1H8B
EF-hands 3,4 from alpha-actinin / Z-repeat 7 from titin
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | SEE PUBLICATION | 0.7 MM COMPLEX | 20 mM | 6.6 | 1 atm | 300 | ||
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Varian | UNITYPLUS | 500 |
| 2 | Varian | UNITY | 600 |
| 3 | Varian | INOVA | 800 |
| 4 | Bruker | DRX | 800 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| TORSION ANGLE DYNAMICS, CARTESIAN DYANMICS | REFINEMENT DETAILS MAY BE FOUND IN THE JRNL CITATION ABOVE THE FIRST RESIDUE OF THE NATURAL SEQUENCE OF ALPHA-ACTININ EF34 IS REPLACED BY A MET. THIS IS PRECEDED BY THE DIPEPTIDE GLY-ALA. THERE ARE NO DISTANCE CONSTRAINTS FOR THESE TWO RESIDUES WHICH ARE OMITTED FROM THE STRUCTURE CALCULATION. THE FIRST RESIDUE OF THE NATURAL SEQUENCE OF TITIN ZR7 IS REPLACED BY A MET. THIS IS PRECEDED BY THE DIPEPTIDE GLY-ALA. THERE ARE NO DISTANCE CONSTRAINTS FOR THE N-TERMINAL 8 RESIDUES AND THE C-TERMINAL 22 RESIDUES WHICH ARE OMITTED FROM THE STRUCTURE CALCULATION. | X-PLOR |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | LOWEST ENERGIES |
| Conformers Calculated Total Number | 50 |
| Conformers Submitted Total Number | 30 |
| Representative Model | 1 (n/a) |
| Additional NMR Experimental Information | |
|---|---|
| Details | THE STRUCTURE OF THE COMPLEX WAS DETERMINED USING CONSTRAINTS FROM 15N-EDITED NOESY, 13C-EDITED NOESY AND F1-FILTERED/F3-EDITED NOESY SPECTRA, RECORDED ON 13C, 15N-LABELLED SAMPLES IN WHICH ONLY ONE OF THE TWO COMPONENTS WAS LABELLED |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | refinement | X-PLOR | 3.1 | BRUNGER |
| 2 | structure solution | DYANA | ||
| 3 | structure solution | X-PLOR | ||
