2kc2

NMR structure of the F1 domain (residues 86-202) of the talin

Method: SOLUTION NMR Dmax: 51.5 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 86–202 Fragment:F1 domain (residues 86-202) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 50;Pressure ambient NMR sample composition:0.6 mM [U-100% 13C; U-100% 15N] F1-1, 10 % [U-100% 2H] D2O-2, 2 mM DTT-3, 50 mM sodium chloride-4, 20 mM sodium phosphate-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.6 mM [U-100% 15N] F1-6, 10 % [U-100% 2H] D2O-7, 2 mM DTT-8, 50 mM sodium chloride-9, 20 mM sodium phosphate-10, 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 12–128; UniProt 86–202

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 2kc2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2kc2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2kc2
Deposition date deposition_date2008-12-13
Structure title titleNMR structure of the F1 domain (residues 86-202) of the talin
Keywords keywordsTalin, FERM, F1, ADHESION, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Phosphoprotein, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.91
Radius of gyration Rg (electron density) rg_electron18.51
Forward intensity I(0) i0349377000.00
Molecular weight molecular_weight150010.0 kDa
Excluded volume excluded_volume186380 ų
Envelope volume envelope_volume79821 ų
Hydration-shell volume shell_volume27534 ų
Envelope diameter envelope_diameter92.7
Shell Rg shell_rg31.73
Envelope Rg envelope_rg25.23
Shape Rg shape_rg18.46
Total Rg total_rg19.30
Total atoms total_atoms21240
Residues n_residues1280
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 dmax51.5
Rg (real space) rg_real17.78
Rg uncertainty (real space) rg_real_error0.08
I(0) (real space) i0_real3.3260e+08
I(0) uncertainty (real space) i0_real_error2.9540e+06
Rg (reciprocal space) rg_reciprocal19.10
I(0) (reciprocal space) i0_reciprocal349400000.0000
Solution quality estimate total_estimate0.6763
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.3
Skewness Skewness skewness0.403
Kurtosis Kurtosis kurtosis-0.335
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha3.6080
Highest regularization parameter α highest_alpha1836000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.945; Stabil: 0.985; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)