6ba6

Solution structure of Rap1b/talin complex

Method: SOLUTION NMR Dmax: 63.0 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–86 Fragment:F0 domain Ras-related protein Rap-1b × 1 (P61224) SOLUTION NMR NMR measurement conditions:pH 6.6;301 K;Ionic strength (raw mmCIF value) 50mM NaCl, 5mM MgCl2;Pressure 101325 NMR measurement conditions:pH 6.6;301 K;Ionic strength (raw mmCIF value) 50mM NaCl, 5mM MgCl2;Pressure 101325 NMR sample composition:0.6 mM [U-13C; U-15N] Rap1b, 0.9 mM talin-F0, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.5 mM [U-13C; U-15N] talin-F0, 0.7 mM Rap1b, 95% H20, 5% D2O | 95% H20, 5% D2O NMR sample composition:0.5 mM [U-15N; U-2H] talin-F0, 0.7 mM Rap1b, 95% H20, 5% D2O | 95% H20, 5% D2O NMR sample composition:0.5 mM [U-13C; U-15N] talin-F0, 0.7 mM Rap1b, 0.2% H20, 99.8% D20 | 0.2% H20, 99.8% D20 NMR sample composition:0.6 mM [U-13C; U-15N] Rap1b, 95% H2O/5% D2O | 95% H2O/5% 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 8–93; UniProt 1–86

Ras-related protein Rap-1b

Homo sapiens

UniProt P61224

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–167 Mutation:G12V Talin-1 × 1 (P26039) SOLUTION NMR NMR measurement conditions:pH 6.6;301 K;Ionic strength (raw mmCIF value) 50mM NaCl, 5mM MgCl2;Pressure 101325 NMR measurement conditions:pH 6.6;301 K;Ionic strength (raw mmCIF value) 50mM NaCl, 5mM MgCl2;Pressure 101325 NMR sample composition:0.6 mM [U-13C; U-15N] Rap1b, 0.9 mM talin-F0, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.5 mM [U-13C; U-15N] talin-F0, 0.7 mM Rap1b, 95% H20, 5% D2O | 95% H20, 5% D2O NMR sample composition:0.5 mM [U-15N; U-2H] talin-F0, 0.7 mM Rap1b, 95% H20, 5% D2O | 95% H20, 5% D2O NMR sample composition:0.5 mM [U-13C; U-15N] talin-F0, 0.7 mM Rap1b, 0.2% H20, 99.8% D20 | 0.2% H20, 99.8% D20 NMR sample composition:0.6 mM [U-13C; U-15N] Rap1b, 95% H2O/5% D2O | 95% H2O/5% 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.

22 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAP1B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–168; UniProt 1–167

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 6ba6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ba6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ba6
Deposition date deposition_date2017-10-12
Structure title titleSolution structure of Rap1b/talin complex
Keywords keywordsComplex, Small GTPase, ubiquitin-like fold, CELL ADHESION; CELL ADHESION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.40
Radius of gyration Rg (electron density) rg_electron18.97
Forward intensity I(0) i04635860000.00
Molecular weight molecular_weight577700.0 kDa
Excluded volume excluded_volume722060 ų
Envelope volume envelope_volume54166 ų
Hydration-shell volume shell_volume22231 ų
Envelope diameter envelope_diameter72.0
Shell Rg shell_rg27.03
Envelope Rg envelope_rg20.64
Shape Rg shape_rg18.96
Total Rg total_rg19.06
Total atoms total_atoms80900
Residues n_residues5060
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 dmax63.0
Rg (real space) rg_real19.36
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real4.6360e+09
I(0) uncertainty (real space) i0_real_error5.5640e+07
Rg (reciprocal space) rg_reciprocal19.37
I(0) (reciprocal space) i0_reciprocal4636000000.0000
Solution quality estimate total_estimate0.8160
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.287
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1941000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6ba6b_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins

CATH v4.4 (2 domains)

Domain ID domain_id6ba6A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id6ba6B00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)