8tyl

Structural and biochemical rationale for Beta variant protein booster vaccine broad cross-neutralization of SARS-CoV-2

Method: ELECTRON MICROSCOPY Dmax: 152.7 Å Quality: GOOD

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

Spike glycoprotein

Severe acute respiratory syndrome coronavirus 2

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 14–1211 Chain B; UniProt 14–1211 Chain C; UniProt 14–1211 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 35 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.85 Å

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 1
Chains and sequence ranges Author chain A; PDBConstruct 19–1216; UniProt 14–1211 Author chain B; PDBConstruct 19–1216; UniProt 14–1211 Author chain C; PDBConstruct 19–1216; UniProt 14–1211

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 8tyl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tyl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tyl
Deposition date deposition_date2023-08-25
Structure title titleStructural and biochemical rationale for Beta variant protein booster vaccine broad cross-neutralization of SARS-CoV-2
Keywords keywordsSpike, trimer, surface, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.65
Radius of gyration Rg (electron density) rg_electron46.28
Forward intensity I(0) i01223890000.00
Molecular weight molecular_weight295060.0 kDa
Excluded volume excluded_volume371000 ų
Envelope volume envelope_volume533970 ų
Hydration-shell volume shell_volume93325 ų
Envelope diameter envelope_diameter155.6
Shell Rg shell_rg52.69
Envelope Rg envelope_rg45.62
Shape Rg shape_rg46.34
Total Rg total_rg46.33
Total atoms total_atoms20801
Residues n_residues2659
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 dmax152.7
Rg (real space) rg_real46.46
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real1.2240e+09
I(0) uncertainty (real space) i0_real_error2.0900e+07
Rg (reciprocal space) rg_reciprocal46.65
I(0) (reciprocal space) i0_reciprocal1224000000.0000
Solution quality estimate total_estimate0.8812
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.9
Skewness Skewness skewness0.239
Kurtosis Kurtosis kurtosis-0.408
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha210100000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.884

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)