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Yorodumi- PDB-1wi7: Solution structure of the SH3 domain of SH3-domain kinase binding... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1wi7 | ||||||
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Title | Solution structure of the SH3 domain of SH3-domain kinase binding protein 1 | ||||||
Components | SH3-domain kinase binding protein 1 | ||||||
Keywords | PROTEIN BINDING / BETA BARREL / Sh3kbp1 / Ruk / structural genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information Reelin signalling pathway / Negative regulation of MET activity / EGFR downregulation / ubiquitin-dependent endocytosis / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / positive regulation of B cell activation / Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / endocytic vesicle / cytoskeleton organization ...Reelin signalling pathway / Negative regulation of MET activity / EGFR downregulation / ubiquitin-dependent endocytosis / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / positive regulation of B cell activation / Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / endocytic vesicle / cytoskeleton organization / actin filament organization / cytoplasmic vesicle membrane / SH3 domain binding / cell-cell junction / cell migration / regulation of cell shape / molecular adaptor activity / cytoskeleton / neuron projection / focal adhesion / apoptotic process / ubiquitin protein ligase binding / synapse Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Inoue, K. / Hayashi, F. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the SH3 domain of SH3-domain kinase binding protein 1 Authors: Inoue, K. / Hayashi, F. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wi7.cif.gz | 386.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wi7.ent.gz | 322.2 KB | Display | PDB format |
PDBx/mmJSON format | 1wi7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1wi7_validation.pdf.gz | 343.6 KB | Display | wwPDB validaton report |
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Full document | 1wi7_full_validation.pdf.gz | 490.6 KB | Display | |
Data in XML | 1wi7_validation.xml.gz | 26.6 KB | Display | |
Data in CIF | 1wi7_validation.cif.gz | 40.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wi/1wi7 ftp://data.pdbj.org/pub/pdb/validation_reports/wi/1wi7 | HTTPS FTP |
-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: 7282.977 Da / Num. of mol.: 1 / Fragment: SH3 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: RIKEN cDNA 5830464D22 / Plasmid: P030128-04 / References: UniProt: Q8R550 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.61mM 13C, 15N-labeled protein; 20mM PiNa; 100mM NaCl; 1mM d-DTT; 0.02% NaN3 Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 6.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 800 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |