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Yorodumi- PDB-1rlf: STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPEC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1rlf | ||||||
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Title | STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR RLF, NMR, 10 STRUCTURES | ||||||
Components | RLF | ||||||
Keywords | SIGNAL TRANSDUCTION PROTEIN | ||||||
Function / homology | Function and homology information regulation of Ral protein signal transduction / negative regulation of cardiac muscle cell apoptotic process / small GTPase-mediated signal transduction / guanyl-nucleotide exchange factor activity / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Esser, D. / Bauer, B. / Wolthuis, R.M.F. / Wittinghofer, A. / Cool, R.H. / Bay, P. | ||||||
Citation | Journal: Biochemistry / Year: 1998 Title: Structure determination of the Ras-binding domain of the Ral-specific guanine nucleotide exchange factor Rlf. Authors: Esser, D. / Bauer, B. / Wolthuis, R.M. / Wittinghofer, A. / Cool, R.H. / Bayer, P. #1: Journal: Embo J. / Year: 1997 Title: Stimulation of Gene Induction and Cell Growth by the Ras Effector Rlf Authors: Wolthuis, R.M. / De Ruiter, N.D. / Cool, R.H. / Bos, J.L. #2: Journal: Oncogene / Year: 1996 Title: Ralgds-Like Factor (Rlf) is a Novel Ras and RAP 1A-Associating Protein Authors: Wolthuis, R.M. / Bauer, B. / Van'T Veer, L.J. / De Vries-Smits, A.M. / Cool, R.H. / Spaargaren, M. / Wittinghofer, A. / Burgering, B.M. / Bos, J.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rlf.cif.gz | 277.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1rlf.ent.gz | 238.4 KB | Display | PDB format |
PDBx/mmJSON format | 1rlf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rl/1rlf ftp://data.pdbj.org/pub/pdb/validation_reports/rl/1rlf | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10048.376 Da / Num. of mol.: 1 / Fragment: RAS BINDING DOMAIN, RESIDUES 646 - 735 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: PGEX4T3 / Production host: Escherichia coli (E. coli) / References: UniProt: Q61193 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TWO- AND THREE-DIMENSIONAL NMR SPECTROSCOPY ON UNLABELED AND 15N LABELED RLF-RBD |
-Sample preparation
Sample conditions | pH: 6.5 / Temperature: 300 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz |
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-Processing
Software |
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NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: TOTAL NUMBER OF NOE CONSTRAINTS 2287; INTRARESIDUE NOE CONSTRAINTS 804; SEQUENTIAL INTERRESIDUE CONSTRAINTS (|I-J|=1) 469; INTERRESIDUE CONSTRAINTS (1<|I-J|<5) 296; INTERRESIDUE CONSTRAINTS (|I-J|>=5) 718; BACKBONE RMSD FROM TARGET DISTANCES (ASP4-ARG90) 0.2A (COMPARED TO AVERAGE STRUCTURE) COORDINATE RMSD FROM THE AVERAGE FOR ALL HEAVY ATOM0.6A; NUMBER OF STRUCTURES USED IN ABOVE STATISTICS 10S | ||||||||||||||||
NMR ensemble | Conformer selection criteria: ENERGY / Conformers calculated total number: 30 / Conformers submitted total number: 10 |