1IRY

Solution structure of the hMTH1, a nucleotide pool sanitization enzyme


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D_15N-separated_NOESY1.7mM hMTH1 U-15N,13C; 50mM K-phosphate buffer, 20mM KCl, 0.1mM EDTA and 1mM DTT; 95% H2O, 5% D2O95% H2O/5% D2O706.9ambient303
24D_13C/15N-separated_NOESY1.7mM hMTH1 U-15N,13C; 50mM K-phosphate buffer, 20mM KCl, 0.1mM EDTA and 1mM DTT; 95% H2O, 5% D2O95% H2O/5% D2O706.9ambient303
3HNHA1.7mM hMTH1 U-15N,13C; 50mM K-phosphate buffer, 20mM KCl, 0.1mM EDTA and 1mM DTT; 95% H2O, 5% D2O95% H2O/5% D2O706.9ambient303
44D_13C-separated_NOESY1.7mM hMTH1 U-15N,13C; 50mM K-phosphate buffer, 20mM KCl, 0.1mM EDTA and 1mM DTT; 99.8% D2O99.8% D2O706.9ambient303
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerDMX500
2BrukerDRX800
NMR Refinement
MethodDetailsSoftware
simulated annealingThe structures are based on a total of 2312 restraints, 2043 are NOE-derived distance constraints, 177 dihedral angle restraints,92 distance restraints from hydrogen bonds detected through 3hJNC.DYANA
NMR Ensemble Information
Conformer Selection Criteriastructures with the lowest energy
Conformers Calculated Total Number100
Conformers Submitted Total Number30
Representative Model1 (lowest energy)
Additional NMR Experimental Information
DetailsSTEREOSPECIFIC ASSIGNMENTS OF THE METHYL GROUPS OF THE LEUCINE AND VALINE RESIDUES WERE ACHIEVED WITH 15% FRACTIONALLY 13C-LABELED hMTH1 DISSOLVED IN 99.8% D2O.
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1structure solutionDYANA1.5Guentert, P.
2processingNMRPipe1.8Delaglio, F.
3collectionXwinNMR2.6Bruker
4refinementCNS1.0Brunger, A.T.
5data analysisNMRpipp4.2.4Garrett, D.