+Open data
-Basic information
Entry | Database: PDB / ID: 1wfy | ||||||
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Title | Solution structure of the Ras-binding domain of mouse RGS14 | ||||||
Components | regulator of G-protein signaling 14; rap1/rap2 interacting protein | ||||||
Keywords | SIGNALING PROTEIN / Regulators of G-protein signaling / Ras family / Structural Genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information : / zygote asymmetric cell division / negative regulation of synaptic plasticity / G alpha (i) signalling events / negative regulation of G protein-coupled receptor signaling pathway / regulation of G protein-coupled receptor signaling pathway / GDP-dissociation inhibitor activity / GTPase activating protein binding / nucleocytoplasmic transport / positive regulation of neurogenesis ...: / zygote asymmetric cell division / negative regulation of synaptic plasticity / G alpha (i) signalling events / negative regulation of G protein-coupled receptor signaling pathway / regulation of G protein-coupled receptor signaling pathway / GDP-dissociation inhibitor activity / GTPase activating protein binding / nucleocytoplasmic transport / positive regulation of neurogenesis / spindle organization / platelet-derived growth factor receptor signaling pathway / G-protein alpha-subunit binding / long-term memory / GTPase activator activity / negative regulation of MAP kinase activity / learning / long-term synaptic potentiation / chromosome segregation / modulation of chemical synaptic transmission / visual learning / negative regulation of ERK1 and ERK2 cascade / PML body / spindle / positive regulation of GTPase activity / spindle pole / signaling receptor complex adaptor activity / mitotic cell cycle / microtubule binding / response to oxidative stress / microtubule / dendritic spine / postsynaptic density / nuclear body / intracellular signal transduction / G protein-coupled receptor signaling pathway / cell division / centrosome / dendrite / glutamatergic synapse / protein kinase binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Nakanishi, T. / Tochio, N. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the Ras-binding domain of mouse RGS14 Authors: Nakanishi, T. / Tochio, N. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wfy.cif.gz | 614 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wfy.ent.gz | 530.3 KB | Display | PDB format |
PDBx/mmJSON format | 1wfy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wf/1wfy ftp://data.pdbj.org/pub/pdb/validation_reports/wf/1wfy | 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: 11169.587 Da / Num. of mol.: 1 / Fragment: Raf-like Ras-binding domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: RIKEN cDNA 0610041O18 / Plasmid: P030120-12 / References: UniProt: P97492 |
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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: 0.18mM RBD U-15N, 13C; 20mM d-Tris-HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.5 / 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: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
-Processing
NMR software |
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NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |