1u89

Solution structure of VBS2 fragment of talin

Method: SOLUTION NMR Dmax: 70.2 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 755–889 Fragment:vbs2 domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;303 K;Ionic strength (raw mmCIF value) 20mM phosphate, 50mM NaCl;Pressure ambient NMR sample composition:1.5mM talin 755-889 U-15N, 13C; 20mM phosphate buffer, 20mM NaCl, 0.02% NaN3 | 90% H2O/10% D2O NMR sample composition:1.5mM talin 755-889 U-15N, 13C; 20mM phosphate buffer, 20mM NaCl, 0.02% NaN3 | 100% D2O NMR sample composition:1.5mM talin 755-889 U-15N; 20mM phosphate buffer, 20mM NaCl, 0.02% NaN3 | 90% H2O/10% D2O NMR sample composition:1.5mM talin 755-889; 20mM phosphate buffer, 20mM NaCl, 0.02% NaN3 | 100% 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 5–139; UniProt 755–889

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 1u89

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1u89
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1u89
Deposition date deposition_date2004-08-05
Structure title titleSolution structure of VBS2 fragment of talin
Keywords keywords4-helix bundle, left-handed, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.26
Radius of gyration Rg (electron density) rg_electron17.61
Forward intensity I(0) i01352320000.00
Molecular weight molecular_weight287480.0 kDa
Excluded volume excluded_volume351100 ų
Envelope volume envelope_volume61616 ų
Hydration-shell volume shell_volume22320 ų
Envelope diameter envelope_diameter77.5
Shell Rg shell_rg30.20
Envelope Rg envelope_rg24.48
Shape Rg shape_rg17.63
Total Rg total_rg17.81
Total atoms total_atoms40040
Residues n_residues2780
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 dmax70.2
Rg (real space) rg_real18.48
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real1.3520e+09
I(0) uncertainty (real space) i0_real_error1.8850e+07
Rg (reciprocal space) rg_reciprocal18.45
I(0) (reciprocal space) i0_reciprocal1352000000.0000
Solution quality estimate total_estimate0.7156
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.1
Skewness Skewness skewness0.626
Kurtosis Kurtosis kurtosis-0.051
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1830000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.329; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.326; Smooth: 0.986

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_idd1u89a1
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
Domain ID domain_idd1u89a2
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_id1u89A00
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)