9ayy

SARS-CoV-2 Omicron-EG.5.1 3-RBD down Spike Protein Trimer 3 (S-GSAS-Omicron-EG.5.1)

Method: ELECTRON MICROSCOPY Dmax: 164.3 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 1–1208 Chain B; UniProt 1–1208 Chain C; UniProt 1–1208 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 30 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 1–1204; UniProt 1–1208 Author chain B; PDBConstruct 1–1204; UniProt 1–1208 Author chain C; PDBConstruct 1–1204; UniProt 1–1208

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 9ayy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ayy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ayy
Deposition date deposition_date2024-03-08
Structure title titleSARS-CoV-2 Omicron-EG.5.1 3-RBD down Spike Protein Trimer 3 (S-GSAS-Omicron-EG.5.1)
Keywords keywordsSARS-COV-2, Glycoprotein, Trimer, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.03
Radius of gyration Rg (electron density) rg_electron48.59
Forward intensity I(0) i01730050000.00
Molecular weight molecular_weight352110.0 kDa
Excluded volume excluded_volume442610 ų
Envelope volume envelope_volume633880 ų
Hydration-shell volume shell_volume105260 ų
Envelope diameter envelope_diameter165.8
Shell Rg shell_rg54.99
Envelope Rg envelope_rg48.05
Shape Rg shape_rg48.64
Total Rg total_rg48.65
Total atoms total_atoms24813
Residues n_residues3123
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 dmax164.3
Rg (real space) rg_real48.90
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real1.7300e+09
I(0) uncertainty (real space) i0_real_error3.4300e+07
Rg (reciprocal space) rg_reciprocal49.03
I(0) (reciprocal space) i0_reciprocal1730000000.0000
Solution quality estimate total_estimate0.8728
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.5
Skewness Skewness skewness0.309
Kurtosis Kurtosis kurtosis-0.342
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha356400000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.878

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)