+Open data
-Basic information
Entry | Database: PDB / ID: 1j4o | ||||||
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Title | REFINED NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53 | ||||||
Components | PROTEIN KINASE SPK1 | ||||||
Keywords | TRANSFERASE / FHA DOMAIN / RAD53 / RAD9 / PHOSPHOTHREONINE / PHOSPHOPROTEIN | ||||||
Function / homology | Function and homology information deoxyribonucleoside triphosphate biosynthetic process / negative regulation of DNA damage checkpoint / meiotic recombination checkpoint signaling / telomere maintenance in response to DNA damage / negative regulation of phosphorylation / dual-specificity kinase / DNA replication origin binding / DNA replication initiation / regulation of DNA repair / protein serine/threonine/tyrosine kinase activity ...deoxyribonucleoside triphosphate biosynthetic process / negative regulation of DNA damage checkpoint / meiotic recombination checkpoint signaling / telomere maintenance in response to DNA damage / negative regulation of phosphorylation / dual-specificity kinase / DNA replication origin binding / 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 / DNA repair / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | 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. | ||||||
Authors | Yuan, C. / Yongkiettrakul, S. / Byeon, I.-J.L. / Zhou, S. / Tsai, M.-D. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2001 Title: Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53. Authors: Yuan, C. / Yongkiettrakul, S. / Byeon, I.J. / Zhou, S. / 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 | 1j4o.cif.gz | 65.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1j4o.ent.gz | 49.3 KB | Display | PDB format |
PDBx/mmJSON format | 1j4o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1j4o_validation.pdf.gz | 249.9 KB | Display | wwPDB validaton report |
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Full document | 1j4o_full_validation.pdf.gz | 249.6 KB | Display | |
Data in XML | 1j4o_validation.xml.gz | 5.6 KB | Display | |
Data in CIF | 1j4o_validation.cif.gz | 7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j4/1j4o ftp://data.pdbj.org/pub/pdb/validation_reports/j4/1j4o | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | 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
-Experiment
Experiment | Method: SOLUTION NMR |
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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. |
-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 |
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Sample conditions | Ionic strength: 10 mM SODIUM PHOSPHATE, 1mM DTT, AND 1 mM EDTA pH: 6.5 / Pressure: AMBIENT / Temperature: 293.00 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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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 |