183 ? 178.850 241.874 207.404 1.00 30.00 ? 183 ASN B O   1 
ATOM   2027 C CB  . ASN B 1 183 ? 178.529 242.626 204.218 1.00 30.00 ? 183 ASN B CB  1 
ATOM   2028 C CG  . ASN B 1 183 ? 177.649 243.211 203.136 1.00 30.00 ? 183 ASN B CG  1 
ATOM   2029 O OD1 . ASN B 1 183 ? 178.144 243.761 202.156 1.00 30.00 ? 183 ASN B OD1 1 
ATOM   2030 N ND2 . ASN B 1 183 ? 176.342 243.116 203.311 1.00 30.00 ? 183 ASN B ND2 1 
ATOM   2031 N N   . TRP B 1 184 ? 180.548 243.125 206.578 1.00 30.00 ? 184 TRP B N   1 
ATOM   2032 C CA  . TRP B 1 184 ? 181.572 242.596 207.512 1.00 30.00 ? 184 TRP B CA  1 
ATOM   2033 C C   . TRP B 1 184 ? 181.176 242.932 208.946 1.00 30.00 ? 184 TRP B C   1 
ATOM   2034 O O   . TRP B 1 184 ? 181.160 242.012 209.785 1.00 30.00 ? 184 TRP B O   1 
ATOM   2035 C CB  . TRP B 1 184 ? 182.928 243.217 207.215 1.00 30.00 ? 184 TRP B CB  1 
ATOM   2036 C CG  . TRP B 1 184 ? 183.921 242.934 208.292 1.00 30.00 ? 184 TRP B CG  1 
ATOM   2037 C CD1 . TRP B 1 184 ? 184.520 241.747 208.586 1.00 30.00 ? 184 TRP B CD1 1 
ATOM   2038 C CD2 . TRP B 1 184 ? 184.304 243.840 209.331 1.00 30.00 ? 184 TRP B CD2 1 
ATOM   2039 N NE1 . TRP B 1 184 ? 185.316 241.880 209.690 1.00 30.00 ? 184 TRP B NE1 1 
ATOM   2040 C CE2 . TRP B 1 184 ? 185.195 243.152 210.175 1.00 30.00 ? 184 TRP B CE2 1 
ATOM   2041 C CE3 . TRP B 1 184 ? 184.001 245.172 209.604 1.00 30.00 ? 184 TRP B CE3 1 
ATOM   2042 C CZ2 . TRP B 1 184 ? 185.784 243.757 211.280 1.00 30.00 ? 184 TRP B CZ2 1 
ATOM   2043 C CZ3 . TRP B 1 184 ? 184.584 245.769 210.694 1.00 30.00 ? 184 TRP B CZ3 1 
ATOM   2044 C CH2 . TRP B 1 184 ? 185.466 245.072 211.515 1.00 30.00 ? 184 TRP B CH2 1 
ATOM   2045 N N   . MET B 1 185 ? 180.832 244.193 209.201 1.00 30.00 ? 185 MET B N   1 
ATOM   2046 C CA  . MET B 1 185 ? 180.412 244.656 210.544 1.00 30.00 ? 185 MET B CA  1 
ATOM   2047 C C   . MET B 1 185 ? 179.164 243.877 210.927 1.00 30.00 ? 185 MET B C   1 
ATOM   2048 O O   . MET B 1 185 ? 179.046 243.454 212.090 1.00 30.00 ? 185 MET B O   1 
ATOM   2049 C CB  . MET B 1 185 ? 180.020 246.129 210.482 1.00 30.00 ? 185 MET B CB  1 
ATOM   2050 C CG  . MET B 1 185 ? 181.144 247.091 210.686 1.00 30.00 ? 185 MET B CG  1 
ATOM   2051 S SD  . MET B 1 185 ? 180.509 248.760 210.490 1.00 30.00 ? 185 MET B SD  1 
ATOM   2052 C CE  . MET B 1 185 ? 182.037 249.685 210.394 1.00 30.00 ? 185 MET B CE  1 
ATOM   2053 N N   . THR B 1 186 ? 178.272 243.684 209.965 1.00 30.00 ? 186 THR B N   1 
ATOM   2054 C CA  . THR B 1 186 ? 176.977 243.013 210.205 1.00 30.00 ? 186 THR B CA  1 
ATOM   2055 C C   . THR B 1 186 ? 177.208 241.575 210.645 1.00 30.00 ? 186 THR B C   1 
ATOM   2056 O O   . THR B 1 186 ? 176.663 241.208 211.689 1.00 30.00 ? 186 THR B O   1 
ATOM   2057 C CB  . THR B 1 186 ? 176.113 243.038 208.937 1.00 30.00 ? 186 THR B CB  1 
ATOM   2058 O OG1 . THR B 1 186 ? 175.641 244.369 208.739 1.00 30.00 ? 186 THR B OG1 1 
ATOM   2059 C CG2 . THR B 1 186 ? 174.920 242.113 208.997 1.00 30.00 ? 186 THR B CG2 1 
ATOM   2060 N N   . GLN B 1 187 ? 178.055 240.827 209.950 1.00 30.00 ? 187 GLN B N   1 
ATOM   2061 C CA  . GLN B 1 187 ? 178.215 239.377 210.216 1.00 30.00 ? 187 GLN B CA  1 
ATOM   2062 C C   . GLN B 1 187 ? 179.223 239.123 211.332 1.00 30.00 ? 187 GLN B C   1 
ATOM   2063 O O   . GLN B 1 187 ? 179.267 237.971 211.806 1.00 30.00 ? 187 GLN B O   1 
ATOM   2064 C CB  . GLN B 1 187 ? 178.719 238.704 208.944 1.00 30.00 ? 187 GLN B CB  1 
ATOM   2065 C CG  . GLN B 1 187 ? 177.855 238.944 207.709 1.00 30.00 ? 187 GLN B CG  1 
ATOM   2066 C CD  . GLN B 1 187 ? 176.570 238.156 207.676 1.00 30.00 ? 187 GLN B CD  1 
ATOM   2067 O OE1 . GLN B 1 187 ? 176.351 237.339 206.786 1.00 30.00 ? 187 GLN B OE1 1 
ATOM   2068 N NE2 . GLN B 1 187 ? 175.693 238.407 208.633 1.00 30.00 ? 187 GLN B NE2 1 
ATOM   2069 N N   . THR B 1 188 ? 179.995 240.131 211.738 1.00 30.00 ? 188 THR B N   1 
ATOM   2070 C CA  . THR B 1 188 ? 181.087 239.937 212.724 1.00 30.00 ? 188 THR B CA  1 
ATOM   2071 C C   . THR B 1 188 ? 181.027 240.909 213.896 1.00 30.00 ? 188 THR B C   1 
ATOM   2072 O O   . THR B 1 188 ? 181.011 240.419 215.018 1.00 30.00 ? 188 THR B O   1 
ATOM   2073 C CB  . THR B 1 188 ? 182.432 240.145 212.037 1.00 30.00 ? 188 THR B CB  1 
ATOM   2074 O OG1 . THR B 1 188 ? 182.415 239.330 210.867 1.00 30.00 ? 188 THR B OG1 1 
ATOM   2075 C CG2 . THR B 1 188 ? 183.608 239.803 212.923 1.00 30.00 ? 188 THR B CG2 1 
ATOM   2076 N N   . LEU B 1 189 ? 181.025 242.218 213.646 1.00 30.00 ? 189 LEU B N   1 
ATOM   2077 C CA  . LEU B 1 189 ? 181.097 243.239 214.724 1.00 30.00 ? 189 LEU B CA  1 
ATOM   2078 C C   . LEU B 1 189 ? 179.870 243.126 215.636 1.00 30.00 ? 189 LEU B C   1 
ATOM   2079 O O   . LEU B 1 189 ? 179.989 243.539 216.795 1.00 30.00 ? 189 LEU B O   1 
ATOM   2080 C CB  . LEU B 1 189 ? 181.225 244.615 214.068 1.00 30.00 ? 189 LEU B CB  1 
ATOM   2081 C CG  . LEU B 1 189 ? 181.387 245.796 215.017 1.00 30.00 ? 189 LEU B CG  1 
ATOM   2082 C CD1 . LEU B 1 189 ? 182.755 245.778 215.672 1.00 30.00 ? 189 LEU B CD1 1 
ATOM   2083 C CD2 . LEU B 1 189 ? 181.172 247.097 214.273 1.00 30.00 ? 189 LEU B CD2 1 
ATOM   2084 N N   . LEU B 1 190 ? 178.727 242.648 215.140 1.00 30.00 ? 190 LEU B N   1 
ATOM   2085 C CA  . LEU B 1 190 ? 177.538 242.388 215.997 1.00 30.00 ? 190 LEU B CA  1 
ATOM   2086 C C   . LEU B 1 190 ? 177.904 241.359 217.063 1.00 30.00 ? 190 LEU B C   1 
ATOM   2087 O O   . LEU B 1 190 ? 177.753 241.675 218.257 1.00 30.00 ? 190 LEU B O   1 
ATOM   2088 C CB  . LEU B 1 190 ? 176.412 241.798 215.146 1.00 30.00 ? 190 LEU B CB  1 
ATOM   2089 C CG  . LEU B 1 190 ? 175.525 242.780 214.389 1.00 30.00 ? 190 LEU B CG  1 
ATOM   2090 C CD1 . LEU B 1 190 ? 174.424 242.039 213.657 1.00 30.00 ? 190 LEU B CD1 1 
ATOM   2091 C CD2 . LEU B 1 190 ? 174.902 243.790 215.334 1.00 30.00 ? 190 LEU B CD2 1 
ATOM   2092 N N   . ILE B 1 191 ? 178.387 240.190 216.649 1.00 30.00 ? 191 ILE B N   1 
ATOM   2093 C CA  . ILE B 1 191 ? 178.699 239.037 217.540 1.00 30.00 ? 191 ILE B CA  1 
ATOM   2094 C C   . ILE B 1 191 ? 179.816 239.416 218.514 1.00 30.00 ? 191 ILE B C   1 
ATOM   2095 O O   . ILE B 1 191 ? 179.696 239.068 219.703 1.00 30.00 ? 191 ILE B O   1 
ATOM   2096 C CB  . ILE B 1 191 ? 179.086 237.831 216.666 1.00 30.00 ? 191 ILE B CB  1 
ATOM   2097 C CG1 . ILE B 1 191 ? 178.019 237.535 215.608 1.00 30.00 ? 191 ILE B CG1 1 
ATOM   2098 C CG2 . ILE B 1 191 ? 179.381 236.617 217.533 1.00 30.00 ? 191 ILE B CG2 1 
ATOM   2099 C CD1 . ILE B 1 191 ? 178.406 236.461 214.627 1.00 30.00 ? 191 ILE B CD1 1 
ATOM   2100 N N   . GLN B 1 192 ? 180.860 240.096 218.039 1.00 30.00 ? 192 GLN B N   1 
ATOM   2101 C CA  . GLN B 1 192 ? 182.017 240.495 218.880 1.00 30.00 ? 192 GLN B CA  1 
ATOM   2102 C C   . GLN B 1 192 ? 181.530 241.427 219.992 1.00 30.00 ? 192 GLN B C   1 
ATOM   2103 O O   . GLN B 1 192 ? 181.795 241.118 221.166 1.00 30.00 ? 192 GLN B O   1 
ATOM   2104 C CB  . GLN B 1 192 ? 183.068 241.142 217.979 1.00 30.00 ? 192 GLN B CB  1 
ATOM   2105 C CG  . GLN B 1 192 ? 184.182 241.886 218.702 1.00 30.00 ? 192 GLN B CG  1 
ATOM   2106 C CD  . GLN B 1 192 ? 184.997 241.013 219.623 1.00 30.00 ? 192 GLN B CD  1 
ATOM   2107 O OE1 . GLN B 1 192 ? 184.512 240.521 220.637 1.00 30.00 ? 192 GLN B OE1 1 
ATOM   2108 N NE2 . GLN B 1 192 ? 186.272 240.866 219.308 1.00 30.00 ? 192 GLN B NE2 1 
ATOM   2109 N N   . ASN B 1 193 ? 180.798 242.489 219.651 1.00 30.00 ? 193 ASN B N   1 
ATOM   2110 C CA  . ASN B 1 193 ? 180.310 243.482 220.644 1.00 30.00 ? 193 ASN B CA  1 
ATOM   2111 C C   . ASN B 1 193 ? 178.941 243.032 221.158 1.00 30.00 ? 193 ASN B C   1 
ATOM   2112 O O   . ASN B 1 193 ? 177.967 243.784 220.964 1.00 30.00 ? 193 ASN B O   1 
ATOM   2113 C CB  . ASN B 1 193 ? 180.256 244.880 220.032 1.00 30.00 ? 193 ASN B CB  1 
ATOM   2114 C CG  . ASN B 1 193 ? 181.618 245.470 219.746 1.00 30.00 ? 193 ASN B CG  1 
ATOM   2115 O OD1 . ASN B 1 193 ? 182.641 244.847 220.013 1.00 30.00 ? 193 ASN B OD1 1 
ATOM   2116 N ND2 . ASN B 1 193 ? 181.638 246.680 219.213 1.00 30.00 ? 193 ASN B ND2 1 
ATOM   2117 N N   . ALA B 1 194 ? 178.862 241.855 221.781 1.00 30.00 ? 194 ALA B N   1 
ATOM   2118 C CA  . ALA B 1 194 ? 177.589 241.288 222.283 1.00 30.00 ? 194 ALA B CA  1 
ATOM   2119 C C   . ALA B 1 194 ? 177.810 240.529 223.590 1.00 30.00 ? 194 ALA B C   1 
ATOM   2120 O O   . ALA B 1 194 ? 178.983 240.325 223.962 1.00 30.00 ? 194 ALA B O   1 
ATOM   2121 C CB  . ALA B 1 194 ? 177.009 240.378 221.243 1.00 30.00 ? 194 ALA B CB  1 
ATOM   2122 N N   . ASN B 1 195 ? 176.727 240.116 224.252 1.00 30.00 ? 195 ASN B N   1 
ATOM   2123 C CA  . ASN B 1 195 ? 176.807 239.324 225.504 1.00 30.00 ? 195 ASN B CA  1 
ATOM   2124 C C   . ASN B 1 195 ? 177.446 237.973 225.193 1.00 30.00 ? 195 ASN B C   1 
ATOM   2125 O O   . ASN B 1 195 ? 177.123 237.409 224.137 1.00 30.00 ? 195 ASN B O   1 
ATOM   2126 C CB  . ASN B 1 195 ? 175.432 239.093 226.123 1.00 30.00 ? 195 ASN B CB  1 
ATOM   2127 C CG  . ASN B 1 195 ? 174.749 240.384 226.504 1.00 30.00 ? 195 ASN B CG  1 
ATOM   2128 O OD1 . ASN B 1 195 ? 175.326 241.456 226.344 1.00 30.00 ? 195 ASN B OD1 1 
ATOM   2129 N ND2 . ASN B 1 195 ? 173.533 240.283 227.014 1.00 30.00 ? 195 ASN B ND2 1 
ATOM   2130 N N   . PRO B 1 196 ? 178.304 237.417 226.072 1.00 30.00 ? 196 PRO B N   1 
ATOM   2131 C CA  . PRO B 1 196 ? 178.997 236.166 225.773 1.00 30.00 ? 196 PRO B CA  1 
ATOM   2132 C C   . PRO B 1 196 ? 178.019 235.005 225.565 1.00 30.00 ? 196 PRO B C   1 
ATOM   2133 O O   . PRO B 1 196 ? 178.226 234.240 224.654 1.00 30.00 ? 196 PRO B O   1 
ATOM   2134 C CB  . PRO B 1 196 ? 179.837 235.902 227.028 1.00 30.00 ? 196 PRO B CB  1 
ATOM   2135 C CG  . PRO B 1 196 ? 179.954 237.250 227.700 1.00 30.00 ? 196 PRO B CG  1 
ATOM   2136 C CD  . PRO B 1 196 ? 178.646 237.942 227.392 1.00 30.00 ? 196 PRO B CD  1 
ATOM   2137 N N   . ASP B 1 197 ? 176.976 234.906 226.391 1.00 30.00 ? 197 ASP B N   1 
ATOM   2138 C CA  . ASP B 1 197 ? 176.006 233.782 226.316 1.00 30.00 ? 197 ASP B CA  1 
ATOM   2139 C C   . ASP B 1 197 ? 175.318 233.771 224.950 1.00 30.00 ? 197 ASP B C   1 
ATOM   2140 O O   . ASP B 1 197 ? 175.314 232.702 224.313 1.00 30.00 ? 197 ASP B O   1 
ATOM   2141 C CB  . ASP B 1 197 ? 174.969 233.868 227.437 1.00 30.00 ? 197 ASP B CB  1 
ATOM   2142 C CG  . ASP B 1 197 ? 174.247 235.200 227.569 1.00 30.00 ? 197 ASP B CG  1 
ATOM   2143 O OD1 . ASP B 1 197 ? 174.562 236.126 226.802 1.00 30.00 ? 197 ASP B OD1 1 
ATOM   2144 O OD2 . ASP B 1 197 ? 173.366 235.296 228.445 1.00 30.00 ? 197 ASP B OD2 1 
