1K4U
Solution structure of the C-terminal SH3 domain of p67phox complexed with the C-terminal tail region of p47phox
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | HNCA, HN(CO)CA, CBCA(CO)NH, HNCACB, HBHA(CO)NH, HCCH-COSY, HCCH-TOCSY, CCH-COSY, 15N-RESOLVED NOESY, 15-RESOLVED TOCSY, HNHA, HNHB, 3D_F1 13C-FILTERED-F3 13C-RESOLVED NOESY, 3D_F1 15N-FILTERED-F3 15N-RESOLVED NOESY, 2D_SPIN-ECHO DIFFERENCE EXPERIMENTS | 0.7mM p67SH3(C) U-15N,13C; 0.77mM p47 tail peptide; 5mM MOPSO buffer; 30 mM d10-DTT; 100mM KCl | 90% H2O, 10% D2O; 100% D2O | 100mM KCl | 7.1 | 1 atm | 298 | |
| 2 | HNCA, HN(CO)CA, CBCA(CO)NH, HNCACB, HBHA(CO)NH, HCCH-COSY, HCCH-TOCSY, CCH-COSY, 15N-RESOLVED NOESY, 15-RESOLVED TOCSY, HNHA, HNHB, 3D_F1 13C-FILTERED-F3 13C-RESOLVED NOESY, 3D_F1 15N-FILTERED-F3 15N-RESOLVED NOESY, 2D_SPIN-ECHO DIFFERENCE EXPERIMENTS | 0.5mM p47 tail peptide U-15N,13C; 0.55mM p67SH3(C); 5mM MOPSO buffer; 30mM d10-DTT; 100mM KCl | 90% H2O, 10% D2O; 100% D2O | 100mM KCl | 7.1 | 1 atm | 298 | |
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | DMX | 600 |
| 2 | Bruker | DMX | 750 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| simulated annealing | The structures are based on a total of 693 restraints, 611 are NOE-derived distance constraints, 82 dihedral angle restraints. No hydrogen bond restraint was used. | CNS |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | structures with the lowest energy |
| Conformers Calculated Total Number | 100 |
| Conformers Submitted Total Number | 22 |
| Representative Model | 7 (lowest energy) |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | structure solution | CNS | 1.0 | Brunger |
| 2 | refinement | CNS | 1.0 | Brunger |
