7tlt

SARS-CoV-2 Spike-derived peptide S489-497 (YFPLQSYGF) presented by HLA-A*29:02

Method: X-RAY DIFFRACTION Dmax: 100.3 Å Quality: EXCELLENT

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

HLA class I histocompatibility antigen, A alpha chain

Homo sapiens

UniProt B0UXQ0

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–365 Not recorded Beta-2-microglobulin × 1 (P61769) Spike protein S1 peptide × 1 (P0DTC2) SO4 SULFATE ION × 3 MG MAGNESIUM ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9 M Ammonium Sulfate, 20 mM Magnesium chloride, 0.1M Bis-tris propane, 2% Ethylene glycol, 2% 2-Methyl-2,4-pentanediol Resolution 2.30 Å R-free 0.238
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–365 Not recorded Beta-2-microglobulin × 1 (P61769) Spike protein S1 peptide × 1 (P0DTC2) SO4 SULFATE ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9 M Ammonium Sulfate, 20 mM Magnesium chloride, 0.1M Bis-tris propane, 2% Ethylene glycol, 2% 2-Methyl-2,4-pentanediol Resolution 2.30 Å R-free 0.238

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name B0UXQ0_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–365; UniProt 1–365 Author chain C; PDBConstruct 1–365; UniProt 1–365

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 21–119 Fragment:UNP residues 21-119 HLA class I histocompatibility antigen, A alpha chain × 1 (B0UXQ0) Spike protein S1 peptide × 1 (P0DTC2) SO4 SULFATE ION × 3 MG MAGNESIUM ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9 M Ammonium Sulfate, 20 mM Magnesium chloride, 0.1M Bis-tris propane, 2% Ethylene glycol, 2% 2-Methyl-2,4-pentanediol Resolution 2.30 Å R-free 0.238
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 21–119 Fragment:UNP residues 21-119 HLA class I histocompatibility antigen, A alpha chain × 1 (B0UXQ0) Spike protein S1 peptide × 1 (P0DTC2) SO4 SULFATE ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9 M Ammonium Sulfate, 20 mM Magnesium chloride, 0.1M Bis-tris propane, 2% Ethylene glycol, 2% 2-Methyl-2,4-pentanediol Resolution 2.30 Å R-free 0.238

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 D; PDBConstruct 2–100; UniProt 21–119

Spike protein S1 peptide

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 489–497 Fragment:UNP residues 489-497 (YFPLQSYGF) HLA class I histocompatibility antigen, A alpha chain × 1 (B0UXQ0) Beta-2-microglobulin × 1 (P61769) SO4 SULFATE ION × 3 MG MAGNESIUM ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9 M Ammonium Sulfate, 20 mM Magnesium chloride, 0.1M Bis-tris propane, 2% Ethylene glycol, 2% 2-Methyl-2,4-pentanediol Resolution 2.30 Å R-free 0.238
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 489–497 Fragment:UNP residues 489-497 (YFPLQSYGF) HLA class I histocompatibility antigen, A alpha chain × 1 (B0UXQ0) Beta-2-microglobulin × 1 (P61769) SO4 SULFATE ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;1.9 M Ammonium Sulfate, 20 mM Magnesium chloride, 0.1M Bis-tris propane, 2% Ethylene glycol, 2% 2-Methyl-2,4-pentanediol Resolution 2.30 Å R-free 0.238

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 E; PDBConstruct 1–9; UniProt 489–497 Author chain F; PDBConstruct 1–9; UniProt 489–497

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 7tlt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7tlt
Deposition date deposition_date2022-01-18
Structure title titleSARS-CoV-2 Spike-derived peptide S489-497 (YFPLQSYGF) presented by HLA-A*29:02
Keywords keywordshuman leukocyte antigen, major histocompatibility complex, HLA-A29, HLA-A*29:02, SARS-CoV-2, Spike, 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_guinier31.72
Radius of gyration Rg (electron density) rg_electron30.74
Forward intensity I(0) i0139944000.00
Molecular weight molecular_weight89609.0 kDa
Excluded volume excluded_volume110060 ų
Envelope volume envelope_volume145160 ų
Hydration-shell volume shell_volume38801 ų
Envelope diameter envelope_diameter107.0
Shell Rg shell_rg38.56
Envelope Rg envelope_rg30.30
Shape Rg shape_rg30.73
Total Rg total_rg31.43
Total atoms total_atoms6313
Residues n_residues767
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 dmax100.3
Rg (real space) rg_real31.60
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real1.3990e+08
I(0) uncertainty (real space) i0_real_error1.9050e+06
Rg (reciprocal space) rg_reciprocal31.65
I(0) (reciprocal space) i0_reciprocal140000000.0000
Solution quality estimate total_estimate0.9047
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.1
Skewness Skewness skewness0.179
Kurtosis Kurtosis kurtosis-0.499
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16690000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.931

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)