. Author manuscript; available in PMC: 2008 Mar 1.

Published in final edited form as: J Struct Biol. 2006 Oct 11;157(3):491–499. doi: 10.1016/j.jsb.2006.10.001

Table 3.

For various precedence times, information on identified helix-predictive residue pairs for villin.^a

	200 ps	1000 ps	2000 ps	5000 ps
H1	Asp5-Ala10, Phe8-Val11; 9468, 454; 84%; 0.28±0.10 Å	Ser4-Leu30, Glu6-Val11; 9468, 454; 70%; 0.55±0.25 Å	Glu6-Ala10, Glu6-Gln27; 9468, 454; 68%; 0.50±0.22 Å	Met2-Leu22, Ser4-Asn29; 9466, 450; 58%; 0.74±0.28 Å
H3	Trp25-Asn29, Asn29-Lys32; 9380, 542; 84%; 0.30±0.12 Å	Asp5-Phe37, Gln27-Lys31; 9380, 542; 70%; 0.54±0.25 Å	Lys26-Leu30, Lys26-Lys31; 9380, 541; 66%; 0.28±0.15 Å	Ala20-Lys32, Leu24-Leu30; 9378, 536; 61%; 0.38±0.21 Å

Each table cell lists the residue-residue pairs, the cardinalities of the negative and positive sets, the predictive accuracy of a nearest neighbor classifier based only on the two distances, and the mean partial DRMSD between members of the negative set and the mean of the positive set.