TABLE 3.

Predicted secondary structures of wild-type BFT (P-BFT) and BFTs with mutations in the C-terminal region^a

Residue	P-BFT	BFT-A394E	BFT-C2	BFT-C4	BFT-C7	BFT-C8	BFT-C9	BFT-C11	BFT-C18
Y373	Strand	Strand	Strand	Strand	Strand	Strand	Strand	Strand	Strand
L374	Strand	Strand	Strand	Strand	Strand	Strand	Strand	Strand	Strand
F375	Strand	Strand	Strand	Strand	Strand	Strand	Strand	Strand	Strand
H376	Strand	Strand	Strand	Strand	Strand	Strand	Strand	Strand	Strand
L377	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Coil
S378	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Coil
E379	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Coil
E380	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Helix
N381	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Helix
M382	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Helix
Y383	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Helix
R384	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Coil
I385	Helix	Helix	Helix	Helix	Helix	Helix	Helix	Coil
A386	Helix	Helix	Helix	Helix	Helix	Helix	Coil	Coil
K387	Helix	Helix	Helix	Helix	Helix	Coil	Coil
N388	Helix	Helix	Helix	Helix	Coil	Coil	Coil
L389	Coil	Coil	Coil	Coil	Coil	Coil
G390	Coil	Coil	Coil	Coil	Coil
W391	Helix	Coil	Helix	Coil
E392	Helix	Coil	Helix	Coil
I393	Helix	Coil	Coil	Coil
A394	Coil	Coil	Coil
D395	Coil	Coil	Coil
G396	Coil	Coil
D397	Coil	Coil

^aStructural changes with respect to wild-type BFT are indicated by boldface. Residues L377 to N388 in P-BFT comprise the putative active-site helix in the C terminus. None of the C-terminal BFT mutations predict secondary structural changes in the metalloprotease active site of BFT (H348 to H358) or in the methionine turn (M366). The predicted secondary structure of BFT was determined by using the DNAMAN version 5.2.9 sequence analysis software (Lynnon BioSoft, Quebec, Canada).