4ywc

Crystal structure of Myc3(5-242) fragment in complex with Jaz9(218-239) peptide

Method: X-RAY DIFFRACTION Dmax: 74.4 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 5–242 Fragment:N-terminal domain (UNP residues 5-242) Protein TIFY 7 × 1 (Q8W4J8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.9;293 K;The purified proteins at a concentration of 15 mg/ml are mixed with 0.2 M magnesium nitrate, 20% (w/v) polyethylene glycol 3,350. Crystals of about 100 um in length appeared in 3 days Resolution 2.40 Å R-free 0.295
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 5–242 Fragment:N-terminal domain (UNP residues 5-242) Protein TIFY 7 × 1 (Q8W4J8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.9;293 K;The purified proteins at a concentration of 15 mg/ml are mixed with 0.2 M magnesium nitrate, 20% (w/v) polyethylene glycol 3,350. Crystals of about 100 um in length appeared in 3 days Resolution 2.40 Å R-free 0.295

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 Author chain B; PDBConstruct 1–238; UniProt 5–242

Protein TIFY 7

OrganismNot specified

UniProt Q8W4J8

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 194–215 Fragment:UNP residues 194-215 Transcription factor MYC3 × 1 (Q9FIP9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.9;293 K;The purified proteins at a concentration of 15 mg/ml are mixed with 0.2 M magnesium nitrate, 20% (w/v) polyethylene glycol 3,350. Crystals of about 100 um in length appeared in 3 days Resolution 2.40 Å R-free 0.295
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 194–215 Fragment:UNP residues 194-215 Transcription factor MYC3 × 1 (Q9FIP9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.9;293 K;The purified proteins at a concentration of 15 mg/ml are mixed with 0.2 M magnesium nitrate, 20% (w/v) polyethylene glycol 3,350. Crystals of about 100 um in length appeared in 3 days Resolution 2.40 Å R-free 0.295

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIF7_ARATH
Isoform Q8W4J8-2
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–22; UniProt 194–215 Author chain D; PDBConstruct 1–22; UniProt 194–215

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 4ywc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ywc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ywc
Deposition date deposition_date2015-03-20
Structure title titleCrystal structure of Myc3(5-242) fragment in complex with Jaz9(218-239) peptide
Keywords keywordshelix-sheet-helix sandwich fold, Jasmonate signaling, Myc transcription factor, Myc-Jaz complex, 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_guinier23.82
Radius of gyration Rg (electron density) rg_electron22.68
Forward intensity I(0) i034795100.00
Molecular weight molecular_weight43809.0 kDa
Excluded volume excluded_volume54153 ų
Envelope volume envelope_volume67699 ų
Hydration-shell volume shell_volume24973 ų
Envelope diameter envelope_diameter76.5
Shell Rg shell_rg29.51
Envelope Rg envelope_rg22.78
Shape Rg shape_rg22.65
Total Rg total_rg23.58
Total atoms total_atoms3086
Residues n_residues402
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 dmax74.4
Rg (real space) rg_real23.75
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real3.4800e+07
I(0) uncertainty (real space) i0_real_error4.4910e+05
Rg (reciprocal space) rg_reciprocal23.77
I(0) (reciprocal space) i0_reciprocal34800000.0000
Solution quality estimate total_estimate0.9072
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.453
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8585000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.937; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)