9h93

Poliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC6b) from a yeast expression system.

Method: ELECTRON MICROSCOPY Dmax: 95.3 Å Quality: GOOD

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

Capsid protein VP1

Poliovirus 2

UniProt Q8QNU4

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 × 180 PDB declaration: 180-meric(180) Consistent with protein copy count Chain A; UniProt 1–301 Mutation:VP1 V107I, VP1 F134L, VP1 V183L Capsid protein, VP0 × 60 (P06210) Capsid protein VP3 × 60 (A0A0K1U2R1) SPH SPHINGOSINE × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;3ul of sample double blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV. Resolution 2.40 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.

2 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8QNU4_9ENTO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–301; UniProt 1–301

Capsid protein, VP0

Poliovirus 2

UniProt P06210

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 × 180 PDB declaration: 180-meric(180) Consistent with protein copy count Chain B; UniProt 1–340 Mutation:VP4 I57V, VP2 D57A Capsid protein VP1 × 60 (Q8QNU4) Capsid protein VP3 × 60 (A0A0K1U2R1) SPH SPHINGOSINE × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;3ul of sample double blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV. Resolution 2.40 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.

7 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_POL2L
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–340; UniProt 1–340

Capsid protein VP3

Poliovirus 2

UniProt A0A0K1U2R1

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 × 180 PDB declaration: 180-meric(180) Consistent with protein copy count Chain C; UniProt 341–578 Mutation:VP3 Q178L Capsid protein VP1 × 60 (Q8QNU4) Capsid protein, VP0 × 60 (P06210) SPH SPHINGOSINE × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;3ul of sample double blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV. Resolution 2.40 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.

3 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0K1U2R1_9ENTO
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–238; UniProt 341–578

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 9h93

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9h93
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9h93
Deposition date deposition_date2024-10-29
Structure title titlePoliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC6b) from a yeast expression system.
Keywords keywordsCapsid protein, virus-like particle, vaccine, VIRUS LIKE PARTICLE; VIRUS LIKE PARTICLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.10
Radius of gyration Rg (electron density) rg_electron28.26
Forward intensity I(0) i094684400.00
Molecular weight molecular_weight77731.0 kDa
Excluded volume excluded_volume97640 ų
Envelope volume envelope_volume119690 ų
Hydration-shell volume shell_volume35411 ų
Envelope diameter envelope_diameter103.0
Shell Rg shell_rg35.28
Envelope Rg envelope_rg28.88
Shape Rg shape_rg28.25
Total Rg total_rg28.98
Total atoms total_atoms5474
Residues n_residues696
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 dmax95.3
Rg (real space) rg_real29.10
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real9.4680e+07
I(0) uncertainty (real space) i0_real_error1.4210e+06
Rg (reciprocal space) rg_reciprocal29.11
I(0) (reciprocal space) i0_reciprocal94680000.0000
Solution quality estimate total_estimate0.8874
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19230000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.890

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)