2KCO

Solution NMR structure of ribosomal protein sso0164 from Sulfolobus solfataricus. Northeast Structural Genomics Consortium (NESG) target SsT4.


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D HNCO0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
23D HNCA0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
33D CBCA(CO)NH0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
43D HBHA(CO)NH0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
53D H(CCO)NH0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
63D C(CO)NH0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
73D 1H-15N NOESY0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
83D HCCH-TOCSY0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
93D HCCH-TOCSY0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
103D 1H-13C NOESY0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
113D 1H-13C_arom NOESY0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
122D 1H-15N HSQC(IPAP)0.5 mM [U-13C; U-15N] sso0164-1, 10 mM TRIS-2, 500 mM sodium chloride-3, 10 uM ZnSO4-4, 10 mM DTT-5, 0.01 % NaN3-6, 10 mM benzamidine-790% H2O/10% D2O5007.7ambient298
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerAVANCE800
2VarianINOVA600
3BrukerAVANCE600
NMR Refinement
MethodDetailsSoftware
restrained molecular dynamics in water bathNMRPipe
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
DetailsThe NMR data suggest that residues 1-60 do not form a globular domain, although residues 38-48 does form an isolated helix. This N-terminal region is likely to be very flexible and the extended structures presented here do not necessarily represent a defined conformation for this region (other than the helix). There do not appear to be any interactions between residues 1-60 and the C-terminal globular part of the protein.
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1processingNMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
2peak pickingSparkyGoddard
3resonanmce assignmentFMCLemak, Steren, Llinas, Arrowsmith
4data analysisTALOSCornilescu, Delaglio and Bax
5refinementCNSBrunger, Adams, Clore, Gros, Nilges and Read