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- PDB-2jsw: Solution Structure of the R13 Domain of Talin -

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Basic information

Entry
Database: PDB / ID: 2jsw
TitleSolution Structure of the R13 Domain of Talin
ComponentsTalin-1
KeywordsACTIN-BINDING PROTEIN / Talin / C-terminal actin binding site / ABS3 / THATCH domain / Cytoskeleton / Phosphorylation / Structural protein
Function / homology
Function and homology information


GRB2:SOS provides linkage to MAPK signaling for Integrins / Integrin signaling / Smooth Muscle Contraction / p130Cas linkage to MAPK signaling for integrins / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / MAP2K and MAPK activation / LIM domain binding / Platelet degranulation / vinculin binding / integrin activation ...GRB2:SOS provides linkage to MAPK signaling for Integrins / Integrin signaling / Smooth Muscle Contraction / p130Cas linkage to MAPK signaling for integrins / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / MAP2K and MAPK activation / LIM domain binding / Platelet degranulation / vinculin binding / integrin activation / cell-substrate junction assembly / cortical actin cytoskeleton organization / phosphatidylserine binding / ruffle / phosphatidylinositol binding / integrin-mediated signaling pathway / adherens junction / structural constituent of cytoskeleton / platelet aggregation / ruffle membrane / cell-cell adhesion / actin filament binding / integrin binding / cytoskeleton / focal adhesion / cell surface / plasma membrane / cytoplasm
Similarity search - Function
I/LWEQ domain / I/LWEQ domain / : / Talin, R4 domain / Vinculin-binding site-containing domain / Talin, central / Talin, N-terminal F0 domain / Talin, central domain superfamily / Talin-1/2, rod-segment / Vinculin Binding Site ...I/LWEQ domain / I/LWEQ domain / : / Talin, R4 domain / Vinculin-binding site-containing domain / Talin, central / Talin, N-terminal F0 domain / Talin, central domain superfamily / Talin-1/2, rod-segment / Vinculin Binding Site / Talin, middle domain / N-terminal or F0 domain of Talin-head FERM / I/LWEQ domain / I/LWEQ domain superfamily / I/LWEQ domain / I/LWEQ domain profile. / I/LWEQ domain / Phosphotyrosine-binding domain / Alpha-catenin/vinculin-like superfamily / FERM domain signature 1. / FERM conserved site / FERM domain signature 2. / FERM central domain / FERM/acyl-CoA-binding protein superfamily / FERM central domain / FERM superfamily, second domain / FERM domain / FERM domain profile. / Band 4.1 domain / Band 4.1 homologues / PH-like domain superfamily / Ubiquitin-like domain superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / simulated annealing, molecular dynamics, torsion angle dynamics
AuthorsGoult, B.T. / Gingras, A.R. / Bate, N. / Critchley, D.R.C. / Barsukov, I.L.
CitationJournal: Embo J. / Year: 2007
Title: The structure of the C-terminal actin-binding domain of talin.
Authors: Gingras, A.R. / Bate, N. / Goult, B.T. / Hazelwood, L. / Canestrelli, I. / Grossmann, J.G. / Liu, H. / Putz, N.S. / Roberts, G.C. / Volkmann, N. / Hanein, D. / Barsukov, I.L. / Critchley, D.R.
History
DepositionJul 17, 2007Deposition site: BMRB / Processing site: RCSB
Revision 1.0Jan 29, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 25, 2021Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_assembly_prop / pdbx_struct_oper_list / struct / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct.title / _struct_ref_seq_dif.details
Revision 1.3May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Talin-1


Theoretical massNumber of molelcules
Total (without water)19,3801
Polymers19,3801
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area0 Å2
ΔGint0 kcal/mol
Surface area10160 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100structures with the least restraint violations
RepresentativeModel #1lowest energy

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Components

#1: Protein Talin-1


Mass: 19379.867 Da / Num. of mol.: 1 / Fragment: Talin1 residues 2300-2482
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Tln1, Tln / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P26039

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1122D 1H-15N HSQC
1232D 1H-13C HSQC
1333D HNCO
1433D HNCA
1533D CBCA(CO)NH
1633D HN(CA)CB
1733D (H)CCH-TOCSY
1823D 1H-15N NOESY
1933D 1H-13C NOESY
11033D HBHA(CO)NH
11112D 1H-1H TOCSY
11212D 1H-1H NOESY
11333D HN(CO)CA
11434D 13C, 13C HMQC-NOESY-HSQC

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Sample preparation

Details
Solution-IDContentsSolvent system
11 mM Talin c-terminal actin binding site (ABS3), 90% H2O/10% D2O90% H2O/10% D2O
21 mM [U-15N] Talin c-terminal actin binding site (ABS3), 90% H2O/10% D2O90% H2O/10% D2O
31 mM [U-13C; U-15N] Talin c-terminal actin binding site (ABS3), 90% H2O/10% D2O90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1 mMTalin c-terminal actin binding site (ABS3)1
1 mMTalin c-terminal actin binding site (ABS3)[U-15N]2
1 mMTalin c-terminal actin binding site (ABS3)[U-13C; U-15N]3
Sample conditionsIonic strength: 50 / pH: 6.0 / Pressure: ambient / Temperature: 318 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX8001
Bruker DRXBrukerDRX6002
Bruker DRXBrukerDRX6003

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Processing

NMR software
NameVersionDeveloperClassification
ARIA1.2Linge, O'Donoghue and Nilgesstructure solution
ARIA1.2Linge, O'Donoghue and Nilgesrefinement
CYANA2.1Guntert, Mumenthaler and Wuthrichchemical shift assignment
CYANA2.1Guntert, Mumenthaler and Wuthrichchemical shift calculation
CYANA2.1Guntert, Mumenthaler and Wuthrichstructure solution
TopSpinBruker Biospincollection
TopSpinBruker Biospinprocessing
CcpNmr Analysis11CCPNpeak picking
CcpNmr Analysis11CCPNchemical shift assignment
TALOSCornilescu, Delaglio and Baxgeometry optimization
RefinementMethod: simulated annealing, molecular dynamics, torsion angle dynamics
Software ordinal: 1
Details: Final Structures refined in explicit water bath as implemented in Aria 1.2/CNS 1.1. 20 lowest energy structures selected from water refinement., CNS, Initial structures generated with Cyana
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 100 / Conformers submitted total number: 20

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