1K3N

NMR Structure of the FHA1 Domain of Rad53 in Complex with a Rad9-derived Phosphothreonine (at T155) Peptide


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D_13C-separated_NOESY0.5 mM FHA1 U-15N,13C; 10 mM sodium phosphate buffer (pH 6.5), 1mM DTT, and 1 mM EDTA; 90% H2O, 10% D2O90% H2O/10% D2O10 mM sodium phosphate, 1mM DTT, and 1 mM EDTA6.5ambient293
23D_15N-separated_NOESY0.5 mM FHA1 U-15N,13C; 10 mM sodium phosphate buffer (pH 6.5), 1mM DTT, and 1 mM EDTA; 90% H2O, 10% D2O90% H2O/10% D2O10 mM sodium phosphate, 1mM DTT, and 1 mM EDTA6.5ambient293
32D_13C/15N-filtered_NOESY0.5 mM FHA1 U-15N,13C; 10 mM sodium phosphate buffer (pH 6.5), 1mM DTT, and 1 mM EDTA; 90% H2O, 10% D2O90% H2O/10% D2O10 mM sodium phosphate, 1mM DTT, and 1 mM EDTA6.5ambient293
43D_13C-edited_13C/15N-filtered_NOESY0.5 mM FHA1 U-15N,13C; 10 mM sodium phosphate buffer (pH 6.5), 1mM DTT, and 1 mM EDTA; 90% H2O, 10% D2O90% H2O/10% D2O10 mM sodium phosphate, 1mM DTT, and 1 mM EDTA6.5ambient293
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerDRX800
NMR Refinement
MethodDetailsSoftware
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 and intra-peptide distance constraints.XwinNMR
NMR Ensemble Information
Conformer Selection Criteriastructures with the least restraint violations,structures with the lowest energy
Conformers Calculated Total Number50
Conformers Submitted Total Number20
Additional NMR Experimental Information
DetailsThe structure was determined using triple-resonance NMR spectroscopy.
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1collectionXwinNMR2.6Bruker
2processingXwinNMR2.6Bruker
3structure solutionCNS1.0Brunger et al.
4refinementCNS1.0Brunger et al.