8zc1

SARS-CoV-2 Omicron BA.2 spike trimer (6P) in complex with D1F6 Fab, focused refinement of RBD region

Method: ELECTRON MICROSCOPY Dmax: 115.9 Å Quality: GOOD

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 B; UniProt 332–527 Fragment:RBD Light chain of D1F6 Fab × 1 Heavy chain of D1F6 Fab × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.17 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 B; PDBConstruct 1–196; UniProt 332–527

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 8zc1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8zc1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8zc1
Deposition date deposition_date2024-04-28
Structure title titleSARS-CoV-2 Omicron BA.2 spike trimer (6P) in complex with D1F6 Fab, focused refinement of RBD region
Keywords keywordsSpike protein, Antibody Fab fragment, Complex, VIRAL PROTEIN/IMMUNE SYSTEM, 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_guinier32.62
Radius of gyration Rg (electron density) rg_electron33.02
Forward intensity I(0) i067468800.00
Molecular weight molecular_weight64735.0 kDa
Excluded volume excluded_volume80879 ų
Envelope volume envelope_volume112720 ų
Hydration-shell volume shell_volume31409 ų
Envelope diameter envelope_diameter121.3
Shell Rg shell_rg36.07
Envelope Rg envelope_rg33.10
Shape Rg shape_rg33.00
Total Rg total_rg33.33
Total atoms total_atoms4570
Residues n_residues597
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 dmax115.9
Rg (real space) rg_real33.09
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real6.7470e+07
I(0) uncertainty (real space) i0_real_error1.1910e+06
Rg (reciprocal space) rg_reciprocal32.89
I(0) (reciprocal space) i0_reciprocal67460000.0000
Solution quality estimate total_estimate0.8089
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.7
Skewness Skewness skewness0.629
Kurtosis Kurtosis kurtosis-0.113
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12440000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.689; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.683; Smooth: 0.763

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)