1PZQ | pdb_00001pzq

Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS 2 and DEBS 3: The A domain


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D_15N-separated_NOESY1mM DOCK23 U-15N,13C: 100mM phosphate buffer NA: trace amounts of sodium azide, AEBSF protease inhibitor cocktail and TSP 1H shift reference: 90% H2O, 10% D2O90% H2O/10% D2O100mM phosphate buffer NA6.5ambient298
23D_13C-separated_NOESY1mM DOCK23 U-15N,13C: 100mM phosphate buffer NA: trace amounts of sodium azide, AEBSF protease inhibitor cocktail and TSP 1H shift reference: 90% H2O, 10% D2O90% H2O/10% D2O
33D_13C_15N_X-filtered_13C-separated_NOESY1mM DOCK23 (50% U-15N,13C: 50% unlabeled): 100mM phosphate buffer NA: trace amounts of sodium azide, AEBSF protease inhibitor cocktail and TSP 1H shift reference: 90% H2O, 10% D2O90% H2O/10% D2O
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerDRX500
2BrukerDRX800
NMR Refinement
MethodDetailsSoftware
simulated annealingthe structures are based on a total of 1811 restraints: 1709 NOE-derived distance constraints, 60 dihedral angle restraints, 42 distance restraints from hydrogen bonds.ANSIG
NMR Ensemble Information
Conformer Selection Criteriastructures with the lowest energy
Conformers Calculated Total Number40
Conformers Submitted Total Number8
Representative Model1 (closest to the average)
Additional NMR Experimental Information
DetailsThe structure was determined using triple-resonance NMR spectroscopy. Intermolecular contacts were obtained from an X-filtered NOESY experiment on a mixed-labeled sample.
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1data analysisANSIG3.3Kraulis
2structure solutionCNS1.0Brunger
3refinementCNS1.0Brunger