1JDQ

Solution Structure of TM006 Protein from Thermotoga maritima


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
1hncacb2 mM TM006 protein U-15N,13C; 50mM phosphate buffer90% H2O/10% D2O150 mM NaCl6.81 atm310
2cbca(co)hn2 mM TM006 protein U-15N,13C; 50mM phosphate buffer90% H2O/10% D2O150 mM NaCl6.81 atm310
315N-hmqc-tocsy2 mM TM006 protein U-15N; 50mM phosphate buffer90% H2O/10% D2O150 mM NaCl6.81 atm310
415N-hmqc-noesy2 mM TM006 protein U-15N; 50mM phosphate buffer90% H2O/10% D2O150 mM NaCl6.81 atm310
5tocsy5 mM TM006 unlabelled protein; 50mM phosphate buffer90% H2O/10% D2O150 mM NaCl6.81 atm310
6noesy5 mM TM006 unlabelled protein; 50mM phosphate buffer90% H2O/10% D2O150 mM NaCl6.81 atm310
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerDRX500
NMR Refinement
MethodDetailsSoftware
simulated annealingAfter determination of protein fold by using manual NOE assigments, values of coupling constants and 13C chemical shifts, automatic peak NOE assigments were made by using ARIA and the structure refined by using standard protocol in CNS.XwinNMR
NMR Ensemble Information
Conformer Selection Criteriastructures with the lowest energy
Conformers Calculated Total Number85
Conformers Submitted Total Number20
Representative Model1 (lowest energy)
Additional NMR Experimental Information
DetailsStructure was determined using 2D and 3D experiments for unlabelled, 15N-labelled and double-labelled protein.
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1collectionXwinNMR2.1BRUKER
2processingXwinNMR2.1BRUKER
3data analysisXEASY1.3.13Bartels et al.
4data analysisARIA14.5.98Nilges et al.
5refinementCNS0.9Brunger et al.