7x38

Cryo-EM structure of Coxsackievirus B1 empty particle in complex with nAb 8A10 (CVB1-E:8A10)

Method: ELECTRON MICROSCOPY Dmax: 101.1 Å Quality: GOOD

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

Virion protein 1

OrganismNot specified

UniProt W8GTF7

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 × 300 PDB declaration: 300-meric(300) Consistent with protein copy count Chain A; UniProt 1–278 Not recorded 8A10 light chain × 60 8A10 heavy chain × 60 VP2 × 60 (A0A2S0RQC2) VP3 × 60 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–278 Not recorded 8A10 light chain × 1 8A10 heavy chain × 1 VP2 × 1 (A0A2S0RQC2) VP3 × 1 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
3 Protein heterocomplex Heteromer Protein × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain A; UniProt 1–278 Not recorded 8A10 light chain × 5 8A10 heavy chain × 5 VP2 × 5 (A0A2S0RQC2) VP3 × 5 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
4 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain A; UniProt 1–278 Not recorded 8A10 light chain × 6 8A10 heavy chain × 6 VP2 × 6 (A0A2S0RQC2) VP3 × 6 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
5 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–278 Not recorded 8A10 light chain × 1 8A10 heavy chain × 1 VP2 × 1 (A0A2S0RQC2) VP3 × 1 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 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.

25 other PDB entries and 125 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name W8GTF7_9ENTO
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–278; UniProt 1–278

VP2

OrganismNot specified

UniProt A0A2S0RQC2

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 × 300 PDB declaration: 300-meric(300) Consistent with protein copy count Chain B; UniProt 70–332 Not recorded 8A10 light chain × 60 8A10 heavy chain × 60 Virion protein 1 × 60 (W8GTF7) VP3 × 60 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 70–332 Not recorded 8A10 light chain × 1 8A10 heavy chain × 1 Virion protein 1 × 1 (W8GTF7) VP3 × 1 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
3 Protein heterocomplex Heteromer Protein × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain B; UniProt 70–332 Not recorded 8A10 light chain × 5 8A10 heavy chain × 5 Virion protein 1 × 5 (W8GTF7) VP3 × 5 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
4 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain B; UniProt 70–332 Not recorded 8A10 light chain × 6 8A10 heavy chain × 6 Virion protein 1 × 6 (W8GTF7) VP3 × 6 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
5 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 70–332 Not recorded 8A10 light chain × 1 8A10 heavy chain × 1 Virion protein 1 × 1 (W8GTF7) VP3 × 1 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 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.

23 other PDB entries and 115 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2S0RQC2_9ENTO
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–263; UniProt 70–332

VP3

OrganismNot specified

UniProt L7UV52

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 × 300 PDB declaration: 300-meric(300) Consistent with protein copy count Chain C; UniProt 333–570 Not recorded 8A10 light chain × 60 8A10 heavy chain × 60 Virion protein 1 × 60 (W8GTF7) VP2 × 60 (A0A2S0RQC2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 333–570 Not recorded 8A10 light chain × 1 8A10 heavy chain × 1 Virion protein 1 × 1 (W8GTF7) VP2 × 1 (A0A2S0RQC2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
3 Protein heterocomplex Heteromer Protein × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain C; UniProt 333–570 Not recorded 8A10 light chain × 5 8A10 heavy chain × 5 Virion protein 1 × 5 (W8GTF7) VP2 × 5 (A0A2S0RQC2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
4 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain C; UniProt 333–570 Not recorded 8A10 light chain × 6 8A10 heavy chain × 6 Virion protein 1 × 6 (W8GTF7) VP2 × 6 (A0A2S0RQC2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å
5 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 333–570 Not recorded 8A10 light chain × 1 8A10 heavy chain × 1 Virion protein 1 × 1 (W8GTF7) VP2 × 1 (A0A2S0RQC2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 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.

23 other PDB entries and 115 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name L7UV52_9ENTO
Isoform
PDB entities 5
Chains and sequence ranges Author chain C; PDBConstruct 1–238; UniProt 333–570

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 7x38

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7x38
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7x38
Deposition date deposition_date2022-02-28
Structure title titleCryo-EM structure of Coxsackievirus B1 empty particle in complex with nAb 8A10 (CVB1-E:8A10)
Keywords keywordsCoxsackievirus B1, Neutralizing antibody, Cryo-EM, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.62
Radius of gyration Rg (electron density) rg_electron30.71
Forward intensity I(0) i0158959000.00
Molecular weight molecular_weight99784.0 kDa
Excluded volume excluded_volume124540 ų
Envelope volume envelope_volume161780 ų
Hydration-shell volume shell_volume43139 ų
Envelope diameter envelope_diameter107.3
Shell Rg shell_rg38.41
Envelope Rg envelope_rg31.18
Shape Rg shape_rg30.67
Total Rg total_rg31.49
Total atoms total_atoms7016
Residues n_residues896
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 dmax101.1
Rg (real space) rg_real31.51
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.5900e+08
I(0) uncertainty (real space) i0_real_error2.5400e+06
Rg (reciprocal space) rg_reciprocal31.56
I(0) (reciprocal space) i0_reciprocal159000000.0000
Solution quality estimate total_estimate0.8983
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.4
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.399
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41270000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.937

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)