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7ssh

Single chain trimer HLA-A*02:01 (Y108A) with HPV.16 E7 peptide YMLDLQPETTDLYC

Method: X-RAY DIFFRACTION Dmax: 239.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Protein E7 peptide,Beta-2-microglobulin,MHC class I antigen chimera

Homo sapiens

UniProt A0A678ZGP6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
10 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain S； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
11 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain U； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
12 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain W； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
13 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain Y； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
14 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain a； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
15 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain c； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
16 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain e； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain C； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
3 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain E； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
4 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain G； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
5 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain I； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
6 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain K； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
7 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain M； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
8 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain O； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
9 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain Q； UniProt 25–299 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 7SSH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7SQP Single chain trimer HLA-A*02:01 (Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-05 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 25–299（275 aa）
Mutation：Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NH4Citrate, 20.0% PEG 3350
Resolution 2.53 Å R-free 0.260
7SQP Single chain trimer HLA-A*02:01 (Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-05 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 25–299（275 aa）
Mutation：Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NH4Citrate, 20.0% PEG 3350
Resolution 2.53 Å R-free 0.260
7SR0 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPET Deposited 2021-11-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 25–299（275 aa）
Mutation：H98L, Y108C PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM HK2PO4, 20% PEG 3350
Resolution 2.54 Å R-free 0.242
7SR0 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPET Deposited 2021-11-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 25–299（275 aa）
Mutation：H98L, Y108C PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM HK2PO4, 20% PEG 3350
Resolution 2.54 Å R-free 0.242
7SR3 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 25–299（275 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM K2SO4, 17% PEG 3350
Resolution 2.49 Å R-free 0.248
7SR3 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 25–299（275 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM K2SO4, 17% PEG 3350
Resolution 2.49 Å R-free 0.248
7SR4 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDLYC Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 25–299（275 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM KCitrate, pH 6.5, 17.5% PEG 3350
Resolution 2.59 Å R-free 0.247
7SR4 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDLYC Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 25–299（275 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM KCitrate, pH 6.5, 17.5% PEG 3350
Resolution 2.59 Å R-free 0.247
7SR5 Single chain trimer HLA-A*02:01 (Y108C, A163C) with Wilms tumor protein peptide RMFPNAPYL Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NH4Citrate, 14.5% PEG 3350
Resolution 2.35 Å R-free 0.248
7SR5 Single chain trimer HLA-A*02:01 (Y108C, A163C) with Wilms tumor protein peptide RMFPNAPYL Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NH4Citrate, 14.5% PEG 3350
Resolution 2.35 Å R-free 0.248
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 10 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain S 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 11 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain U 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 12 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain W 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 13 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain Y 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 14 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain a 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 15 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain c 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 16 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain e 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 4 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 5 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 6 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain K 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 7 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain M 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 8 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain O 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 9 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain Q 25–299（275 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 10 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain S 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 11 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain U 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 12 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain W 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 13 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain Y 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 14 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain a 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 15 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain c 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 16 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain e 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 4 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 5 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 6 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain K 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 7 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain M 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 8 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain O 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 9 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain Q 25–299（275 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276

7 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A678ZGP6_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 149–423； UniProt 25–299 Author chain C； PDBConstruct 149–423； UniProt 25–299 Author chain E； PDBConstruct 149–423； UniProt 25–299 Author chain G； PDBConstruct 149–423； UniProt 25–299 Author chain I； PDBConstruct 149–423； UniProt 25–299 Author chain K； PDBConstruct 149–423； UniProt 25–299 Author chain M； PDBConstruct 149–423； UniProt 25–299 Author chain O； PDBConstruct 149–423； UniProt 25–299 Author chain Q； PDBConstruct 149–423； UniProt 25–299 Author chain S； PDBConstruct 149–423； UniProt 25–299 Author chain U； PDBConstruct 149–423； UniProt 25–299 Author chain W； PDBConstruct 149–423； UniProt 25–299 Author chain Y； PDBConstruct 149–423； UniProt 25–299 Author chain a； PDBConstruct 149–423； UniProt 25–299 Author chain c； PDBConstruct 149–423； UniProt 25–299 Author chain e； PDBConstruct 149–423； UniProt 25–299

