7kwz

TDP-43 LCD amyloid fibrils

Method: ELECTRON MICROSCOPY Dmax: 96.9 Å Quality: GOOD

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

Isoform 2 of 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 151–298 Chain B; UniProt 151–298 Chain C; UniProt 151–298 Chain D; UniProt 151–298 Chain E; UniProt 151–298 Mutation:low complexity domain (UNP residues 151-298) No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 1–148; UniProt 151–298 Author chain B; PDBConstruct 1–148; UniProt 151–298 Author chain C; PDBConstruct 1–148; UniProt 151–298 Author chain D; PDBConstruct 1–148; UniProt 151–298 Author chain E; PDBConstruct 1–148; UniProt 151–298

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 7kwz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7kwz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7kwz
Deposition date deposition_date2020-12-02
Structure title titleTDP-43 LCD amyloid fibrils
Keywords keywordsTDP-43, amyloid, neurodegenerative diseases, amyotropic lateral sclerosis, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.17
Radius of gyration Rg (electron density) rg_electron28.63
Forward intensity I(0) i099645900.00
Molecular weight molecular_weight67257.0 kDa
Excluded volume excluded_volume79028 ų
Envelope volume envelope_volume96955 ų
Hydration-shell volume shell_volume29343 ų
Envelope diameter envelope_diameter99.4
Shell Rg shell_rg34.70
Envelope Rg envelope_rg29.03
Shape Rg shape_rg28.65
Total Rg total_rg29.07
Total atoms total_atoms4695
Residues n_residues695
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 dmax96.9
Rg (real space) rg_real29.30
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real9.9650e+07
I(0) uncertainty (real space) i0_real_error1.4540e+06
Rg (reciprocal space) rg_reciprocal29.25
I(0) (reciprocal space) i0_reciprocal99640000.0000
Solution quality estimate total_estimate0.8797
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.7
Skewness Skewness skewness0.423
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha17550000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.904; Smooth: 0.896

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)