+Open data
-Basic information
Entry | Database: PDB / ID: 1g3g | |||||||||
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Title | NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53 | |||||||||
Components | PROTEIN KINASE SPK1 | |||||||||
Keywords | TRANSFERASE / FHA domain / Rad53 / Phosphopeptide / Phosphoprotein | |||||||||
Function / homology | Function and homology information deoxyribonucleoside triphosphate biosynthetic process / G2/M DNA damage checkpoint / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / meiotic recombination checkpoint signaling / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / negative regulation of phosphorylation / dual-specificity kinase / DNA replication origin binding / negative regulation of DNA damage checkpoint ...deoxyribonucleoside triphosphate biosynthetic process / G2/M DNA damage checkpoint / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / meiotic recombination checkpoint signaling / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / negative regulation of phosphorylation / dual-specificity kinase / DNA replication origin binding / negative regulation of DNA damage checkpoint / DNA replication initiation / regulation of DNA repair / protein serine/threonine/tyrosine kinase activity / DNA damage checkpoint signaling / protein localization / protein tyrosine kinase activity / protein kinase activity / phosphorylation / DNA repair / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Authors | Yuan, C. / Liao, H. / Su, M. / Yongkiettrakul, S. / Byeon, I.-J.L. / Tsai, M.-D. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: Structure of the FHA1 domain of yeast Rad53 and identification of binding sites for both FHA1 and its target protein Rad9 Authors: Liao, H. / Yuan, C. / Su, M.I. / Yongkiettrakul, S. / Qin, D. / Li, H. / Byeon, I.J. / Pei, D. / Tsai, M.D. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g3g.cif.gz | 1016 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g3g.ent.gz | 876.6 KB | Display | PDB format |
PDBx/mmJSON format | 1g3g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g3/1g3g ftp://data.pdbj.org/pub/pdb/validation_reports/g3/1g3g | 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: 18506.938 Da / Num. of mol.: 1 / Fragment: THE N-TERMINAL FHA DOMAIN (FHA1), RESIDUES 1-164 / Mutation: M1G Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: SPK1 OR RAD53 / Plasmid: PGEX-4T / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: P22216, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor |
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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 triple-resonance NMR spectroscopy. |
-Sample preparation
Details | Contents: 0.5 mM protein U-15N, 13C; 10 mM sodium phosphate buffer (pH 6.5), 1 mM DTT, and 1 mM EDTA; 95 % H2O, 5 % D2O Solvent system: 95% H2O/5% D2O |
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Sample conditions | Ionic strength: 10 mM sodium phosphate, 1 mM DTT, and 1 mM EDTA pH: 6.5 / Pressure: ambient / Temperature: 293 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 2156 restraints, 1886 are NOE-derived distance constraints, 192 TALOS-derived dihedral angle restraints,78 distance restraints from hydrogen bonds. ...Details: The structures are based on a total of 2156 restraints, 1886 are NOE-derived distance constraints, 192 TALOS-derived dihedral angle restraints,78 distance restraints from hydrogen bonds. RESIDUES 1-14 ARE POORLY DEFINED BY THE EXPERIMENTAL DATA. THUS, NO MEANING SHOULD BE GIVEN TO THOSE RESIDUES' COORDINATES. | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 |