2l7n

Solution Structure of the R5 Domain of Talin

Method: SOLUTION NMR Dmax: 60.6 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 1046–1207 Fragment:sequence database residues 1046-1207 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:1 mM [U-100% 15N] DomB, 10 % [U-100% 2H] D2O, 90 % H2O, 2 mM DTT, 50 mM sodium chloride, 20 mM sodium phosphate, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1 mM [U-100% 13C; U-100% 15N] DomB, 10 % [U-100% 2H] D2O, 90 % H2O, 2 mM DTT, 50 mM sodium chloride, 20 mM sodium phosphate, 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 7–168; UniProt 1046–1207

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 2l7n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2l7n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2l7n
Deposition date deposition_date2010-12-14
Structure title titleSolution Structure of the R5 Domain of Talin
Keywords keywordsIntegrin, Bundle, Focal Adhesion, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.19
Radius of gyration Rg (electron density) rg_electron17.06
Forward intensity I(0) i01806850000.00
Molecular weight molecular_weight346570.0 kDa
Excluded volume excluded_volume429420 ų
Envelope volume envelope_volume47880 ų
Hydration-shell volume shell_volume19811 ų
Envelope diameter envelope_diameter69.8
Shell Rg shell_rg26.93
Envelope Rg envelope_rg21.10
Shape Rg shape_rg17.08
Total Rg total_rg17.14
Total atoms total_atoms48980
Residues n_residues3360
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 dmax60.6
Rg (real space) rg_real17.27
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real1.8070e+09
I(0) uncertainty (real space) i0_real_error2.1870e+07
Rg (reciprocal space) rg_reciprocal17.26
I(0) (reciprocal space) i0_reciprocal1807000000.0000
Solution quality estimate total_estimate0.7427
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.5
Skewness Skewness skewness0.474
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1205000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.611; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.827; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2l7nA00
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)