7sqp

Single chain trimer HLA-A*02:01 (Y108C) with HPV.16 E7 peptide YMLDLQPETTDL

Method: X-RAY DIFFRACTION Dmax: 136.4 Å Quality: GOOD

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:Y108C VHH × 1 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
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 25–299 Mutation:Y108C VHH × 1 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

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.

7 other PDB entries and 56 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 147–421; UniProt 25–299 Author chain C; PDBConstruct 147–421; 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 11–22 Mutation:Y108C VHH × 1 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
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 11–22 Mutation:Y108C VHH × 1 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

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.

8 other PDB entries and 41 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 1–12; UniProt 11–22 Author chain C; PDBConstruct 1–12; UniProt 11–22

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:Y108C VHH × 1 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
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 21–119 Mutation:Y108C VHH × 1 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

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.

8 other PDB entries and 58 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 28–126; UniProt 21–119 Author chain C; PDBConstruct 28–126; 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 7sqp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7sqp
Deposition date deposition_date2021-11-05
Structure title titleSingle chain trimer HLA-A*02:01 (Y108C) with HPV.16 E7 peptide YMLDLQPETTDL
Keywords keywordsHLA, VHH, HPV, SCT, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier41.29
Radius of gyration Rg (electron density) rg_electron41.13
Forward intensity I(0) i0181917000.00
Molecular weight molecular_weight106090.0 kDa
Excluded volume excluded_volume130720 ų
Envelope volume envelope_volume189470 ų
Hydration-shell volume shell_volume38609 ų
Envelope diameter envelope_diameter140.1
Shell Rg shell_rg46.58
Envelope Rg envelope_rg39.91
Shape Rg shape_rg41.17
Total Rg total_rg41.32
Total atoms total_atoms7503
Residues n_residues993
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax136.4
Rg (real space) rg_real41.43
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real1.8190e+08
I(0) uncertainty (real space) i0_real_error3.4760e+06
Rg (reciprocal space) rg_reciprocal41.30
I(0) (reciprocal space) i0_reciprocal181900000.0000
Solution quality estimate total_estimate0.8713
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.9
Skewness Skewness skewness0.281
Kurtosis Kurtosis kurtosis-0.725
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9982000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.890; Smooth: 0.784

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7sqpB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7sqpD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)