5c6q

Crystal structure of the apo TOPLESS related protein 2 (TPR2) N-terminal domain (1-209) from rice

Method: X-RAY DIFFRACTION Dmax: 91.9 Å Quality: REASONABLE

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

ASPR2 protein

Oryza sativa

UniProt Q5NBT9

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–209 Fragment:N-terminal domain (UNP residues 1-209) ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;25% PEG 3350, 0.2 M magnesium chloride, 0.1 M BIS-TRIS, pH 6.5 Resolution 3.25 Å R-free 0.270

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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5NBT9_ORYSJ
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–209; UniProt 1–209

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 5c6q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5c6q
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5c6q
Deposition date deposition_date2015-06-23
Structure title titleCrystal structure of the apo TOPLESS related protein 2 (TPR2) N-terminal domain (1-209) from rice
Keywords keywords;Transcriptional corepressor, alpha-helical structure, tetrameric protein, plant transcriptional repression, TRANSCRIPTION, plant development ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.67
Radius of gyration Rg (electron density) rg_electron24.16
Forward intensity I(0) i09848740.00
Molecular weight molecular_weight24179.0 kDa
Excluded volume excluded_volume30623 ų
Envelope volume envelope_volume39642 ų
Hydration-shell volume shell_volume16104 ų
Envelope diameter envelope_diameter91.9
Shell Rg shell_rg27.08
Envelope Rg envelope_rg24.85
Shape Rg shape_rg24.08
Total Rg total_rg24.82
Total atoms total_atoms1704
Residues n_residues205
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 dmax91.9
Rg (real space) rg_real25.32
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real9.8490e+06
I(0) uncertainty (real space) i0_real_error1.5220e+05
Rg (reciprocal space) rg_reciprocal25.16
I(0) (reciprocal space) i0_reciprocal9848000.0000
Solution quality estimate total_estimate0.7110
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.774
Kurtosis Kurtosis kurtosis-0.013
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1011000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.395; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.147; Smooth: 0.905

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)