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- PDB-1k3n: NMR Structure of the FHA1 Domain of Rad53 in Complex with a Rad9-... -
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Basic information
Entry | Database: PDB / ID: 1k3n | ||||||
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Title | NMR Structure of the FHA1 Domain of Rad53 in Complex with a Rad9-derived Phosphothreonine (at T155) Peptide | ||||||
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![]() | TRANSFERASE/CELL CYCLE / FHA domain / ![]() ![]() ![]() | ||||||
Function / homology | ![]() deoxyribonucleoside triphosphate biosynthetic process / G2/M DNA damage checkpoint / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / negative regulation of DNA strand resection involved in replication fork processing / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / meiotic recombination checkpoint signaling / SUMOylation of transcription factors / negative regulation of phosphorylation / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Yuan, C. / Yongkiettrakul, S. / Byeon, I.-J.L. / Zhou, S. / Tsai, M.-D. | ||||||
![]() | ![]() 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. #1: ![]() 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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PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
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PDB format | ![]() | 898.9 KB | Display | ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 17093.490 Da / Num. of mol.: 1 / Fragment: N-terminal FHA domain (FHA1) 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, ![]() |
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#2: Protein/peptide | ![]() Mass: 1617.754 Da / Num. of mol.: 1 / Fragment: Residues 149-161 / Source method: obtained synthetically Details: This phosphothreonine peptide was chemically synthesized. References: UniProt: P14737 |
-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||
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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 FHA1 U-15N,13C; 10 mM sodium phosphate buffer (pH 6.5), 1mM DTT, and 1 mM EDTA; 90% H2O, 10% D2O Solvent system: 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 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model![]() |
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Processing
NMR software |
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Refinement | Method: The complex structures are generated using a total of 2438 restraints. Among them, 3 artifical constraints, 192 TALOS-derived dihedral angle restrains, 78 restraints from H-bond, 16 ...Method: The complex structures are generated using a total of 2438 restraints. Among them, 3 artifical constraints, 192 TALOS-derived dihedral angle restrains, 78 restraints from H-bond, 16 intermolecular distance constrains, and 2149 intra-FHA1, intra-peptide distance constraints. Software ordinal: 1 | ||||||||||||||||||||
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 |