Table 2.

Prediction of the catalytic residues in TT1542

Residues	CNa	Clocalb	Cspacec	Sd	Re	Df	Lg	pcath	Decisioni
His 10	1.00	0.90	0.78	−0.91	3	0.25	2	0.81	✓
Asp 12	1.00	0.90	0.79	1.13	13	2.60	3	0.68	✓
Asp 13	1.00	0.88	0.83	0.86	14	2.17	3	0.68	✓
Glu 15	1.00	0.93	0.78	0.89	17	2.37	0	0.50	✓
Thr 38	1.00	0.73	0.68	−1.23	1	0.00	0	0.09
Arg 51	1.00	0.77	0.65	−0.25	9	0.73	3	0.61	✓
Glu 54	1.00	0.60	0.61	0.10	13	0.54	2	0.50	✓
Asp 74	1.00	0.65	0.68	−0.20	9	0.95	1	0.78	✓
His 108	1.00	0.57	0.53	−0.74	6	0.40	1	0.10
Tyr 145	1.00	0.70	0.65	−1.77	1	0.00	0	0.09

^a Conservation number (CN) defined using the amino-acid grouping scheme by Taylor (Taylor 1986; Zvelebil et al. 1987).

^b Averaged conservation numbers estimated within a local window along the sequence.

^c Averaged conservation numbers estimated over the contact sites in the 3D space.

^d Score, ^eRank, and ^fScore difference, which indicate the stability of the mutant protein.

^g Location number assigned to each category: 3 for hole, 2 for cleft, 1 for surface, and 0 for inside the protein structure according to the preference for the catalytic residues.

^h Probability of the catalytic resides.

ⁱ Catalytic residues are predicted if p_cat ≥ 0.5 (✓).