4rru

Myc3 N-terminal JAZ-binding domain[5-242] from arabidopsis

Method: X-RAY DIFFRACTION Dmax: 55.2 Å Quality: GOOD

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

Transcription factor MYC3

Arabidopsis thaliana

UniProt Q9FIP9

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 5–242 Fragment:Myc3 N-terminal JAZ-binding domain (UNP residues 5-242) CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;0.2 M magnesium chloride, 0.1 M Tris, pH 8.5, 30% (w/v) polyethylene glycol 4000, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.10 Å R-free 0.276
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 5–242 Fragment:Myc3 N-terminal JAZ-binding domain (UNP residues 5-242) CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;0.2 M magnesium chloride, 0.1 M Tris, pH 8.5, 30% (w/v) polyethylene glycol 4000, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.10 Å R-free 0.276

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.

8 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYC3_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–238; UniProt 5–242

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 4rru

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4rru
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4rru
Deposition date deposition_date2014-11-06
Structure title titleMyc3 N-terminal JAZ-binding domain[5-242] from arabidopsis
Keywords keywordsHelix-Sheet-Helix fold, Transcription factor, JAZ repressors, Nuclear, TRANSCRIPTION REGULATOR; TRANSCRIPTION REGULATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.54
Radius of gyration Rg (electron density) rg_electron16.17
Forward intensity I(0) i08453970.00
Molecular weight molecular_weight20579.0 kDa
Excluded volume excluded_volume25411 ų
Envelope volume envelope_volume29405 ų
Hydration-shell volume shell_volume15385 ų
Envelope diameter envelope_diameter54.3
Shell Rg shell_rg22.22
Envelope Rg envelope_rg16.56
Shape Rg shape_rg16.15
Total Rg total_rg17.25
Total atoms total_atoms1446
Residues n_residues189
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 dmax55.2
Rg (real space) rg_real17.45
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real8.4540e+06
I(0) uncertainty (real space) i0_real_error8.4760e+04
Rg (reciprocal space) rg_reciprocal17.46
I(0) (reciprocal space) i0_reciprocal8454000.0000
Solution quality estimate total_estimate0.8939
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.205
Kurtosis Kurtosis kurtosis-0.313
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1690000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)