2bbp

NMR structures of the peptide linked to the genome (VPg) of poliovirus

Method: SOLUTION NMR Dmax: 31.8 Å Quality: REASONABLE

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

Genome linked protein VPg

OrganismNot specified

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1544–1565 Fragment:residues 1-22 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.2;283 K;Ionic strength (raw mmCIF value) 10 mM;Pressure 1 NMR sample composition:3.7 mM peptide, 10 mM Na phosphate buffer, pH 7.2, DSS, 10% D20, 90% H2O | 10% D20, 90% H2O Resolution not provided

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 250 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_POL1M
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–22; UniProt 1544–1565

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 2bbp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2bbp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2bbp
Deposition date deposition_date2005-10-17
Structure title titleNMR structures of the peptide linked to the genome (VPg) of poliovirus
Keywords keywordsVPg, RNA transcription primer, flexible structure, viral polymerase, picornavirus, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier7.72
Radius of gyration Rg (electron density) rg_electron7.71
Forward intensity I(0) i07592450.00
Molecular weight molecular_weight23408.0 kDa
Excluded volume excluded_volume29951 ų
Envelope volume envelope_volume4927 ų
Hydration-shell volume shell_volume5263 ų
Envelope diameter envelope_diameter31.1
Shell Rg shell_rg13.43
Envelope Rg envelope_rg9.11
Shape Rg shape_rg7.67
Total Rg total_rg8.34
Total atoms total_atoms3400
Residues n_residues220
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 dmax31.8
Rg (real space) rg_real7.76
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real7.5920e+06
I(0) uncertainty (real space) i0_real_error8.8750e+04
Rg (reciprocal space) rg_reciprocal7.76
I(0) (reciprocal space) i0_reciprocal7592000.0000
Solution quality estimate total_estimate0.7337
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary9.7
Skewness Skewness skewness0.440
Kurtosis Kurtosis kurtosis0.297
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5504.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.315; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.651; Smooth: 0.948

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2bbpa1
Class classj — Peptides
Fold Fold foldj.120 — Genome linked protein vpg
Superfamily Superfamily superfamilyj.120.1 — Genome linked protein vpg
Family Family familyj.120.1.1 — Genome linked protein vpg

8. Citations (2)

9. Files and Curves (10)