5x4f

Solution Structure of the N-terminal Domain of TDP-43

Method: SOLUTION NMR Dmax: 38.0 Å Quality: GOOD

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 1–77 Fragment:UNP residues 1-77 Mutation:C39S/C50S No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 0.08;Pressure 1 NMR sample composition:1 mM U-99% 13C; U-99% 15N TDP(1-77)-GB1-C39/C50S, 20 mM sodium phosphate, 50 mM sodium chloride, 0.05 v/v sodium azide, 90 % H2O, 10 % D2O, 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 1–77; UniProt 1–77

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 5x4f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5x4f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5x4f
Deposition date deposition_date2017-02-13
Structure title titleSolution Structure of the N-terminal Domain of TDP-43
Keywords keywordsDimerization, 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_guinier12.08
Radius of gyration Rg (electron density) rg_electron11.65
Forward intensity I(0) i0110016000.00
Molecular weight molecular_weight84894.0 kDa
Excluded volume excluded_volume105040 ų
Envelope volume envelope_volume16145 ų
Hydration-shell volume shell_volume10793 ų
Envelope diameter envelope_diameter40.9
Shell Rg shell_rg18.45
Envelope Rg envelope_rg13.11
Shape Rg shape_rg11.60
Total Rg total_rg12.07
Total atoms total_atoms11730
Residues n_residues770
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 dmax38.0
Rg (real space) rg_real11.98
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real1.1000e+08
I(0) uncertainty (real space) i0_real_error1.1010e+06
Rg (reciprocal space) rg_reciprocal11.99
I(0) (reciprocal space) i0_reciprocal110000000.0000
Solution quality estimate total_estimate0.8844
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.9
Skewness Skewness skewness-0.005
Kurtosis Kurtosis kurtosis-0.398
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha97980.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)