2b0h

Solution structure of VBS3 fragment of talin

Method: SOLUTION NMR Dmax: 47.0 Å Quality: REASONABLE

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 1843–1973 Fragment:residues 1843-1973 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 50 mM NaCl;Pressure ambient NMR sample composition:1.5 mM talin 1843-1973 [15N,13C]; 20 mM phosphate, (pH 6.5), 50 mM NaCl, 2 mM DTT, 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:1.5 mM talin 1843-1973 [15N,13C]; 20 mM phosphate, (pH 6.5), 50 mM NaCl, 2 mM DTT, 100% D2O | 100% D2O NMR sample composition:1.0 mM talin 1843-1973 [15N]; 20 mM phosphate, (pH 6.5), 50 mM NaCl, 2 mM DTT, 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:1.0 mM talin 1843-1973; 20 mM phosphate, (pH 6.5), 50 mM NaCl, 2 mM DTT, 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.

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 7–137; UniProt 1843–1973

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 2b0h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2b0h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2b0h
Deposition date deposition_date2005-09-14
Structure title titleSolution structure of VBS3 fragment of talin
Keywords keywordstalin, vinculin, helical bundle, VBS, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.23
Radius of gyration Rg (electron density) rg_electron17.36
Forward intensity I(0) i01282710000.00
Molecular weight molecular_weight291290.0 kDa
Excluded volume excluded_volume360160 ų
Envelope volume envelope_volume44266 ų
Hydration-shell volume shell_volume17584 ų
Envelope diameter envelope_diameter80.4
Shell Rg shell_rg28.07
Envelope Rg envelope_rg24.00
Shape Rg shape_rg17.37
Total Rg total_rg17.49
Total atoms total_atoms40860
Residues n_residues2740
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 dmax47.0
Rg (real space) rg_real16.14
Rg uncertainty (real space) rg_real_error0.09
I(0) (real space) i0_real1.2240e+09
I(0) uncertainty (real space) i0_real_error1.1740e+07
Rg (reciprocal space) rg_reciprocal17.48
I(0) (reciprocal space) i0_reciprocal1283000000.0000
Solution quality estimate total_estimate0.6609
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary16.1
Skewness Skewness skewness0.470
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha3.0770
Highest regularization parameter α highest_alpha1330000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.004; Oscil: 0.883; Stabil: 0.991; Sysdev: 0.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2b0ha1
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.9 — alpha-catenin/vinculin-like
Family Family familya.24.9.2 — VBS domain
Domain ID domain_idd2b0ha2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2b0hA01
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)