1NMW

Solution structure of the PPIase domain of human Pin1


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D_15N-separated_NOESY0.6-0.8mM Pin1(PPIase) U-15N,13C; 50mM phosphate buffer, 1mM DTT, 5mM EDTA, 50-100mM Na sulphate90% H2O/10% D2On.c.6.6ambient300
23D_13C-separated_NOESY0.6-0.8mM Pin1(PPIase) U-15N,13C; 50mM phosphate buffer, 1mM DTT, 5mM EDTA, 50-100mM Na sulphate90% H2O/10% D2On.c.6.6ambient300
33D_15N-separated_NOESY0.6-0.8mM Pin1(PPIase) U-15N,13C;50mM Tris/HCl buffer, 1mM DTT, 5mM EDTA90% H2O/10% D2On.c.6.6ambient300
4HNHA0.6-0.8mM Pin1(PPIase) U-15N,13C; 50mM phosphate buffer, 1mM DTT, 5mM EDTA, 50-100mM Na sulphate90% H2O/10% D2On.c.6.6ambient300
52D NOESY0.8mM Pin1(PPIase); 50mM phosphate buffer, 1mM DTT, 5mM EDTA, 50-100mM Na sulphate90% H2O/10% D2On.c.6.6ambient300
62D TOCSY0.8mM Pin1(PPIase); 50mM phosphate buffer, 1mM DTT, 5mM EDTA, 50-100mM Na sulphate90% H2O/10% D2On.c.6.6ambient300
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1VarianINOVA600
NMR Refinement
MethodDetailsSoftware
torsion angle dynamicsXwinNMR
NMR Ensemble Information
Conformer Selection Criteriastructures with the least restraint violations,structures with the lowest energy
Conformers Calculated Total Number100
Conformers Submitted Total Number10
Representative Model7 (lowest energy)
Additional NMR Experimental Information
DetailsHydrogen bonds were extracted from HSQC spectra in D2O
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1processingXwinNMR3.2Bruker
2data analysisAURELIA2.8.11Bruker
3collectionVNMR6.18Varian
4refinementCNS1.0Bruenger
5data analysisNDEE1.2Spin-Up