1I0U
SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF A CONCATEMER OF EGF-HOMOLOGY MODULES OF THE HUMAN LOW DENSITY LIPOPROTEIN RECEPTOR
SOLUTION NMR
NMR Experiment | ||||||||
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Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
1 | HNHA | 1.5mM EGF-A, 20mM CaCl2 | 95% H2O/5% D2O | 0.060 | 5.5 | ambient | 310 | |
2 | 2D NOESY | 1mM 15N-EGF-AB, 20mM CaCl2 | 95% H2O/5% D2O | 0.060 | 5.5 | ambient | 310 | |
3 | 2D NOESY | 1.5mM EGF-A, 20mM CaCl2 | 99% D2O | 0.060 | 5.5 | ambient | 310 | |
4 | 2D NOESY | 1mM EGF-AB, 20mM CaCl2 | 95% H2O/5% D2O | 0.060 | 5.5 | ambient | 283 | |
5 | DQF-COSY | 1mM EGF-AB, 20mM CaCl2 | 95% H2O/5% D2O | 0.060 | 5.5 | ambient | 283 | |
6 | 3D_15N-separated_NOESY | 1.5mM EGF-A, 20mM CaCl2 | 95% H2O/5% D2O | 0.060 | 5.5 | ambient | 295 |
NMR Spectrometer Information | |||
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Spectrometer | Manufacturer | Model | Field Strength |
1 | Bruker | DMX | 750 |
NMR Refinement | ||
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Method | Details | Software |
1. Torsion angles dynamics 2. Restrained molecular dynamics with calcium 3. Energy minimisation | The structures are based on: 874 NOE restraints, 64 phi dihedral angles, 14 chi1 dihedral angles, 14 hydrogen bonds, 9 calcium ion ligand restraints | XwinNMR |
NMR Ensemble Information | |
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Conformer Selection Criteria | Energy minimised average structure from 30 selected structure with lowest energy |
Conformers Calculated Total Number | 100 |
Conformers Submitted Total Number | 1 |
Additional NMR Experimental Information | |
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Details | 15N T1, T2, and NOE relaxations to obtain backbone dynamics information T1/T2 data were not used for structure refinement |
Computation: NMR Software | ||||
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# | Classification | Version | Software Name | Author |
1 | collection | XwinNMR | 2.6 | Bruker |
2 | processing | Sparky | 3.95 | T. Goddard & D. G. Kneller |
3 | structure solution | DYANA | 1.5 | P. Guntert |
4 | refinement | X-PLOR | 3.85 | A. Brunger |
5 | data analysis | MOLMOL | 2.6 | R. Koradi |