Table 1.

Salt bridges/H-bonds between Bni1p knob helices and actin.

					Formin construct simulated
Formin residue	FH2 domain	Actin residue	Actin subunit	WT	R1423N	K1467L	R1423N/K1467L
Salt-bridges a
Residues binding the TBC
E1463	FH2L	R147	A2	82.6c	47.6	89.6	77.0
E1463	FH2T	R147	A3	85.8	81.5	81.1	91.3
K1467	FH2L	E167	A2	43.4	0	0	0
K1467	FH2T	E167	A3	98.9	98.4	0	0
Residues binding outside the TBC
D1424	FH2T	K50	A1	55.2	93.6	88.1	98.9
E1469	FH2T	K61	A1	92.6	99.6	54.8	5.6
E1472	FH2T	R95	A1	1.1	0	0	90.9
R1479	FH2T	E2	A1	0	0	83.0	0
R1479	FH2T	E100	A1	88.3	89.1	70.0	75.4
H-bonds b
Residues binding the TBC
R1423	FH2L	Q354	A2	31.1	20.0	3.7	10.2
R1423	FH2T	Q354	A3	18.3	5.3	0.2	14.4
E1463	FH2L	R147	A2	97.3	74.6	96.3	89.4
E1463	FH2T	R147	A3	96.4	96.4	97.6	98.8
K1467	FH2L	E167	A2	33.0	0	0	0
K1467	FH2T	E167	A3	95.1	95.4	0	0
Residues binding outside the TBC
D1424	FH2T	K50	A1	49.4	82.2	81.4	94.3
D1424	FH2T	Q49	A1	15.0	0.5	1.0	1.9
E1469	FH2T	K61	A1	74.8	82.8	49.3	4.2
E1472	FH2T	R95	A1	55.8	5.1	0.1	92.5
R1479	FH2T	E2	A1	0	0	97.1	0
R1479	FH2T	E100	A1	94.9	96.0	87.2	81.8

^aThe salt-bridge calculation was carried out with the Salt Bridges plugin that is provided with VMD (Humphrey, et al., 1996), using a distance cutoff of 4.0 Å between the position of oxygen and nitrogen atoms of the contributing residues.

^bH-bonds were calculated using a 3.5 Å distance cutoff and a 30° angle of linearity using the HBonds plugin of VMD.

^cAll values in the table are unitless percentages, representing the percentage time that each salt-bridge and H-bond is observed.