2L2S

Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei complexed with 1-{[(4-methylphenyl)thio]acetyl}piperidine


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D HNCA0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase95% H2O/5% D2O10071 atm298
23D HNCACB0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase95% H2O/5% D2O10071 atm298
33D HN(CO)CA0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase95% H2O/5% D2O10071 atm298
43D CBCA(CO)NH0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase95% H2O/5% D2O10071 atm298
52D 1H-15N HSQC0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase95% H2O/5% D2O10071 atm298
62D 1H-1H TOCSY0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase100% D2O10071 atm298
72D 1H-1H NOESY0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase100% D2O10071 atm298
82D 1H-15N HSQC0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase100% D2O10071 atm298
93D 1H-15N NOESY0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase95% H2O/5% D2O10071 atm298
103D 1H-15N TOCSY0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase95% H2O/5% D2O10071 atm298
113D HCCH-TOCSY0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase100% D2O10071 atm298
123D 1H-13C NOESY0.6-1.5 mM [U-99% 13C; U-99% 15N] isomerase100% D2O10071 atm298
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerAVANCE500
2BrukerAVANCE600
NMR Refinement
MethodDetailsSoftware
torsion angle dynamicsNMRPipe
NMR Ensemble Information
Conformer Selection Criteriatarget function
Conformers Calculated Total Number100
Conformers Submitted Total Number20
Representative Model1 (lowest energy)
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1processingNMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
2structure solutionCYANA2.1Guntert, Mumenthaler and Wuthrich
3chemical shift assignmentAnalysisCCPN
4refinementCYANA2.1Guntert, Mumenthaler and Wuthrich