Table III.
Global analysis of molecular contacts
| Protein | PDB code | Tm (°C) | H-bondsa | Salt bridge interactions <7 Åa | ASA (Å2)b | GRAVY scorec | Negatively charged residuesd | Positively charged residuesd |
|---|---|---|---|---|---|---|---|---|
| FN3con | 4U3H | >100 | 46 | 48 | 4545.5 | –0.536 | 10 | 7 |
| Fibcon | 3TEU | 89.6 | 42 | 14 | 4882.3 | –0.190 | 8 | 3 |
| FNfn10 | 1FNF | 82.5 | 41 | 9 | 5470.8 | –0.115 | 8 | 8 |
| Tencon | 3TES | 78.0 | 44 | 28 | 5093.3 | –0.307 | 12 | 7 |
| FNfn8 | 1FNF | 58.0 | 43 | 28 | 5239.0 | –0.377 | 11 | 7 |
| TNfn3 | 1TEN | 57.1 | 45 | 41 | 5163.5 | –0.577 | 18 | 9 |
a
Hydrogen bonds and salt bridges were calculated using the WHATIF server (Hekkelman et al., 2010).
b
Calculated using the ASA tool from ccp4 (Winn et al., 2011).
c
Calculated using the ProtParam tool provided by ExPASy and uses the Kyte and Doolittle hydropathy value for each amino acid (Kyte and Doolittle, 1982).
d
Negatively charged amino acids are counted as Asp and Glu, while positively charged amino acids are counted as Arg and Lys.