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Yorodumi- PDB-2kxc: 1H, 13C, and 15N Chemical Shift Assignments for IRTKS-SH3 and Esp... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2kxc | ||||||
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Title | 1H, 13C, and 15N Chemical Shift Assignments for IRTKS-SH3 and EspFu-R47 complex | ||||||
Components |
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Keywords | PROTEIN BINDING / IRTKS-SH3 / EspFu / Complex Structure | ||||||
Function / homology | Function and homology information plasma membrane organization / actin crosslink formation / cadherin binding involved in cell-cell adhesion / RHOF GTPase cycle / proline-rich region binding / positive regulation of actin filament polymerization / actin filament bundle assembly / RAC3 GTPase cycle / RAC2 GTPase cycle / RAC1 GTPase cycle ...plasma membrane organization / actin crosslink formation / cadherin binding involved in cell-cell adhesion / RHOF GTPase cycle / proline-rich region binding / positive regulation of actin filament polymerization / actin filament bundle assembly / RAC3 GTPase cycle / RAC2 GTPase cycle / RAC1 GTPase cycle / regulation of actin cytoskeleton organization / adherens junction / actin binding / host cell cytoplasm / cytoskeleton / extracellular exosome / extracellular region / nucleoplasm / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / molecular dynamics, TORSION ANGLE DYNAMICS | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Aitio, O. / Hellman, M. / Kazlauskas, A. / Vingadassalom, D.F. / Leong, J.M. / Saksela, K. / Permi, P. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2010 Title: Recognition of tandem PxxP motifs as a unique Src homology 3-binding mode triggers pathogen-driven actin assembly Authors: Aitio, O. / Hellman, M. / Kazlauskas, A. / Vingadassalom, D.F. / Leong, J.M. / Saksela, K. / Permi, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kxc.cif.gz | 508.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kxc.ent.gz | 449 KB | Display | PDB format |
PDBx/mmJSON format | 2kxc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kx/2kxc ftp://data.pdbj.org/pub/pdb/validation_reports/kx/2kxc | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7559.607 Da / Num. of mol.: 1 / Fragment: IRTKS-SH3 domain, UNP residues 339-402 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BAIAP2L1, IRTKS / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9UHR4 |
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#2: Protein/peptide | Mass: 5301.970 Da / Num. of mol.: 1 / Fragment: EspFu-R47 domain, UNP residues 268-314 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: O157:H7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q8X2D5, UniProt: P0DJ89*PLUS |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 50 / pH: 7.0 / Pressure: AMBIENT / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics, TORSION ANGLE DYNAMICS / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20 / Representative conformer: 1 |