1EIW | pdb_00001eiw

Solution structure of hypothetical protein MTH538 from Methanobacterium thermoautotrophicum


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
14D_13C-separated_NOESY2mM MTH538 U-15N,13C; 25 mM phosphate buffer pH 7.1, 150 mM NaCl, 5 mM DTT99% D2O150 mM salt, 25 mM phosphate buffer7.4ambient298
23D_15N-separated_NOESY2mM MTH538 U-15N; 25 mM phosphate buffer pH 7.4, 150 mM NaCl, 90% H2O, 10% D2O, 5 mM DTT90% H2O/10% D2O150 mM salt, 25 mM phosphate buffer7.4ambient298
3HMQC-J2mM MTH538 U-15N; 25 mM phosphate buffer pH 7.4, 150 mM NaCl, 90% H2O, 10% D2O, 5 mM DTT90% H2O/10% D2O150 mM salt, 25 mM phosphate buffer7.4ambient298
43D_13C,15N-simultaneous NOESY2mM MTH538 U-15N,13C; 25 mM phosphate buffer pH 7.4, 150 mM NaCl, 90% H2O, 10% D2O, 5 mM DTT90% H2O/10% D2O150 mM salt, 25 mM phosphate buffer7.4ambient298
51H-15N HSQC D2O exchange2mM MTH538 U-15N; 25 mM phosphate buffer pH 7.1, 150 mM NaCl, 5 mM DTT99% D2O150 mM salt, 25 mM phosphate buffer7.4ambient298
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1VarianINOVA600
2VarianUNITYPLUS500
NMR Refinement
MethodDetailsSoftware
distance geometry and simulated annealing519 NOE-derived distance constraints 55 dihedral angle constraints (phi) 28 hydrogen bonds (2 constraints per H-bond)X-PLOR
NMR Ensemble Information
Conformer Selection Criteriastructures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy
Conformers Calculated Total Number20
Conformers Submitted Total Number16
Representative Model1 (fewest violations)
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1structure solutionX-PLOR3.1Brunger
2processingFelix98MSI
3collectionVNMRVarian
4refinementX-PLOR3.1Brunger