7bg6

HRV14 native particle solved by cryoEM

Method: ELECTRON MICROSCOPY Dmax: 96.5 Å Quality: REASONABLE

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

Genome polyprotein

OrganismNot specified

UniProt P03303

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–RNA Homooligomer Protein × 240 RNA 60 PDB declaration: 300-meric(300) Consistent with all polymer counts Chain 1; UniProt 584–856 Chain 2; UniProt 70–331 Chain 3; UniProt 332–567 Chain 4; UniProt 2–69 Not recorded ;RNA-octamer (5'-R(P*UP*GP*UP*UP*UP*UP*UP*A)-3') ; × 60 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;PBS with ph = 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

58 other PDB entries and 240 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_HRV14
Isoform
PDB entities 2, 3, 4, 5
Chains and sequence ranges Author chain 1; PDBConstruct 1–273; UniProt 584–856 Author chain 2; PDBConstruct 1–262; UniProt 70–331 Author chain 3; PDBConstruct 1–236; UniProt 332–567 Author chain 4; PDBConstruct 1–68; UniProt 2–69

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 7bg6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7bg6
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7bg6
Deposition date deposition_date2021-01-06
Structure title titleHRV14 native particle solved by cryoEM
Keywords keywordsenterovirus, rhinovirus 14, HRV14, RV14, native particle, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.91
Radius of gyration Rg (electron density) rg_electron28.65
Forward intensity I(0) i0137842000.00
Molecular weight molecular_weight91608.0 kDa
Excluded volume excluded_volume113980 ų
Envelope volume envelope_volume141250 ų
Hydration-shell volume shell_volume40170 ų
Envelope diameter envelope_diameter101.0
Shell Rg shell_rg36.54
Envelope Rg envelope_rg29.45
Shape Rg shape_rg28.64
Total Rg total_rg29.37
Total atoms total_atoms6439
Residues n_residues813
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 dmax96.5
Rg (real space) rg_real29.87
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real1.3780e+08
I(0) uncertainty (real space) i0_real_error1.8840e+06
Rg (reciprocal space) rg_reciprocal29.89
I(0) (reciprocal space) i0_reciprocal137800000.0000
Solution quality estimate total_estimate0.6919
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.6
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.295
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25690000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 0.135; Positv: 1.000; Valcen: 1.000; Smooth: 0.934

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd7bg61_
Class classb — All beta proteins
Fold Fold foldb.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamilyb.121.4 — Positive stranded ssRNA viruses
Family Family familyb.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)
Domain ID domain_idd7bg63_
Class classb — All beta proteins
Fold Fold foldb.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamilyb.121.4 — Positive stranded ssRNA viruses
Family Family familyb.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

CATH v4.4 (1 domains)

Domain ID domain_id7bg6201
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)