5l7a

The crystal structure of the Human SNF5/INI1 domain

Method: X-RAY DIFFRACTION Dmax: 59.9 Å Quality: EXCELLENT

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

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1

Homo sapiens

UniProt Q12824

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 184–252 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;277 K;1.4 M tri-sodium citrate and 100 mM HEPES pH 7.5 Resolution 2.10 Å R-free 0.260
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 184–252 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;277 K;1.4 M tri-sodium citrate and 100 mM HEPES pH 7.5 Resolution 2.10 Å R-free 0.260
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 184–252 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;277 K;1.4 M tri-sodium citrate and 100 mM HEPES pH 7.5 Resolution 2.10 Å R-free 0.260
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 184–252 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;277 K;1.4 M tri-sodium citrate and 100 mM HEPES pH 7.5 Resolution 2.10 Å R-free 0.260

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.

15 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNF5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–72; UniProt 184–252 Author chain B; PDBConstruct 4–72; UniProt 184–252 Author chain C; PDBConstruct 4–72; UniProt 184–252 Author chain D; PDBConstruct 4–72; UniProt 184–252

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 5l7a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5l7a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5l7a
Deposition date deposition_date2016-06-02
Structure title titleThe crystal structure of the Human SNF5/INI1 domain
Keywords keywordsSNF5 INI1 domain crystal, DNA binding protein; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.96
Radius of gyration Rg (electron density) rg_electron18.78
Forward intensity I(0) i015834800.00
Molecular weight molecular_weight30266.0 kDa
Excluded volume excluded_volume38059 ų
Envelope volume envelope_volume46469 ų
Hydration-shell volume shell_volume20466 ų
Envelope diameter envelope_diameter60.1
Shell Rg shell_rg25.17
Envelope Rg envelope_rg18.89
Shape Rg shape_rg18.78
Total Rg total_rg19.74
Total atoms total_atoms2117
Residues n_residues265
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 dmax59.9
Rg (real space) rg_real19.79
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real1.5830e+07
I(0) uncertainty (real space) i0_real_error1.5950e+05
Rg (reciprocal space) rg_reciprocal19.82
I(0) (reciprocal space) i0_reciprocal15840000.0000
Solution quality estimate total_estimate0.9046
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.082
Kurtosis Kurtosis kurtosis-0.497
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4797000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)