MUTANT R122A OF QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED STRUCTURE
Mutational analysis and NMR spectroscopy of quail cysteine and glycine-rich protein CRP2 reveal an intrinsic segmental flexibility of LIM domains.
MDRGERLGIKPESSPSPHRPTTNPNTSKFAQKFGGAEKCSACGDSVYAAEKVIGAGKPWHKNCFRCAKCGKSLESTTLTE KEGEIYCKGCYAKNFGPKGFGYGQGAGALVHAQ
RELATED WILD-TYPE PEPTIDE: CARBOXYLTERMINAL LIM DOMAIN OF QCRP2
THIS STRUCTURE WAS DETERMINED USING STANDARD 15N-EDITED SPECTRA AND HOMONUCLEAR 2D SPECTRA
STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS,STRUCTURES WITH THE LOWEST ENERGY
THE STRUCTURE IS BASED ON 340 NOE-DERIVED DISTANCE RESTRAINTS AS WELL AS 16 DISTANCE RESTRAINTS DERIVED FROM HYDROGEN BONDS
SIMULATED ANNEALING, MOLECULAR DYNAMICS REFINEMENT, ENERGY MINIMIZATION
1.1MM QCRP2(LIM2)R122A 15N; 20MM POTASSIUM PHOSPHATE; 50MM POTASSIUM CHLORIDE; 0.5MM DTT;
DELAGLIO, F., GRZESISEK, S., VUISTER, G., ZHU, G. PFEIFER, J., BAX, A.
LIM DOMAIN CONTAINING PROTEINS, METAL-BINDING PROTEIN, SIGNALING PROTEIN