1Q59
Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2
SOLUTION NMR
NMR Experiment | ||||||||
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Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
1 | 3D_13C-separated_NOESY | U-15N,13C 0.5-1.0 mM BHRF1-EBV-BCL2 , containing 20 mM Tris (pH 7.5) and 2 mM 2H-dithiothreitol | 90% H2O/10%2H2O | 20mM | 7.5 | ambient | 303 | |
2 | 3D_15N-separated_NOESY | U-15N,13C 0.5-1.0 mM BHRF1-EBV-BCL2 , containing 20 mM Tris (pH 7.5) and 2 mM 2H-dithiothreitol | 90% H2O/10%2H2O | 20mM | 7.5 | ambient | 303 |
NMR Spectrometer Information | |||
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Spectrometer | Manufacturer | Model | Field Strength |
1 | Bruker | DRX | 500 |
2 | Bruker | DRX | 800 |
3 | Bruker | DRX | 600 |
NMR Refinement | ||
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Method | Details | Software |
BHRF1 structures were calculated using a simulated annealing protocol with the program CNX | CNS |
NMR Ensemble Information | |
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Conformer Selection Criteria | |
Conformers Calculated Total Number | |
Conformers Submitted Total Number | 1 |
Representative Model | 1 (minimized average structure) |
Computation: NMR Software | ||||
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# | Classification | Version | Software Name | Author |
1 | refinement | CNS | 2000 |