Protein E7 peptide,Beta-2-microglobulin,MHC class I antigen chimera

Homo sapiens

UniProt P03129

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
10 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain S； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
11 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain U； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
12 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain W； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
13 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain Y； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
14 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain a； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
15 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain c； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
16 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain e； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain C； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
3 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain E； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
4 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain G； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
5 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain I； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
6 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain K； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
7 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain M； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
8 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain O； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
9 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain Q； UniProt 11–24 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 7SSH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7SQP Single chain trimer HLA-A*02:01 (Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-05 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 11–22（12 aa）
Mutation：Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NH4Citrate, 20.0% PEG 3350
Resolution 2.53 Å R-free 0.260
7SQP Single chain trimer HLA-A*02:01 (Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-05 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 11–22（12 aa）
Mutation：Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NH4Citrate, 20.0% PEG 3350
Resolution 2.53 Å R-free 0.260
7SR0 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPET Deposited 2021-11-07 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 11–19（9 aa）
Mutation：H98L, Y108C PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM HK2PO4, 20% PEG 3350
Resolution 2.54 Å R-free 0.242
7SR0 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPET Deposited 2021-11-07 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 11–19（9 aa）
Mutation：H98L, Y108C PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM HK2PO4, 20% PEG 3350
Resolution 2.54 Å R-free 0.242
7SR3 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-07 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 11–22（12 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM K2SO4, 17% PEG 3350
Resolution 2.49 Å R-free 0.248
7SR3 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-07 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 11–22（12 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM K2SO4, 17% PEG 3350
Resolution 2.49 Å R-free 0.248
7SR4 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDLYC Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 11–24（14 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM KCitrate, pH 6.5, 17.5% PEG 3350
Resolution 2.59 Å R-free 0.247
7SR4 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDLYC Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 11–24（14 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM KCitrate, pH 6.5, 17.5% PEG 3350
Resolution 2.59 Å R-free 0.247
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 10 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain S 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 11 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain U 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 12 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain W 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 13 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain Y 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 14 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain a 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 15 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain c 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 16 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain e 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 4 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 5 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 6 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain K 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 7 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain M 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 8 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain O 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 9 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain Q 11–24（14 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
9UUJ Crystal structure of the mu2 subunit of the clathrin-adaptor protein 2 (AP2) bound to HPV16 E7(residues 22-39) Deposited 2025-05-07 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 22–39（18 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；2.0 M sodium formate and 100 mM sodium acetate trihydrate (pH 4.6)
Resolution 3.70 Å R-free 0.234
9UUK Crystal structure of the mu2 subunit of the clathrin-adaptor protein 2 (AP2) bound to HPV16 E7(residues 22-32; S31E and S32E) Deposited 2025-05-07 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 22–32（11 aa）
Mutation：S31E, S32E No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；2.5 M sodium chloride and 100 mM potassium phosphate monobasic/sodium phosphate dibasic (pH 6.2)
Resolution 3.20 Å R-free 0.244
9UUL Crystal structure of the mu2 subunit of the clathrin-adaptor protein 2 (AP2) bound to HPV16 E7(residues 22-39; S31E and S32E) Deposited 2025-05-07 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 22–39（18 aa）
Mutation：S31E, S32E No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；3.5 M ammonium chloride and 100 mM sodium acetate trihydrate (pH 4.5)
Resolution 3.30 Å R-free 0.225

