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Figure 1.
Figure 1: SCA-based protein design. a, Structure of a
representative WW domain (Nedd4.3, Protein Data Bank 1I5H) in
complex with a target peptide (in stick representation). The two
canonical tryptophans are shown as space-filling side chains.
The figure was prepared using PyMol51. b, SCA conservation
scores for each position in the WW alignment in arbitrary units
of statistical energy12. Position numbers (x axis) and the
secondary structure diagram at the top coincide with matrix
columns in c-e. c, A matrix representation of statistical
coupling values from perturbation analysis of five positions
(rows) in the WW domain MSA. d, The matrix for an alignment of
IC sequences, built by randomly selecting amino acids at each
site from the observed frequency distributions in the natural
alignment. e, The matrix for an alignment of CC sequences,
derived from a design algorithm where both the conservation
pattern and the pattern of statistical couplings in the natural
alignment are preserved. Scale bar shows the SCA coevolution
score, ranging from 0 (blue) to 2 (red).
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