1M7T

Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
1HNCO1 mM protein in 100 mM sodium phosphate buffer (pH 7.0), 20 M EDTA, 0.02% sodium azide, and 10% D2O.90% H2O/10% D2O7.0308
2HNCACB1 mM protein in 100 mM sodium phosphate buffer (pH 7.0), 20 M EDTA, 0.02% sodium azide, and 10% D2O.90% H2O/10% D2O7.0308
315N TOCSY-HSQC1 mM protein in 100 mM sodium phosphate buffer (pH 7.0), 20 M EDTA, 0.02% sodium azide, and 10% D2O.90% H2O/10% D2O7.0308
4HCCH-TOCSY1 mM protein in 100 mM sodium phosphate buffer (pH 7.0), 20 M EDTA, 0.02% sodium azide, and 10% D2O.90% H2O/10% D2O7.0308
5H(CCO)NH-TOCSY1 mM protein in 100 mM sodium phosphate buffer (pH 7.0), 20 M EDTA, 0.02% sodium azide, and 10% D2O.90% H2O/10% D2O7.0308
6C(CO)NH-TOCSY1 mM protein in 100 mM sodium phosphate buffer (pH 7.0), 20 M EDTA, 0.02% sodium azide, and 10% D2O.90% H2O/10% D2O7.0308
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerDMX500
2BrukerDMX750
3BrukerDMX600
4BrukerDRX800
NMR Refinement
MethodDetailsSoftware
see publicationDYANA
NMR Ensemble Information
Conformer Selection CriteriaBack calculated data agree with experimental NOESY spectrum,structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy,target function
Conformers Calculated Total Number100
Conformers Submitted Total Number21
Representative Model21 (closest to the average, minimized average structure)
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1structure solutionDYANA1.5
2refinementXPLOR