5wia

Crystal structure of the segment, GNNSYS, from the low complexity domain of TDP-43, residues 370-375

Method: X-RAY DIFFRACTION Dmax: 25.8 Å Quality: GOOD

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

TAR DNA-binding protein 43

OrganismNot specified

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 homooligomer Homooligomer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 370–375 Fragment:UNP residues 370-375 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;298 K;100mM bis tris propane 8.5, 200mM sodium nitrate, 20% PEG 3350 Resolution 1.00 Å R-free 0.181

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 1–6; UniProt 370–375

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 5wia

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5wia
Deposition date deposition_date2017-07-18
Structure title titleCrystal structure of the segment, GNNSYS, from the low complexity domain of TDP-43, residues 370-375
Keywords keywordsAmyloid, TDP-43, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier7.32
Radius of gyration Rg (electron density) rg_electron5.92
Forward intensity I(0) i028876.70
Molecular weight molecular_weight640.6 kDa
Excluded volume excluded_volume726 ų
Envelope volume envelope_volume909 ų
Hydration-shell volume shell_volume1863 ų
Envelope diameter envelope_diameter21.3
Shell Rg shell_rg9.12
Envelope Rg envelope_rg6.36
Shape Rg shape_rg5.84
Total Rg total_rg7.59
Total atoms total_atoms45
Residues n_residues6
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 dmax25.8
Rg (real space) rg_real7.41
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real2.8880e+04
I(0) uncertainty (real space) i0_real_error3.1070e+02
Rg (reciprocal space) rg_reciprocal7.41
I(0) (reciprocal space) i0_reciprocal28880.0000
Solution quality estimate total_estimate0.8477
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary7.8
Skewness Skewness skewness0.516
Kurtosis Kurtosis kurtosis-0.136
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1639.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.631; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)