8 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VE7_HPV16
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–14； UniProt 11–24 Author chain C； PDBConstruct 1–14； UniProt 11–24 Author chain E； PDBConstruct 1–14； UniProt 11–24 Author chain G； PDBConstruct 1–14； UniProt 11–24 Author chain I； PDBConstruct 1–14； UniProt 11–24 Author chain K； PDBConstruct 1–14； UniProt 11–24 Author chain M； PDBConstruct 1–14； UniProt 11–24 Author chain O； PDBConstruct 1–14； UniProt 11–24 Author chain Q； PDBConstruct 1–14； UniProt 11–24 Author chain S； PDBConstruct 1–14； UniProt 11–24 Author chain U； PDBConstruct 1–14； UniProt 11–24 Author chain W； PDBConstruct 1–14； UniProt 11–24 Author chain Y； PDBConstruct 1–14； UniProt 11–24 Author chain a； PDBConstruct 1–14； UniProt 11–24 Author chain c； PDBConstruct 1–14； UniProt 11–24 Author chain e； PDBConstruct 1–14； UniProt 11–24

Protein E7 peptide,Beta-2-microglobulin,MHC class I antigen chimera

Homo sapiens

UniProt P16213

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
10 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain S； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
11 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain U； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
12 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain W； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
13 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain Y； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
14 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain a； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
15 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain c； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
16 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain e； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain C； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
3 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain E； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
4 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain G； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
5 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain I； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
6 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain K； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
7 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain M； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
8 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain O； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294
9 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain Q； UniProt 21–119 Mutation：Y108A VHH × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NaCl, 100 mM HEPES, pH 7.0, 1.45 M (NH4)2SO4 Resolution 2.73 Å R-free 0.294

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 7SSH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7SQP Single chain trimer HLA-A*02:01 (Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-05 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 21–119（99 aa）
Mutation：Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NH4Citrate, 20.0% PEG 3350
Resolution 2.53 Å R-free 0.260
7SQP Single chain trimer HLA-A*02:01 (Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-05 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 21–119（99 aa）
Mutation：Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NH4Citrate, 20.0% PEG 3350
Resolution 2.53 Å R-free 0.260
7SR0 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPET Deposited 2021-11-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 21–119（99 aa）
Mutation：H98L, Y108C PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM HK2PO4, 20% PEG 3350
Resolution 2.54 Å R-free 0.242
7SR0 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPET Deposited 2021-11-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 21–119（99 aa）
Mutation：H98L, Y108C PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM HK2PO4, 20% PEG 3350
Resolution 2.54 Å R-free 0.242
7SR3 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 21–119（99 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM K2SO4, 17% PEG 3350
Resolution 2.49 Å R-free 0.248
7SR3 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDL Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 21–119（99 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM K2SO4, 17% PEG 3350
Resolution 2.49 Å R-free 0.248
7SR4 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDLYC Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 21–119（99 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM KCitrate, pH 6.5, 17.5% PEG 3350
Resolution 2.59 Å R-free 0.247
7SR4 Single chain trimer HLA-A*02:01 (H98L, Y108C) with HPV.16 E7 peptide YMLDLQPETTDLYC Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 21–119（99 aa）
Mutation：H98L, Y108C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM KCitrate, pH 6.5, 17.5% PEG 3350
Resolution 2.59 Å R-free 0.247
7SR5 Single chain trimer HLA-A*02:01 (Y108C, A163C) with Wilms tumor protein peptide RMFPNAPYL Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NH4Citrate, 14.5% PEG 3350
Resolution 2.35 Å R-free 0.248
7SR5 Single chain trimer HLA-A*02:01 (Y108C, A163C) with Wilms tumor protein peptide RMFPNAPYL Deposited 2021-11-07 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；200 mM NH4Citrate, 14.5% PEG 3350
Resolution 2.35 Å R-free 0.248
7SRK Single chain trimer HLA-A*24:02 (Y108C, A163C) with 8mer peptide YPPVPETF Deposited 2021-11-08 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM MES, pH 6.0, 200 mM KSCN, 18% Peg 3350
Resolution 2.50 Å R-free 0.260
7SRK Single chain trimer HLA-A*24:02 (Y108C, A163C) with 8mer peptide YPPVPETF Deposited 2021-11-08 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM MES, pH 6.0, 200 mM KSCN, 18% Peg 3350
Resolution 2.50 Å R-free 0.260
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 10 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain S 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 11 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain U 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 12 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain W 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 13 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain Y 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 14 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain a 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 15 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain c 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 16 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain e 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 4 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 5 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 6 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain K 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 7 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain M 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 8 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain O 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7ST3 Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-11 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 9 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain Q 21–119（99 aa）
Mutation：Y108C,A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 7.5, 200 mM Li2SO4, 1.6 M AmSO4
Resolution 2.78 Å R-free 0.275
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 10 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain S 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 11 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain U 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 12 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain W 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 13 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain Y 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 14 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain a 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 15 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain c 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 16 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain e 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 4 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 5 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 6 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain K 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 7 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain M 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 8 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain O 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276
7STG Consequences of HLA single chain trimer mutations on peptide presentation and binding affinity Deposited 2021-11-12 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 9 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain Q 21–119（99 aa）
Mutation：Y108C, A163C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；100 mM Tris, pH 8.0, 200 mM Li2SO4, 1.1 M AmSO4
Resolution 2.70 Å R-free 0.276

8 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_PONPY
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 30–128； UniProt 21–119 Author chain C； PDBConstruct 30–128； UniProt 21–119 Author chain E； PDBConstruct 30–128； UniProt 21–119 Author chain G； PDBConstruct 30–128； UniProt 21–119 Author chain I； PDBConstruct 30–128； UniProt 21–119 Author chain K； PDBConstruct 30–128； UniProt 21–119 Author chain M； PDBConstruct 30–128； UniProt 21–119 Author chain O； PDBConstruct 30–128； UniProt 21–119 Author chain Q； PDBConstruct 30–128； UniProt 21–119 Author chain S； PDBConstruct 30–128； UniProt 21–119 Author chain U； PDBConstruct 30–128； UniProt 21–119 Author chain W； PDBConstruct 30–128； UniProt 21–119 Author chain Y； PDBConstruct 30–128； UniProt 21–119 Author chain a； PDBConstruct 30–128； UniProt 21–119 Author chain c； PDBConstruct 30–128； UniProt 21–119 Author chain e； PDBConstruct 30–128； UniProt 21–119

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 7ssh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ssh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ssh
Deposition date deposition_date2021-11-11
Structure title titleSingle chain trimer HLA-A*02:01 (Y108A) with HPV.16 E7 peptide YMLDLQPETTDLYC
Keywords keywordsHLA, VHH, HPV, SCT, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier88.96 Å
Radius of gyration Rg (electron density) rg_electron89.36 Å
Forward intensity I(0) i09639580000.00
Molecular weight molecular_weight800010.0 kDa
Excluded volume excluded_volume983850 ų
Envelope volume envelope_volume2015300 ų
Hydration-shell volume shell_volume200520 ų
Envelope diameter envelope_diameter292.4 Å
Shell Rg shell_rg81.32 Å
Envelope Rg envelope_rg82.95 Å
Shape Rg shape_rg89.36 Å
Total Rg total_rg89.25 Å
Total atoms total_atoms106329
Residues n_residues7582
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax239.9 Å
Rg (real space) rg_real86.07 Å
Rg uncertainty (real space) rg_real_error0.72 Å
I(0) (real space) i0_real9.2710e+09
I(0) uncertainty (real space) i0_real_error1.8270e+08
Rg (reciprocal space) rg_reciprocal87.34 Å
I(0) (reciprocal space) i0_reciprocal9591000000.0000
Solution quality estimate total_estimate0.8914
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary84.7 Å
Skewness Skewness skewness0.387
Kurtosis Kurtosis kurtosis-0.438
Angular range angular_range— – 0.0850 Å−1
Current regularization parameter α current_alpha0.6786
Highest regularization parameter α highest_alpha1662000000.0000
Real-space data points n_real_points18
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 0.967; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.145
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)