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- PDB-1rlf: STRUCTURE DETERMINATION OF THE RAS-BINDING DOMAIN OF THE RAL-SPEC... -
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Open data
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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 | ||||||
![]() | RLF | ||||||
![]() | SIGNAL TRANSDUCTION PROTEIN | ||||||
Function / homology | ![]() regulation of Ral protein signal transduction / RAF/MAP kinase cascade / negative regulation of cardiac muscle cell apoptotic process / guanyl-nucleotide exchange factor activity / Ras protein signal transduction / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Esser, D. / Bauer, B. / Wolthuis, R.M.F. / Wittinghofer, A. / Cool, R.H. / Bay, P. | ||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 280.7 KB | Display | ![]() |
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PDB format | ![]() | 230.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 353.8 KB | Display | ![]() |
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Full document | ![]() | 477.8 KB | Display | |
Data in XML | ![]() | 39 KB | Display | |
Data in CIF | ![]() | 52.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() ![]() ![]() ![]() |
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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 |
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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
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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 |