ATOM   2145 N N   . CYS B 1 198 ? 174.808 234.914 224.491 1.00 30.00 ? 198 CYS B N   1 
ATOM   2146 C CA  . CYS B 1 198 ? 174.110 235.030 223.185 1.00 30.00 ? 198 CYS B CA  1 
ATOM   2147 C C   . CYS B 1 198 ? 175.147 234.925 222.069 1.00 30.00 ? 198 CYS B C   1 
ATOM   2148 O O   . CYS B 1 198 ? 174.807 234.390 221.007 1.00 30.00 ? 198 CYS B O   1 
ATOM   2149 C CB  . CYS B 1 198 ? 173.342 236.339 223.088 1.00 30.00 ? 198 CYS B CB  1 
ATOM   2150 S SG  . CYS B 1 198 ? 172.534 236.562 221.482 1.00 30.00 ? 198 CYS B SG  1 
ATOM   2151 N N   . LYS B 1 199 ? 176.365 235.406 222.311 1.00 30.00 ? 199 LYS B N   1 
ATOM   2152 C CA  . LYS B 1 199 ? 177.464 235.333 221.317 1.00 30.00 ? 199 LYS B CA  1 
ATOM   2153 C C   . LYS B 1 199 ? 177.700 233.859 221.002 1.00 30.00 ? 199 LYS B C   1 
ATOM   2154 O O   . LYS B 1 199 ? 177.743 233.521 219.809 1.00 30.00 ? 199 LYS B O   1 
ATOM   2155 C CB  . LYS B 1 199 ? 178.707 236.002 221.903 1.00 30.00 ? 199 LYS B CB  1 
ATOM   2156 C CG  . LYS B 1 199 ? 179.934 236.017 221.011 1.00 30.00 ? 199 LYS B CG  1 
ATOM   2157 C CD  . LYS B 1 199 ? 181.034 236.884 221.562 1.00 30.00 ? 199 LYS B CD  1 
ATOM   2158 C CE  . LYS B 1 199 ? 182.181 237.068 220.593 1.00 30.00 ? 199 LYS B CE  1 
ATOM   2159 N NZ  . LYS B 1 199 ? 183.199 237.990 221.143 1.00 30.00 ? 199 LYS B NZ  1 
ATOM   2160 N N   . LEU B 1 200 ? 177.769 233.012 222.030 1.00 30.00 ? 200 LEU B N   1 
ATOM   2161 C CA  . LEU B 1 200 ? 177.965 231.549 221.865 1.00 30.00 ? 200 LEU B CA  1 
ATOM   2162 C C   . LEU B 1 200 ? 176.718 230.938 221.226 1.00 30.00 ? 200 LEU B C   1 
ATOM   2163 O O   . LEU B 1 200 ? 176.874 229.996 220.433 1.00 30.00 ? 200 LEU B O   1 
ATOM   2164 C CB  . LEU B 1 200 ? 178.224 230.941 223.244 1.00 30.00 ? 200 LEU B CB  1 
ATOM   2165 C CG  . LEU B 1 200 ? 179.539 231.343 223.911 1.00 30.00 ? 200 LEU B CG  1 
ATOM   2166 C CD1 . LEU B 1 200 ? 179.781 230.513 225.157 1.00 30.00 ? 200 LEU B CD1 1 
ATOM   2167 C CD2 . LEU B 1 200 ? 180.712 231.214 222.954 1.00 30.00 ? 200 LEU B CD2 1 
ATOM   2168 N N   . VAL B 1 201 ? 175.532 231.428 221.586 1.00 30.00 ? 201 VAL B N   1 
ATOM   2169 C CA  . VAL B 1 201 ? 174.239 230.912 221.048 1.00 30.00 ? 201 VAL B CA  1 
ATOM   2170 C C   . VAL B 1 201 ? 174.162 231.192 219.543 1.00 30.00 ? 201 VAL B C   1 
ATOM   2171 O O   . VAL B 1 201 ? 173.696 230.295 218.820 1.00 30.00 ? 201 VAL B O   1 
ATOM   2172 C CB  . VAL B 1 201 ? 173.064 231.527 221.828 1.00 30.00 ? 201 VAL B CB  1 
ATOM   2173 C CG1 . VAL B 1 201 ? 171.768 231.543 221.030 1.00 30.00 ? 201 VAL B CG1 1 
ATOM   2174 C CG2 . VAL B 1 201 ? 172.867 230.826 223.161 1.00 30.00 ? 201 VAL B CG2 1 
ATOM   2175 N N   . LEU B 1 202 ? 174.579 232.377 219.088 1.00 30.00 ? 202 LEU B N   1 
ATOM   2176 C CA  . LEU B 1 202 ? 174.613 232.728 217.641 1.00 30.00 ? 202 LEU B CA  1 
ATOM   2177 C C   . LEU B 1 202 ? 175.762 231.963 216.986 1.00 30.00 ? 202 LEU B C   1 
ATOM   2178 O O   . LEU B 1 202 ? 175.652 231.651 215.788 1.00 30.00 ? 202 LEU B O   1 
ATOM   2179 C CB  . LEU B 1 202 ? 174.804 234.238 217.488 1.00 30.00 ? 202 LEU B CB  1 
ATOM   2180 C CG  . LEU B 1 202 ? 173.660 235.115 217.994 1.00 30.00 ? 202 LEU B CG  1 
ATOM   2181 C CD1 . LEU B 1 202 ? 173.860 236.554 217.561 1.00 30.00 ? 202 LEU B CD1 1 
ATOM   2182 C CD2 . LEU B 1 202 ? 172.311 234.610 217.513 1.00 30.00 ? 202 LEU B CD2 1 
ATOM   2183 N N   . LYS B 1 203 ? 176.846 231.725 217.724 1.00 30.00 ? 203 LYS B N   1 
ATOM   2184 C CA  . LYS B 1 203 ? 177.998 230.931 217.225 1.00 30.00 ? 203 LYS B CA  1 
ATOM   2185 C C   . LYS B 1 203 ? 177.540 229.483 217.043 1.00 30.00 ? 203 LYS B C   1 
ATOM   2186 O O   . LYS B 1 203 ? 178.027 228.832 216.098 1.00 30.00 ? 203 LYS B O   1 
ATOM   2187 C CB  . LYS B 1 203 ? 179.169 231.071 218.197 1.00 30.00 ? 203 LYS B CB  1 
ATOM   2188 C CG  . LYS B 1 203 ? 179.952 232.365 218.047 1.00 30.00 ? 203 LYS B CG  1 
ATOM   2189 C CD  . LYS B 1 203 ? 180.919 232.621 219.171 1.00 30.00 ? 203 LYS B CD  1 
ATOM   2190 C CE  . LYS B 1 203 ? 181.678 233.919 218.999 1.00 30.00 ? 203 LYS B CE  1 
ATOM   2191 N NZ  . LYS B 1 203 ? 182.526 233.915 217.785 1.00 30.00 ? 203 LYS B NZ  1 
ATOM   2192 N N   . GLY B 1 204 ? 176.640 229.003 217.905 1.00 30.00 ? 204 GLY B N   1 
ATOM   2193 C CA  . GLY B 1 204 ? 176.087 227.640 217.797 1.00 30.00 ? 204 GLY B CA  1 
ATOM   2194 C C   . GLY B 1 204 ? 175.066 227.592 216.679 1.00 30.00 ? 204 GLY B C   1 
ATOM   2195 O O   . GLY B 1 204 ? 174.843 226.489 216.144 1.00 30.00 ? 204 GLY B O   1 
ATOM   2196 N N   . LEU B 1 205 ? 174.468 228.733 216.317 1.00 30.00 ? 205 LEU B N   1 
ATOM   2197 C CA  . LEU B 1 205 ? 173.520 228.825 215.177 1.00 30.00 ? 205 LEU B CA  1 
ATOM   2198 C C   . LEU B 1 205 ? 174.252 228.291 213.945 1.00 30.00 ? 205 LEU B C   1 
ATOM   2199 O O   . LEU B 1 205 ? 173.624 227.531 213.182 1.00 30.00 ? 205 LEU B O   1 
ATOM   2200 C CB  . LEU B 1 205 ? 173.097 230.288 215.011 1.00 30.00 ? 205 LEU B CB  1 
ATOM   2201 C CG  . LEU B 1 205 ? 171.737 230.549 214.368 1.00 30.00 ? 205 LEU B CG  1 
ATOM   2202 C CD1 . LEU B 1 205 ? 171.492 232.041 214.250 1.00 30.00 ? 205 LEU B CD1 1 
ATOM   2203 C CD2 . LEU B 1 205 ? 171.618 229.895 213.002 1.00 30.00 ? 205 LEU B CD2 1 
ATOM   2204 N N   . GLY B 1 206 ? 175.544 228.612 213.788 1.00 30.00 ? 206 GLY B N   1 
ATOM   2205 C CA  . GLY B 1 206 ? 176.366 228.088 212.678 1.00 30.00 ? 206 GLY B CA  1 
ATOM   2206 C C   . GLY B 1 206 ? 177.198 229.159 211.998 1.00 30.00 ? 206 GLY B C   1 
ATOM   2207 O O   . GLY B 1 206 ? 177.395 230.224 212.615 1.00 30.00 ? 206 GLY B O   1 
ATOM   2208 N N   . MET B 1 207 ? 177.673 228.895 210.776 1.00 30.00 ? 207 MET B N   1 
ATOM   2209 C CA  . MET B 1 207 ? 178.517 229.838 209.998 1.00 30.00 ? 207 MET B CA  1 
ATOM   2210 C C   . MET B 1 207 ? 177.624 230.854 209.287 1.00 30.00 ? 207 MET B C   1 
ATOM   2211 O O   . MET B 1 207 ? 176.436 230.548 209.104 1.00 30.00 ? 207 MET B O   1 
ATOM   2212 C CB  . MET B 1 207 ? 179.302 229.080 208.930 1.00 30.00 ? 207 MET B CB  1 
ATOM   2213 C CG  . MET B 1 207 ? 180.566 228.416 209.431 1.00 30.00 ? 207 MET B CG  1 
ATOM   2214 S SD  . MET B 1 207 ? 181.967 229.547 209.569 1.00 30.00 ? 207 MET B SD  1 
ATOM   2215 C CE  . MET B 1 207 ? 183.317 228.429 209.196 1.00 30.00 ? 207 MET B CE  1 
ATOM   2216 N N   . ASN B 1 208 ? 178.176 231.995 208.874 1.00 30.00 ? 208 ASN B N   1 
ATOM   2217 C CA  . ASN B 1 208 ? 177.423 233.064 208.165 1.00 30.00 ? 208 ASN B CA  1 
ATOM   2218 C C   . ASN B 1 208 ? 175.922 232.962 208.461 1.00 30.00 ? 208 ASN B C   1 
ATOM   2219 O O   . ASN B 1 208 ? 175.148 232.720 207.523 1.00 30.00 ? 208 ASN B O   1 
ATOM   2220 C CB  . ASN B 1 208 ? 177.717 232.994 206.667 1.00 30.00 ? 208 ASN B CB  1 
ATOM   2221 C CG  . ASN B 1 208 ? 177.681 231.579 206.133 1.00 30.00 ? 208 ASN B CG  1 
ATOM   2222 O OD1 . ASN B 1 208 ? 176.659 230.901 206.204 1.00 30.00 ? 208 ASN B OD1 1 
ATOM   2223 N ND2 . ASN B 1 208 ? 178.802 231.119 205.604 1.00 30.00 ? 208 ASN B ND2 1 
ATOM   2224 N N   . PRO B 1 209 ? 175.462 233.178 209.710 1.00 30.00 ? 209 PRO B N   1 
ATOM   2225 C CA  . PRO B 1 209 ? 174.039 233.134 210.006 1.00 30.00 ? 209 PRO B CA  1 
ATOM   2226 C C   . PRO B 1 209 ? 173.322 234.303 209.323 1.00 30.00 ? 209 PRO B C   1 
ATOM   2227 O O   . PRO B 1 209 ? 174.014 235.169 208.831 1.00 30.00 ? 209 PRO B O   1 
ATOM   2228 C CB  . PRO B 1 209 ? 173.956 233.269 211.531 1.00 30.00 ? 209 PRO B CB  1 
ATOM   2229 C CG  . PRO B 1 209 ? 175.345 232.943 212.020 1.00 30.00 ? 209 PRO B CG  1 
ATOM   2230 C CD  . PRO B 1 209 ? 176.259 233.423 210.915 1.00 30.00 ? 209 PRO B CD  1 
ATOM   2231 N N   . THR B 1 210 ? 171.986 234.320 209.318 1.00 30.00 ? 210 THR B N   1 
ATOM   2232 C CA  . THR B 1 210 ? 171.181 235.448 208.776 1.00 30.00 ? 210 THR B CA  1 
ATOM   2233 C C   . THR B 1 210 ? 170.513 236.109 209.982 1.00 30.00 ? 210 THR B C   1 
ATOM   2234 O O   . THR B 1 210 ? 170.312 235.394 210.982 1.00 30.00 ? 210 THR B O   1 
ATOM   2235 C CB  . THR B 1 210 ? 170.188 234.975 207.711 1.00 30.00 ? 210 THR B CB  1 
ATOM   2236 O OG1 . THR B 1 210 ? 169.513 236.129 207.212 1.00 30.00 ? 210 THR B OG1 1 
ATOM   2237 C CG2 . THR B 1 210 ? 169.173 233.983 208.234 1.00 30.00 ? 210 THR B CG2 1 
ATOM   2238 N N   . LEU B 1 211 ? 170.183 237.401 209.918 1.00 30.00 ? 211 LEU B N   1 
ATOM   2239 C CA  . LEU B 1 211 ? 169.646 238.119 211.105 1.00 30.00 ? 211 LEU B CA  1 
ATOM   2240 C C   . LEU B 1 211 ? 168.357 237.423 211.535 1.00 30.00 ? 211 LEU B C   1 
ATOM   2241 O O   . LEU B 1 211 ? 168.156 237.274 212.746 1.00 30.00 ? 211 LEU B O   1 
ATOM   2242 C CB  . LEU B 1 211 ? 169.410 239.600 210.789 1.00 30.00 ? 211 LEU B CB  1 
ATOM   2243 C CG  . LEU B 1 211 ? 168.758 240.414 211.905 1.00 30.00 ? 211 LEU B CG  1 
ATOM   2244 C CD1 . LEU B 1 211 ? 169.682 240.540 213.104 1.00 30.00 ? 211 LEU B CD1 1 
ATOM   2245 C CD2 . LEU B 1 211 ? 168.363 241.788 211.398 1.00 30.00 ? 211 LEU B CD2 1 
ATOM   2246 N N   . GLU B 1 212 ? 167.542 236.966 210.589 1.00 30.00 ? 212 GLU B N   1 
ATOM   2247 C CA  . GLU B 1 212 ? 166.231 236.367 210.933 1.00 30.00 ? 212 GLU B CA  1 
ATOM   2248 C C   . GLU B 1 212 ? 166.499 235.230 211.916 1.00 30.00 ? 212 GLU B C   1 
ATOM   2249 O O   . GLU B 1 212 ? 165.841 235.190 212.973 1.00 30.00 ? 212 GLU B O   1 
ATOM   2250 C CB  . GLU B 1 212 ? 165.549 235.911 209.646 1.00 30.00 ? 212 GLU B CB  1 
ATOM   2251 C CG  . GLU B 1 212 ? 164.174 235.304 209.857 1.00 30.00 ? 212 GLU B CG  1 
ATOM   2252 C CD  . GLU B 1 212 ? 164.136 233.835 210.244 1.00 30.00 ? 212 GLU B CD  1 
ATOM   2253 O OE1 . GLU B 1 212 ? 165.210 233.213 210.346 1.00 30.00 ? 212 GLU B OE1 1 
ATOM   2254 O OE2 . GLU B 1 212 ? 163.021 233.312 210.433 1.00 30.00 ? 212 GLU B OE2 1 
ATOM   2255 N N   . GLU B 1 213 ? 167.473 234.382 211.609 1.00 30.00 ? 213 GLU B N   1 
ATOM   2256 C CA  . GLU B 1 213 ? 167.819 233.220 212.461 1.00 30.00 ? 213 GLU B CA  1 
ATOM   2257 C C   . GLU B 1 213 ? 168.477 233.720 213.739 1.00 30.00 ? 213 GLU B C   1 
ATOM   2258 O O   . GLU B 1 213 ? 168.182 233.164 214.805 1.00 30.00 ? 213 GLU B O   1 
ATOM   2259 C CB  . GLU B 1 213 ? 168.751 232.283 211.700 1.00 30.00 ? 213 GLU B CB  1 
ATOM   2260 C CG  . GLU B 1 213 ? 168.102 231.654 210.485 1.00 30.00 ? 213 GLU B CG  1 
ATOM   2261 C CD  . GLU B 1 213 ? 169.020 230.763 209.669 1.00 30.00 ? 213 GLU B CD  1 
ATOM   2262 O OE1 . GLU B 1 213 ? 170.198 230.622 210.050 1.00 30.00 ? 213 GLU B OE1 1 
