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Overlay of computational and solid-state NMR structures (in red) for α-factor receptor M6 (1pjd) and VPU (1pje). The 10-solution NMR structures of a synthetic peptide derived from the NR1 subunit of the NMDA receptor exhibited two minimum energy conformations (2nr1, models 1 and 3). Each helix lies flat in the plane of the graph except for model 3 of 2nr1, which lies perpendicular. The cytoplasmic side is down (+ve z axis).
