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. Author manuscript; available in PMC: 2016 Nov 26.
Published in final edited form as: Biochemistry. 2016 Apr 22;55(17):2479–2490. doi: 10.1021/acs.biochem.6b00056

Table 4.

Phi/Psi values of the nucleophile position (Nu) and the position after the nucleophile (Nu+1) in wild type and glycine mutants extracted from their respective crystal structures. Additionally, distances of main chain hydrogen bonds formed by these positions and their angles are listed.


Nucleophile (Nu) position
Protein omega (ω) [-Cα(Nu)-CO(Nu)- NH(Nu+1)-Cα(Nu+1)-] (°) phi (φ) (°) psi (ψ) (°) C=O(Nu)…H–N(Nu+3) (Å) H-bond Angle (°)
TEM-1 WT 177 −65.2 −8.15 3.01 140
TEM-1 S70G 179 −54.4 −15.4 2.91 147
CTX-M-14 WT 172 −71.3 −4.76 1.96 138
CTX-M-14 S70G 176 −67.2 −4.19 2.00 134
P99 WT 176 −61.2 −14.9 1.97 156
P99 S64G 177 −58.9 −12.8 3.19 163
OXA-48 WT 174 −68.1 −10.8 2.94 136
OXA-48 S70A 175 −67.1 −10.3 2.97 135
OXA-48 S70G 177 −53.5 −21.5 3.04 163
OXA-163 WT 176 −72.4 −10.4 2.91 135
OXA-163 S70G 179 −58.8 −19.9 2.94 160