SOLUTION STRUCTURE OF THE REPS1 EH DOMAIN
Solution structure of the Reps1 EH domain and characterization of its binding to NPF target sequences.
Chapter 3: Studies of Protein Structure and Interaction using Nuclear Magnetic Resonance Spectroscopy:Applications to the Reps1 EH Domain and MicrocinB17 Propeptide
WKITDEQRQYYVNQFKTIQPDLNGFIPGSAAKEFFTKSKLPILELSHIWELSDFDKDGALTLDEFCAAFHLVVARKNGYD LPEKLPESLMPK
BMRB-4788 is 1H, 13C, and 15N resonance assignments
The structure was determined using heteronuclear 2D and 3D NMR spectroscopy.
The structures are based on a total of 1265 restraints, 1143 are NOE-derived distance constraints, 122 dihedral angle restraints.
1mM Reps1 EH domain U-15N,13C; 10mM d-imidazole buffer, 1.5mM CaCl2; 90% H2O, 10% D2O
1mM Reps1 EH domain U-15N; 10mM d-imidazole buffer, 1.5mM CaCl2; 90% H2O, 10% D2O
1mM Reps1 EH domain; 10mM d-imidazole buffer, 1.5mM CaCl2
EPS15 HOMOLOGY DOMAIN, EF HAND, CALCIUM, RAS SIGNAL TRANSDUCTION, endocytosis-exocytosis COMPLEX