1POQ

Solution Structure of a Superantigen from Yersinia pseudotuberculosis


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
12D NOESY0.5mM YPM protein (33-151), 95% H2O, 5% D2O95% H2O/5% D2O6.5ambient298
22D TOCSY0.5mM YPM protein (33-151), 95% H2O, 5% D2O95% H2O/5% D2O6.5ambient298
3DQF-COSY0.5mM YPM protein (33-151), 95% H2O, 5% D2O95% H2O/5% D2O6.5ambient298
4HNHA0.5mM YPM protein (33-151), 95% H2O, 5% D2O95% H2O/5% D2O6.5ambient298
5HN(CO)CA0.5mM YPM protein (33-151), 95% H2O, 5% D2O95% H2O/5% D2O6.5ambient298
6HNCA0.5mM YPM protein (33-151), 95% H2O, 5% D2O95% H2O/5% D2O6.5ambient298
7CBCA(CO)NH0.5mM YPM protein (33-151), 95% H2O, 5% D2O95% H2O/5% D2O6.5ambient298
8HNCACB0.5mM YPM protein (33-151), 95% H2O, 5% D2O95% H2O/5% D2O6.5ambient298
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerDRX600
NMR Refinement
MethodDetailsSoftware
simulated annealing, molecular dynamics, torsion angle dynamicsFinal structures were based on 1934 unambiguous NOE-derived distance constraints, 139 ambiguous constraints, 135 dihedral angle restraints and 26 hydrogen bond distance restraints.XwinNMR
NMR Ensemble Information
Conformer Selection Criteriastructures with the lowest energy
Conformers Calculated Total Number100
Conformers Submitted Total Number20
Representative Model1 (lowest energy)
Additional NMR Experimental Information
DetailsThis structure was determined using standard 2D homonuclear and triple-resonance NMR spectroscopy.
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1processingXwinNMR2.6Bruker
2data analysisXEASY1.3.13Bartels et al
3refinementDYANA1.5Guntert et al
4structure solutionARIA1.1.2Linge et al