8jag

Cryo-EM structure of SARS-CoV-1 RBD in complex with W328-6H2 (local refinement)

Method: ELECTRON MICROSCOPY Dmax: 184.1 Å Quality: GOOD

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

Spike glycoprotein

Severe acute respiratory syndrome-related coronavirus

UniProt P59594

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 1–1255 Not recorded H chain of 6H2 Fab region × 1 L chain of 6H2 Fab region × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.55 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.

76 other PDB entries and 98 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1255; UniProt 1–1255

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 8jag

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8jag
Deposition date deposition_date2023-05-06
Structure title titleCryo-EM structure of SARS-CoV-1 RBD in complex with W328-6H2 (local refinement)
Keywords keywordsCryo-EM, Complex, SARS-CoV-1, antibody, Homo sapiens, IgG, RBD, local refinement, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.59
Radius of gyration Rg (electron density) rg_electron51.08
Forward intensity I(0) i0277183000.00
Molecular weight molecular_weight138670.0 kDa
Excluded volume excluded_volume174030 ų
Envelope volume envelope_volume276220 ų
Hydration-shell volume shell_volume49036 ų
Envelope diameter envelope_diameter181.9
Shell Rg shell_rg48.77
Envelope Rg envelope_rg49.84
Shape Rg shape_rg51.10
Total Rg total_rg50.90
Total atoms total_atoms9772
Residues n_residues1244
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 dmax184.1
Rg (real space) rg_real50.89
Rg uncertainty (real space) rg_real_error2.68
I(0) (real space) i0_real2.7720e+08
I(0) uncertainty (real space) i0_real_error5.9000e+06
Rg (reciprocal space) rg_reciprocal50.33
I(0) (reciprocal space) i0_reciprocal277000000.0000
Solution quality estimate total_estimate0.8335
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.5
Skewness Skewness skewness0.465
Kurtosis Kurtosis kurtosis-0.279
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10200000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.768; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.759; Smooth: 0.771

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)