SOLID-STATE MAS NMR STRUCTURE OF THE A-SPECTRIN SH3 DOMAIN
Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
SRC HOMOLOGY 3 DOMAIN (RESIDUES 965-1025)
SPECTRIN, NON-ERYTHROID ALPHA CHAIN, FODRIN ALPHA CHAIN
THIS SOLID-STATE NMR STRUCTURE WAS DETERMINED BY COMBINING BROAD-BAND RECOUPLING METHODS WITH DILUTION OF THE 13C SPINS
13C-13C PROTON-DRIVEN SPIN- DIFFUSION (PDSD)
15N-15N PROTON-DRIVEN SPIN-DIFFUSION (PDSD)
THE STRUCTURES ARE BASED ON A TOTAL OF 286 13C-13C RESTRAINTS AND 6 15N-15N RESTRAINTS. ALL RESTRAINTS ARE EXTRACTED FROM PDSD SPECTRA.
SIMULATED ANNEALING, TORSION ANGLE DYNAMICS
A 200 MM (NH4)2SO4 SOLUTION WAS ADDED TO A 1.15 MM SH3 SOLUTION (PH=3.5) AT A VOLUME RATIO 1:1. THE SOLID SAMPLE WAS OBTAINED BY PRECIPITATION, CHANGING THE PH TO 7.5 IN NH3 ATMOSPHERE.
SOLID-STATE MAS NMR STRUCTURE, STRUCTURAL PROTEIN