1FAD
DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183
SOLUTION NMR
NMR Experiment | ||||||||
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Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
1 | 3D-15N-HSQC-NOESY | 2 MM | 4.0 | 303 | ||||
2 | 3D-13C | 2 MM | 4.0 | 303 | ||||
3 | 15N-EDITED NOESY | 2 MM | 4.0 | 303 | ||||
4 | 13C-HCCH-TOCSY | 2 MM | 4.0 | 303 | ||||
5 | 3D-15N-HSQC-TOCSY | 2 MM | 4.0 | 303 | ||||
6 | NOESY | 2 MM | 4.0 | 303 | ||||
7 | 3D HNHA | 2 MM | 4.0 | 303 |
NMR Spectrometer Information | |||
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Spectrometer | Manufacturer | Model | Field Strength |
1 | Varian | UNITYPLUS600 | 500 |
2 | Varian | INOVA500 | 600 |
NMR Refinement | ||
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Method | Details | Software |
DISTANCE GEOMETRY AND SIMMULATED ANNEALING | X-PLOR |
NMR Ensemble Information | |
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Conformer Selection Criteria | LOWEST ENERGY |
Conformers Calculated Total Number | 50 |
Conformers Submitted Total Number | 21 |
Representative Model | 21 (n/a) |
Additional NMR Experimental Information | |
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Details | DISTANCE CONSTRAINTS ARE DERIVED FROM THE 3D-13C, 15N-EDITED NOESY. J-COUPLING CONSTANTS FROM HNHA AND 13C CHEMICAL SHIFTS WERE USED AS CONTRAINTS. DURING THE REFINEMENT, DATABASE POTENTIAL WAS USED. |
Computation: NMR Software | ||||
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# | Classification | Version | Software Name | Author |
1 | refinement | X-PLOR | 3.851 | BRUNGER |
2 | structure solution | X-PLOR |