TABLE 3.

N-terminal sequences of proteolytic fragments generated by trypsin and chymotrypsin

Banda	N-terminal sequenceb	Starts at position:	Molecular mass (kDa)c
			Apparent (on gel)	Predicted (to C terminus)
A	?-Thr-Ile-Lys-His-Gln	83	32.2	28.4
B	Val-Leu-Val-Thr-Asp	124	27.9	23.9
C	Asp-Val-Gln-Thr-Ala	142	26.8	21.9
D	Ala-Leu-Gln-Ala-Ala	185	17.6	17.1
E	Glu/Gly-Ala-Ser-Leu-Leu	263	9.1	8.4
F	Lys-?-Ile-Arg-Ser-Thr	79	32.2	28.9

^aThose indicated in Fig. 2 to 4. 

^bThe sequences were determined by Edman degradation, and the first five or six residues are shown. Despite blanks in some sequences, each was consistent with only one position in ParB, assuming that each N-terminal residue was preceded by either an arginine or a lysine for tryptic fragments and by a hydrophobic residue for chymotryptic fragments. 

^cThe apparent molecular masses were determined by linear regression analysis (Multi-Analyst software) of the protein gels, and the predicted masses were calculated on the assumption that the fragments extend to the C terminus of the protein.