1c20

SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN

Method: SOLUTION NMR Dmax: 53.4 Å Quality: GOOD

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

DEAD RINGER PROTEIN

Drosophila melanogaster

UniProt Q24573

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 262–389 Fragment:DNA-BINDING DOMAIN No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.7;303 K;Ionic strength (raw mmCIF value) 0.10;Pressure AMBIENT NMR sample composition:1.5MM DEAD RINGER U-15N; 20MM TRIS-HCL (PH 6.7); 100MM NACL; 1.5MM ZNCL2; 2MM DTT; 0.01% NAN3 NMR sample composition:1.5MM DEAD RINGER U-15N,13C; 20MM TRIS-HCL (PH 6.7); 100MM NACL; 1.5MM ZNCL2; 2MM DTT; 0.01% NAN3 Resolution not provided

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 DRI_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–128; UniProt 262–389

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 1c20

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c20
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c20
Deposition date deposition_date1999-07-22
Structure title titleSOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN FROM THE DEAD RINGER PROTEIN
Keywords keywordsDNA-BINDING DOMAIN, ARID, AT-RICH INTERACTION DOMAIN, DNA-BINDING PROTEIN, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.72
Radius of gyration Rg (electron density) rg_electron15.10
Forward intensity I(0) i01232770000.00
Molecular weight molecular_weight313940.0 kDa
Excluded volume excluded_volume399120 ų
Envelope volume envelope_volume33919 ų
Hydration-shell volume shell_volume16825 ų
Envelope diameter envelope_diameter56.9
Shell Rg shell_rg23.05
Envelope Rg envelope_rg17.18
Shape Rg shape_rg15.08
Total Rg total_rg15.29
Total atoms total_atoms44604
Residues n_residues2688
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 dmax53.4
Rg (real space) rg_real15.63
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real1.2330e+09
I(0) uncertainty (real space) i0_real_error1.4920e+07
Rg (reciprocal space) rg_reciprocal15.64
I(0) (reciprocal space) i0_reciprocal1233000000.0000
Solution quality estimate total_estimate0.8486
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.6
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.366
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha236300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.682; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1c20a_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.3 — ARID-like
Family Family familya.4.3.1 — ARID domain

CATH v4.4 (1 domains)

Domain ID domain_id1c20A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily60 — ARID DNA-binding domain

8. Citations (1)

9. Files and Curves (10)