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Figure 2.
Fig. 2. High-quality NMR solution structures of target
proteins are displayed in the order of Table 1. For each
structure, a ribbon drawing is shown on the left.  -Helices
are enumerated with roman numerals, and  -strands are indicated
with letters (for sequence locations of the regular secondary
structure elements, see footnote of Table 1). The N and C
termini of the polypeptide chains are labeled with N and C. On
the right, a "sausage" representation of the backboneis shown
for which a spline function was drawn through the C^ positions and where the
thickness of the cylindrical rod is proportional to the mean of
the global displacements of the 20 DYANA conformers calculated
after superposition of the backbone heavy atoms N, C^ , and C'
of the regular secondary structure elements for minimal rmsd.
Hence, the thickness reflects the precision achieved for the
determination of the polypeptide backbone conformation. A
superposition of the best-defined side chains having the lowest
global displacement for the side-chain heavy atoms also are
shown (best third of all residues; for residue numbers, see
footnote of Table 1) to indicate precision of the determination
of side-chain conformations. Helices are shown in red, the -stands
are depicted in cyan, other polypeptide segments are displayed
in gray, and the side chains of the molecular core are shown in
blue. The figure was generated by using the program MOLMOL (37).
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