2ovn

NMR structure of the GCN4 trigger peptide

Method: SOLUTION NMR Dmax: 30.9 Å Quality: REASONABLE

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

General control protein GCN4

OrganismNot specified

UniProt P03069

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 264–280 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

162 other PDB entries and 200 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCN4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–17; UniProt 264–280

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 2ovn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2ovn
Deposition date deposition_date2007-02-14
Structure title titleNMR structure of the GCN4 trigger peptide
Keywords keywordsGCN4, coiled-coil, trigger peptide, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier7.91
Radius of gyration Rg (electron density) rg_electron8.14
Forward intensity I(0) i023542700.00
Molecular weight molecular_weight40246.0 kDa
Excluded volume excluded_volume50554 ų
Envelope volume envelope_volume5792 ų
Hydration-shell volume shell_volume5422 ų
Envelope diameter envelope_diameter34.4
Shell Rg shell_rg14.57
Envelope Rg envelope_rg10.90
Shape Rg shape_rg8.13
Total Rg total_rg8.49
Total atoms total_atoms5720
Residues n_residues340
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 dmax30.9
Rg (real space) rg_real8.13
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.3540e+07
I(0) uncertainty (real space) i0_real_error2.2460e+05
Rg (reciprocal space) rg_reciprocal8.12
I(0) (reciprocal space) i0_reciprocal23540000.0000
Solution quality estimate total_estimate0.6799
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary6.3
Skewness Skewness skewness0.669
Kurtosis Kurtosis kurtosis-0.197
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1147.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.343; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.025; Smooth: 0.779

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)