1MW4
Solution structure of the human Grb7-SH2 domain in complex with a 10 amino acid peptide pY1139
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | 3D_13C-separated_NOESY | 0.7mM Grb7 SH2 U-15N, 13C, 50mM acetate | 90% H2O/10% D2O | 100 mM NaCl | 6.6 | 1 atm | 298 | |
| 2 | 3D_15N-separated_NOESY | 0.7mM Grb7 SH2 U-15N, 13C, 50mM acetate | 90% H2O/10% D2O | 100 mM NaCl | 6.6 | 1 atm | 298 | |
| 3 | HNHA | 0.7mM Grb7 SH2 U-15N, 13C, 50mM acetate | 90% H2O/10% D2O | 100 mM NaCl | 6.6 | 1 atm | 298 | |
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Varian | INOVA | 500 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| torsion angle dynamics | THE STRUCTURE IS BASED ON A TOTAL OF 1904 RESTRAINTS: 1660 ARE NOE DERIVED, 120 ARE DIHEDRAL RESTRAINTS AND 124 ARE DISTANCE RESTRAINTS FROM HYDROGEN BONDS. | AZARA |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | structures with favorable non-bond energy |
| Conformers Calculated Total Number | 50 |
| Conformers Submitted Total Number | 10 |
| Representative Model | 5 (closest to the average) |
| Additional NMR Experimental Information | |
|---|---|
| Details | The structure was determined using triple-resonance NMR spectroscopy. |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | processing | AZARA | 2.6 | Boucher |
| 2 | data analysis | ANSIG | 3.3 | Kraulis |
| 3 | structure solution | CNS | 1.1 | Brunger |
| 4 | refinement | CNS | 1.1 | Brunger |
