3tir

Pseudo-atomic model of the Rous Sarcoma Virus capsid hexamer

Method: X-RAY DIFFRACTION Dmax: 75.1 Å Quality: GOOD

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

Rous Sarcoma Virus Capsid Protein p27

Rous sarcoma virus

UniProt P03354

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 240–465 Fragment:UNP resides 240-465 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 10.3;291.15 K;2-7 %(w/v) PEG 8000 0.2M CAPS/KOH, pH 10.3, VAPOR DIFFUSION, SITTING DROP, temperature 291.15K Resolution 4.10 Å R-free 0.391

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.

36 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POL_RSVP
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–226; UniProt 240–465

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 3tir

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3tir
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3tir
Deposition date deposition_date2011-08-21
Structure title titlePseudo-atomic model of the Rous Sarcoma Virus capsid hexamer
Keywords keywordsviral capsid protein, Viral Protein; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.10
Radius of gyration Rg (electron density) rg_electron22.23
Forward intensity I(0) i010157700.00
Molecular weight molecular_weight24095.0 kDa
Excluded volume excluded_volume30356 ų
Envelope volume envelope_volume38243 ų
Hydration-shell volume shell_volume15504 ų
Envelope diameter envelope_diameter76.2
Shell Rg shell_rg27.43
Envelope Rg envelope_rg22.21
Shape Rg shape_rg22.23
Total Rg total_rg22.98
Total atoms total_atoms1694
Residues n_residues222
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 dmax75.1
Rg (real space) rg_real23.24
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real1.0160e+07
I(0) uncertainty (real space) i0_real_error1.4180e+05
Rg (reciprocal space) rg_reciprocal23.21
I(0) (reciprocal space) i0_reciprocal10160000.0000
Solution quality estimate total_estimate0.8709
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.6
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis-0.654
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1849000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.756; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)