1YWL

Solution NMR structure of the protein EF2693 from E. faecalis: Northeast Structural Genomics Consortium target EFR36


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D_15N-separated_NOESY5% D2O, 0.02% NaN3, 10mM DTT, 5mM CaCl2, 100mM NaCl, 20mM MES5 % D20, 95 % H20100 mM NaCl, 5 mM CaCl26.51 atm293
23D_13C-separated_NOESY5% D2O, 0.02% NaN3, 10mM DTT, 5mM CaCl2, 100mM NaCl, 20mM MES5 % D20, 95 % H20100 mM NaCl, 5 mM CaCl26.51 atm293
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerAVANCE500
2VarianINOVA600
NMR Refinement
MethodDetailsSoftware
torsion angle dynamics simulated annealingThe structures are based on a total of 912 conformationally-restricting noe-derived distance restraints, 216 dihedral restraints and 54 hydrogen bond restraints.DYANA
NMR Ensemble Information
Conformer Selection CriteriaStructures with lowest energy
Conformers Calculated Total Number56
Conformers Submitted Total Number10
Representative Model1 (lowest energy)
Additional NMR Experimental Information
DetailsThe structure was determined using triple-resonance NMR spectroscopy. Automatic backbone resonance assignments were made using AutoAssign. Side-chain assignments were made manually. Automatic NOE assignments were made using AutoStructure. Dihedral angle restraints were made using Hyper and Talos. The SPINS database software was used as an integrating agent. PSVS was used to validate structure quality.
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1refinementDYANA1.5Guentert, et al
2structure solutionAutoStructure2.0.0Huang
3data analysisAutoAssign1.14Moseley, et al
4processingNMRPipe2.1Delaglio, et al
5collectionVNMR6.1BVarian
6collectionXwinNMR3.5Bruker
7structure solutionPdbStat4.01Tejero and Montelione
8structure solutionHYPER3.2Tejero and Montelione
9structure solutionTALOS2.1Cornilescu, et al
10data analysisSPINS5.0Baran
11refinementPSVS1.0Bhattacharya