Table 2.
Per-residue properties of the TS ensemble
| Property | Fold class |
|||
|---|---|---|---|---|
| All | All-α | All-β | Mixed α/β | |
| Number of total contacts∗ | 2.73 (0.31) | 2.80 (0.27) | 2.57 (0.31) | 2.81 (0.25) |
| Number of native contacts∗ | 2.23 (0.35) | 2.36 (0.31) | 2.02 (0.35) | 2.31 (0.27) |
| Number of nonnative contacts∗ | 0.50 (0.12) | 0.44 (0.12) | 0.55 (0.13) | 0.49 (0.12) |
| Number of hydrogen bonds | 0.55 (0.12) | 0.66 (0.11) | 0.44 (0.11) | 0.56 (0.09) |
| Number of hydrophobic contacts† | 10.78 (1.30) | 10.76 (1.28) | 10.46 (1.37) | 11.10 (1.10) |
| Number of other contacts† | 17.45 (2.01) | 19.25 (1.77) | 15.82 (1.71) | 17.57 (1.22) |
| Mc SASA (Å2) | 17.30 (3.11) | 16.12 (2.73) | 18.77 (3.00) | 16.70 (2.31) |
| Sc SASA (Å2) | 65.13 (8.25) | 70.46 (7.34) | 63.84 (7.39) | 62.60 (7.53) |
| Total SASA (Å2) | 82.43 (9.84) | 86.58 (8.43) | 82.61 (9.31) | 79.30 (8.92) |
For each property, the mean value over the TS ensemble was calculated and divided by the number of residues in the protein. The values given in this table are the mean over all proteins; the standard deviation is in parentheses. Mc, main chain; Sc, side chain.
∗
Contacts counted on a residue-residue basis.
†
Contacts counted on an atom-atom basis.