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. 2008 Jul 25;95(9):4384–4395. doi: 10.1529/biophysj.108.136747

TABLE 1.

Structural stability values obtained from FoldX analysis at 298 K

PDB code* Protein Resolution (Å) ΔG (kcal/mol) ΔΔGmut-WT (kcal/mol) ΔGPro-50 (kcal/mol) ΔGPro-91 (kcal/mol) ΔGPro-186 (kcal/mol)
1py6 bR WT 1.80 −95.10 −1.86 −2.14 −2.50
1pxr bR P50A 1.70 −84.15 10.95 −1.10 −1.34 −2.50
1q5j bR P91A 2.10 −89.10 6.00 −1.82 −0.02 −2.50
1q5i bR P186A 2.30 −83.80 11.30 −1.80 −2.10 −0.82
*

ΔG values shown correspond to the average of the analysis of FoldX applied separately to chain A and B of the respective structure.

The residue indicated in the respective structure corresponds to Ala.