7tpk

SARS-CoV-2 E406W mutant RBD - Local Refinement

Method: ELECTRON MICROSCOPY Dmax: 69.1 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 333–526 Fragment:Receptor-binding domain Mutation:E406W NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 1–194; UniProt 333–526

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 7tpk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7tpk
Deposition date deposition_date2022-01-25
Structure title titleSARS-CoV-2 E406W mutant RBD - Local Refinement
Keywords keywordsviral entry protein, viral glycoprotein, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier19.20
Radius of gyration Rg (electron density) rg_electron17.92
Forward intensity I(0) i07557300.00
Molecular weight molecular_weight20378.0 kDa
Excluded volume excluded_volume25572 ų
Envelope volume envelope_volume31353 ų
Hydration-shell volume shell_volume15424 ų
Envelope diameter envelope_diameter67.9
Shell Rg shell_rg23.31
Envelope Rg envelope_rg18.42
Shape Rg shape_rg17.86
Total Rg total_rg19.06
Total atoms total_atoms1446
Residues n_residues194
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 dmax69.1
Rg (real space) rg_real19.25
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real7.5570e+06
I(0) uncertainty (real space) i0_real_error1.0880e+05
Rg (reciprocal space) rg_reciprocal19.24
I(0) (reciprocal space) i0_reciprocal7557000.0000
Solution quality estimate total_estimate0.5752
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.1
Skewness Skewness skewness0.455
Kurtosis Kurtosis kurtosis-0.073
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1819000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.685; Stabil: 0.999; Sysdev: 0.182; Positv: 1.000; Valcen: 0.875; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)