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

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

FragmentsResidueaAcceptorDonorOccupancy rate (%)AcceptorDonorOccupancy rate (%)
M3116S_115@OGE_116@H11
118P_118@OV_121@N47F_77@OS_118@HG45
119F_119@ON_123@N48D_119@OD2S_123@OG57
120E_81@OW_130@HE165
121P_118@OF_122@H13S_118@OF_122@N28
122F_119@ON_123@H48
123P_124@OF_126@H15E_130@OE2K_124@NZ11
124P_124@OF_126@H15
M6201V_197@OK_201@H91A_237@OR_201@NH183
202L_200@OA_202@H10S_198@OK_201@N42
203E_153@OE2R_203@HH1288E_153@OE1R_203@HH2275
204K_201@ON_204@N31R_201@OG_208@H26
M9336E_346@OF_336@H81E_340@ON_336@H64
337E_337@OD1L_345@H60
338P_338@ON_342@HD2210N_336@OD1F_338@HG137
339D_339@OD1N_342@HD2264
340G_340@OF_343@H24
342D_339@OD1N_342@HD2264
343G_340@OF_343@H24
344P_344@OK_60@H2118
  1. 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
  2. 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