Table 1.

Residues of importance for catalytic activity, structure or correct folding. Residues for which the importance has been previously determined are shown in Fig. 2, giving their numbers, their role and the bibliographic reference of the appropriate mutation study.

Nb. in Fig. 2	Importance:	Position is homologous to:	Reference:
1	structure	Arg62 (R) in TycB1	[34]
2	folding	Arg67 (R) in TycB1	[34]
3	folding	His146 in TycB1 (1st His of active site His-motif)	[34]
4	catalytic activity	His126 (2nd His of the active site His-motif) in VibH	[14,33,34]
5	structure	Asp130 (D) in VibH	[14,33,34]
6	catalytic activity	Gly131 (G of the active site His-motif) in VibH	[33]
7	folding	Trp202 (W) in TycB1	[34]
8	structure	Arg263 (R) in VibH = Arg278 (R) in EntF	[14,33]
9	catalytic activity	Trp264 (W) in VibH according to Keating et al., but absent in LCL, DCL and Starter C domains	[14]
10	catalytic activity	Asn335 (N) in VibH	[33]