5ejo

Crystal structure of the winged helix domain in Chromatin assembly factor 1 subunit p90

Method: X-RAY DIFFRACTION Dmax: 45.4 Å Quality: GOOD

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

Chromatin assembly factor 1 subunit p90

Saccharomyces cerevisiae S288c

UniProt Q12495

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 519–606 Fragment:UNP residues 519-606 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;0.1 M NaCl, 1.5 M (NH4)2SO4, 0.1 M BIS-Tris Resolution 2.75 Å R-free 0.230

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.

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RLF2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–94; UniProt 519–606

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 5ejo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ejo
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5ejo
Deposition date deposition_date2015-11-02
Structure title titleCrystal structure of the winged helix domain in Chromatin assembly factor 1 subunit p90
Keywords keywordsChromatin assembly factor 1, Winged helix domain, Nucleosome assembly, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.98
Radius of gyration Rg (electron density) rg_electron12.59
Forward intensity I(0) i01769750.00
Molecular weight molecular_weight8967.0 kDa
Excluded volume excluded_volume11220 ų
Envelope volume envelope_volume12704 ų
Hydration-shell volume shell_volume9098 ų
Envelope diameter envelope_diameter45.6
Shell Rg shell_rg17.61
Envelope Rg envelope_rg12.98
Shape Rg shape_rg12.56
Total Rg total_rg13.89
Total atoms total_atoms631
Residues n_residues79
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 dmax45.4
Rg (real space) rg_real13.94
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real1.7700e+06
I(0) uncertainty (real space) i0_real_error1.7820e+04
Rg (reciprocal space) rg_reciprocal13.95
I(0) (reciprocal space) i0_reciprocal1770000.0000
Solution quality estimate total_estimate0.8867
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.1
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.266
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha236400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)