ATOM   2263 O OE2 . GLU B 1 213 ? 168.556 230.221 208.649 1.00 30.00 ? 213 GLU B OE2 1 
ATOM   2264 N N   . MET B 1 214 ? 169.330 234.731 213.635 1.00 30.00 ? 214 MET B N   1 
ATOM   2265 C CA  . MET B 1 214 ? 170.075 235.241 214.808 1.00 30.00 ? 214 MET B CA  1 
ATOM   2266 C C   . MET B 1 214 ? 169.045 235.710 215.834 1.00 30.00 ? 214 MET B C   1 
ATOM   2267 O O   . MET B 1 214 ? 169.215 235.392 217.026 1.00 30.00 ? 214 MET B O   1 
ATOM   2268 C CB  . MET B 1 214 ? 170.994 236.390 214.394 1.00 30.00 ? 214 MET B CB  1 
ATOM   2269 C CG  . MET B 1 214 ? 172.315 235.911 213.838 1.00 30.00 ? 214 MET B CG  1 
ATOM   2270 S SD  . MET B 1 214 ? 173.238 237.220 212.999 1.00 30.00 ? 214 MET B SD  1 
ATOM   2271 C CE  . MET B 1 214 ? 174.209 237.862 214.361 1.00 30.00 ? 214 MET B CE  1 
ATOM   2272 N N   . LEU B 1 215 ? 167.985 236.383 215.384 1.00 30.00 ? 215 LEU B N   1 
ATOM   2273 C CA  . LEU B 1 215 ? 166.937 236.918 216.290 1.00 30.00 ? 215 LEU B CA  1 
ATOM   2274 C C   . LEU B 1 215 ? 166.225 235.754 216.980 1.00 30.00 ? 215 LEU B C   1 
ATOM   2275 O O   . LEU B 1 215 ? 166.092 235.807 218.216 1.00 30.00 ? 215 LEU B O   1 
ATOM   2276 C CB  . LEU B 1 215 ? 165.949 237.752 215.468 1.00 30.00 ? 215 LEU B CB  1 
ATOM   2277 C CG  . LEU B 1 215 ? 166.454 239.094 214.938 1.00 30.00 ? 215 LEU B CG  1 
ATOM   2278 C CD1 . LEU B 1 215 ? 165.361 239.810 214.166 1.00 30.00 ? 215 LEU B CD1 1 
ATOM   2279 C CD2 . LEU B 1 215 ? 166.953 239.979 216.064 1.00 30.00 ? 215 LEU B CD2 1 
ATOM   2280 N N   . THR B 1 216 ? 165.834 234.723 216.231 1.00 30.00 ? 216 THR B N   1 
ATOM   2281 C CA  . THR B 1 216 ? 165.062 233.576 216.773 1.00 30.00 ? 216 THR B CA  1 
ATOM   2282 C C   . THR B 1 216 ? 165.919 232.782 217.752 1.00 30.00 ? 216 THR B C   1 
ATOM   2283 O O   . THR B 1 216 ? 165.397 232.411 218.809 1.00 30.00 ? 216 THR B O   1 
ATOM   2284 C CB  . THR B 1 216 ? 164.588 232.676 215.631 1.00 30.00 ? 216 THR B CB  1 
ATOM   2285 O OG1 . THR B 1 216 ? 163.852 233.489 214.717 1.00 30.00 ? 216 THR B OG1 1 
ATOM   2286 C CG2 . THR B 1 216 ? 163.734 231.521 216.103 1.00 30.00 ? 216 THR B CG2 1 
ATOM   2287 N N   . ALA B 1 217 ? 167.194 232.597 217.454 1.00 30.00 ? 217 ALA B N   1 
ATOM   2288 C CA  . ALA B 1 217 ? 168.076 231.756 218.282 1.00 30.00 ? 217 ALA B CA  1 
ATOM   2289 C C   . ALA B 1 217 ? 168.376 232.460 219.597 1.00 30.00 ? 217 ALA B C   1 
ATOM   2290 O O   . ALA B 1 217 ? 168.414 231.777 220.624 1.00 30.00 ? 217 ALA B O   1 
ATOM   2291 C CB  . ALA B 1 217 ? 169.344 231.479 217.529 1.00 30.00 ? 217 ALA B CB  1 
ATOM   2292 N N   . CYS B 1 218 ? 168.549 233.774 219.571 1.00 30.00 ? 218 CYS B N   1 
ATOM   2293 C CA  . CYS B 1 218 ? 168.937 234.526 220.788 1.00 30.00 ? 218 CYS B CA  1 
ATOM   2294 C C   . CYS B 1 218 ? 167.661 234.951 221.510 1.00 30.00 ? 218 CYS B C   1 
ATOM   2295 O O   . CYS B 1 218 ? 167.761 235.657 222.525 1.00 30.00 ? 218 CYS B O   1 
ATOM   2296 C CB  . CYS B 1 218 ? 169.807 235.723 220.440 1.00 30.00 ? 218 CYS B CB  1 
ATOM   2297 S SG  . CYS B 1 218 ? 170.547 236.521 221.890 1.00 30.00 ? 218 CYS B SG  1 
ATOM   2298 N N   . GLN B 1 219 ? 166.499 234.559 220.995 1.00 30.00 ? 219 GLN B N   1 
ATOM   2299 C CA  . GLN B 1 219 ? 165.221 234.838 221.691 1.00 30.00 ? 219 GLN B CA  1 
ATOM   2300 C C   . GLN B 1 219 ? 165.362 234.268 223.098 1.00 30.00 ? 219 GLN B C   1 
ATOM   2301 O O   . GLN B 1 219 ? 165.754 233.101 223.210 1.00 30.00 ? 219 GLN B O   1 
ATOM   2302 C CB  . GLN B 1 219 ? 164.052 234.192 220.953 1.00 30.00 ? 219 GLN B CB  1 
ATOM   2303 C CG  . GLN B 1 219 ? 162.702 234.416 221.612 1.00 30.00 ? 219 GLN B CG  1 
ATOM   2304 C CD  . GLN B 1 219 ? 162.350 235.879 221.702 1.00 30.00 ? 219 GLN B CD  1 
ATOM   2305 O OE1 . GLN B 1 219 ? 162.169 236.424 222.787 1.00 30.00 ? 219 GLN B OE1 1 
ATOM   2306 N NE2 . GLN B 1 219 ? 162.258 236.529 220.553 1.00 30.00 ? 219 GLN B NE2 1 
ATOM   2307 N N   . GLY B 1 220 ? 165.056 235.050 224.127 1.00 30.00 ? 220 GLY B N   1 
ATOM   2308 C CA  . GLY B 1 220 ? 165.217 234.605 225.521 1.00 30.00 ? 220 GLY B CA  1 
ATOM   2309 C C   . GLY B 1 220 ? 166.631 234.119 225.772 1.00 30.00 ? 220 GLY B C   1 
ATOM   2310 O O   . GLY B 1 220 ? 166.774 233.134 226.515 1.00 30.00 ? 220 GLY B O   1 
ATOM   2311 N N   . VAL B 1 221 ? 167.639 234.758 225.169 1.00 30.00 ? 221 VAL B N   1 
ATOM   2312 C CA  . VAL B 1 221 ? 169.077 234.425 225.394 1.00 30.00 ? 221 VAL B CA  1 
ATOM   2313 C C   . VAL B 1 221 ? 169.794 235.714 225.802 1.00 30.00 ? 221 VAL B C   1 
ATOM   2314 O O   . VAL B 1 221 ? 169.957 236.574 224.917 1.00 30.00 ? 221 VAL B O   1 
ATOM   2315 C CB  . VAL B 1 221 ? 169.732 233.792 224.155 1.00 30.00 ? 221 VAL B CB  1 
ATOM   2316 C CG1 . VAL B 1 221 ? 171.224 233.588 224.346 1.00 30.00 ? 221 VAL B CG1 1 
ATOM   2317 C CG2 . VAL B 1 221 ? 169.065 232.487 223.762 1.00 30.00 ? 221 VAL B CG2 1 
ATOM   2318 N N   . THR C 1 148 ? 144.363 208.425 224.247 1.00 30.00 ? 148 THR C N   1 
ATOM   2319 C CA  . THR C 1 148 ? 144.364 209.827 224.748 1.00 30.00 ? 148 THR C CA  1 
ATOM   2320 C C   . THR C 1 148 ? 144.489 210.780 223.555 1.00 30.00 ? 148 THR C C   1 
ATOM   2321 O O   . THR C 1 148 ? 144.348 210.294 222.415 1.00 30.00 ? 148 THR C O   1 
ATOM   2322 C CB  . THR C 1 148 ? 145.476 210.041 225.785 1.00 30.00 ? 148 THR C CB  1 
ATOM   2323 O OG1 . THR C 1 148 ? 146.725 209.700 225.184 1.00 30.00 ? 148 THR C OG1 1 
ATOM   2324 C CG2 . THR C 1 148 ? 145.278 209.221 227.039 1.00 30.00 ? 148 THR C CG2 1 
ATOM   2325 N N   . ASN C 1 149 ? 144.744 212.071 223.796 1.00 30.00 ? 149 ASN C N   1 
ATOM   2326 C CA  . ASN C 1 149 ? 144.858 213.094 222.724 1.00 30.00 ? 149 ASN C CA  1 
ATOM   2327 C C   . ASN C 1 149 ? 146.300 213.583 222.619 1.00 30.00 ? 149 ASN C C   1 
ATOM   2328 O O   . ASN C 1 149 ? 147.037 213.413 223.593 1.00 30.00 ? 149 ASN C O   1 
ATOM   2329 C CB  . ASN C 1 149 ? 143.938 214.286 222.978 1.00 30.00 ? 149 ASN C CB  1 
ATOM   2330 C CG  . ASN C 1 149 ? 142.477 213.966 222.745 1.00 30.00 ? 149 ASN C CG  1 
ATOM   2331 O OD1 . ASN C 1 149 ? 142.127 212.841 222.398 1.00 30.00 ? 149 ASN C OD1 1 
ATOM   2332 N ND2 . ASN C 1 149 ? 141.617 214.952 222.934 1.00 30.00 ? 149 ASN C ND2 1 
ATOM   2333 N N   . ILE C 1 150 ? 146.660 214.208 221.501 1.00 30.00 ? 150 ILE C N   1 
ATOM   2334 C CA  . ILE C 1 150 ? 148.036 214.724 221.248 1.00 30.00 ? 150 ILE C CA  1 
ATOM   2335 C C   . ILE C 1 150 ? 148.365 215.809 222.274 1.00 30.00 ? 150 ILE C C   1 
ATOM   2336 O O   . ILE C 1 150 ? 149.552 215.926 222.635 1.00 30.00 ? 150 ILE C O   1 
ATOM   2337 C CB  . ILE C 1 150 ? 148.137 215.262 219.810 1.00 30.00 ? 150 ILE C CB  1 
ATOM   2338 C CG1 . ILE C 1 150 ? 147.311 216.535 219.610 1.00 30.00 ? 150 ILE C CG1 1 
ATOM   2339 C CG2 . ILE C 1 150 ? 147.776 214.176 218.814 1.00 30.00 ? 150 ILE C CG2 1 
ATOM   2340 C CD1 . ILE C 1 150 ? 147.401 217.109 218.226 1.00 30.00 ? 150 ILE C CD1 1 
ATOM   2341 N N   . LEU C 1 151 ? 147.369 216.589 222.698 1.00 30.00 ? 151 LEU C N   1 
ATOM   2342 C CA  . LEU C 1 151 ? 147.571 217.706 223.657 1.00 30.00 ? 151 LEU C CA  1 
ATOM   2343 C C   . LEU C 1 151 ? 147.801 217.110 225.046 1.00 30.00 ? 151 LEU C C   1 
ATOM   2344 O O   . LEU C 1 151 ? 148.574 217.715 225.811 1.00 30.00 ? 151 LEU C O   1 
ATOM   2345 C CB  . LEU C 1 151 ? 146.324 218.593 223.637 1.00 30.00 ? 151 LEU C CB  1 
ATOM   2346 C CG  . LEU C 1 151 ? 145.866 219.079 222.262 1.00 30.00 ? 151 LEU C CG  1 
ATOM   2347 C CD1 . LEU C 1 151 ? 144.735 220.081 222.398 1.00 30.00 ? 151 LEU C CD1 1 
ATOM   2348 C CD2 . LEU C 1 151 ? 147.013 219.692 221.477 1.00 30.00 ? 151 LEU C CD2 1 
ATOM   2349 N N   . ASP C 1 152 ? 147.172 215.974 225.363 1.00 30.00 ? 152 ASP C N   1 
ATOM   2350 C CA  . ASP C 1 152 ? 147.326 215.270 226.664 1.00 30.00 ? 152 ASP C CA  1 
ATOM   2351 C C   . ASP C 1 152 ? 148.505 214.301 226.579 1.00 30.00 ? 152 ASP C C   1 
ATOM   2352 O O   . ASP C 1 152 ? 148.819 213.679 227.612 1.00 30.00 ? 152 ASP C O   1 
ATOM   2353 C CB  . ASP C 1 152 ? 146.043 214.529 227.033 1.00 30.00 ? 152 ASP C CB  1 
ATOM   2354 C CG  . ASP C 1 152 ? 144.848 215.443 227.233 1.00 30.00 ? 152 ASP C CG  1 
ATOM   2355 O OD1 . ASP C 1 152 ? 144.933 216.332 228.102 1.00 30.00 ? 152 ASP C OD1 1 
ATOM   2356 O OD2 . ASP C 1 152 ? 143.838 215.246 226.532 1.00 30.00 ? 152 ASP C OD2 1 
ATOM   2357 N N   . VAL C 1 153 ? 149.139 214.187 225.411 1.00 30.00 ? 153 VAL C N   1 
ATOM   2358 C CA  . VAL C 1 153 ? 150.327 213.310 225.204 1.00 30.00 ? 153 VAL C CA  1 
ATOM   2359 C C   . VAL C 1 153 ? 151.562 214.204 225.281 1.00 30.00 ? 153 VAL C C   1 
ATOM   2360 O O   . VAL C 1 153 ? 151.640 215.151 224.475 1.00 30.00 ? 153 VAL C O   1 
ATOM   2361 C CB  . VAL C 1 153 ? 150.226 212.554 223.867 1.00 30.00 ? 153 VAL C CB  1 
ATOM   2362 C CG1 . VAL C 1 153 ? 151.581 212.123 223.334 1.00 30.00 ? 153 VAL C CG1 1 
ATOM   2363 C CG2 . VAL C 1 153 ? 149.300 211.355 223.972 1.00 30.00 ? 153 VAL C CG2 1 
ATOM   2364 N N   . LYS C 1 154 ? 152.450 213.969 226.252 1.00 30.00 ? 154 LYS C N   1 
ATOM   2365 C CA  . LYS C 1 154 ? 153.654 214.815 226.462 1.00 30.00 ? 154 LYS C CA  1 
ATOM   2366 C C   . LYS C 1 154 ? 154.833 213.960 226.926 1.00 30.00 ? 154 LYS C C   1 
ATOM   2367 O O   . LYS C 1 154 ? 154.643 213.161 227.862 1.00 30.00 ? 154 LYS C O   1 
ATOM   2368 C CB  . LYS C 1 154 ? 153.364 215.880 227.517 1.00 30.00 ? 154 LYS C CB  1 
ATOM   2369 C CG  . LYS C 1 154 ? 152.096 216.688 227.293 1.00 30.00 ? 154 LYS C CG  1 
ATOM   2370 C CD  . LYS C 1 154 ? 152.025 217.907 228.172 1.00 30.00 ? 154 LYS C CD  1 
ATOM   2371 C CE  . LYS C 1 154 ? 150.770 218.719 227.951 1.00 30.00 ? 154 LYS C CE  1 
ATOM   2372 N NZ  . LYS C 1 154 ? 150.728 219.897 228.847 1.00 30.00 ? 154 LYS C NZ  1 
ATOM   2373 N N   . GLN C 1 155 ? 156.019 214.175 226.357 1.00 30.00 ? 155 GLN C N   1 
ATOM   2374 C CA  . GLN C 1 155 ? 157.223 213.382 226.711 1.00 30.00 ? 155 GLN C CA  1 
ATOM   2375 C C   . GLN C 1 155 ? 157.465 213.494 228.216 1.00 30.00 ? 155 GLN C C   1 
ATOM   2376 O O   . GLN C 1 155 ? 157.420 214.631 228.728 1.00 30.00 ? 155 GLN C O   1 
ATOM   2377 C CB  . GLN C 1 155 ? 158.440 213.875 225.931 1.00 30.00 ? 155 GLN C CB  1 
ATOM   2378 C CG  . GLN C 1 155 ? 159.718 213.123 226.268 1.00 30.00 ? 155 GLN C CG  1 
ATOM   2379 C CD  . GLN C 1 155 ? 160.877 213.534 225.394 1.00 30.00 ? 155 GLN C CD  1 
ATOM   2380 O OE1 . GLN C 1 155 ? 160.742 214.370 224.505 1.00 30.00 ? 155 GLN C OE1 1 
