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Open data
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Basic information
Entry | Database: PDB / ID: 1g3g | |||||||||
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Title | NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53 | |||||||||
![]() | PROTEIN KINASE SPK1 | |||||||||
![]() | TRANSFERASE / FHA domain / Rad53 / Phosphopeptide / Phosphoprotein | |||||||||
Function / homology | ![]() deoxyribonucleoside triphosphate biosynthetic process / meiotic recombination checkpoint signaling / negative regulation of phosphorylation / dual-specificity kinase / calcium/calmodulin-dependent protein kinase activity / DNA replication origin binding / negative regulation of DNA damage checkpoint / DNA replication initiation / regulation of DNA repair / protein serine/threonine/tyrosine kinase activity ...deoxyribonucleoside triphosphate biosynthetic process / meiotic recombination checkpoint signaling / negative regulation of phosphorylation / dual-specificity kinase / calcium/calmodulin-dependent protein kinase activity / 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 / cellular response to oxidative stress / protein tyrosine kinase activity / calmodulin binding / protein kinase activity / phosphorylation / DNA repair / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
![]() | Yuan, C. / Liao, H. / Su, M. / Yongkiettrakul, S. / Byeon, I.-J.L. / Tsai, M.-D. | |||||||||
![]() | ![]() 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. | |||||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1019.6 KB | Display | ![]() |
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PDB format | ![]() | 850.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 345 KB | Display | ![]() |
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Full document | ![]() | 551.1 KB | Display | |
Data in XML | ![]() | 88 KB | Display | |
Data in CIF | ![]() | 112.7 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: 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.) ![]() ![]() Gene: SPK1 OR RAD53 / Plasmid: PGEX-4T / Species (production host): Escherichia coli / Production host: ![]() ![]() 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. |
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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 |