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. Author manuscript; available in PMC: 2011 Aug 1.
Published in final edited form as: Proteins. 2010 Aug 1;78(10):2338–2348. doi: 10.1002/prot.22746

Table III.

Comparison Between the Results Given by Wild-Type Sequences, Sequences Designed by RosettaDesign 2.3 and by RosettaDesign-SR

% Polar residuesa
Seq. ID (%)b % LCc % LLLd % VVVe All α β Coil
Wild-type 100 3.1% 0.063 0.045 50.1 51.8 44.7 52.5
RosettaDesign 31.4 9.1% 0.244 0.093 45.6 50.1 36.1 48.3
RosettaDesign-SR 33.9 4.0% 0.039 0.038 48.2 51.1 41.5 50.3

The results are obtained for the test set of 944 proteins with the top 1 ranked sequence in 100 sequences designed for each protein.

a

Frequency of polar residues for helical, strand, and coil positions, respectively.

b

The average sequence identity to wild type sequences of target proteins.

c

Percent of low-complexity regions defined by program SEG72

d

Percent of occurrence for three sequentially linked Leu residues.

e

Percent of occurrence for three sequentially linked Val residues.