ATOM   2381 N NE2 . GLN C 1 155 ? 162.035 212.948 225.647 1.00 30.00 ? 155 GLN C NE2 1 
ATOM   2382 N N   . GLY C 1 156 ? 157.730 212.370 228.887 1.00 30.00 ? 156 GLY C N   1 
ATOM   2383 C CA  . GLY C 1 156 ? 158.003 212.343 230.336 1.00 30.00 ? 156 GLY C CA  1 
ATOM   2384 C C   . GLY C 1 156 ? 159.492 212.232 230.598 1.00 30.00 ? 156 GLY C C   1 
ATOM   2385 O O   . GLY C 1 156 ? 160.238 211.986 229.635 1.00 30.00 ? 156 GLY C O   1 
ATOM   2386 N N   . PRO C 1 157 ? 159.973 212.412 231.847 1.00 30.00 ? 157 PRO C N   1 
ATOM   2387 C CA  . PRO C 1 157 ? 161.407 212.407 232.119 1.00 30.00 ? 157 PRO C CA  1 
ATOM   2388 C C   . PRO C 1 157 ? 161.992 211.054 231.702 1.00 30.00 ? 157 PRO C C   1 
ATOM   2389 O O   . PRO C 1 157 ? 163.045 211.046 231.092 1.00 30.00 ? 157 PRO C O   1 
ATOM   2390 C CB  . PRO C 1 157 ? 161.499 212.595 233.640 1.00 30.00 ? 157 PRO C CB  1 
ATOM   2391 C CG  . PRO C 1 157 ? 160.184 213.237 234.017 1.00 30.00 ? 157 PRO C CG  1 
ATOM   2392 C CD  . PRO C 1 157 ? 159.179 212.649 233.051 1.00 30.00 ? 157 PRO C CD  1 
ATOM   2393 N N   . LYS C 1 158 ? 161.298 209.959 232.019 1.00 30.00 ? 158 LYS C N   1 
ATOM   2394 C CA  . LYS C 1 158 ? 161.742 208.585 231.665 1.00 30.00 ? 158 LYS C CA  1 
ATOM   2395 C C   . LYS C 1 158 ? 161.589 208.356 230.160 1.00 30.00 ? 158 LYS C C   1 
ATOM   2396 O O   . LYS C 1 158 ? 162.450 207.655 229.593 1.00 30.00 ? 158 LYS C O   1 
ATOM   2397 C CB  . LYS C 1 158 ? 160.928 207.559 232.455 1.00 30.00 ? 158 LYS C CB  1 
ATOM   2398 C CG  . LYS C 1 158 ? 161.040 207.687 233.968 1.00 30.00 ? 158 LYS C CG  1 
ATOM   2399 C CD  . LYS C 1 158 ? 162.463 207.603 234.474 1.00 30.00 ? 158 LYS C CD  1 
ATOM   2400 C CE  . LYS C 1 158 ? 162.565 207.729 235.978 1.00 30.00 ? 158 LYS C CE  1 
ATOM   2401 N NZ  . LYS C 1 158 ? 163.971 207.634 236.431 1.00 30.00 ? 158 LYS C NZ  1 
ATOM   2402 N N   . GLU C 1 159 ? 160.526 208.884 229.547 1.00 30.00 ? 159 GLU C N   1 
ATOM   2403 C CA  . GLU C 1 159 ? 160.241 208.636 228.110 1.00 30.00 ? 159 GLU C CA  1 
ATOM   2404 C C   . GLU C 1 159 ? 161.198 209.439 227.240 1.00 30.00 ? 159 GLU C C   1 
ATOM   2405 O O   . GLU C 1 159 ? 161.327 210.644 227.497 1.00 30.00 ? 159 GLU C O   1 
ATOM   2406 C CB  . GLU C 1 159 ? 158.847 209.101 227.696 1.00 30.00 ? 159 GLU C CB  1 
ATOM   2407 C CG  . GLU C 1 159 ? 157.713 208.482 228.479 1.00 30.00 ? 159 GLU C CG  1 
ATOM   2408 C CD  . GLU C 1 159 ? 156.346 208.935 227.998 1.00 30.00 ? 159 GLU C CD  1 
ATOM   2409 O OE1 . GLU C 1 159 ? 156.298 209.734 227.043 1.00 30.00 ? 159 GLU C OE1 1 
ATOM   2410 O OE2 . GLU C 1 159 ? 155.338 208.492 228.578 1.00 30.00 ? 159 GLU C OE2 1 
ATOM   2411 N N   . PRO C 1 160 ? 161.883 208.854 226.237 1.00 30.00 ? 160 PRO C N   1 
ATOM   2412 C CA  . PRO C 1 160 ? 162.690 209.641 225.304 1.00 30.00 ? 160 PRO C CA  1 
ATOM   2413 C C   . PRO C 1 160 ? 161.771 210.385 224.328 1.00 30.00 ? 160 PRO C C   1 
ATOM   2414 O O   . PRO C 1 160 ? 160.584 210.413 224.583 1.00 30.00 ? 160 PRO C O   1 
ATOM   2415 C CB  . PRO C 1 160 ? 163.521 208.600 224.547 1.00 30.00 ? 160 PRO C CB  1 
ATOM   2416 C CG  . PRO C 1 160 ? 163.417 207.351 225.393 1.00 30.00 ? 160 PRO C CG  1 
ATOM   2417 C CD  . PRO C 1 160 ? 162.031 207.422 225.992 1.00 30.00 ? 160 PRO C CD  1 
ATOM   2418 N N   . PHE C 1 161 ? 162.311 210.939 223.240 1.00 30.00 ? 161 PHE C N   1 
ATOM   2419 C CA  . PHE C 1 161 ? 161.498 211.606 222.191 1.00 30.00 ? 161 PHE C CA  1 
ATOM   2420 C C   . PHE C 1 161 ? 161.104 210.547 221.163 1.00 30.00 ? 161 PHE C C   1 
ATOM   2421 O O   . PHE C 1 161 ? 160.416 210.884 220.199 1.00 30.00 ? 161 PHE C O   1 
ATOM   2422 C CB  . PHE C 1 161 ? 162.259 212.753 221.529 1.00 30.00 ? 161 PHE C CB  1 
ATOM   2423 C CG  . PHE C 1 161 ? 161.489 213.446 220.437 1.00 30.00 ? 161 PHE C CG  1 
ATOM   2424 C CD1 . PHE C 1 161 ? 160.314 214.120 220.721 1.00 30.00 ? 161 PHE C CD1 1 
ATOM   2425 C CD2 . PHE C 1 161 ? 161.906 213.370 219.121 1.00 30.00 ? 161 PHE C CD2 1 
ATOM   2426 C CE1 . PHE C 1 161 ? 159.593 214.739 219.714 1.00 30.00 ? 161 PHE C CE1 1 
ATOM   2427 C CE2 . PHE C 1 161 ? 161.179 213.982 218.114 1.00 30.00 ? 161 PHE C CE2 1 
ATOM   2428 C CZ  . PHE C 1 161 ? 160.026 214.666 218.413 1.00 30.00 ? 161 PHE C CZ  1 
ATOM   2429 N N   . GLN C 1 162 ? 161.542 209.304 221.351 1.00 30.00 ? 162 GLN C N   1 
ATOM   2430 C CA  . GLN C 1 162 ? 161.144 208.179 220.470 1.00 30.00 ? 162 GLN C CA  1 
ATOM   2431 C C   . GLN C 1 162 ? 159.867 207.587 221.054 1.00 30.00 ? 162 GLN C C   1 
ATOM   2432 O O   . GLN C 1 162 ? 158.983 207.209 220.264 1.00 30.00 ? 162 GLN C O   1 
ATOM   2433 C CB  . GLN C 1 162 ? 162.234 207.112 220.445 1.00 30.00 ? 162 GLN C CB  1 
ATOM   2434 C CG  . GLN C 1 162 ? 161.849 205.854 219.682 1.00 30.00 ? 162 GLN C CG  1 
ATOM   2435 C CD  . GLN C 1 162 ? 161.494 206.145 218.246 1.00 30.00 ? 162 GLN C CD  1 
ATOM   2436 O OE1 . GLN C 1 162 ? 162.308 206.646 217.476 1.00 30.00 ? 162 GLN C OE1 1 
ATOM   2437 N NE2 . GLN C 1 162 ? 160.267 205.824 217.874 1.00 30.00 ? 162 GLN C NE2 1 
ATOM   2438 N N   . SER C 1 163 ? 159.767 207.533 222.383 1.00 30.00 ? 163 SER C N   1 
ATOM   2439 C CA  . SER C 1 163 ? 158.601 206.947 223.094 1.00 30.00 ? 163 SER C CA  1 
ATOM   2440 C C   . SER C 1 163 ? 157.458 207.955 223.066 1.00 30.00 ? 163 SER C C   1 
ATOM   2441 O O   . SER C 1 163 ? 156.316 207.549 222.775 1.00 30.00 ? 163 SER C O   1 
ATOM   2442 C CB  . SER C 1 163 ? 158.953 206.597 224.503 1.00 30.00 ? 163 SER C CB  1 
ATOM   2443 O OG  . SER C 1 163 ? 157.810 206.147 225.213 1.00 30.00 ? 163 SER C OG  1 
ATOM   2444 N N   . TYR C 1 164 ? 157.764 209.223 223.326 1.00 30.00 ? 164 TYR C N   1 
ATOM   2445 C CA  . TYR C 1 164 ? 156.760 210.310 223.306 1.00 30.00 ? 164 TYR C CA  1 
ATOM   2446 C C   . TYR C 1 164 ? 156.196 210.446 221.893 1.00 30.00 ? 164 TYR C C   1 
ATOM   2447 O O   . TYR C 1 164 ? 155.017 210.789 221.791 1.00 30.00 ? 164 TYR C O   1 
ATOM   2448 C CB  . TYR C 1 164 ? 157.392 211.627 223.742 1.00 30.00 ? 164 TYR C CB  1 
ATOM   2449 C CG  . TYR C 1 164 ? 156.588 212.817 223.302 1.00 30.00 ? 164 TYR C CG  1 
ATOM   2450 C CD1 . TYR C 1 164 ? 155.284 212.984 223.725 1.00 30.00 ? 164 TYR C CD1 1 
ATOM   2451 C CD2 . TYR C 1 164 ? 157.106 213.736 222.410 1.00 30.00 ? 164 TYR C CD2 1 
ATOM   2452 C CE1 . TYR C 1 164 ? 154.525 214.056 223.299 1.00 30.00 ? 164 TYR C CE1 1 
ATOM   2453 C CE2 . TYR C 1 164 ? 156.359 214.817 221.978 1.00 30.00 ? 164 TYR C CE2 1 
ATOM   2454 C CZ  . TYR C 1 164 ? 155.062 214.977 222.424 1.00 30.00 ? 164 TYR C CZ  1 
ATOM   2455 O OH  . TYR C 1 164 ? 154.287 216.029 222.013 1.00 30.00 ? 164 TYR C OH  1 
ATOM   2456 N N   . VAL C 1 165 ? 157.020 210.250 220.861 1.00 30.00 ? 165 VAL C N   1 
ATOM   2457 C CA  . VAL C 1 165 ? 156.608 210.347 219.428 1.00 30.00 ? 165 VAL C CA  1 
ATOM   2458 C C   . VAL C 1 165 ? 155.751 209.137 219.057 1.00 30.00 ? 165 VAL C C   1 
ATOM   2459 O O   . VAL C 1 165 ? 154.922 209.270 218.152 1.00 30.00 ? 165 VAL C O   1 
ATOM   2460 C CB  . VAL C 1 165 ? 157.844 210.454 218.518 1.00 30.00 ? 165 VAL C CB  1 
ATOM   2461 C CG1 . VAL C 1 165 ? 157.593 209.950 217.106 1.00 30.00 ? 165 VAL C CG1 1 
ATOM   2462 C CG2 . VAL C 1 165 ? 158.386 211.871 218.480 1.00 30.00 ? 165 VAL C CG2 1 
ATOM   2463 N N   . ASP C 1 166 ? 155.920 208.002 219.734 1.00 30.00 ? 166 ASP C N   1 
ATOM   2464 C CA  . ASP C 1 166 ? 155.166 206.767 219.397 1.00 30.00 ? 166 ASP C CA  1 
ATOM   2465 C C   . ASP C 1 166 ? 153.772 206.875 220.015 1.00 30.00 ? 166 ASP C C   1 
ATOM   2466 O O   . ASP C 1 166 ? 152.957 205.968 219.760 1.00 30.00 ? 166 ASP C O   1 
ATOM   2467 C CB  . ASP C 1 166 ? 155.930 205.525 219.850 1.00 30.00 ? 166 ASP C CB  1 
ATOM   2468 C CG  . ASP C 1 166 ? 157.124 205.203 218.973 1.00 30.00 ? 166 ASP C CG  1 
ATOM   2469 O OD1 . ASP C 1 166 ? 157.324 205.922 217.975 1.00 30.00 ? 166 ASP C OD1 1 
ATOM   2470 O OD2 . ASP C 1 166 ? 157.852 204.247 219.303 1.00 30.00 ? 166 ASP C OD2 1 
ATOM   2471 N N   . ARG C 1 167 ? 153.503 207.939 220.777 1.00 30.00 ? 167 ARG C N   1 
ATOM   2472 C CA  . ARG C 1 167 ? 152.169 208.186 221.382 1.00 30.00 ? 167 ARG C CA  1 
ATOM   2473 C C   . ARG C 1 167 ? 151.538 209.434 220.762 1.00 30.00 ? 167 ARG C C   1 
ATOM   2474 O O   . ARG C 1 167 ? 150.310 209.425 220.576 1.00 30.00 ? 167 ARG C O   1 
ATOM   2475 C CB  . ARG C 1 167 ? 152.318 208.369 222.890 1.00 30.00 ? 167 ARG C CB  1 
ATOM   2476 C CG  . ARG C 1 167 ? 152.971 207.191 223.595 1.00 30.00 ? 167 ARG C CG  1 
ATOM   2477 C CD  . ARG C 1 167 ? 153.055 207.444 225.084 1.00 30.00 ? 167 ARG C CD  1 
ATOM   2478 N NE  . ARG C 1 167 ? 153.722 208.714 225.328 1.00 30.00 ? 167 ARG C NE  1 
ATOM   2479 C CZ  . ARG C 1 167 ? 153.159 209.784 225.878 1.00 30.00 ? 167 ARG C CZ  1 
ATOM   2480 N NH1 . ARG C 1 167 ? 151.852 209.852 226.067 1.00 30.00 ? 167 ARG C NH1 1 
ATOM   2481 N NH2 . ARG C 1 167 ? 153.907 210.827 226.178 1.00 30.00 ? 167 ARG C NH2 1 
ATOM   2482 N N   . PHE C 1 168 ? 152.334 210.464 220.452 1.00 30.00 ? 168 PHE C N   1 
ATOM   2483 C CA  . PHE C 1 168 ? 151.829 211.710 219.821 1.00 30.00 ? 168 PHE C CA  1 
ATOM   2484 C C   . PHE C 1 168 ? 151.220 211.352 218.470 1.00 30.00 ? 168 PHE C C   1 
ATOM   2485 O O   . PHE C 1 168 ? 150.102 211.805 218.189 1.00 30.00 ? 168 PHE C O   1 
ATOM   2486 C CB  . PHE C 1 168 ? 152.943 212.731 219.590 1.00 30.00 ? 168 PHE C CB  1 
ATOM   2487 C CG  . PHE C 1 168 ? 152.584 213.783 218.571 1.00 30.00 ? 168 PHE C CG  1 
ATOM   2488 C CD1 . PHE C 1 168 ? 151.504 214.625 218.769 1.00 30.00 ? 168 PHE C CD1 1 
ATOM   2489 C CD2 . PHE C 1 168 ? 153.294 213.895 217.389 1.00 30.00 ? 168 PHE C CD2 1 
ATOM   2490 C CE1 . PHE C 1 168 ? 151.163 215.574 217.819 1.00 30.00 ? 168 PHE C CE1 1 
ATOM   2491 C CE2 . PHE C 1 168 ? 152.955 214.848 216.442 1.00 30.00 ? 168 PHE C CE2 1 
ATOM   2492 C CZ  . PHE C 1 168 ? 151.891 215.686 216.660 1.00 30.00 ? 168 PHE C CZ  1 
ATOM   2493 N N   . TYR C 1 169 ? 151.919 210.539 217.682 1.00 30.00 ? 169 TYR C N   1 
ATOM   2494 C CA  . TYR C 1 169 ? 151.459 210.118 216.337 1.00 30.00 ? 169 TYR C CA  1 
ATOM   2495 C C   . TYR C 1 169 ? 150.233 209.214 216.451 1.00 30.00 ? 169 TYR C C   1 
ATOM   2496 O O   . TYR C 1 169 ? 149.302 209.385 215.649 1.00 30.00 ? 169 TYR C O   1 
ATOM   2497 C CB  . TYR C 1 169 ? 152.587 209.378 215.626 1.00 30.00 ? 169 TYR C CB  1 
ATOM   2498 C CG  . TYR C 1 169 ? 153.648 210.259 215.021 1.00 30.00 ? 169 TYR C CG  1 
