Table 1.

Changes in secondary structure, ligand free energy of binding and ligand affinity upon mutation of A. thaliana ent-CPS

Nr	Mutation	Secondary structure change and accuracy of prediction (%)	ΔΔGBIND (kcal/mol)	KA (nM)
–	WT	–	− 8.91	292.88
1	T114F	None 100%, coil → coil	− 0.77	79.99
2	D336L	None 100% helix → helix	− 0.59	108.56
3	D377L	None, 100%, coil → coil	− 0.76	82.31
4	D377K	None, 100%, coil → coil	− 0.23	200.67
5	H391L	Change, 0% helix → other than helix and sheet	− 0.40	150.11
6	H391M	Change, 0% helix → other than helix and sheet	− 0.13	237.97
7	G422L	None, 100% helix → helix	− 0.54	119.32
8	G422M	None, 100% helix → helix	− 0.12	241.61
9	S597W	None, 100% helix → helix	− 0.60	106.92
10	K778F	None, 100% helix → helix	− 0.54	118.12
11	K778W	None, 100% helix → helix	− 0.44	140.55
12	H793F	Change, 0%, other than helix and heet → other than helix and sheet	− 0.52	123.21
13	H793L	Change, 0%, other than helix and heet → other than helix and sheet	− 0.61	104.43
14	H793M	Change, 0%, other than helix and heet → other than helix and sheet	− 0.61	104.43

Six selected single mutants that passed the presented quality test are marked in bold