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 |
Hydrogen bonds and salt bridges were calculated using the WHATIF server (Hekkelman et al., 2010).
Calculated using the ASA tool from ccp4 (Winn et al., 2011).
Calculated using the ProtParam tool provided by ExPASy and uses the Kyte and Doolittle hydropathy value for each amino acid (Kyte and Doolittle, 1982).
Negatively charged amino acids are counted as Asp and Glu, while positively charged amino acids are counted as Arg and Lys.