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- PDB-1zvz: Vinculin Head (0-258) in Complex with the Talin Rod Residue 820-844 -

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Basic information

Entry
Database: PDB / ID: 1zvz
TitleVinculin Head (0-258) in Complex with the Talin Rod Residue 820-844
Components
  • Talin 1
  • Vinculin
KeywordsPROTEIN BINDING / talin / vinculin / complex
Function / homology
Function and homology information


muscle tendon junction / Platelet degranulation / Smooth Muscle Contraction / regulation of protein localization to adherens junction / podosome ring / outer dense plaque of desmosome / inner dense plaque of desmosome / terminal web / epithelial cell-cell adhesion / zonula adherens ...muscle tendon junction / Platelet degranulation / Smooth Muscle Contraction / regulation of protein localization to adherens junction / podosome ring / outer dense plaque of desmosome / inner dense plaque of desmosome / terminal web / epithelial cell-cell adhesion / zonula adherens / dystroglycan binding / vinculin binding / muscle alpha-actinin binding / MAP2K and MAPK activation / alpha-catenin binding / fascia adherens / cell-cell contact zone / costamere / apical junction assembly / regulation of establishment of endothelial barrier / adherens junction assembly / axon extension / protein localization to cell surface / lamellipodium assembly / regulation of focal adhesion assembly / alpha-actinin binding / brush border / skeletal muscle myofibril / stress fiber / regulation of cell migration / ruffle / cell projection / Neutrophil degranulation / morphogenesis of an epithelium / adherens junction / sarcolemma / neuromuscular junction / structural constituent of cytoskeleton / cell-cell adhesion / ruffle membrane / Z disc / beta-catenin binding / actin filament binding / cell-cell junction / actin cytoskeleton / integrin binding / scaffold protein binding / mitochondrial inner membrane / cytoskeleton / cell adhesion / cadherin binding / focal adhesion / ubiquitin protein ligase binding / structural molecule activity / cell surface / protein homodimerization activity / protein-containing complex / plasma membrane / cytosol / cytoplasm
Similarity search - Function
: / 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 ...: / 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 / Vinculin repeated domain signature. / Vinculin / Alpha-catenin/vinculin-like / I/LWEQ domain / I/LWEQ domain superfamily / I/LWEQ domain / I/LWEQ domain profile. / I/LWEQ domain / Vinculin, conserved site / Vinculin family talin-binding region signature. / Phosphotyrosine-binding domain / Vinculin/alpha-catenin / Vinculin family / Alpha-catenin/vinculin-like superfamily / FERM, N-terminal / FERM N-terminal domain / 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 / Four Helix Bundle (Hemerythrin (Met), subunit A) / PH-like domain superfamily / Ubiquitin-like domain superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesGallus gallus (chicken)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsGingras, A.R. / Ziegler, W.H. / Barsukov, I.L. / Roberts, G.C. / Critchley, D.R. / Emsley, J.
CitationJournal: J.Biol.Chem. / Year: 2005
Title: Mapping and consensus sequence identification for multiple vinculin binding sites within the talin rod
Authors: Gingras, A.R. / Ziegler, W.H. / Frank, R. / Barsukov, I.L. / Roberts, G.C. / Critchley, D.R. / Emsley, J.
History
DepositionJun 3, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 20, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Aug 23, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Vinculin
B: Talin 1


Theoretical massNumber of molelcules
Total (without water)33,8412
Polymers33,8412
Non-polymers00
Water4,522251
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2150 Å2
ΔGint-24 kcal/mol
Surface area14360 Å2
MethodPISA
Unit cell
Length a, b, c (Å)36.013, 52.164, 153.841
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Vinculin / / Metavinculin


Mass: 31195.908 Da / Num. of mol.: 1 / Fragment: Residues 0-258
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: VCL, VINC1 / Plasmid: pET-15b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P12003
#2: Protein/peptide Talin 1


Mass: 2645.021 Da / Num. of mol.: 1 / Fragment: Residues 820-844 / Source method: obtained synthetically
Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN GALLUS GALLUS(CHICKEN).
References: UniProt: P54939
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 251 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.1 Å3/Da / Density % sol: 42 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.934 / Wavelength: 0.934 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Mar 13, 2005 / Details: TOROIDAL ZERODUR MIRROR
RadiationMonochromator: Diamond (111), Ge(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.934 Å / Relative weight: 1
ReflectionResolution: 1.8→30 Å / Num. all: 27873 / % possible obs: 97.7 % / Rmerge(I) obs: 0.078 / Net I/σ(I): 16.1
Reflection shellResolution: 1.8→1.86 Å / Rmerge(I) obs: 0.346 / Mean I/σ(I) obs: 2.09 / % possible all: 95.4

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1XWJ

1xwj


Resolution: 1.8→26.29 Å / Cor.coef. Fo:Fc: 0.926 / Cor.coef. Fo:Fc free: 0.895 / SU B: 6.398 / SU ML: 0.115 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.169 / ESU R Free: 0.155 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.27636 1375 5.1 %RANDOM
Rwork0.23903 ---
obs0.24095 25784 97.87 %-
all-27873 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 29.204 Å2
Baniso -1Baniso -2Baniso -3
1--0.23 Å20 Å20 Å2
2---0.35 Å20 Å2
3---0.57 Å2
Refinement stepCycle: LAST / Resolution: 1.8→26.29 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2143 0 0 251 2394
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0222167
X-RAY DIFFRACTIONr_bond_other_d0.0020.022086
X-RAY DIFFRACTIONr_angle_refined_deg1.0971.9792931
X-RAY DIFFRACTIONr_angle_other_deg0.87834858
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.3155273
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.98825.16989
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.46715422
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.3661514
X-RAY DIFFRACTIONr_chiral_restr0.1570.2362
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.022338
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02375
X-RAY DIFFRACTIONr_nbd_refined0.1960.2535
X-RAY DIFFRACTIONr_nbd_other0.1560.22092
X-RAY DIFFRACTIONr_nbtor_refined0.1620.21078
X-RAY DIFFRACTIONr_nbtor_other0.0840.21117
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.0810.2192
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.0960.218
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2290.257
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.0820.220
X-RAY DIFFRACTIONr_mcbond_it0.2461.51819
X-RAY DIFFRACTIONr_mcbond_other0.031.5554
X-RAY DIFFRACTIONr_mcangle_it0.2822242
X-RAY DIFFRACTIONr_scbond_it0.4193871
X-RAY DIFFRACTIONr_scangle_it0.6254.5689
LS refinement shellResolution: 1.8→1.847 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.307 85 -
Rwork0.292 1809 -
obs--95.42 %

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