1LKN | pdb_00001lkn

Solution NMR Structure of Protein TM_1112 from Thermotoga maritima. Ontario Centre for Structural Proteomics Target TM1112_1_89; Northeast Structural Genomics Consortium Target VT74.


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D_13C/15N-separated_NOESY1mM tm1112 U-15N,13C; 25mM phosphate buffer NA; 95% H2O, 5% D2O95% H2O/5% D2O20uM Zn2+6.5ambient298
23D_15N/15N-separated_NOESY1mM tm1112 U-15N,13C; 25mM phosphate buffer NA; 95% H2O, 5% D2O95% H2O/5% D2O20uM Zn2+6.5ambient298
3HNHA1mM tm1112 U-15N,13C; 25mM phosphate buffer NA; 95% H2O, 5% D2O95% H2O/5% D2O20uM Zn2+6.5ambient298
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1VarianINOVA500
2VarianINOVA600
NMR Refinement
MethodDetailsSoftware
simulated annealingThe structures are based on a total of 2619 restraints, in which 2508 are NOE-derived distance constraints, 111 are dihedral angle restraints from TALOS analysis and HNHA experiment.NMRPipe
NMR Ensemble Information
Conformer Selection Criteriaall calculated structures submitted,back calculated data agree with experimental NOESY spectrum,structures with the lowest energy
Conformers Calculated Total Number30
Conformers Submitted Total Number10
Representative Model1 (lowest energy)
Additional NMR Experimental Information
DetailsThe structure was determined using triple-resonance NMR spectroscopy
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1processingNMRPipe2.1F. Delaglio
2data analysisSparkySPARKY 3T. D. Goddard and D. G. Kneller
3structure solutionARIA BASED ON XPLOR3.851M. NILGES, A.T. Brunger
4refinementARIA BASED ON XPLOR3.851M. NILGES, A.T. Brunger