8g55

Temperature-dependent structures of tau aggregates

Method: SOLID-STATE NMR Dmax: 115.0 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 198–399 Chain B; UniProt 198–399 Chain C; UniProt 198–399 Chain D; UniProt 198–399 Chain E; UniProt 198–399 Chain F; UniProt 198–399 Chain G; UniProt 198–399 Chain H; UniProt 198–399 Chain I; UniProt 198–399 Chain J; UniProt 198–399 Not recorded No other associated polymer SOLID-STATE NMR NMR measurement conditions:pH 7.4;285 K;Ionic strength (raw mmCIF value) 135;Pressure 1 NMR sample composition:5 uM [U-13C; U-15N] P2R tau, 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 P10636-8
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–202; UniProt 198–399 Author chain B; PDBConstruct 1–202; UniProt 198–399 Author chain C; PDBConstruct 1–202; UniProt 198–399 Author chain D; PDBConstruct 1–202; UniProt 198–399 Author chain E; PDBConstruct 1–202; UniProt 198–399 Author chain F; PDBConstruct 1–202; UniProt 198–399 Author chain G; PDBConstruct 1–202; UniProt 198–399 Author chain H; PDBConstruct 1–202; UniProt 198–399 Author chain I; PDBConstruct 1–202; UniProt 198–399 Author chain J; PDBConstruct 1–202; UniProt 198–399

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 8g55

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8g55
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8g55
Deposition date deposition_date2023-02-11
Structure title titleTemperature-dependent structures of tau aggregates
Keywords keywordstau, amyloid fibril, 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_guinier33.54
Radius of gyration Rg (electron density) rg_electron33.21
Forward intensity I(0) i06110520000.00
Molecular weight molecular_weight660370.0 kDa
Excluded volume excluded_volume829490 ų
Envelope volume envelope_volume228120 ų
Hydration-shell volume shell_volume51641 ų
Envelope diameter envelope_diameter125.4
Shell Rg shell_rg43.15
Envelope Rg envelope_rg36.80
Shape Rg shape_rg33.26
Total Rg total_rg33.16
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 dmax115.0
Rg (real space) rg_real33.69
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real6.1110e+09
I(0) uncertainty (real space) i0_real_error9.7220e+07
Rg (reciprocal space) rg_reciprocal33.60
I(0) (reciprocal space) i0_reciprocal6110000000.0000
Solution quality estimate total_estimate0.6457
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.2
Skewness Skewness skewness0.423
Kurtosis Kurtosis kurtosis-0.348
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5356000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 1.000; Sysdev: 0.078; Positv: 1.000; Valcen: 0.825; Smooth: 0.820

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)