6ccj

NMR structure of the Rous sarcoma virus matrix protein (M domain)

Method: SOLUTION NMR Dmax: 39.9 Å Quality: GOOD

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

virus matrix protein

Rous sarcoma virus (strain Prague C)

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–87 Mutation:M1S No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;305 K;Ionic strength (raw mmCIF value) 0.1;Pressure 1 NMR sample composition:0.5 mM [U-95% 13C; U-95% 15N] RSV MA, 50 mM sodium phosphate, 50 mM sodium chloride, 2 mM TCEP, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:.5 mM [U-95% 15N] Matrix protein, 50 mM sodium phosphate, 50 mM sodium chloride, 2 M TCEP, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.5 mM [U-95% 13C] Matrix protein, 50 mM sodium phosphate, 50 mM sodium chloride, 2 mM TCEP, 100% D2O | 100% D2O 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.

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 2–87; UniProt 2–87

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 6ccj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ccj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ccj
Deposition date deposition_date2018-02-07
Structure title titleNMR structure of the Rous sarcoma virus matrix protein (M domain)
Keywords keywordsRSV, ASV, matrix, Gag, helix, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.56
Radius of gyration Rg (electron density) rg_electron12.30
Forward intensity I(0) i0435834000.00
Molecular weight molecular_weight183700.0 kDa
Excluded volume excluded_volume233430 ų
Envelope volume envelope_volume18765 ų
Hydration-shell volume shell_volume11660 ų
Envelope diameter envelope_diameter46.5
Shell Rg shell_rg19.48
Envelope Rg envelope_rg14.22
Shape Rg shape_rg12.26
Total Rg total_rg12.60
Total atoms total_atoms26360
Residues n_residues1740
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 dmax39.9
Rg (real space) rg_real12.48
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real4.3580e+08
I(0) uncertainty (real space) i0_real_error4.7980e+06
Rg (reciprocal space) rg_reciprocal12.48
I(0) (reciprocal space) i0_reciprocal435800000.0000
Solution quality estimate total_estimate0.8830
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.9
Skewness Skewness skewness0.006
Kurtosis Kurtosis kurtosis-0.413
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha82500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6ccja1
Class classa — All alpha proteins
Fold Fold folda.61 — Retroviral matrix proteins
Superfamily Superfamily superfamilya.61.1 — Retroviral matrix proteins
Family Family familya.61.1.4 — GAG polyprotein M-domain
Domain ID domain_idd6ccja2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)