ATOM   2499 C CD1 . TYR C 1 169 ? 154.376 211.143 215.797 1.00 30.00 ? 169 TYR C CD1 1 
ATOM   2500 C CD2 . TYR C 1 169 ? 153.919 210.216 213.664 1.00 30.00 ? 169 TYR C CD2 1 
ATOM   2501 C CE1 . TYR C 1 169 ? 155.346 211.960 215.244 1.00 30.00 ? 169 TYR C CE1 1 
ATOM   2502 C CE2 . TYR C 1 169 ? 154.890 211.023 213.095 1.00 30.00 ? 169 TYR C CE2 1 
ATOM   2503 C CZ  . TYR C 1 169 ? 155.607 211.898 213.890 1.00 30.00 ? 169 TYR C CZ  1 
ATOM   2504 O OH  . TYR C 1 169 ? 156.574 212.709 213.354 1.00 30.00 ? 169 TYR C OH  1 
ATOM   2505 N N   . LYS C 1 170 ? 150.237 208.280 217.403 1.00 30.00 ? 170 LYS C N   1 
ATOM   2506 C CA  . LYS C 1 170 ? 149.119 207.317 217.582 1.00 30.00 ? 170 LYS C CA  1 
ATOM   2507 C C   . LYS C 1 170 ? 147.874 208.092 218.013 1.00 30.00 ? 170 LYS C C   1 
ATOM   2508 O O   . LYS C 1 170 ? 146.789 207.788 217.484 1.00 30.00 ? 170 LYS C O   1 
ATOM   2509 C CB  . LYS C 1 170 ? 149.521 206.258 218.609 1.00 30.00 ? 170 LYS C CB  1 
ATOM   2510 C CG  . LYS C 1 170 ? 148.528 205.124 218.809 1.00 30.00 ? 170 LYS C CG  1 
ATOM   2511 C CD  . LYS C 1 170 ? 148.261 204.339 217.549 1.00 30.00 ? 170 LYS C CD  1 
ATOM   2512 C CE  . LYS C 1 170 ? 147.439 203.092 217.787 1.00 30.00 ? 170 LYS C CE  1 
ATOM   2513 N NZ  . LYS C 1 170 ? 148.188 202.085 218.574 1.00 30.00 ? 170 LYS C NZ  1 
ATOM   2514 N N   . SER C 1 171 ? 148.020 209.053 218.928 1.00 30.00 ? 171 SER C N   1 
ATOM   2515 C CA  . SER C 1 171 ? 146.899 209.902 219.409 1.00 30.00 ? 171 SER C CA  1 
ATOM   2516 C C   . SER C 1 171 ? 146.472 210.850 218.290 1.00 30.00 ? 171 SER C C   1 
ATOM   2517 O O   . SER C 1 171 ? 145.265 211.089 218.164 1.00 30.00 ? 171 SER C O   1 
ATOM   2518 C CB  . SER C 1 171 ? 147.295 210.647 220.642 1.00 30.00 ? 171 SER C CB  1 
ATOM   2519 O OG  . SER C 1 171 ? 147.469 209.749 221.725 1.00 30.00 ? 171 SER C OG  1 
ATOM   2520 N N   . LEU C 1 172 ? 147.424 211.367 217.513 1.00 30.00 ? 172 LEU C N   1 
ATOM   2521 C CA  . LEU C 1 172 ? 147.132 212.249 216.355 1.00 30.00 ? 172 LEU C CA  1 
ATOM   2522 C C   . LEU C 1 172 ? 146.289 211.438 215.377 1.00 30.00 ? 172 LEU C C   1 
ATOM   2523 O O   . LEU C 1 172 ? 145.319 211.996 214.830 1.00 30.00 ? 172 LEU C O   1 
ATOM   2524 C CB  . LEU C 1 172 ? 148.474 212.682 215.755 1.00 30.00 ? 172 LEU C CB  1 
ATOM   2525 C CG  . LEU C 1 172 ? 148.460 213.329 214.373 1.00 30.00 ? 172 LEU C CG  1 
ATOM   2526 C CD1 . LEU C 1 172 ? 149.682 214.214 214.200 1.00 30.00 ? 172 LEU C CD1 1 
ATOM   2527 C CD2 . LEU C 1 172 ? 148.435 212.277 213.277 1.00 30.00 ? 172 LEU C CD2 1 
ATOM   2528 N N   . ARG C 1 173 ? 146.606 210.152 215.223 1.00 30.00 ? 173 ARG C N   1 
ATOM   2529 C CA  . ARG C 1 173 ? 145.882 209.256 214.290 1.00 30.00 ? 173 ARG C CA  1 
ATOM   2530 C C   . ARG C 1 173 ? 144.495 208.990 214.872 1.00 30.00 ? 173 ARG C C   1 
ATOM   2531 O O   . ARG C 1 173 ? 143.548 208.892 214.076 1.00 30.00 ? 173 ARG C O   1 
ATOM   2532 C CB  . ARG C 1 173 ? 146.688 207.970 214.105 1.00 30.00 ? 173 ARG C CB  1 
ATOM   2533 C CG  . ARG C 1 173 ? 146.319 207.184 212.857 1.00 30.00 ? 173 ARG C CG  1 
ATOM   2534 C CD  . ARG C 1 173 ? 146.639 207.971 211.601 1.00 30.00 ? 173 ARG C CD  1 
ATOM   2535 N NE  . ARG C 1 173 ? 146.513 207.174 210.390 1.00 30.00 ? 173 ARG C NE  1 
ATOM   2536 C CZ  . ARG C 1 173 ? 146.752 207.618 209.160 1.00 30.00 ? 173 ARG C CZ  1 
ATOM   2537 N NH1 . ARG C 1 173 ? 146.938 208.906 208.931 1.00 30.00 ? 173 ARG C NH1 1 
ATOM   2538 N NH2 . ARG C 1 173 ? 146.793 206.765 208.153 1.00 30.00 ? 173 ARG C NH2 1 
ATOM   2539 N N   . ALA C 1 174 ? 144.372 208.885 216.197 1.00 30.00 ? 174 ALA C N   1 
ATOM   2540 C CA  . ALA C 1 174 ? 143.069 208.717 216.881 1.00 30.00 ? 174 ALA C CA  1 
ATOM   2541 C C   . ALA C 1 174 ? 142.269 210.008 216.709 1.00 30.00 ? 174 ALA C C   1 
ATOM   2542 O O   . ALA C 1 174 ? 141.033 209.917 216.590 1.00 30.00 ? 174 ALA C O   1 
ATOM   2543 C CB  . ALA C 1 174 ? 143.288 208.393 218.331 1.00 30.00 ? 174 ALA C CB  1 
ATOM   2544 N N   . GLU C 1 175 ? 142.943 211.161 216.719 1.00 30.00 ? 175 GLU C N   1 
ATOM   2545 C CA  . GLU C 1 175 ? 142.297 212.482 216.505 1.00 30.00 ? 175 GLU C CA  1 
ATOM   2546 C C   . GLU C 1 175 ? 141.938 212.613 215.026 1.00 30.00 ? 175 GLU C C   1 
ATOM   2547 O O   . GLU C 1 175 ? 141.135 213.508 214.699 1.00 30.00 ? 175 GLU C O   1 
ATOM   2548 C CB  . GLU C 1 175 ? 143.233 213.614 216.917 1.00 30.00 ? 175 GLU C CB  1 
ATOM   2549 C CG  . GLU C 1 175 ? 143.267 213.866 218.404 1.00 30.00 ? 175 GLU C CG  1 
ATOM   2550 C CD  . GLU C 1 175 ? 144.073 215.095 218.776 1.00 30.00 ? 175 GLU C CD  1 
ATOM   2551 O OE1 . GLU C 1 175 ? 144.648 215.717 217.864 1.00 30.00 ? 175 GLU C OE1 1 
ATOM   2552 O OE2 . GLU C 1 175 ? 144.084 215.450 219.964 1.00 30.00 ? 175 GLU C OE2 1 
ATOM   2553 N N   . GLN C 1 176 ? 142.508 211.764 214.170 1.00 30.00 ? 176 GLN C N   1 
ATOM   2554 C CA  . GLN C 1 176 ? 142.207 211.770 212.718 1.00 30.00 ? 176 GLN C CA  1 
ATOM   2555 C C   . GLN C 1 176 ? 142.444 213.183 212.183 1.00 30.00 ? 176 GLN C C   1 
ATOM   2556 O O   . GLN C 1 176 ? 141.480 213.782 211.670 1.00 30.00 ? 176 GLN C O   1 
ATOM   2557 C CB  . GLN C 1 176 ? 140.768 211.303 212.500 1.00 30.00 ? 176 GLN C CB  1 
ATOM   2558 C CG  . GLN C 1 176 ? 140.429 209.982 213.175 1.00 30.00 ? 176 GLN C CG  1 
ATOM   2559 C CD  . GLN C 1 176 ? 141.162 208.794 212.603 1.00 30.00 ? 176 GLN C CD  1 
ATOM   2560 O OE1 . GLN C 1 176 ? 141.938 208.904 211.657 1.00 30.00 ? 176 GLN C OE1 1 
ATOM   2561 N NE2 . GLN C 1 176 ? 140.912 207.631 213.181 1.00 30.00 ? 176 GLN C NE2 1 
ATOM   2562 N N   . THR C 1 177 ? 143.674 213.695 212.280 1.00 30.00 ? 177 THR C N   1 
ATOM   2563 C CA  . THR C 1 177 ? 144.046 215.056 211.802 1.00 30.00 ? 177 THR C CA  1 
ATOM   2564 C C   . THR C 1 177 ? 144.368 214.947 210.305 1.00 30.00 ? 177 THR C C   1 
ATOM   2565 O O   . THR C 1 177 ? 144.323 213.807 209.801 1.00 30.00 ? 177 THR C O   1 
ATOM   2566 C CB  . THR C 1 177 ? 145.175 215.602 212.690 1.00 30.00 ? 177 THR C CB  1 
ATOM   2567 O OG1 . THR C 1 177 ? 144.765 215.467 214.051 1.00 30.00 ? 177 THR C OG1 1 
ATOM   2568 C CG2 . THR C 1 177 ? 145.535 217.046 212.416 1.00 30.00 ? 177 THR C CG2 1 
ATOM   2569 N N   . ASP C 1 178 ? 144.614 216.062 209.604 1.00 30.00 ? 178 ASP C N   1 
ATOM   2570 C CA  . ASP C 1 178 ? 144.969 216.076 208.157 1.00 30.00 ? 178 ASP C CA  1 
ATOM   2571 C C   . ASP C 1 178 ? 146.440 216.466 208.016 1.00 30.00 ? 178 ASP C C   1 
ATOM   2572 O O   . ASP C 1 178 ? 146.883 217.294 208.811 1.00 30.00 ? 178 ASP C O   1 
ATOM   2573 C CB  . ASP C 1 178 ? 144.085 217.044 207.373 1.00 30.00 ? 178 ASP C CB  1 
ATOM   2574 C CG  . ASP C 1 178 ? 142.602 216.804 207.578 1.00 30.00 ? 178 ASP C CG  1 
ATOM   2575 O OD1 . ASP C 1 178 ? 142.143 215.688 207.271 1.00 30.00 ? 178 ASP C OD1 1 
ATOM   2576 O OD2 . ASP C 1 178 ? 141.922 217.735 208.046 1.00 30.00 ? 178 ASP C OD2 1 
ATOM   2577 N N   . PRO C 1 179 ? 147.187 216.015 206.984 1.00 30.00 ? 179 PRO C N   1 
ATOM   2578 C CA  . PRO C 1 179 ? 148.635 216.269 206.917 1.00 30.00 ? 179 PRO C CA  1 
ATOM   2579 C C   . PRO C 1 179 ? 149.005 217.753 207.011 1.00 30.00 ? 179 PRO C C   1 
ATOM   2580 O O   . PRO C 1 179 ? 149.963 218.046 207.690 1.00 30.00 ? 179 PRO C O   1 
ATOM   2581 C CB  . PRO C 1 179 ? 149.036 215.750 205.529 1.00 30.00 ? 179 PRO C CB  1 
ATOM   2582 C CG  . PRO C 1 179 ? 147.968 214.730 205.195 1.00 30.00 ? 179 PRO C CG  1 
ATOM   2583 C CD  . PRO C 1 179 ? 146.701 215.273 205.821 1.00 30.00 ? 179 PRO C CD  1 
ATOM   2584 N N   . ALA C 1 180 ? 148.269 218.641 206.340 1.00 30.00 ? 180 ALA C N   1 
ATOM   2585 C CA  . ALA C 1 180 ? 148.506 220.102 206.402 1.00 30.00 ? 180 ALA C CA  1 
ATOM   2586 C C   . ALA C 1 180 ? 148.211 220.588 207.821 1.00 30.00 ? 180 ALA C C   1 
ATOM   2587 O O   . ALA C 1 180 ? 149.002 221.400 208.340 1.00 30.00 ? 180 ALA C O   1 
ATOM   2588 C CB  . ALA C 1 180 ? 147.628 220.792 205.398 1.00 30.00 ? 180 ALA C CB  1 
ATOM   2589 N N   . VAL C 1 181 ? 147.130 220.097 208.429 1.00 30.00 ? 181 VAL C N   1 
ATOM   2590 C CA  . VAL C 1 181 ? 146.721 220.474 209.813 1.00 30.00 ? 181 VAL C CA  1 
ATOM   2591 C C   . VAL C 1 181 ? 147.742 219.892 210.790 1.00 30.00 ? 181 VAL C C   1 
ATOM   2592 O O   . VAL C 1 181 ? 147.997 220.540 211.824 1.00 30.00 ? 181 VAL C O   1 
ATOM   2593 C CB  . VAL C 1 181 ? 145.306 219.950 210.119 1.00 30.00 ? 181 VAL C CB  1 
ATOM   2594 C CG1 . VAL C 1 181 ? 144.858 220.307 211.527 1.00 30.00 ? 181 VAL C CG1 1 
ATOM   2595 C CG2 . VAL C 1 181 ? 144.286 220.433 209.102 1.00 30.00 ? 181 VAL C CG2 1 
ATOM   2596 N N   . LYS C 1 182 ? 148.326 218.740 210.463 1.00 30.00 ? 182 LYS C N   1 
ATOM   2597 C CA  . LYS C 1 182 ? 149.252 218.018 211.369 1.00 30.00 ? 182 LYS C CA  1 
ATOM   2598 C C   . LYS C 1 182 ? 150.632 218.660 211.419 1.00 30.00 ? 182 LYS C C   1 
ATOM   2599 O O   . LYS C 1 182 ? 151.254 218.427 212.397 1.00 30.00 ? 182 LYS C O   1 
ATOM   2600 C CB  . LYS C 1 182 ? 149.484 216.601 210.852 1.00 30.00 ? 182 LYS C CB  1 
ATOM   2601 C CG  . LYS C 1 182 ? 148.319 215.636 210.994 1.00 30.00 ? 182 LYS C CG  1 
ATOM   2602 C CD  . LYS C 1 182 ? 148.561 214.335 210.275 1.00 30.00 ? 182 LYS C CD  1 
ATOM   2603 C CE  . LYS C 1 182 ? 147.306 213.504 210.149 1.00 30.00 ? 182 LYS C CE  1 
ATOM   2604 N NZ  . LYS C 1 182 ? 147.602 212.113 209.740 1.00 30.00 ? 182 LYS C NZ  1 
ATOM   2605 N N   . ASN C 1 183 ? 151.094 219.336 210.372 1.00 30.00 ? 183 ASN C N   1 
ATOM   2606 C CA  . ASN C 1 183 ? 152.433 219.967 210.255 1.00 30.00 ? 183 ASN C CA  1 
ATOM   2607 C C   . ASN C 1 183 ? 152.606 220.993 211.379 1.00 30.00 ? 183 ASN C C   1 
ATOM   2608 O O   . ASN C 1 183 ? 153.736 221.103 211.880 1.00 30.00 ? 183 ASN C O   1 
ATOM   2609 C CB  . ASN C 1 183 ? 152.646 220.559 208.862 1.00 30.00 ? 183 ASN C CB  1 
ATOM   2610 C CG  . ASN C 1 183 ? 152.821 219.501 207.794 1.00 30.00 ? 183 ASN C CG  1 
ATOM   2611 O OD1 . ASN C 1 183 ? 152.826 218.308 208.087 1.00 30.00 ? 183 ASN C OD1 1 
ATOM   2612 N ND2 . ASN C 1 183 ? 152.982 219.930 206.555 1.00 30.00 ? 183 ASN C ND2 1 
ATOM   2613 N N   . TRP C 1 184 ? 151.550 221.709 211.778 1.00 30.00 ? 184 TRP C N   1 
ATOM   2614 C CA  . TRP C 1 184 ? 151.654 222.650 212.923 1.00 30.00 ? 184 TRP C CA  1 
ATOM   2615 C C   . TRP C 1 184 ? 152.007 221.880 214.198 1.00 30.00 ? 184 TRP C C   1 
ATOM   2616 O O   . TRP C 1 184 ? 153.105 222.105 214.713 1.00 30.00 ? 184 TRP C O   1 
