7pbe

Emergence of immune escape at dominant SARS-CoV-2 killer T-cell epitope

Method: X-RAY DIFFRACTION Dmax: 220.4 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

MHC class I antigen

Homo sapiens

UniProt A0A5B8RNS7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 25–300 Not recorded Beta-2-microglobulin × 1 (P61769) Spike protein S1 × 1 (P0DTC2) Human T-cell Receptor YLQ36, alpha chain × 1 Human T-cell Receptor YLQ36, beta chain × 1 PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M ammonium sulphate, 0.1 M Tris, pH 8.5, and 25 % w/v PEG 4000 Resolution 3.00 Å R-free 0.296
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 25–300 Not recorded Beta-2-microglobulin × 1 (P61769) Spike protein S1 × 1 (P0DTC2) Human T-cell Receptor YLQ36, alpha chain × 1 Human T-cell Receptor YLQ36, beta chain × 1 PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M ammonium sulphate, 0.1 M Tris, pH 8.5, and 25 % w/v PEG 4000 Resolution 3.00 Å R-free 0.296

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.

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

View Construct and Data Evidence
UniProt name A0A5B8RNS7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–276; UniProt 25–300 Author chain F; PDBConstruct 1–276; UniProt 25–300

Beta-2-microglobulin

Homo sapiens

UniProt P61769

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 21–119 Not recorded MHC class I antigen × 1 (A0A5B8RNS7) Spike protein S1 × 1 (P0DTC2) Human T-cell Receptor YLQ36, alpha chain × 1 Human T-cell Receptor YLQ36, beta chain × 1 PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M ammonium sulphate, 0.1 M Tris, pH 8.5, and 25 % w/v PEG 4000 Resolution 3.00 Å R-free 0.296
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 21–119 Not recorded MHC class I antigen × 1 (A0A5B8RNS7) Spike protein S1 × 1 (P0DTC2) Human T-cell Receptor YLQ36, alpha chain × 1 Human T-cell Receptor YLQ36, beta chain × 1 PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M ammonium sulphate, 0.1 M Tris, pH 8.5, and 25 % w/v PEG 4000 Resolution 3.00 Å R-free 0.296

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.

1313 other PDB entries and 1997 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–100; UniProt 21–119 Author chain G; PDBConstruct 2–100; UniProt 21–119

Spike protein S1

OrganismNot specified

UniProt P0DTC2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 269–277 Not recorded MHC class I antigen × 1 (A0A5B8RNS7) Beta-2-microglobulin × 1 (P61769) Human T-cell Receptor YLQ36, alpha chain × 1 Human T-cell Receptor YLQ36, beta chain × 1 PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M ammonium sulphate, 0.1 M Tris, pH 8.5, and 25 % w/v PEG 4000 Resolution 3.00 Å R-free 0.296
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 269–277 Not recorded MHC class I antigen × 1 (A0A5B8RNS7) Beta-2-microglobulin × 1 (P61769) Human T-cell Receptor YLQ36, alpha chain × 1 Human T-cell Receptor YLQ36, beta chain × 1 PEG DI(HYDROXYETHYL)ETHER × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M ammonium sulphate, 0.1 M Tris, pH 8.5, and 25 % w/v PEG 4000 Resolution 3.00 Å R-free 0.296

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.

2152 other PDB entries and 2472 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS2
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–9; UniProt 269–277 Author chain H; PDBConstruct 1–9; UniProt 269–277

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 7pbe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7pbe
Deposition date deposition_date2021-08-02
Structure title titleEmergence of immune escape at dominant SARS-CoV-2 killer T-cell epitope
Keywords keywordsMHC I, A02, Wuhan epitope, SARS-COV-2, Spike protein, 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_guinier64.86
Radius of gyration Rg (electron density) rg_electron66.47
Forward intensity I(0) i0558987000.00
Molecular weight molecular_weight190080.0 kDa
Excluded volume excluded_volume234300 ų
Envelope volume envelope_volume388350 ų
Hydration-shell volume shell_volume53680 ų
Envelope diameter envelope_diameter240.7
Shell Rg shell_rg56.48
Envelope Rg envelope_rg66.06
Shape Rg shape_rg66.48
Total Rg total_rg66.16
Total atoms total_atoms13403
Residues n_residues1652
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 dmax220.4
Rg (real space) rg_real66.32
Rg uncertainty (real space) rg_real_error2.66
I(0) (real space) i0_real5.5890e+08
I(0) uncertainty (real space) i0_real_error1.1170e+07
Rg (reciprocal space) rg_reciprocal63.54
I(0) (reciprocal space) i0_reciprocal556300000.0000
Solution quality estimate total_estimate0.7026
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary36.7
Skewness Skewness skewness0.554
Kurtosis Kurtosis kurtosis-0.425
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha11960000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.531; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.435; Smooth: 0.105

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7pbeA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily10 — MHC class I-like antigen recognition-like
Domain ID domain_id7pbeA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7pbeF01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology500 — Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1
Homologous superfamily homologous superfamily10 — MHC class I-like antigen recognition-like
Domain ID domain_id7pbeF02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)