2OUT

Solution Structure of HI1506, a Novel Two Domain Protein from Haemophilus influenzae


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D_13C-separated_NOESY1mM HI1506 U-13C, 15N50mM Potassium phosphate pH 7.0, 100mM NaCl, 1mM DTT; 90% H2O, 10% D2O50mM Potassium phosphate, 100mM NaCl, 1mM DTT7.0ambient298
23D_15N-separated_NOESY1mM HI1506 U-13C, 15N50mM Potassium phosphate pH 7.0, 100mM NaCl, 1mM DTT; 90% H2O, 10% D2O50mM Potassium phosphate, 100mM NaCl, 1mM DTT7.0ambient298
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerAVANCE600
NMR Refinement
MethodDetailsSoftware
structures were calculated using standard simulated annealing and torsion angle dynamics protocols in CNS version 1.1XwinNMR
NMR Ensemble Information
Conformer Selection Criteriastructures with acceptable covalent geometry
Conformers Calculated Total Number100
Conformers Submitted Total Number20
Representative Model1 (closest to the average)
Additional NMR Experimental Information
DetailsThe structure was determined using triple-resonance NMR spectroscopy. The protein consists of two domains connected by a linker loop (30 a.a residues long). The pdb file is generated by superimposing the N-domain (residues 7-56) in which case C-domain (residues 89-120) cannot be superimposed. The same is true for the case where C-domain is superimposed. N-domain shows up all over the superimposed domain.
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1collectionXwinNMR3.5Bruker-biospin
2structure solutionCNS1.1Brunger
3processingNMRPipeDelaglio
4data analysisSparkyGoddard and Kneller
5refinementCNS1.1Brunger