5n5a

Structure of Tau(254-290) bound to F-actin

Method: SOLUTION NMR Dmax: 76.5 Å Quality: REASONABLE

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

Microtubule-associated protein tau

OrganismNot specified

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 571–607 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.8;278 K;Pressure ambient NMR measurement conditions:pH 6.8;278 K;Pressure ambient NMR sample composition:800 uM Tau(254-290), 27 uM F-actin, 50 mM sodium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:800 uM Tau(254-290), 50 mM sodium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O 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 1–37; UniProt 571–607

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 5n5a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5n5a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5n5a
Deposition date deposition_date2017-02-13
Structure title titleStructure of Tau(254-290) bound to F-actin
Keywords keywords;tau, F-actin, protein binding, Alzheimer's disease, structural protein ;; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.54
Radius of gyration Rg (electron density) rg_electron20.58
Forward intensity I(0) i092557900.00
Molecular weight molecular_weight80454.0 kDa
Excluded volume excluded_volume101640 ų
Envelope volume envelope_volume20466 ų
Hydration-shell volume shell_volume9411 ų
Envelope diameter envelope_diameter81.3
Shell Rg shell_rg25.29
Envelope Rg envelope_rg24.31
Shape Rg shape_rg20.47
Total Rg total_rg21.13
Total atoms total_atoms11820
Residues n_residues740
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 dmax76.5
Rg (real space) rg_real20.35
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real9.2560e+07
I(0) uncertainty (real space) i0_real_error1.3370e+06
Rg (reciprocal space) rg_reciprocal20.23
I(0) (reciprocal space) i0_reciprocal92550000.0000
Solution quality estimate total_estimate0.5406
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary7.5
Skewness Skewness skewness0.664
Kurtosis Kurtosis kurtosis-0.380
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14480.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.007; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.002; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)