2MH5 | pdb_00002mh5

Structure and NMR assignments of lantibiotic NAI-107 in DPC micelles


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
12D 1H-1H TOCSY3.5 mM entity_1, 150 mM [U-2H] dodecylphosphocholine-d38, 10 mM potassium phosphate, 0.02 mM 2,2,3,3-D TSP-d495% H2O/5% D2O6.2ambient310.1
22D 1H-1H NOESY3.5 mM entity_1, 150 mM [U-2H] dodecylphosphocholine-d38, 10 mM potassium phosphate, 0.02 mM 2,2,3,3-D TSP-d495% H2O/5% D2O6.2ambient310.1
32D 1H-13C HSQC aliphatic3.5 mM entity_1, 150 mM [U-2H] dodecylphosphocholine-d38, 10 mM potassium phosphate, 0.02 mM 2,2,3,3-D TSP-d495% H2O/5% D2O6.2ambient310.1
42D 1H-13C HSQC aromatic3.5 mM entity_1, 150 mM [U-2H] dodecylphosphocholine-d38, 10 mM potassium phosphate, 0.02 mM 2,2,3,3-D TSP-d495% H2O/5% D2O6.2ambient310.1
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1BrukerAVIII600
2BrukerAVANCE900
3BrukerDRX600
NMR Refinement
MethodDetailsSoftware
molecular dynamicsRefinement was done in two steps: first in vacuo and then with explicit micelle/water system. The pseudo atoms labeled ANI are included in the constraint file. These define an alignment frame used in the structural interpretation of rdc data.TopSpin
NMR Ensemble Information
Conformer Selection Criteriastructures with the least restraint violations
Conformers Calculated Total Number80
Conformers Submitted Total Number20
Representative Model1 (fewest violations)
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1collectionTopSpin3.1Bruker Biospin
2chemical shift assignmentCARAKeller and Wuthrich
3structure solutionCYANA3.0Guntert, Mumenthaler and Wuthrich
4refinementYASARAYasara Biosciences