8ay5

Human rhinovirus 2 empty particle in situ

Method: ELECTRON MICROSCOPY Dmax: 93.2 Å Quality: GOOD

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

Capsid protein VP1

OrganismNot specified

UniProt P04936

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 A; UniProt 600–850 Chain B; UniProt 81–330 Chain C; UniProt 331–567 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.10 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.

17 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_HRV2
Isoform
PDB entities 1, 2, 3
Chains and sequence ranges Author chain A; PDBConstruct 1–251; UniProt 600–850 Author chain B; PDBConstruct 1–250; UniProt 81–330 Author chain C; PDBConstruct 1–237; UniProt 331–567

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 8ay5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ay5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ay5
Deposition date deposition_date2022-09-01
最后修订 last_revision2023-09-13
Structure title titleHuman rhinovirus 2 empty particle in situ
Keywords keywordsHuman rhinovirus 2, empty particle, in situ, cryo-EM., VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.67
Radius of gyration Rg (electron density) rg_electron27.95
Forward intensity I(0) i0110216000.00
Molecular weight molecular_weight82653.0 kDa
Excluded volume excluded_volume103240 ų
Envelope volume envelope_volume125400 ų
Hydration-shell volume shell_volume37012 ų
Envelope diameter envelope_diameter100.7
Shell Rg shell_rg35.59
Envelope Rg envelope_rg28.58
Shape Rg shape_rg27.94
Total Rg total_rg28.70
Total atoms total_atoms11499
Residues n_residues738
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 dmax93.2
Rg (real space) rg_real28.65
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.1020e+08
I(0) uncertainty (real space) i0_real_error1.6400e+06
Rg (reciprocal space) rg_reciprocal28.66
I(0) (reciprocal space) i0_reciprocal110200000.0000
Solution quality estimate total_estimate0.8899
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.9
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.258
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25830000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.935

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)