1U4A

Solution structure of human SUMO-3 C47S


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D_15N-separated_NOESY0.8mM 15N-labeled protein25mM phosphate buffer, 75mM Nacl 90% H2O, 10% D2O25mM phosphate buffer, 75mM Nacl6.251 atm298
23D_13C-separated_NOESY0.6mM 13C,15N-labeled protein25mM phosphate buffer, 75mM Nacl 90% H2O, 10% D2O25mM phosphate buffer, 75mM Nacl6.251 atm298
32D NOESY0.8mM 15N-labeled protein25mM phosphate buffer, 75mM Nacl 90% H2O, 10% D2O25mM phosphate buffer, 75mM Nacl6.251 atm298
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerDMX500
2BrukerDMX600
NMR Refinement
MethodDetailsSoftware
simulated annealingThe structures are based on a total of 1540 restraints, 1406 are NOE-derived distance constraints, 78 dihedral angle restraints, 56 distance restraints from hydrogen bondsNMRPipe
NMR Ensemble Information
Conformer Selection Criteriastructures with the lowest energy
Conformers Calculated Total Number200
Conformers Submitted Total Number20
Representative Model1 (lowest energy)
Additional NMR Experimental Information
DetailsThe structure was determined using triple-resonance NMR spectroscopy.
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1processingNMRPipe2.2F. Delaglio
2processingSparky3T.D.Goddard , D.G.Kneller
3structure solutionCNS1.1A.T.Brunger ,D.D.Adanis etal
4data analysisCSI1.0David S. Wishart
5structure solutionMOLMOL2k.2Koradi
6refinementMOLMOL2k.2Koradi