1sj8

Solution Structure of the R1R2 Domains of Talin

Method: X-RAY DIFFRACTION Dmax: 88.3 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 482–789 Fragment:Residues 482-789 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;295 K;0.1M Sodium Citrate, 20% PEG 6000, 0.1M MgCl2, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.60 Å R-free 0.297

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 1–308; UniProt 482–789

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 1sj8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1sj8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1sj8
Deposition date deposition_date2004-03-03
Structure title titleSolution Structure of the R1R2 Domains of Talin
Keywords keywordsStructural protein; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.21
Radius of gyration Rg (electron density) rg_electron22.82
Forward intensity I(0) i017436700.00
Molecular weight molecular_weight30204.0 kDa
Excluded volume excluded_volume37346 ų
Envelope volume envelope_volume45036 ų
Hydration-shell volume shell_volume18346 ų
Envelope diameter envelope_diameter90.5
Shell Rg shell_rg27.35
Envelope Rg envelope_rg23.32
Shape Rg shape_rg22.85
Total Rg total_rg23.34
Total atoms total_atoms2113
Residues n_residues297
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 dmax88.3
Rg (real space) rg_real23.50
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real1.7440e+07
I(0) uncertainty (real space) i0_real_error2.5140e+05
Rg (reciprocal space) rg_reciprocal23.43
I(0) (reciprocal space) i0_reciprocal17440000.0000
Solution quality estimate total_estimate0.7704
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.7
Skewness Skewness skewness0.705
Kurtosis Kurtosis kurtosis0.299
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4748000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.539; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.498; Smooth: 0.897

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1sj8a1
Class classa — All alpha proteins
Fold Fold folda.215 — A middle domain of Talin 1
Superfamily Superfamily superfamilya.215.1 — A middle domain of Talin 1
Family Family familya.215.1.1 — A middle domain of Talin 1
Domain ID domain_idd1sj8a2
Class classa — All alpha proteins
Fold Fold folda.216 — I/LWEQ domain
Superfamily Superfamily superfamilya.216.1 — I/LWEQ domain
Family Family familya.216.1.1 — I/LWEQ domain

CATH v4.4 (2 domains)

Domain ID domain_id1sj8A01
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_id1sj8A02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily230 — Alpha-catenin/vinculin-like

8. Citations (1)

9. Files and Curves (10)