Determination of a Protein Structure in the Solid State from NMR Chemical Shifts
Determination of protein structures in the solid state from NMR chemical shifts.
Solid-state protein-structure determination with proton-detected triple-resonance 3D magic-angle-spinning NMR spectroscopy.
Proton-detected solid-state NMR spectroscopy of fully protonated proteins at 40 kHz magic-angle spinning.
Protein structure determination from NMR chemical shifts.
Solid-state structure of Beta-1 Immunoglobulin binding domain of protein G (GB1) solved from Ha, Ca, Cb, and N backbone chemical shifts.
For Experimental Data See BMRB Entry 15156
Structure Selection and Refinement were performed according to CHESHIRE protocol for calculation of structures from NMR Chemical Shifts (Cavalli et al., 2007, PNAS, 104, 9615-9620)
MD/MC hybrid refinment against Target Fuction weighted by chemical shift accuracy and a molecular mechanics force field
10 mg/mL [U-100% 13C; U-100% 15N] GB1, 0.5 v/v Methyl Pentane diol, 0.25 v/v Isopropanol
0.5 v/v Methyl Pentane diol/0.25 v/v Isopropanol
solid-state, chemical shift restraints, GB1, Cell wall, IgG-binding protein, Peptidoglycan-anchor, Secreted, PROTEIN BINDING