9fof

Structure of heteromeric amyloid filament of TDP-43 and AXNA11 from FTLD-TDP Type C (variant 2)

Method: ELECTRON MICROSCOPY Dmax: 84.6 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 heterocomplex Heteromer Protein × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain A; UniProt 282–345 Chain C; UniProt 282–345 Chain E; UniProt 282–345 Chain G; UniProt 282–345 Chain I; UniProt 282–345 Chain q; UniProt 282–345 Not recorded Annexin A11 × 6 (P50995) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–64; UniProt 282–345 Author chain C; PDBConstruct 1–64; UniProt 282–345 Author chain E; PDBConstruct 1–64; UniProt 282–345 Author chain G; PDBConstruct 1–64; UniProt 282–345 Author chain I; PDBConstruct 1–64; UniProt 282–345 Author chain q; PDBConstruct 1–64; UniProt 282–345

Annexin A11

OrganismNot specified

UniProt P50995

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 heterocomplex Heteromer Protein × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain B; UniProt 39–74 Chain D; UniProt 39–74 Chain F; UniProt 39–74 Chain H; UniProt 39–74 Chain J; UniProt 39–74 Chain r; UniProt 39–74 Not recorded TAR DNA-binding protein 43 × 6 (Q13148) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANX11_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–36; UniProt 39–74 Author chain D; PDBConstruct 1–36; UniProt 39–74 Author chain F; PDBConstruct 1–36; UniProt 39–74 Author chain H; PDBConstruct 1–36; UniProt 39–74 Author chain J; PDBConstruct 1–36; UniProt 39–74 Author chain r; PDBConstruct 1–36; UniProt 39–74

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 9fof

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fof
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fof
Deposition date deposition_date2024-06-11
Structure title titleStructure of heteromeric amyloid filament of TDP-43 and AXNA11 from FTLD-TDP Type C (variant 2)
Keywords keywordsTDP-43, ANXA11, amyloid, heteromeric amyloid, FTLD-TDP, neurodegeneration, dementia, brain, protein filament, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier25.48
Radius of gyration Rg (electron density) rg_electron24.52
Forward intensity I(0) i072944900.00
Molecular weight molecular_weight60006.0 kDa
Excluded volume excluded_volume72058 ų
Envelope volume envelope_volume89323 ų
Hydration-shell volume shell_volume29978 ų
Envelope diameter envelope_diameter88.5
Shell Rg shell_rg32.46
Envelope Rg envelope_rg24.86
Shape Rg shape_rg24.61
Total Rg total_rg25.06
Total atoms total_atoms4176
Residues n_residues600
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 dmax84.6
Rg (real space) rg_real25.42
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real7.2940e+07
I(0) uncertainty (real space) i0_real_error9.9170e+05
Rg (reciprocal space) rg_reciprocal25.44
I(0) (reciprocal space) i0_reciprocal72950000.0000
Solution quality estimate total_estimate0.8905
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.7
Skewness Skewness skewness0.273
Kurtosis Kurtosis kurtosis-0.428
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10940000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (3)

9. Files and Curves (10)