8t2i

Negative stain EM assembly of MYC, JAZ, and NINJA complex

Method: ELECTRON MICROSCOPY Dmax: 137.5 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 49–238 Not recorded Maltose/maltodextrin-binding periplasmic protein × 1 (P0AEY0) Protein TIFY 10A × 1 (Q9LMA8) AFP homolog 2 × 1 (Q9SV55) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 Resolution 10.40 Å

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 13 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 1–190; UniProt 49–238

Maltose/maltodextrin-binding periplasmic protein

Escherichia coli

UniProt P0AEY0

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain M; UniProt 27–392 Not recorded Transcription factor MYC3 × 1 (Q9FIP9) Protein TIFY 10A × 1 (Q9LMA8) AFP homolog 2 × 1 (Q9SV55) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 Resolution 10.40 Å

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.

109 other PDB entries and 148 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECO57
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 32–397; UniProt 27–392

Protein TIFY 10A

Arabidopsis thaliana

UniProt Q9LMA8

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain J; UniProt 1–253 Not recorded Transcription factor MYC3 × 1 (Q9FIP9) Maltose/maltodextrin-binding periplasmic protein × 1 (P0AEY0) AFP homolog 2 × 1 (Q9SV55) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 Resolution 10.40 Å

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 TI10A_ARATH
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–253; UniProt 1–253

AFP homolog 2

Arabidopsis thaliana

UniProt Q9SV55

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain N; UniProt 1–425 Not recorded Transcription factor MYC3 × 1 (Q9FIP9) Maltose/maltodextrin-binding periplasmic protein × 1 (P0AEY0) Protein TIFY 10A × 1 (Q9LMA8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 Resolution 10.40 Å

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 NINJA_ARATH
Isoform
PDB entities 4
Chains and sequence ranges Author chain N; PDBConstruct 1–425; UniProt 1–425

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 8t2i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t2i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t2i
Deposition date deposition_date2023-06-06
Structure title titleNegative stain EM assembly of MYC, JAZ, and NINJA complex
Keywords keywordsJasmonate signaling, MYC, JAZ, NINJA, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.26
Radius of gyration Rg (electron density) rg_electron42.78
Forward intensity I(0) i0279211000.00
Molecular weight molecular_weight131410.0 kDa
Excluded volume excluded_volume162500 ų
Envelope volume envelope_volume274420 ų
Hydration-shell volume shell_volume53759 ų
Envelope diameter envelope_diameter141.6
Shell Rg shell_rg48.53
Envelope Rg envelope_rg40.57
Shape Rg shape_rg42.76
Total Rg total_rg43.18
Total atoms total_atoms9243
Residues n_residues1220
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 dmax137.5
Rg (real space) rg_real43.12
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real2.7920e+08
I(0) uncertainty (real space) i0_real_error4.6980e+06
Rg (reciprocal space) rg_reciprocal43.26
I(0) (reciprocal space) i0_reciprocal279300000.0000
Solution quality estimate total_estimate0.9043
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.1
Skewness Skewness skewness0.071
Kurtosis Kurtosis kurtosis-0.722
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25960000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.922

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)