ATOM   2617 C CB  . TRP C 1 184 ? 150.351 223.415 213.161 1.00 30.00 ? 184 TRP C CB  1 
ATOM   2618 C CG  . TRP C 1 184 ? 150.440 224.181 214.444 1.00 30.00 ? 184 TRP C CG  1 
ATOM   2619 C CD1 . TRP C 1 184 ? 151.228 225.265 214.693 1.00 30.00 ? 184 TRP C CD1 1 
ATOM   2620 C CD2 . TRP C 1 184 ? 149.869 223.809 215.711 1.00 30.00 ? 184 TRP C CD2 1 
ATOM   2621 N NE1 . TRP C 1 184 ? 151.115 225.647 216.002 1.00 30.00 ? 184 TRP C NE1 1 
ATOM   2622 C CE2 . TRP C 1 184 ? 150.294 224.768 216.654 1.00 30.00 ? 184 TRP C CE2 1 
ATOM   2623 C CE3 . TRP C 1 184 ? 149.011 222.788 216.132 1.00 30.00 ? 184 TRP C CE3 1 
ATOM   2624 C CZ2 . TRP C 1 184 ? 149.886 224.737 217.985 1.00 30.00 ? 184 TRP C CZ2 1 
ATOM   2625 C CZ3 . TRP C 1 184 ? 148.611 222.756 217.449 1.00 30.00 ? 184 TRP C CZ3 1 
ATOM   2626 C CH2 . TRP C 1 184 ? 149.042 223.719 218.361 1.00 30.00 ? 184 TRP C CH2 1 
ATOM   2627 N N   . MET C 1 185 ? 151.092 221.055 214.713 1.00 30.00 ? 185 MET C N   1 
ATOM   2628 C CA  . MET C 1 185 ? 151.323 220.234 215.933 1.00 30.00 ? 185 MET C CA  1 
ATOM   2629 C C   . MET C 1 185 ? 152.595 219.407 215.746 1.00 30.00 ? 185 MET C C   1 
ATOM   2630 O O   . MET C 1 185 ? 153.350 219.253 216.716 1.00 30.00 ? 185 MET C O   1 
ATOM   2631 C CB  . MET C 1 185 ? 150.152 219.281 216.198 1.00 30.00 ? 185 MET C CB  1 
ATOM   2632 C CG  . MET C 1 185 ? 149.655 218.550 214.961 1.00 30.00 ? 185 MET C CG  1 
ATOM   2633 S SD  . MET C 1 185 ? 148.042 217.788 215.205 1.00 30.00 ? 185 MET C SD  1 
ATOM   2634 C CE  . MET C 1 185 ? 146.976 219.170 214.807 1.00 30.00 ? 185 MET C CE  1 
ATOM   2635 N N   . THR C 1 186 ? 152.840 218.896 214.543 1.00 30.00 ? 186 THR C N   1 
ATOM   2636 C CA  . THR C 1 186 ? 154.002 218.009 214.283 1.00 30.00 ? 186 THR C CA  1 
ATOM   2637 C C   . THR C 1 186 ? 155.295 218.786 214.495 1.00 30.00 ? 186 THR C C   1 
ATOM   2638 O O   . THR C 1 186 ? 156.197 218.226 215.129 1.00 30.00 ? 186 THR C O   1 
ATOM   2639 C CB  . THR C 1 186 ? 153.970 217.432 212.863 1.00 30.00 ? 186 THR C CB  1 
ATOM   2640 O OG1 . THR C 1 186 ? 152.915 216.473 212.796 1.00 30.00 ? 186 THR C OG1 1 
ATOM   2641 C CG2 . THR C 1 186 ? 155.262 216.755 212.463 1.00 30.00 ? 186 THR C CG2 1 
ATOM   2642 N N   . GLN C 1 187 ? 155.368 220.026 214.017 1.00 30.00 ? 187 GLN C N   1 
ATOM   2643 C CA  . GLN C 1 187 ? 156.612 220.835 214.077 1.00 30.00 ? 187 GLN C CA  1 
ATOM   2644 C C   . GLN C 1 187 ? 156.544 221.799 215.265 1.00 30.00 ? 187 GLN C C   1 
ATOM   2645 O O   . GLN C 1 187 ? 157.516 222.560 215.441 1.00 30.00 ? 187 GLN C O   1 
ATOM   2646 C CB  . GLN C 1 187 ? 156.772 221.582 212.751 1.00 30.00 ? 187 GLN C CB  1 
ATOM   2647 C CG  . GLN C 1 187 ? 156.740 220.699 211.508 1.00 30.00 ? 187 GLN C CG  1 
ATOM   2648 C CD  . GLN C 1 187 ? 158.005 219.908 211.283 1.00 30.00 ? 187 GLN C CD  1 
ATOM   2649 O OE1 . GLN C 1 187 ? 158.697 220.088 210.283 1.00 30.00 ? 187 GLN C OE1 1 
ATOM   2650 N NE2 . GLN C 1 187 ? 158.320 219.014 212.205 1.00 30.00 ? 187 GLN C NE2 1 
ATOM   2651 N N   . THR C 1 188 ? 155.458 221.774 216.045 1.00 30.00 ? 188 THR C N   1 
ATOM   2652 C CA  . THR C 1 188 ? 155.258 222.686 217.203 1.00 30.00 ? 188 THR C CA  1 
ATOM   2653 C C   . THR C 1 188 ? 154.973 221.905 218.485 1.00 30.00 ? 188 THR C C   1 
ATOM   2654 O O   . THR C 1 188 ? 155.767 222.057 219.417 1.00 30.00 ? 188 THR C O   1 
ATOM   2655 C CB  . THR C 1 188 ? 154.090 223.643 216.953 1.00 30.00 ? 188 THR C CB  1 
ATOM   2656 O OG1 . THR C 1 188 ? 154.339 224.301 215.712 1.00 30.00 ? 188 THR C OG1 1 
ATOM   2657 C CG2 . THR C 1 188 ? 153.912 224.662 218.056 1.00 30.00 ? 188 THR C CG2 1 
ATOM   2658 N N   . LEU C 1 189 ? 153.879 221.141 218.551 1.00 30.00 ? 189 LEU C N   1 
ATOM   2659 C CA  . LEU C 1 189 ? 153.462 220.412 219.780 1.00 30.00 ? 189 LEU C CA  1 
ATOM   2660 C C   . LEU C 1 189 ? 154.526 219.388 220.188 1.00 30.00 ? 189 LEU C C   1 
ATOM   2661 O O   . LEU C 1 189 ? 154.711 219.207 221.405 1.00 30.00 ? 189 LEU C O   1 
ATOM   2662 C CB  . LEU C 1 189 ? 152.123 219.723 219.506 1.00 30.00 ? 189 LEU C CB  1 
ATOM   2663 C CG  . LEU C 1 189 ? 151.416 219.124 220.720 1.00 30.00 ? 189 LEU C CG  1 
ATOM   2664 C CD1 . LEU C 1 189 ? 150.855 220.211 221.619 1.00 30.00 ? 189 LEU C CD1 1 
ATOM   2665 C CD2 . LEU C 1 189 ? 150.308 218.187 220.280 1.00 30.00 ? 189 LEU C CD2 1 
ATOM   2666 N N   . LEU C 1 190 ? 155.198 218.745 219.229 1.00 30.00 ? 190 LEU C N   1 
ATOM   2667 C CA  . LEU C 1 190 ? 156.197 217.686 219.538 1.00 30.00 ? 190 LEU C CA  1 
ATOM   2668 C C   . LEU C 1 190 ? 157.301 218.272 220.418 1.00 30.00 ? 190 LEU C C   1 
ATOM   2669 O O   . LEU C 1 190 ? 157.617 217.657 221.450 1.00 30.00 ? 190 LEU C O   1 
ATOM   2670 C CB  . LEU C 1 190 ? 156.782 217.131 218.237 1.00 30.00 ? 190 LEU C CB  1 
ATOM   2671 C CG  . LEU C 1 190 ? 156.109 215.880 217.673 1.00 30.00 ? 190 LEU C CG  1 
ATOM   2672 C CD1 . LEU C 1 190 ? 156.869 215.345 216.472 1.00 30.00 ? 190 LEU C CD1 1 
ATOM   2673 C CD2 . LEU C 1 190 ? 156.000 214.794 218.733 1.00 30.00 ? 190 LEU C CD2 1 
ATOM   2674 N N   . ILE C 1 191 ? 157.840 219.431 220.047 1.00 30.00 ? 191 ILE C N   1 
ATOM   2675 C CA  . ILE C 1 191 ? 158.914 220.102 220.833 1.00 30.00 ? 191 ILE C CA  1 
ATOM   2676 C C   . ILE C 1 191 ? 158.275 220.733 222.069 1.00 30.00 ? 191 ILE C C   1 
ATOM   2677 O O   . ILE C 1 191 ? 158.889 220.660 223.144 1.00 30.00 ? 191 ILE C O   1 
ATOM   2678 C CB  . ILE C 1 191 ? 159.648 221.160 219.989 1.00 30.00 ? 191 ILE C CB  1 
ATOM   2679 C CG1 . ILE C 1 191 ? 159.901 220.686 218.555 1.00 30.00 ? 191 ILE C CG1 1 
ATOM   2680 C CG2 . ILE C 1 191 ? 160.928 221.579 220.694 1.00 30.00 ? 191 ILE C CG2 1 
ATOM   2681 C CD1 . ILE C 1 191 ? 160.685 221.656 217.707 1.00 30.00 ? 191 ILE C CD1 1 
ATOM   2682 N N   . GLN C 1 192 ? 157.070 221.287 221.933 1.00 30.00 ? 192 GLN C N   1 
ATOM   2683 C CA  . GLN C 1 192 ? 156.395 222.027 223.032 1.00 30.00 ? 192 GLN C CA  1 
ATOM   2684 C C   . GLN C 1 192 ? 156.126 221.106 224.225 1.00 30.00 ? 192 GLN C C   1 
ATOM   2685 O O   . GLN C 1 192 ? 156.320 221.572 225.362 1.00 30.00 ? 192 GLN C O   1 
ATOM   2686 C CB  . GLN C 1 192 ? 155.106 222.643 222.490 1.00 30.00 ? 192 GLN C CB  1 
ATOM   2687 C CG  . GLN C 1 192 ? 154.433 223.593 223.465 1.00 30.00 ? 192 GLN C CG  1 
ATOM   2688 C CD  . GLN C 1 192 ? 153.420 222.897 224.335 1.00 30.00 ? 192 GLN C CD  1 
ATOM   2689 O OE1 . GLN C 1 192 ? 152.404 222.401 223.854 1.00 30.00 ? 192 GLN C OE1 1 
ATOM   2690 N NE2 . GLN C 1 192 ? 153.671 222.891 225.633 1.00 30.00 ? 192 GLN C NE2 1 
ATOM   2691 N N   . ASN C 1 193 ? 155.714 219.858 223.990 1.00 30.00 ? 193 ASN C N   1 
ATOM   2692 C CA  . ASN C 1 193 ? 155.353 218.905 225.072 1.00 30.00 ? 193 ASN C CA  1 
ATOM   2693 C C   . ASN C 1 193 ? 156.538 217.987 225.364 1.00 30.00 ? 193 ASN C C   1 
ATOM   2694 O O   . ASN C 1 193 ? 156.403 217.123 226.253 1.00 30.00 ? 193 ASN C O   1 
ATOM   2695 C CB  . ASN C 1 193 ? 154.119 218.093 224.690 1.00 30.00 ? 193 ASN C CB  1 
ATOM   2696 C CG  . ASN C 1 193 ? 152.847 218.908 224.689 1.00 30.00 ? 193 ASN C CG  1 
ATOM   2697 O OD1 . ASN C 1 193 ? 152.851 220.067 225.089 1.00 30.00 ? 193 ASN C OD1 1 
ATOM   2698 N ND2 . ASN C 1 193 ? 151.745 218.294 224.290 1.00 30.00 ? 193 ASN C ND2 1 
ATOM   2699 N N   . ALA C 1 194 ? 157.658 218.170 224.665 1.00 30.00 ? 194 ALA C N   1 
ATOM   2700 C CA  . ALA C 1 194 ? 158.886 217.387 224.913 1.00 30.00 ? 194 ALA C CA  1 
ATOM   2701 C C   . ALA C 1 194 ? 159.364 217.707 226.329 1.00 30.00 ? 194 ALA C C   1 
ATOM   2702 O O   . ALA C 1 194 ? 159.191 218.868 226.752 1.00 30.00 ? 194 ALA C O   1 
ATOM   2703 C CB  . ALA C 1 194 ? 159.937 217.737 223.900 1.00 30.00 ? 194 ALA C CB  1 
ATOM   2704 N N   . ASN C 1 195 ? 159.955 216.739 227.030 1.00 30.00 ? 195 ASN C N   1 
ATOM   2705 C CA  . ASN C 1 195 ? 160.507 216.990 228.386 1.00 30.00 ? 195 ASN C CA  1 
ATOM   2706 C C   . ASN C 1 195 ? 161.588 218.053 228.175 1.00 30.00 ? 195 ASN C C   1 
ATOM   2707 O O   . ASN C 1 195 ? 162.225 218.033 227.108 1.00 30.00 ? 195 ASN C O   1 
ATOM   2708 C CB  . ASN C 1 195 ? 160.938 215.698 229.093 1.00 30.00 ? 195 ASN C CB  1 
ATOM   2709 C CG  . ASN C 1 195 ? 161.965 214.888 228.335 1.00 30.00 ? 195 ASN C CG  1 
ATOM   2710 O OD1 . ASN C 1 195 ? 162.394 215.279 227.256 1.00 30.00 ? 195 ASN C OD1 1 
ATOM   2711 N ND2 . ASN C 1 195 ? 162.360 213.754 228.887 1.00 30.00 ? 195 ASN C ND2 1 
ATOM   2712 N N   . PRO C 1 196 ? 161.830 218.980 229.123 1.00 30.00 ? 196 PRO C N   1 
ATOM   2713 C CA  . PRO C 1 196 ? 162.742 220.109 228.878 1.00 30.00 ? 196 PRO C CA  1 
ATOM   2714 C C   . PRO C 1 196 ? 164.163 219.732 228.440 1.00 30.00 ? 196 PRO C C   1 
ATOM   2715 O O   . PRO C 1 196 ? 164.675 220.393 227.558 1.00 30.00 ? 196 PRO C O   1 
ATOM   2716 C CB  . PRO C 1 196 ? 162.825 220.774 230.258 1.00 30.00 ? 196 PRO C CB  1 
ATOM   2717 C CG  . PRO C 1 196 ? 161.522 220.410 230.926 1.00 30.00 ? 196 PRO C CG  1 
ATOM   2718 C CD  . PRO C 1 196 ? 161.257 218.995 230.468 1.00 30.00 ? 196 PRO C CD  1 
ATOM   2719 N N   . ASP C 1 197 ? 164.748 218.688 229.027 1.00 30.00 ? 197 ASP C N   1 
ATOM   2720 C CA  . ASP C 1 197 ? 166.139 218.261 228.717 1.00 30.00 ? 197 ASP C CA  1 
ATOM   2721 C C   . ASP C 1 197 ? 166.247 217.920 227.227 1.00 30.00 ? 197 ASP C C   1 
ATOM   2722 O O   . ASP C 1 197 ? 167.334 218.149 226.665 1.00 30.00 ? 197 ASP C O   1 
ATOM   2723 C CB  . ASP C 1 197 ? 166.573 217.100 229.614 1.00 30.00 ? 197 ASP C CB  1 
ATOM   2724 C CG  . ASP C 1 197 ? 165.657 215.888 229.584 1.00 30.00 ? 197 ASP C CG  1 
ATOM   2725 O OD1 . ASP C 1 197 ? 164.635 215.938 228.880 1.00 30.00 ? 197 ASP C OD1 1 
ATOM   2726 O OD2 . ASP C 1 197 ? 165.981 214.898 230.265 1.00 30.00 ? 197 ASP C OD2 1 
ATOM   2727 N N   . CYS C 1 198 ? 165.194 217.368 226.618 1.00 30.00 ? 198 CYS C N   1 
ATOM   2728 C CA  . CYS C 1 198 ? 165.171 216.999 225.177 1.00 30.00 ? 198 CYS C CA  1 
ATOM   2729 C C   . CYS C 1 198 ? 164.562 218.124 224.340 1.00 30.00 ? 198 CYS C C   1 
ATOM   2730 O O   . CYS C 1 198 ? 164.924 218.236 223.157 1.00 30.00 ? 198 CYS C O   1 
ATOM   2731 C CB  . CYS C 1 198 ? 164.320 215.761 224.947 1.00 30.00 ? 198 CYS C CB  1 
ATOM   2732 S SG  . CYS C 1 198 ? 164.135 215.334 223.200 1.00 30.00 ? 198 CYS C SG  1 
ATOM   2733 N N   . LYS C 1 199 ? 163.683 218.933 224.928 1.00 30.00 ? 199 LYS C N   1 
ATOM   2734 C CA  . LYS C 1 199 ? 162.989 220.012 224.182 1.00 30.00 ? 199 LYS C CA  1 
ATOM   2735 C C   . LYS C 1 199 ? 164.055 220.941 223.607 1.00 30.00 ? 199 LYS C C   1 
