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. 2015 Feb 16;28(3):67–78. doi: 10.1093/protein/gzv002

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.