7n1e

SARS-CoV-2 RLQ peptide-specific TCR pRLQ3 binds to RLQ-HLA-A2

Method: X-RAY DIFFRACTION Dmax: 136.7 Å Quality: GOOD

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

MHC class I antigen, A-2 alpha chain

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 25–299 Not recorded Beta-2-microglobulin × 1 (P61769) Spike protein S2 × 1 (P0DTC2) pRLQ3 T cell receptor alpha chain × 1 pRLQ3 T cell receptor beta chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;295 K;0.2M Ammonium sulfate, 0.1M MES (pH 6.0), 12% (w/v) PEG 4000 Resolution 2.30 Å R-free 0.258

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 43 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 1–275; UniProt 25–299

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 Fragment:UNP residues 21-119 MHC class I antigen, A-2 alpha chain × 1 (A0A5B8RNS7) Spike protein S2 × 1 (P0DTC2) pRLQ3 T cell receptor alpha chain × 1 pRLQ3 T cell receptor beta chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;295 K;0.2M Ammonium sulfate, 0.1M MES (pH 6.0), 12% (w/v) PEG 4000 Resolution 2.30 Å R-free 0.258

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 1998 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

Spike protein S2

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 1000–1008 Not recorded MHC class I antigen, A-2 alpha chain × 1 (A0A5B8RNS7) Beta-2-microglobulin × 1 (P61769) pRLQ3 T cell receptor alpha chain × 1 pRLQ3 T cell receptor beta chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;295 K;0.2M Ammonium sulfate, 0.1M MES (pH 6.0), 12% (w/v) PEG 4000 Resolution 2.30 Å R-free 0.258

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 2473 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 1000–1008

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 7n1e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7n1e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7n1e
Deposition date deposition_date2021-05-27
Structure title titleSARS-CoV-2 RLQ peptide-specific TCR pRLQ3 binds to RLQ-HLA-A2
Keywords keywordsTCR-pMHC, SARS-CoV-2, SPIKE, RLQ, 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_guinier37.97
Radius of gyration Rg (electron density) rg_electron38.24
Forward intensity I(0) i0142842000.00
Molecular weight molecular_weight93954.0 kDa
Excluded volume excluded_volume116380 ų
Envelope volume envelope_volume155820 ų
Hydration-shell volume shell_volume37481 ų
Envelope diameter envelope_diameter142.8
Shell Rg shell_rg39.47
Envelope Rg envelope_rg38.50
Shape Rg shape_rg38.24
Total Rg total_rg38.34
Total atoms total_atoms6631
Residues n_residues826
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 dmax136.7
Rg (real space) rg_real38.64
Rg uncertainty (real space) rg_real_error1.92
I(0) (real space) i0_real1.4280e+08
I(0) uncertainty (real space) i0_real_error2.6120e+06
Rg (reciprocal space) rg_reciprocal38.23
I(0) (reciprocal space) i0_reciprocal142800000.0000
Solution quality estimate total_estimate0.7662
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.5
Skewness Skewness skewness0.655
Kurtosis Kurtosis kurtosis-0.239
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17410000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.545; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.595; Smooth: 0.727

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (2)

9. Files and Curves (10)