3j48

Cryo-EM structure of Poliovirus 135S particles

Method: ELECTRON MICROSCOPY Dmax: 93.1 Å Quality: GOOD

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

Protein VP1

Human poliovirus 1

UniProt P03300

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 homooligomer Homooligomer Protein × 180 PDB declaration: 180-meric(180) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–579 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-579 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:20 mM HEPES, 2 mM CaCl2;pH 7.4;20 mM HEPES, 2 mM CaCl2 cryo-EM vitrification conditions:Blotted manually before plunge freezing into liquid ethane;90 K;Cryogen ETHANE;Blotted manually in ambient atmosphere before plunging into ethane cooled by liquid nitrogen. Resolution 5.50 Å
2 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–579 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-579 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:20 mM HEPES, 2 mM CaCl2;pH 7.4;20 mM HEPES, 2 mM CaCl2 cryo-EM vitrification conditions:Blotted manually before plunge freezing into liquid ethane;90 K;Cryogen ETHANE;Blotted manually in ambient atmosphere before plunging into ethane cooled by liquid nitrogen. Resolution 5.50 Å
3 Protein homooligomer Homooligomer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–579 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-579 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:20 mM HEPES, 2 mM CaCl2;pH 7.4;20 mM HEPES, 2 mM CaCl2 cryo-EM vitrification conditions:Blotted manually before plunge freezing into liquid ethane;90 K;Cryogen ETHANE;Blotted manually in ambient atmosphere before plunging into ethane cooled by liquid nitrogen. Resolution 5.50 Å
4 Protein homooligomer Homooligomer Protein × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–579 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-579 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:20 mM HEPES, 2 mM CaCl2;pH 7.4;20 mM HEPES, 2 mM CaCl2 cryo-EM vitrification conditions:Blotted manually before plunge freezing into liquid ethane;90 K;Cryogen ETHANE;Blotted manually in ambient atmosphere before plunging into ethane cooled by liquid nitrogen. Resolution 5.50 Å
5 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–579 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-579 No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:20 mM HEPES, 2 mM CaCl2;pH 7.4;20 mM HEPES, 2 mM CaCl2 cryo-EM vitrification conditions:Blotted manually before plunge freezing into liquid ethane;90 K;Cryogen ETHANE;Blotted manually in ambient atmosphere before plunging into ethane cooled by liquid nitrogen. Resolution 5.50 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.

80 other PDB entries and 246 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_POL1M
Isoform
PDB entities 1, 2, 3
Chains and sequence ranges Author chain 1; PDBConstruct 1–302; UniProt 580–881 Author chain 2; PDBConstruct 1–272; UniProt 70–341 Author chain 3; PDBConstruct 1–238; UniProt 342–579

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 3j48

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j48
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3j48
Deposition date deposition_date2013-06-28
Structure title titleCryo-EM structure of Poliovirus 135S particles
Keywords keywordscell entry, single particle analysis, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.28
Radius of gyration Rg (electron density) rg_electron28.73
Forward intensity I(0) i091194700.00
Molecular weight molecular_weight77162.0 kDa
Excluded volume excluded_volume94358 ų
Envelope volume envelope_volume78222 ų
Hydration-shell volume shell_volume25332 ų
Envelope diameter envelope_diameter99.3
Shell Rg shell_rg32.19
Envelope Rg envelope_rg27.52
Shape Rg shape_rg28.87
Total Rg total_rg28.98
Total atoms total_atoms
Residues n_residues
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 dmax93.1
Rg (real space) rg_real29.31
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real9.1190e+07
I(0) uncertainty (real space) i0_real_error1.4750e+06
Rg (reciprocal space) rg_reciprocal29.30
I(0) (reciprocal space) i0_reciprocal91190000.0000
Solution quality estimate total_estimate0.8959
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.7
Skewness Skewness skewness0.393
Kurtosis Kurtosis kurtosis-0.279
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12660000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.894

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)