Improvement in catalytic activity and thermostability of a GH10 xylanase and its synergistic degradation of biomass with cellulase

Table 2 Comparison of the hydrogen bond quantity and occupancy rates of XylE and its hybrid mutants

Fragments	Residue^a	Acceptor	Donor	Occupancy rate (%)	Acceptor	Donor	Occupancy rate (%)
M3	116	S_115@OG	E_116@H	11	–	–	–
	118	P_118@O	V_121@N	47	F_77@O	S_118@HG	45
	119	F_119@O	N_123@N	48	D_119@OD2	S_123@OG	57
	120	E_81@O	W_130@HE1	65	–	–	–
	121	P_118@O	F_122@H	13	S_118@O	F_122@N	28
	122	F_119@O	N_123@H	48	–	–	–
	123	P_124@O	F_126@H	15	E_130@OE2	K_124@NZ	11
	124	P_124@O	F_126@H	15	–	–	–
M6	201	V_197@O	K_201@H	91	A_237@O	R_201@NH1	83
	202	L_200@O	A_202@H	10	S_198@O	K_201@N	42
	203	E_153@OE2	R_203@HH12	88	E_153@OE1	R_203@HH22	75
	204	K_201@O	N_204@N	31	R_201@O	G_208@H	26
M9	336	E_346@O	F_336@H	81	E_340@O	N_336@H	64
	337	E_337@OD1	L_345@H	60	–	–	–
	338	P_338@O	N_342@HD22	10	N_336@OD1	F_338@HG1	37
	339	D_339@OD1	N_342@HD22	64	–	–	–
	340	G_340@O	F_343@H	24	–	–	–
	342	D_339@OD1	N_342@HD22	64	–	–	–
	343	G_340@O	F_343@H	24	–	–	–
	344	P_344@O	K_60@H21	18	–	–	–

The number of hydrogen bonds and occupancy rates are shown for the fragments M3, M6, and M9 during the last 5 ns of the trajectories
^aResidue numbering corresponds to Fig. 2, in which the Ala18 of XylE is the first residue. The residues of wild-type XylE with lower occupancy rates are indicated in italic

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