6n37

SegA-sym, conformation of TDP-43 low complexity domain segment A sym

Method: ELECTRON MICROSCOPY Dmax: 85.9 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 homooligomer Homooligomer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 195–244 Chain B; UniProt 195–244 Chain C; UniProt 195–244 Chain D; UniProt 195–244 Chain E; UniProt 195–244 Chain F; UniProt 195–244 Chain G; UniProt 195–244 Chain H; UniProt 195–244 Chain I; UniProt 195–244 Chain J; UniProt 195–244 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 Å

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 Q13148-4
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–50; UniProt 195–244 Author chain B; PDBConstruct 1–50; UniProt 195–244 Author chain C; PDBConstruct 1–50; UniProt 195–244 Author chain D; PDBConstruct 1–50; UniProt 195–244 Author chain E; PDBConstruct 1–50; UniProt 195–244 Author chain F; PDBConstruct 1–50; UniProt 195–244 Author chain G; PDBConstruct 1–50; UniProt 195–244 Author chain H; PDBConstruct 1–50; UniProt 195–244 Author chain I; PDBConstruct 1–50; UniProt 195–244 Author chain J; PDBConstruct 1–50; UniProt 195–244

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 6n37

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6n37
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6n37
Deposition date deposition_date2018-11-14
Structure title titleSegA-sym, conformation of TDP-43 low complexity domain segment A sym
Keywords keywordsAmyloid, TDP43, ALS, FTLD-TDP, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier23.09
Radius of gyration Rg (electron density) rg_electron22.08
Forward intensity I(0) i027451300.00
Molecular weight molecular_weight37323.0 kDa
Excluded volume excluded_volume45436 ų
Envelope volume envelope_volume53923 ų
Hydration-shell volume shell_volume21375 ų
Envelope diameter envelope_diameter79.8
Shell Rg shell_rg28.53
Envelope Rg envelope_rg22.34
Shape Rg shape_rg22.10
Total Rg total_rg22.77
Total atoms total_atoms2580
Residues n_residues360
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 dmax85.9
Rg (real space) rg_real23.20
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real2.7450e+07
I(0) uncertainty (real space) i0_real_error3.9690e+05
Rg (reciprocal space) rg_reciprocal23.17
I(0) (reciprocal space) i0_reciprocal27450000.0000
Solution quality estimate total_estimate0.7347
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.5
Skewness Skewness skewness0.500
Kurtosis Kurtosis kurtosis-0.182
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17390000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.609; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.720; 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)