8g58

Tau (297-391) in vitro untwisted fibril

Method: SOLID-STATE NMR Dmax: 132.5 Å Quality: REASONABLE

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 614–708 Chain B; UniProt 614–708 Chain C; UniProt 614–708 Chain D; UniProt 614–708 Chain E; UniProt 614–708 Chain F; UniProt 614–708 Chain G; UniProt 614–708 Chain H; UniProt 614–708 Chain I; UniProt 614–708 Chain J; UniProt 614–708 Not recorded No other associated polymer SOLID-STATE NMR NMR measurement conditions:pH 5;287 K;Ionic strength (raw mmCIF value) 0.6;Pressure 1 NMR sample composition:1 uM UCN Tau (297-391), 100% H2O | 100% H2O NMR sample composition:0.5 uM UCN Tau (297-391), 0.5 uM Tau (297-391), 100% H2O | 100% H2O NMR sample composition:1 uM 1,3-Glycerol,15N Tau (297-391), 100% H2O | 100% H2O Resolution not provided

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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–96; UniProt 614–708 Author chain B; PDBConstruct 2–96; UniProt 614–708 Author chain C; PDBConstruct 2–96; UniProt 614–708 Author chain D; PDBConstruct 2–96; UniProt 614–708 Author chain E; PDBConstruct 2–96; UniProt 614–708 Author chain F; PDBConstruct 2–96; UniProt 614–708 Author chain G; PDBConstruct 2–96; UniProt 614–708 Author chain H; PDBConstruct 2–96; UniProt 614–708 Author chain I; PDBConstruct 2–96; UniProt 614–708 Author chain J; PDBConstruct 2–96; UniProt 614–708

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 8g58

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8g58
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8g58
Deposition date deposition_date2023-02-12
Structure title titleTau (297-391) in vitro untwisted fibril
Keywords keywordsAD tau core, untwisted filament, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodSOLID-STATE NMR

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

Radius of gyration Rg (Guinier) rg_guinier34.09
Radius of gyration Rg (electron density) rg_electron34.08
Forward intensity I(0) i06194810000.00
Molecular weight molecular_weight665660.0 kDa
Excluded volume excluded_volume834210 ų
Envelope volume envelope_volume159150 ų
Hydration-shell volume shell_volume38802 ų
Envelope diameter envelope_diameter143.7
Shell Rg shell_rg38.85
Envelope Rg envelope_rg39.11
Shape Rg shape_rg34.01
Total Rg total_rg34.37
Total atoms total_atoms95300
Residues n_residues6300
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 dmax132.5
Rg (real space) rg_real34.76
Rg uncertainty (real space) rg_real_error2.10
I(0) (real space) i0_real6.1950e+09
I(0) uncertainty (real space) i0_real_error1.3220e+08
Rg (reciprocal space) rg_reciprocal34.34
I(0) (reciprocal space) i0_reciprocal6193000000.0000
Solution quality estimate total_estimate0.6807
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.753
Kurtosis Kurtosis kurtosis0.037
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7427000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.276; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.149; Smooth: 0.866

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)