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
Serine/threonine-protein kinase Rad53 / Tumour Suppressor Smad4 - #20 / Tumour Suppressor Smad4 / Forkhead associated domain / Forkhead-associated (FHA) domain profile. / FHA domain / Forkhead-associated (FHA) domain / SMAD/FHA domain superfamily / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. ...Serine/threonine-protein kinase Rad53 / Tumour Suppressor Smad4 - #20 / Tumour Suppressor Smad4 / Forkhead associated domain / Forkhead-associated (FHA) domain profile. / FHA domain / Forkhead-associated (FHA) domain / SMAD/FHA domain superfamily / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Sandwich / Mainly Beta Similarity search - Domain/homology
SOLUTION NMR / THE STRUCTURES ARE BASED ON A TOTAL OF 2377 RESTRAINTS. AMONG THEM, 2107 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 192 TALOS-DERIVED DIHEDRAL ANGLE RESTRAINTS, AND 78 RESTRAINTS FROM HYDROGEN BONDS.
Mass: 17093.490 Da / Num. of mol.: 1 / Fragment: N-TERMINAL FHA DOMAIN (FHA1) 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
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Type: 3D 13C-SEPARATED NOESY
NMR details
Text: THE STRUCTURE WAS REFINED BY ADDING 221 NOE- DERIVED DISTANCE CONSTRAINTS AND BY REVISING A FEW PREVIOUS NOE ASSIGNMENTS.
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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; 90% H2O, 10% D2O
Sample conditions
Ionic strength: 10 mM SODIUM PHOSPHATE, 1mM DTT, AND 1 mM EDTA pH: 6.50 / Pressure: AMBIENT / Temperature: 293.00 K
Crystal grow
*PLUS
Method: other / Details: NMR
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NMR measurement
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Bruker DRX
Bruker
DRX
800
1
Bruker DMX
Bruker
DMX
600
2
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Processing
NMR software
Name
Version
Classification
XwinNMR
2.6
structuresolution
CNS
1
structuresolution
CNS
1
refinement
Refinement
Method: THE STRUCTURES ARE BASED ON A TOTAL OF 2377 RESTRAINTS. AMONG THEM, 2107 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 192 TALOS-DERIVED DIHEDRAL ANGLE RESTRAINTS, AND 78 RESTRAINTS FROM HYDROGEN BONDS. Software ordinal: 1
NMR ensemble
Conformers submitted total number: 1
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