8vdr

Cryogenic electron microscopy model of full-length talin without R12 and FABD

Method: ELECTRON MICROSCOPY Dmax: 141.6 Å Quality: GOOD

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

Green fluorescent protein,Talin-1

Mus musculus

UniProt P26039

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 1–2541 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

50 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TLN1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 264–2804; UniProt 1–2541

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 8vdr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vdr
Deposition date deposition_date2023-12-17
Structure title titleCryogenic electron microscopy model of full-length talin without R12 and FABD
Keywords keywordsTalin, focal adhesion, f-actin binding, CELL ADHESION; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.26
Radius of gyration Rg (electron density) rg_electron43.01
Forward intensity I(0) i0596926000.00
Molecular weight molecular_weight193510.0 kDa
Excluded volume excluded_volume239910 ų
Envelope volume envelope_volume337940 ų
Hydration-shell volume shell_volume66147 ų
Envelope diameter envelope_diameter140.8
Shell Rg shell_rg47.64
Envelope Rg envelope_rg42.36
Shape Rg shape_rg43.04
Total Rg total_rg43.13
Total atoms total_atoms13547
Residues n_residues1852
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 dmax141.6
Rg (real space) rg_real43.14
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real5.9690e+08
I(0) uncertainty (real space) i0_real_error1.0750e+07
Rg (reciprocal space) rg_reciprocal43.26
I(0) (reciprocal space) i0_reciprocal597000000.0000
Solution quality estimate total_estimate0.8263
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.1
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.498
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42830000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; 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)