8vdq

Cryogenic electron microscopy model of full-length talin

Method: ELECTRON MICROSCOPY Dmax: 143.3 Å Quality: EXCELLENT

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 Insufficient information 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 5.50 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

Green fluorescent protein,Talin-1

Mus musculus

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–238 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.50 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–250; UniProt 2–238

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 8vdq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vdq
Deposition date deposition_date2023-12-17
Structure title titleCryogenic electron microscopy model of full-length talin
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_guinier44.83
Radius of gyration Rg (electron density) rg_electron44.44
Forward intensity I(0) i0829396000.00
Molecular weight molecular_weight229660.0 kDa
Excluded volume excluded_volume284990 ų
Envelope volume envelope_volume402840 ų
Hydration-shell volume shell_volume75405 ų
Envelope diameter envelope_diameter139.7
Shell Rg shell_rg49.96
Envelope Rg envelope_rg43.01
Shape Rg shape_rg44.46
Total Rg total_rg44.64
Total atoms total_atoms16077
Residues n_residues2192
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 dmax143.3
Rg (real space) rg_real44.64
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real8.2940e+08
I(0) uncertainty (real space) i0_real_error1.6200e+07
Rg (reciprocal space) rg_reciprocal44.83
I(0) (reciprocal space) i0_reciprocal829600000.0000
Solution quality estimate total_estimate0.9012
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.2
Skewness Skewness skewness0.149
Kurtosis Kurtosis kurtosis-0.563
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha62330000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)