8seh

PHF Tau from Down Syndrome

Method: ELECTRON MICROSCOPY Dmax: 135.4 Å Quality: GOOD

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

Microtubule-associated protein tau

Homo sapiens

UniProt P10636

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 275–347 Chain B; UniProt 275–347 Chain C; UniProt 275–347 Chain D; UniProt 275–347 Chain E; UniProt 275–347 Chain F; UniProt 275–347 Chain G; UniProt 275–347 Chain H; UniProt 275–347 Chain I; UniProt 275–347 Chain J; UniProt 275–347 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 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.

248 other PDB entries and 270 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAU_HUMAN
Isoform P10636-5
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–73; UniProt 275–347 Author chain B; PDBConstruct 1–73; UniProt 275–347 Author chain C; PDBConstruct 1–73; UniProt 275–347 Author chain D; PDBConstruct 1–73; UniProt 275–347 Author chain E; PDBConstruct 1–73; UniProt 275–347 Author chain F; PDBConstruct 1–73; UniProt 275–347 Author chain G; PDBConstruct 1–73; UniProt 275–347 Author chain H; PDBConstruct 1–73; UniProt 275–347 Author chain I; PDBConstruct 1–73; UniProt 275–347 Author chain J; PDBConstruct 1–73; UniProt 275–347

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 8seh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8seh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8seh
Deposition date deposition_date2023-04-10
Structure title titlePHF Tau from Down Syndrome
Keywords keywordsPHF Tau, Tau Filament, Down Syndrome, NEUROPEPTIDE, Human Trisomy 21; NEUROPEPTIDE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.61
Radius of gyration Rg (electron density) rg_electron36.63
Forward intensity I(0) i095805500.00
Molecular weight molecular_weight79122.0 kDa
Excluded volume excluded_volume99845 ų
Envelope volume envelope_volume129940 ų
Hydration-shell volume shell_volume33378 ų
Envelope diameter envelope_diameter137.5
Shell Rg shell_rg37.64
Envelope Rg envelope_rg36.68
Shape Rg shape_rg36.60
Total Rg total_rg36.79
Total atoms total_atoms5570
Residues n_residues730
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 dmax135.4
Rg (real space) rg_real35.07
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real9.5810e+07
I(0) uncertainty (real space) i0_real_error1.8700e+06
Rg (reciprocal space) rg_reciprocal34.78
I(0) (reciprocal space) i0_reciprocal95780000.0000
Solution quality estimate total_estimate0.7634
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.3
Skewness Skewness skewness0.706
Kurtosis Kurtosis kurtosis0.190
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4840000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.452; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.589; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)