3dyj

Crystal Structure of the R11R12 Domains of Talin

Method: X-RAY DIFFRACTION Dmax: 113.0 Å Quality: GOOD

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

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 1974–2293 Fragment:TALIN ROD (UNP RESIDUES:1974-2293) Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;10% PEG 8000, 1% PEG 3350, 100MM HEPES (PH 7.5), 10MM SODIUM THIOCYANATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 273K, pH 7.50, temperature 293K Resolution 1.85 Å R-free 0.260
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1974–2293 Fragment:TALIN ROD (UNP RESIDUES:1974-2293) Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;10% PEG 8000, 1% PEG 3350, 100MM HEPES (PH 7.5), 10MM SODIUM THIOCYANATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 273K, pH 7.50, temperature 293K Resolution 1.85 Å R-free 0.260

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 69 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 13–332; UniProt 1974–2293 Author chain B; PDBConstruct 13–332; UniProt 1974–2293

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 3dyj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3dyj
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3dyj
Deposition date deposition_date2008-07-28
Structure title titleCrystal Structure of the R11R12 Domains of Talin
Keywords keywords;TALIN, HELIX BUNDLES, CYTOSKELETAL PROTEIN, integrin-bindin site, IBS2, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Phosphoprotein, Structural protein ;; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.69
Radius of gyration Rg (electron density) rg_electron33.46
Forward intensity I(0) i075612600.00
Molecular weight molecular_weight67402.0 kDa
Excluded volume excluded_volume83713 ų
Envelope volume envelope_volume110540 ų
Hydration-shell volume shell_volume29081 ų
Envelope diameter envelope_diameter118.4
Shell Rg shell_rg37.85
Envelope Rg envelope_rg32.99
Shape Rg shape_rg33.44
Total Rg total_rg33.86
Total atoms total_atoms4678
Residues n_residues622
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 dmax113.0
Rg (real space) rg_real33.75
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real7.5610e+07
I(0) uncertainty (real space) i0_real_error1.2560e+06
Rg (reciprocal space) rg_reciprocal33.71
I(0) (reciprocal space) i0_reciprocal75610000.0000
Solution quality estimate total_estimate0.8746
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.3
Skewness Skewness skewness0.252
Kurtosis Kurtosis kurtosis-0.606
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5538000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.807; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3dyjA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1420 — A middle domain of Talin 1
Homologous superfamily homologous superfamily10 — Talin, central domain
Domain ID domain_id3dyjA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1420 — A middle domain of Talin 1
Homologous superfamily homologous superfamily10 — Talin, central domain
Domain ID domain_id3dyjB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1420 — A middle domain of Talin 1
Homologous superfamily homologous superfamily10 — Talin, central domain
Domain ID domain_id3dyjB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1420 — A middle domain of Talin 1
Homologous superfamily homologous superfamily10 — Talin, central domain

8. Citations (1)

9. Files and Curves (10)