ATOM   2736 O O   . LYS C 1 199 ? 163.980 221.216 222.402 1.00 30.00 ? 199 LYS C O   1 
ATOM   2737 C CB  . LYS C 1 199 ? 162.037 220.767 225.109 1.00 30.00 ? 199 LYS C CB  1 
ATOM   2738 C CG  . LYS C 1 199 ? 161.371 221.976 224.473 1.00 30.00 ? 199 LYS C CG  1 
ATOM   2739 C CD  . LYS C 1 199 ? 160.182 222.481 225.246 1.00 30.00 ? 199 LYS C CD  1 
ATOM   2740 C CE  . LYS C 1 199 ? 159.426 223.562 224.506 1.00 30.00 ? 199 LYS C CE  1 
ATOM   2741 N NZ  . LYS C 1 199 ? 158.223 223.989 225.255 1.00 30.00 ? 199 LYS C NZ  1 
ATOM   2742 N N   . LEU C 1 200 ? 165.050 221.317 224.411 1.00 30.00 ? 200 LEU C N   1 
ATOM   2743 C CA  . LEU C 1 200 ? 166.154 222.218 223.986 1.00 30.00 ? 200 LEU C CA  1 
ATOM   2744 C C   . LEU C 1 200 ? 166.916 221.586 222.821 1.00 30.00 ? 200 LEU C C   1 
ATOM   2745 O O   . LEU C 1 200 ? 167.405 222.343 221.971 1.00 30.00 ? 200 LEU C O   1 
ATOM   2746 C CB  . LEU C 1 200 ? 167.086 222.441 225.179 1.00 30.00 ? 200 LEU C CB  1 
ATOM   2747 C CG  . LEU C 1 200 ? 167.715 221.181 225.774 1.00 30.00 ? 200 LEU C CG  1 
ATOM   2748 C CD1 . LEU C 1 200 ? 169.072 220.887 225.154 1.00 30.00 ? 200 LEU C CD1 1 
ATOM   2749 C CD2 . LEU C 1 200 ? 167.841 221.303 227.282 1.00 30.00 ? 200 LEU C CD2 1 
ATOM   2750 N N   . VAL C 1 201 ? 167.078 220.263 222.821 1.00 30.00 ? 201 VAL C N   1 
ATOM   2751 C CA  . VAL C 1 201 ? 167.825 219.540 221.752 1.00 30.00 ? 201 VAL C CA  1 
ATOM   2752 C C   . VAL C 1 201 ? 167.058 219.704 220.441 1.00 30.00 ? 201 VAL C C   1 
ATOM   2753 O O   . VAL C 1 201 ? 167.713 219.956 219.412 1.00 30.00 ? 201 VAL C O   1 
ATOM   2754 C CB  . VAL C 1 201 ? 168.007 218.058 222.113 1.00 30.00 ? 201 VAL C CB  1 
ATOM   2755 C CG1 . VAL C 1 201 ? 168.736 217.294 221.021 1.00 30.00 ? 201 VAL C CG1 1 
ATOM   2756 C CG2 . VAL C 1 201 ? 168.701 217.876 223.453 1.00 30.00 ? 201 VAL C CG2 1 
ATOM   2757 N N   . LEU C 1 202 ? 165.730 219.567 220.474 1.00 30.00 ? 202 LEU C N   1 
ATOM   2758 C CA  . LEU C 1 202 ? 164.874 219.768 219.275 1.00 30.00 ? 202 LEU C CA  1 
ATOM   2759 C C   . LEU C 1 202 ? 164.945 221.242 218.880 1.00 30.00 ? 202 LEU C C   1 
ATOM   2760 O O   . LEU C 1 202 ? 164.953 221.519 217.666 1.00 30.00 ? 202 LEU C O   1 
ATOM   2761 C CB  . LEU C 1 202 ? 163.439 219.343 219.592 1.00 30.00 ? 202 LEU C CB  1 
ATOM   2762 C CG  . LEU C 1 202 ? 163.149 217.854 219.423 1.00 30.00 ? 202 LEU C CG  1 
ATOM   2763 C CD1 . LEU C 1 202 ? 163.694 217.047 220.584 1.00 30.00 ? 202 LEU C CD1 1 
ATOM   2764 C CD2 . LEU C 1 202 ? 161.663 217.611 219.266 1.00 30.00 ? 202 LEU C CD2 1 
ATOM   2765 N N   . LYS C 1 203 ? 164.990 222.148 219.859 1.00 30.00 ? 203 LYS C N   1 
ATOM   2766 C CA  . LYS C 1 203 ? 165.143 223.599 219.586 1.00 30.00 ? 203 LYS C CA  1 
ATOM   2767 C C   . LYS C 1 203 ? 166.479 223.790 218.870 1.00 30.00 ? 203 LYS C C   1 
ATOM   2768 O O   . LYS C 1 203 ? 166.522 224.581 217.909 1.00 30.00 ? 203 LYS C O   1 
ATOM   2769 C CB  . LYS C 1 203 ? 165.135 224.423 220.877 1.00 30.00 ? 203 LYS C CB  1 
ATOM   2770 C CG  . LYS C 1 203 ? 163.869 224.371 221.720 1.00 30.00 ? 203 LYS C CG  1 
ATOM   2771 C CD  . LYS C 1 203 ? 162.600 224.690 220.972 1.00 30.00 ? 203 LYS C CD  1 
ATOM   2772 C CE  . LYS C 1 203 ? 161.384 224.642 221.870 1.00 30.00 ? 203 LYS C CE  1 
ATOM   2773 N NZ  . LYS C 1 203 ? 160.129 224.811 221.103 1.00 30.00 ? 203 LYS C NZ  1 
ATOM   2774 N N   . GLY C 1 204 ? 167.520 223.083 219.316 1.00 30.00 ? 204 GLY C N   1 
ATOM   2775 C CA  . GLY C 1 204 ? 168.865 223.172 218.718 1.00 30.00 ? 204 GLY C CA  1 
ATOM   2776 C C   . GLY C 1 204 ? 168.826 222.917 217.224 1.00 30.00 ? 204 GLY C C   1 
ATOM   2777 O O   . GLY C 1 204 ? 169.470 223.690 216.489 1.00 30.00 ? 204 GLY C O   1 
ATOM   2778 N N   . LEU C 1 205 ? 168.102 221.886 216.774 1.00 30.00 ? 205 LEU C N   1 
ATOM   2779 C CA  . LEU C 1 205 ? 168.052 221.517 215.334 1.00 30.00 ? 205 LEU C CA  1 
ATOM   2780 C C   . LEU C 1 205 ? 167.476 222.704 214.567 1.00 30.00 ? 205 LEU C C   1 
ATOM   2781 O O   . LEU C 1 205 ? 168.167 223.196 213.653 1.00 30.00 ? 205 LEU C O   1 
ATOM   2782 C CB  . LEU C 1 205 ? 167.165 220.283 215.145 1.00 30.00 ? 205 LEU C CB  1 
ATOM   2783 C CG  . LEU C 1 205 ? 167.601 219.021 215.884 1.00 30.00 ? 205 LEU C CG  1 
ATOM   2784 C CD1 . LEU C 1 205 ? 166.883 217.806 215.331 1.00 30.00 ? 205 LEU C CD1 1 
ATOM   2785 C CD2 . LEU C 1 205 ? 169.105 218.821 215.809 1.00 30.00 ? 205 LEU C CD2 1 
ATOM   2786 N N   . GLY C 1 206 ? 166.274 223.156 214.928 1.00 30.00 ? 206 GLY C N   1 
ATOM   2787 C CA  . GLY C 1 206 ? 165.678 224.365 214.328 1.00 30.00 ? 206 GLY C CA  1 
ATOM   2788 C C   . GLY C 1 206 ? 165.489 224.258 212.832 1.00 30.00 ? 206 GLY C C   1 
ATOM   2789 O O   . GLY C 1 206 ? 165.697 223.158 212.283 1.00 30.00 ? 206 GLY C O   1 
ATOM   2790 N N   . MET C 1 207 ? 165.146 225.369 212.185 1.00 30.00 ? 207 MET C N   1 
ATOM   2791 C CA  . MET C 1 207 ? 165.019 225.426 210.708 1.00 30.00 ? 207 MET C CA  1 
ATOM   2792 C C   . MET C 1 207 ? 164.195 224.236 210.209 1.00 30.00 ? 207 MET C C   1 
ATOM   2793 O O   . MET C 1 207 ? 164.728 223.467 209.391 1.00 30.00 ? 207 MET C O   1 
ATOM   2794 C CB  . MET C 1 207 ? 166.409 225.417 210.065 1.00 30.00 ? 207 MET C CB  1 
ATOM   2795 C CG  . MET C 1 207 ? 167.239 226.648 210.391 1.00 30.00 ? 207 MET C CG  1 
ATOM   2796 S SD  . MET C 1 207 ? 166.460 228.210 209.911 1.00 30.00 ? 207 MET C SD  1 
ATOM   2797 C CE  . MET C 1 207 ? 165.763 228.737 211.475 1.00 30.00 ? 207 MET C CE  1 
ATOM   2798 N N   . ASN C 1 208 ? 162.972 224.056 210.709 1.00 30.00 ? 208 ASN C N   1 
ATOM   2799 C CA  . ASN C 1 208 ? 162.050 222.994 210.216 1.00 30.00 ? 208 ASN C CA  1 
ATOM   2800 C C   . ASN C 1 208 ? 162.809 221.673 210.037 1.00 30.00 ? 208 ASN C C   1 
ATOM   2801 O O   . ASN C 1 208 ? 162.896 221.188 208.899 1.00 30.00 ? 208 ASN C O   1 
ATOM   2802 C CB  . ASN C 1 208 ? 161.313 223.469 208.958 1.00 30.00 ? 208 ASN C CB  1 
ATOM   2803 C CG  . ASN C 1 208 ? 162.214 224.069 207.900 1.00 30.00 ? 208 ASN C CG  1 
ATOM   2804 O OD1 . ASN C 1 208 ? 163.036 223.380 207.301 1.00 30.00 ? 208 ASN C OD1 1 
ATOM   2805 N ND2 . ASN C 1 208 ? 162.032 225.350 207.628 1.00 30.00 ? 208 ASN C ND2 1 
ATOM   2806 N N   . PRO C 1 209 ? 163.327 221.041 211.110 1.00 30.00 ? 209 PRO C N   1 
ATOM   2807 C CA  . PRO C 1 209 ? 164.131 219.829 210.968 1.00 30.00 ? 209 PRO C CA  1 
ATOM   2808 C C   . PRO C 1 209 ? 163.289 218.633 210.508 1.00 30.00 ? 209 PRO C C   1 
ATOM   2809 O O   . PRO C 1 209 ? 162.094 218.683 210.713 1.00 30.00 ? 209 PRO C O   1 
ATOM   2810 C CB  . PRO C 1 209 ? 164.677 219.591 212.384 1.00 30.00 ? 209 PRO C CB  1 
ATOM   2811 C CG  . PRO C 1 209 ? 163.663 220.238 213.299 1.00 30.00 ? 209 PRO C CG  1 
ATOM   2812 C CD  . PRO C 1 209 ? 163.090 221.397 212.510 1.00 30.00 ? 209 PRO C CD  1 
ATOM   2813 N N   . THR C 1 210 ? 163.908 217.605 209.911 1.00 30.00 ? 210 THR C N   1 
ATOM   2814 C CA  . THR C 1 210 ? 163.207 216.376 209.445 1.00 30.00 ? 210 THR C CA  1 
ATOM   2815 C C   . THR C 1 210 ? 163.102 215.438 210.647 1.00 30.00 ? 210 THR C C   1 
ATOM   2816 O O   . THR C 1 210 ? 163.908 215.616 211.580 1.00 30.00 ? 210 THR C O   1 
ATOM   2817 C CB  . THR C 1 210 ? 163.925 215.731 208.254 1.00 30.00 ? 210 THR C CB  1 
ATOM   2818 O OG1 . THR C 1 210 ? 163.089 214.693 207.744 1.00 30.00 ? 210 THR C OG1 1 
ATOM   2819 C CG2 . THR C 1 210 ? 165.278 215.157 208.608 1.00 30.00 ? 210 THR C CG2 1 
ATOM   2820 N N   . LEU C 1 211 ? 162.173 214.478 210.657 1.00 30.00 ? 211 LEU C N   1 
ATOM   2821 C CA  . LEU C 1 211 ? 161.979 213.669 211.885 1.00 30.00 ? 211 LEU C CA  1 
ATOM   2822 C C   . LEU C 1 211 ? 163.285 212.930 212.160 1.00 30.00 ? 211 LEU C C   1 
ATOM   2823 O O   . LEU C 1 211 ? 163.684 212.889 213.312 1.00 30.00 ? 211 LEU C O   1 
ATOM   2824 C CB  . LEU C 1 211 ? 160.811 212.697 211.705 1.00 30.00 ? 211 LEU C CB  1 
ATOM   2825 C CG  . LEU C 1 211 ? 160.607 211.701 212.847 1.00 30.00 ? 211 LEU C CG  1 
ATOM   2826 C CD1 . LEU C 1 211 ? 160.227 212.409 214.136 1.00 30.00 ? 211 LEU C CD1 1 
ATOM   2827 C CD2 . LEU C 1 211 ? 159.550 210.674 212.484 1.00 30.00 ? 211 LEU C CD2 1 
ATOM   2828 N N   . GLU C 1 212 ? 163.912 212.372 211.131 1.00 30.00 ? 212 GLU C N   1 
ATOM   2829 C CA  . GLU C 1 212 ? 165.184 211.627 211.281 1.00 30.00 ? 212 GLU C CA  1 
ATOM   2830 C C   . GLU C 1 212 ? 166.111 212.428 212.190 1.00 30.00 ? 212 GLU C C   1 
ATOM   2831 O O   . GLU C 1 212 ? 166.626 211.831 213.122 1.00 30.00 ? 212 GLU C O   1 
ATOM   2832 C CB  . GLU C 1 212 ? 165.800 211.381 209.905 1.00 30.00 ? 212 GLU C CB  1 
ATOM   2833 C CG  . GLU C 1 212 ? 167.033 210.496 209.934 1.00 30.00 ? 212 GLU C CG  1 
ATOM   2834 C CD  . GLU C 1 212 ? 168.345 211.173 210.290 1.00 30.00 ? 212 GLU C CD  1 
ATOM   2835 O OE1 . GLU C 1 212 ? 168.353 212.401 210.489 1.00 30.00 ? 212 GLU C OE1 1 
ATOM   2836 O OE2 . GLU C 1 212 ? 169.362 210.459 210.375 1.00 30.00 ? 212 GLU C OE2 1 
ATOM   2837 N N   . GLU C 1 213 ? 166.206 213.738 211.995 1.00 30.00 ? 213 GLU C N   1 
ATOM   2838 C CA  . GLU C 1 213 ? 167.145 214.588 212.766 1.00 30.00 ? 213 GLU C CA  1 
ATOM   2839 C C   . GLU C 1 213 ? 166.678 214.698 214.215 1.00 30.00 ? 213 GLU C C   1 
ATOM   2840 O O   . GLU C 1 213 ? 167.521 214.533 215.105 1.00 30.00 ? 213 GLU C O   1 
ATOM   2841 C CB  . GLU C 1 213 ? 167.228 215.969 212.125 1.00 30.00 ? 213 GLU C CB  1 
ATOM   2842 C CG  . GLU C 1 213 ? 167.903 215.956 210.770 1.00 30.00 ? 213 GLU C CG  1 
ATOM   2843 C CD  . GLU C 1 213 ? 167.849 217.276 210.022 1.00 30.00 ? 213 GLU C CD  1 
ATOM   2844 O OE1 . GLU C 1 213 ? 167.258 218.236 210.555 1.00 30.00 ? 213 GLU C OE1 1 
ATOM   2845 O OE2 . GLU C 1 213 ? 168.398 217.340 208.906 1.00 30.00 ? 213 GLU C OE2 1 
ATOM   2846 N N   . MET C 1 214 ? 165.394 214.952 214.449 1.00 30.00 ? 214 MET C N   1 
ATOM   2847 C CA  . MET C 1 214 ? 164.874 215.169 215.824 1.00 30.00 ? 214 MET C CA  1 
ATOM   2848 C C   . MET C 1 214 ? 165.095 213.901 216.646 1.00 30.00 ? 214 MET C C   1 
ATOM   2849 O O   . MET C 1 214 ? 165.486 214.028 217.821 1.00 30.00 ? 214 MET C O   1 
ATOM   2850 C CB  . MET C 1 214 ? 163.385 215.507 215.787 1.00 30.00 ? 214 MET C CB  1 
ATOM   2851 C CG  . MET C 1 214 ? 163.115 216.976 215.539 1.00 30.00 ? 214 MET C CG  1 
ATOM   2852 S SD  . MET C 1 214 ? 161.358 217.425 215.547 1.00 30.00 ? 214 MET C SD  1 
ATOM   2853 C CE  . MET C 1 214 ? 160.599 215.961 214.846 1.00 30.00 ? 214 MET C CE  1 
