1XPW

Solution NMR Structure of human protein HSPCO34. Northeast Structural Genomics Target HR1958


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D_15N-separated_NOESY1 mM U-15N,13C protein, 20 mM MES, 100 mM NaCl, 10 mM DTT, 5 mM CaCl2, 0.02% NaN3, 95% H2O, 5% D2O95% H2O/5% D2O100 mM NaCl6.5ambient298
23D_13C-separated_NOESY1 mM U-15N,13C protein, 20 mM MES, 100 mM NaCl, 10 mM DTT, 5 mM CaCl2, 0.02% NaN3, 95% H2O, 5% D2O95% H2O/5% D2O100 mM NaCl6.5ambient298
3HNHA1 mM U-15N,13C protein, 20 mM MES, 100 mM NaCl, 10 mM DTT, 5 mM CaCl2, 0.02% NaN3, 95% H2O, 5% D2O95% H2O/5% D2O100 mM NaCl6.5ambient298
413C_HSQC1 mM U-15N,13C protein, 20 mM MES, 100 mM NaCl, 10 mM DTT, 5 mM CaCl2, 0.02% NaN3100% D2O100 mM NaCl6.5ambient298
54D_13C-separated_NOESY1 mM U-15N,5%-13C protein, 20 mM MES, 100 mM NaCl, 10 mM DTT, 5 mM CaCl2, 0.02% NaN3, 95% H2O, 5% D2O95% H2O/5% D2O100 mM NaCl6.5ambient298
6H/D exchange1 mM U-15N,5%-13C protein, 20 mM MES, 100 mM NaCl, 10 mM DTT, 5 mM CaCl2, 0.02% NaN3, 95% H2O, 5% D2O95% H2O/5% D2O100 mM NaCl6.5ambient298
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1VarianINOVA800
2VarianINOVA750
3VarianINOVA600
4VarianUNITY600
NMR Refinement
MethodDetailsSoftware
XPLOR SIMULATED ANNEALING, CNS WATER REFINEMENTThe unstructured 10 residue N-terminal His tag (MGHHHHHHSH) was not included in the structure calculation.NMRPipe
NMR Ensemble Information
Conformer Selection Criteriastructures with the least restraint violations
Conformers Calculated Total Number25
Conformers Submitted Total Number20
Representative Model1 (closest to the average)
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1processingNMRPipenmrpipe.linuxDelaglio
2processingFelix98Accelrys
3data analysisAutoStructure2.1.0Y.J. Huang, G.T. Montelione
4structure solutionX-PLORXPLOR-NIH-2.0.6C.D. Schwieters, J.J. Kuszewski, N. Tjandra, G.M. Clore
5refinementCNS1.1Brunger
6data analysisSparky3.106T. Goddard, UCSF