7x3y

Cryo-EM structure of Coxsackievirus B1 empty particle in complex with nAb 9A3 (CVB1-E:9A3)

Method: ELECTRON MICROSCOPY Dmax: 104.8 Å Quality: EXCELLENT

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 9A3 heavy chain × 60 9A3 light chain × 60 VP2 × 60 (A0A2S0RQC2) VP3 × 60 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 Å
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–278 Not recorded 9A3 heavy chain × 1 9A3 light chain × 1 VP2 × 1 (A0A2S0RQC2) VP3 × 1 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 Å
3 Protein heterocomplex Heteromer Protein × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain A; UniProt 1–278 Not recorded 9A3 heavy chain × 5 9A3 light chain × 5 VP2 × 5 (A0A2S0RQC2) VP3 × 5 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 Å
4 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain A; UniProt 1–278 Not recorded 9A3 heavy chain × 6 9A3 light chain × 6 VP2 × 6 (A0A2S0RQC2) VP3 × 6 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 Å
5 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–278 Not recorded 9A3 heavy chain × 1 9A3 light chain × 1 VP2 × 1 (A0A2S0RQC2) VP3 × 1 (L7UV52) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.32 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 9A3 heavy chain × 60 9A3 light 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 3.32 Å
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 70–332 Not recorded 9A3 heavy chain × 1 9A3 light 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 3.32 Å
3 Protein heterocomplex Heteromer Protein × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain B; UniProt 70–332 Not recorded 9A3 heavy chain × 5 9A3 light 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 3.32 Å
4 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain B; UniProt 70–332 Not recorded 9A3 heavy chain × 6 9A3 light 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 3.32 Å
5 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 70–332 Not recorded 9A3 heavy chain × 1 9A3 light 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 3.32 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 9A3 heavy chain × 60 9A3 light 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 3.32 Å
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 333–570 Not recorded 9A3 heavy chain × 1 9A3 light 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 3.32 Å
3 Protein heterocomplex Heteromer Protein × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain C; UniProt 333–570 Not recorded 9A3 heavy chain × 5 9A3 light 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 3.32 Å
4 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain C; UniProt 333–570 Not recorded 9A3 heavy chain × 6 9A3 light 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 3.32 Å
5 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 333–570 Not recorded 9A3 heavy chain × 1 9A3 light 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 3.32 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 7x3y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7x3y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7x3y
Deposition date deposition_date2022-03-01
Structure title titleCryo-EM structure of Coxsackievirus B1 empty particle in complex with nAb 9A3 (CVB1-E:9A3)
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_guinier32.47
Radius of gyration Rg (electron density) rg_electron31.68
Forward intensity I(0) i0155018000.00
Molecular weight molecular_weight98929.0 kDa
Excluded volume excluded_volume123550 ų
Envelope volume envelope_volume161790 ų
Hydration-shell volume shell_volume42399 ų
Envelope diameter envelope_diameter111.7
Shell Rg shell_rg38.69
Envelope Rg envelope_rg32.23
Shape Rg shape_rg31.66
Total Rg total_rg32.36
Total atoms total_atoms6957
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 dmax104.8
Rg (real space) rg_real32.39
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real1.5500e+08
I(0) uncertainty (real space) i0_real_error2.0730e+06
Rg (reciprocal space) rg_reciprocal32.43
I(0) (reciprocal space) i0_reciprocal155000000.0000
Solution quality estimate total_estimate0.9036
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.5
Skewness Skewness skewness0.253
Kurtosis Kurtosis kurtosis-0.476
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30020000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.976

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)