ATOM   2854 N N   . LEU C 1 215 ? 164.898 212.730 216.045 1.00 30.00 ? 215 LEU C N   1 
ATOM   2855 C CA  . LEU C 1 215 ? 165.018 211.435 216.764 1.00 30.00 ? 215 LEU C CA  1 
ATOM   2856 C C   . LEU C 1 215 ? 166.490 211.186 217.083 1.00 30.00 ? 215 LEU C C   1 
ATOM   2857 O O   . LEU C 1 215 ? 166.803 211.033 218.273 1.00 30.00 ? 215 LEU C O   1 
ATOM   2858 C CB  . LEU C 1 215 ? 164.442 210.325 215.880 1.00 30.00 ? 215 LEU C CB  1 
ATOM   2859 C CG  . LEU C 1 215 ? 162.963 210.460 215.517 1.00 30.00 ? 215 LEU C CG  1 
ATOM   2860 C CD1 . LEU C 1 215 ? 162.471 209.221 214.791 1.00 30.00 ? 215 LEU C CD1 1 
ATOM   2861 C CD2 . LEU C 1 215 ? 162.108 210.720 216.747 1.00 30.00 ? 215 LEU C CD2 1 
ATOM   2862 N N   . THR C 1 216 ? 167.362 211.199 216.075 1.00 30.00 ? 216 THR C N   1 
ATOM   2863 C CA  . THR C 1 216 ? 168.806 210.920 216.266 1.00 30.00 ? 216 THR C CA  1 
ATOM   2864 C C   . THR C 1 216 ? 169.349 211.946 217.255 1.00 30.00 ? 216 THR C C   1 
ATOM   2865 O O   . THR C 1 216 ? 170.252 211.588 218.028 1.00 30.00 ? 216 THR C O   1 
ATOM   2866 C CB  . THR C 1 216 ? 169.566 210.945 214.935 1.00 30.00 ? 216 THR C CB  1 
ATOM   2867 O OG1 . THR C 1 216 ? 170.898 210.502 215.190 1.00 30.00 ? 216 THR C OG1 1 
ATOM   2868 C CG2 . THR C 1 216 ? 169.619 212.305 214.276 1.00 30.00 ? 216 THR C CG2 1 
ATOM   2869 N N   . ALA C 1 217 ? 168.742 213.129 217.302 1.00 30.00 ? 217 ALA C N   1 
ATOM   2870 C CA  . ALA C 1 217 ? 169.214 214.229 218.165 1.00 30.00 ? 217 ALA C CA  1 
ATOM   2871 C C   . ALA C 1 217 ? 168.837 213.962 219.615 1.00 30.00 ? 217 ALA C C   1 
ATOM   2872 O O   . ALA C 1 217 ? 169.727 214.062 220.474 1.00 30.00 ? 217 ALA C O   1 
ATOM   2873 C CB  . ALA C 1 217 ? 168.600 215.517 217.706 1.00 30.00 ? 217 ALA C CB  1 
ATOM   2874 N N   . CYS C 1 218 ? 167.594 213.583 219.877 1.00 30.00 ? 218 CYS C N   1 
ATOM   2875 C CA  . CYS C 1 218 ? 167.113 213.430 221.272 1.00 30.00 ? 218 CYS C CA  1 
ATOM   2876 C C   . CYS C 1 218 ? 167.534 212.069 221.823 1.00 30.00 ? 218 CYS C C   1 
ATOM   2877 O O   . CYS C 1 218 ? 166.728 211.127 221.729 1.00 30.00 ? 218 CYS C O   1 
ATOM   2878 C CB  . CYS C 1 218 ? 165.601 213.569 221.336 1.00 30.00 ? 218 CYS C CB  1 
ATOM   2879 S SG  . CYS C 1 218 ? 164.963 213.503 223.027 1.00 30.00 ? 218 CYS C SG  1 
ATOM   2880 N N   . GLN C 1 219 ? 168.753 211.964 222.349 1.00 30.00 ? 219 GLN C N   1 
ATOM   2881 C CA  . GLN C 1 219 ? 169.259 210.715 222.971 1.00 30.00 ? 219 GLN C CA  1 
ATOM   2882 C C   . GLN C 1 219 ? 169.742 211.061 224.378 1.00 30.00 ? 219 GLN C C   1 
ATOM   2883 O O   . GLN C 1 219 ? 170.492 212.045 224.504 1.00 30.00 ? 219 GLN C O   1 
ATOM   2884 C CB  . GLN C 1 219 ? 170.389 210.120 222.136 1.00 30.00 ? 219 GLN C CB  1 
ATOM   2885 C CG  . GLN C 1 219 ? 169.994 209.822 220.700 1.00 30.00 ? 219 GLN C CG  1 
ATOM   2886 C CD  . GLN C 1 219 ? 168.924 208.763 220.619 1.00 30.00 ? 219 GLN C CD  1 
ATOM   2887 O OE1 . GLN C 1 219 ? 169.103 207.637 221.075 1.00 30.00 ? 219 GLN C OE1 1 
ATOM   2888 N NE2 . GLN C 1 219 ? 167.792 209.125 220.041 1.00 30.00 ? 219 GLN C NE2 1 
ATOM   2889 N N   . GLY C 1 220 ? 169.310 210.313 225.394 1.00 30.00 ? 220 GLY C N   1 
ATOM   2890 C CA  . GLY C 1 220 ? 169.704 210.563 226.794 1.00 30.00 ? 220 GLY C CA  1 
ATOM   2891 C C   . GLY C 1 220 ? 168.759 211.550 227.447 1.00 30.00 ? 220 GLY C C   1 
ATOM   2892 O O   . GLY C 1 220 ? 168.977 211.866 228.633 1.00 30.00 ? 220 GLY C O   1 
ATOM   2893 N N   . VAL C 1 221 ? 167.755 212.030 226.710 1.00 30.00 ? 221 VAL C N   1 
ATOM   2894 C CA  . VAL C 1 221 ? 166.774 213.030 227.217 1.00 30.00 ? 221 VAL C CA  1 
ATOM   2895 C C   . VAL C 1 221 ? 165.388 212.649 226.691 1.00 30.00 ? 221 VAL C C   1 
ATOM   2896 O O   . VAL C 1 221 ? 165.344 211.735 225.850 1.00 30.00 ? 221 VAL C O   1 
ATOM   2897 C CB  . VAL C 1 221 ? 167.191 214.453 226.803 1.00 30.00 ? 221 VAL C CB  1 
ATOM   2898 C CG1 . VAL C 1 221 ? 168.370 214.946 227.623 1.00 30.00 ? 221 VAL C CG1 1 
ATOM   2899 C CG2 . VAL C 1 221 ? 167.509 214.552 225.320 1.00 30.00 ? 221 VAL C CG2 1 
HETATM 2900 C C1  . IHP D 2 .   ? 226.843 224.711 189.006 0.17 20.00 ? 301 IHP A C1  1 
HETATM 2901 C C2  . IHP D 2 .   ? 226.652 226.101 189.568 0.17 20.00 ? 301 IHP A C2  1 
HETATM 2902 C C3  . IHP D 2 .   ? 225.480 226.779 188.895 0.17 20.00 ? 301 IHP A C3  1 
HETATM 2903 C C4  . IHP D 2 .   ? 224.207 226.005 189.184 0.17 20.00 ? 301 IHP A C4  1 
HETATM 2904 C C5  . IHP D 2 .   ? 224.330 224.551 188.754 0.17 20.00 ? 301 IHP A C5  1 
HETATM 2905 C C6  . IHP D 2 .   ? 225.598 223.878 189.259 0.17 20.00 ? 301 IHP A C6  1 
HETATM 2906 O O11 . IHP D 2 .   ? 227.967 224.087 189.708 0.17 20.00 ? 301 IHP A O11 1 
HETATM 2907 P P1  . IHP D 2 .   ? 229.425 224.752 189.890 0.17 20.00 ? 301 IHP A P1  1 
HETATM 2908 O O21 . IHP D 2 .   ? 230.345 223.617 190.290 0.17 20.00 ? 301 IHP A O21 1 
HETATM 2909 O O31 . IHP D 2 .   ? 229.813 225.363 188.558 0.17 20.00 ? 301 IHP A O31 1 
HETATM 2910 O O41 . IHP D 2 .   ? 229.301 225.792 190.989 0.17 20.00 ? 301 IHP A O41 1 
HETATM 2911 O O12 . IHP D 2 .   ? 226.371 225.927 190.992 0.17 20.00 ? 301 IHP A O12 1 
HETATM 2912 P P2  . IHP D 2 .   ? 225.990 227.072 192.045 0.17 20.00 ? 301 IHP A P2  1 
HETATM 2913 O O22 . IHP D 2 .   ? 226.985 228.191 191.809 0.17 20.00 ? 301 IHP A O22 1 
HETATM 2914 O O32 . IHP D 2 .   ? 226.193 226.375 193.376 0.17 20.00 ? 301 IHP A O32 1 
HETATM 2915 O O42 . IHP D 2 .   ? 224.556 227.531 191.870 0.17 20.00 ? 301 IHP A O42 1 
HETATM 2916 O O13 . IHP D 2 .   ? 225.400 228.145 189.422 0.17 20.00 ? 301 IHP A O13 1 
HETATM 2917 P P3  . IHP D 2 .   ? 224.299 229.286 189.119 0.17 20.00 ? 301 IHP A P3  1 
HETATM 2918 O O23 . IHP D 2 .   ? 224.098 229.325 187.617 0.17 20.00 ? 301 IHP A O23 1 
HETATM 2919 O O33 . IHP D 2 .   ? 224.920 230.567 189.638 0.17 20.00 ? 301 IHP A O33 1 
HETATM 2920 O O43 . IHP D 2 .   ? 223.030 228.932 189.871 0.17 20.00 ? 301 IHP A O43 1 
HETATM 2921 O O14 . IHP D 2 .   ? 223.111 226.639 188.448 0.17 20.00 ? 301 IHP A O14 1 
HETATM 2922 P P4  . IHP D 2 .   ? 221.539 226.360 188.691 0.17 20.00 ? 301 IHP A P4  1 
HETATM 2923 O O24 . IHP D 2 .   ? 221.353 226.329 190.195 0.17 20.00 ? 301 IHP A O24 1 
HETATM 2924 O O34 . IHP D 2 .   ? 221.156 225.052 188.028 0.17 20.00 ? 301 IHP A O34 1 
HETATM 2925 O O44 . IHP D 2 .   ? 220.826 227.538 188.062 0.17 20.00 ? 301 IHP A O44 1 
HETATM 2926 O O15 . IHP D 2 .   ? 223.170 223.850 189.311 0.17 20.00 ? 301 IHP A O15 1 
HETATM 2927 P P5  . IHP D 2 .   ? 222.831 222.277 189.222 0.17 20.00 ? 301 IHP A P5  1 
HETATM 2928 O O25 . IHP D 2 .   ? 223.806 221.539 190.121 0.17 20.00 ? 301 IHP A O25 1 
HETATM 2929 O O35 . IHP D 2 .   ? 222.980 221.881 187.767 0.17 20.00 ? 301 IHP A O35 1 
HETATM 2930 O O45 . IHP D 2 .   ? 221.402 222.149 189.706 0.17 20.00 ? 301 IHP A O45 1 
HETATM 2931 O O16 . IHP D 2 .   ? 225.740 222.592 188.570 0.17 20.00 ? 301 IHP A O16 1 
HETATM 2932 P P6  . IHP D 2 .   ? 226.885 221.490 188.862 0.17 20.00 ? 301 IHP A P6  1 
HETATM 2933 O O26 . IHP D 2 .   ? 226.354 220.194 188.290 0.17 20.00 ? 301 IHP A O26 1 
HETATM 2934 O O36 . IHP D 2 .   ? 228.150 221.932 188.153 0.17 20.00 ? 301 IHP A O36 1 
HETATM 2935 O O46 . IHP D 2 .   ? 227.059 221.426 190.365 0.17 20.00 ? 301 IHP A O46 1 
HETATM 2936 C C1  . IHP E 2 .   ? 225.716 224.496 201.004 0.17 20.00 ? 302 IHP A C1  1 
HETATM 2937 C C2  . IHP E 2 .   ? 224.549 224.894 201.891 0.17 20.00 ? 302 IHP A C2  1 
HETATM 2938 C C3  . IHP E 2 .   ? 223.950 226.215 201.439 0.17 20.00 ? 302 IHP A C3  1 
HETATM 2939 C C4  . IHP E 2 .   ? 225.007 227.307 201.471 0.17 20.00 ? 302 IHP A C4  1 
HETATM 2940 C C5  . IHP E 2 .   ? 226.246 226.924 200.675 0.17 20.00 ? 302 IHP A C5  1 
HETATM 2941 C C6  . IHP E 2 .   ? 226.795 225.562 201.066 0.17 20.00 ? 302 IHP A C6  1 
HETATM 2942 O O11 . IHP E 2 .   ? 225.294 224.362 199.604 0.17 20.00 ? 302 IHP A O11 1 
HETATM 2943 P P1  . IHP E 2 .   ? 224.394 223.207 198.917 0.17 20.00 ? 302 IHP A P1  1 
HETATM 2944 O O21 . IHP E 2 .   ? 224.500 223.503 197.438 0.17 20.00 ? 302 IHP A O21 1 
HETATM 2945 O O31 . IHP E 2 .   ? 225.049 221.891 199.283 0.17 20.00 ? 302 IHP A O31 1 
HETATM 2946 O O41 . IHP E 2 .   ? 222.956 223.283 199.388 0.17 20.00 ? 302 IHP A O41 1 
HETATM 2947 O O12 . IHP E 2 .   ? 223.528 223.847 201.844 0.17 20.00 ? 302 IHP A O12 1 
HETATM 2948 P P2  . IHP E 2 .   ? 222.295 223.748 202.880 0.17 20.00 ? 302 IHP A P2  1 
HETATM 2949 O O22 . IHP E 2 .   ? 221.422 224.977 202.729 0.17 20.00 ? 302 IHP A O22 1 
HETATM 2950 O O32 . IHP E 2 .   ? 222.914 223.657 204.261 0.17 20.00 ? 302 IHP A O32 1 
HETATM 2951 O O42 . IHP E 2 .   ? 221.554 222.483 202.502 0.17 20.00 ? 302 IHP A O42 1 
HETATM 2952 O O13 . IHP E 2 .   ? 223.432 226.054 200.076 0.17 20.00 ? 302 IHP A O13 1 
HETATM 2953 P P3  . IHP E 2 .   ? 222.318 226.977 199.356 0.17 20.00 ? 302 IHP A P3  1 
HETATM 2954 O O23 . IHP E 2 .   ? 222.829 228.401 199.319 0.17 20.00 ? 302 IHP A O23 1 
HETATM 2955 O O33 . IHP E 2 .   ? 221.062 226.851 200.191 0.17 20.00 ? 302 IHP A O33 1 
HETATM 2956 O O43 . IHP E 2 .   ? 222.130 226.403 197.963 0.17 20.00 ? 302 IHP A O43 1 
HETATM 2957 O O14 . IHP E 2 .   ? 225.372 227.512 202.876 0.17 20.00 ? 302 IHP A O14 1 
HETATM 2958 P P4  . IHP E 2 .   ? 226.338 228.684 203.423 0.17 20.00 ? 302 IHP A P4  1 
HETATM 2959 O O24 . IHP E 2 .   ? 225.841 229.970 202.793 0.17 20.00 ? 302 IHP A O24 1 
HETATM 2960 O O34 . IHP E 2 .   ? 227.770 228.366 203.036 0.17 20.00 ? 302 IHP A O34 1 
HETATM 2961 O O44 . IHP E 2 .   ? 226.147 228.685 204.926 0.17 20.00 ? 302 IHP A O44 1 
HETATM 2962 O O15 . IHP E 2 .   ? 225.881 226.882 199.260 0.17 20.00 ? 302 IHP A O15 1 
HETATM 2963 P P5  . IHP E 2 .   ? 225.820 228.180 198.313 0.17 20.00 ? 302 IHP A P5  1 
HETATM 2964 O O25 . IHP E 2 .   ? 224.744 227.838 197.310 0.17 20.00 ? 302 IHP A O25 1 
HETATM 2965 O O35 . IHP E 2 .   ? 227.193 228.280 197.674 0.17 20.00 ? 302 IHP A O35 1 
HETATM 2966 O O45 . IHP E 2 .   ? 225.479 229.410 199.132 0.17 20.00 ? 302 IHP A O45 1 
HETATM 2967 O O16 . IHP E 2 .   ? 227.306 225.652 202.437 0.17 20.00 ? 302 IHP A O16 1 
HETATM 2968 P P6  . IHP E 2 .   ? 228.029 224.452 203.240 0.17 20.00 ? 302 IHP A P6  1 
HETATM 2969 O O26 . IHP E 2 .   ? 229.070 223.881 202.299 0.17 20.00 ? 302 IHP A O26 1 
HETATM 2970 O O36 . IHP E 2 .   ? 228.664 225.107 204.450 0.17 20.00 ? 302 IHP A O36 1 
HETATM 2971 O O46 . IHP E 2 .   ? 226.980 223.429 203.634 0.17 20.00 ? 302 IHP A O46 1 
# 
