2n4g

Solution Structure of the G335D Mutant of TDP-43 Amyloidogenic Core Region

Method: SOLUTION NMR Dmax: 93.5 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 311–360 Fragment:UNP residues 311-360 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 80;Pressure ambient NMR sample composition:600 uM [U-99% 13C; U-99% 15N] GB1-TDP(311-360)-G335D-1, 20 mM sodium phosphate-2, 50 mM sodium chloride-3, 8 % [U-99% 2H] D2O-4, 0.02 w/v sodium azide-5, 92 % H2O-6, 93% H2O/7% D2O | 93% H2O/7% 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 1–50; UniProt 311–360

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 2n4g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n4g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2n4g
Deposition date deposition_date2015-06-17
Structure title titleSolution Structure of the G335D Mutant of TDP-43 Amyloidogenic Core Region
Keywords keywordsTDP-43, Amyloidogenic Core Region, G335D, 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_guinier25.74
Radius of gyration Rg (electron density) rg_electron24.90
Forward intensity I(0) i058315700.00
Molecular weight molecular_weight52649.0 kDa
Excluded volume excluded_volume62587 ų
Envelope volume envelope_volume72891 ų
Hydration-shell volume shell_volume22670 ų
Envelope diameter envelope_diameter101.3
Shell Rg shell_rg33.36
Envelope Rg envelope_rg29.89
Shape Rg shape_rg24.90
Total Rg total_rg25.61
Total atoms total_atoms6980
Residues n_residues500
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 dmax93.5
Rg (real space) rg_real25.97
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real5.8320e+07
I(0) uncertainty (real space) i0_real_error1.0160e+06
Rg (reciprocal space) rg_reciprocal25.90
I(0) (reciprocal space) i0_reciprocal58310000.0000
Solution quality estimate total_estimate0.7599
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.395
Kurtosis Kurtosis kurtosis-0.335
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha195500.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.756; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.614; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)