7wth

SARS-CoV-2 Omicron variant spike RBD in complex with Fab XGv264

Method: ELECTRON MICROSCOPY Dmax: 84.3 Å Quality: REASONABLE

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

Spike protein S1

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 330–530 Fragment:RBD Light chain of XGv264 × 1 Heavy chain of XGv264 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 E; PDBConstruct 1–201; UniProt 330–530

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 7wth

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7wth
Deposition date deposition_date2022-02-04
Structure title titleSARS-CoV-2 Omicron variant spike RBD in complex with Fab XGv264
Keywords keywordsSARS-CoV-2, Omicron, Spike-Fab complex, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier26.42
Radius of gyration Rg (electron density) rg_electron25.56
Forward intensity I(0) i035491000.00
Molecular weight molecular_weight46159.0 kDa
Excluded volume excluded_volume57866 ų
Envelope volume envelope_volume75303 ų
Hydration-shell volume shell_volume25548 ų
Envelope diameter envelope_diameter88.2
Shell Rg shell_rg31.85
Envelope Rg envelope_rg25.68
Shape Rg shape_rg25.48
Total Rg total_rg26.58
Total atoms total_atoms3257
Residues n_residues421
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 dmax84.3
Rg (real space) rg_real26.42
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real3.5490e+07
I(0) uncertainty (real space) i0_real_error5.1870e+05
Rg (reciprocal space) rg_reciprocal26.42
I(0) (reciprocal space) i0_reciprocal35490000.0000
Solution quality estimate total_estimate0.7427
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.289
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8294000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 0.291; Positv: 1.000; Valcen: 0.971; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)