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Figure 2.
Wall-eye stereo views of the NMR structure of the protein
Asl1650. (A) Bundle of 20 energy-minimized DYANA conformers.
(Blue) Polypeptide backbone, (gold) hydrophobic side chains of
the protein core. The positions of selected hydrophobic core
residues are identified with the sequence numbers. (B) Ribbon
diagram of the Asl1650 conformer with the lowest RMSD to the
mean coordinates of the bundle of 20 conformers in panel A. The
four helices forming a helix bundle (see text) are labeled
[alpha]I, [alpha]II, 3[10](III), and [alpha]IV at their N
termini. The chain-terminal residues [minus sign]3 and 85 are
indicated.
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