1wf0

Solution structure of RRM domain in TAR DNA-binding protein-43

Method: SOLUTION NMR Dmax: 58.5 Å Quality: REASONABLE

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

TAR DNA-binding protein-43

Homo sapiens

UniProt Q13148

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 193–267 Fragment:RRM domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR sample composition:0.8mM U-15, 13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O | 90% H2O/10% D2O 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.

41 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TADBP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–82; UniProt 193–267

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 1wf0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1wf0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1wf0
Deposition date deposition_date2004-05-25
Structure title titleSolution structure of RRM domain in TAR DNA-binding protein-43
Keywords keywords;structural genomics, RRM domain, TAR DNA-binding protein-43, RIKEN Structural Genomics/Proteomics Initiative, RSGI, RNA binding protein ;; RNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.70
Radius of gyration Rg (electron density) rg_electron13.98
Forward intensity I(0) i0538788000.00
Molecular weight molecular_weight187710.0 kDa
Excluded volume excluded_volume230930 ų
Envelope volume envelope_volume31789 ų
Hydration-shell volume shell_volume15167 ų
Envelope diameter envelope_diameter62.0
Shell Rg shell_rg24.36
Envelope Rg envelope_rg20.30
Shape Rg shape_rg13.95
Total Rg total_rg14.32
Total atoms total_atoms25560
Residues n_residues1760
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 dmax58.5
Rg (real space) rg_real14.83
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real5.3880e+08
I(0) uncertainty (real space) i0_real_error6.8220e+06
Rg (reciprocal space) rg_reciprocal14.82
I(0) (reciprocal space) i0_reciprocal538800000.0000
Solution quality estimate total_estimate0.7308
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.3
Skewness Skewness skewness0.633
Kurtosis Kurtosis kurtosis0.346
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha255300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.305; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.586; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1wf0a1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.1 — Canonical RBD
Domain ID domain_idd1wf0a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1wf0a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1wf0A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain

8. Citations (1)

9. Files and Curves (10)