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. Author manuscript; available in PMC: 2016 Oct 1.
Published in final edited form as: J Biomol Screen. 2015 Jun 26;20(9):1160–1170. doi: 10.1177/1087057115591120

Figure 1.

Figure 1

Amino acid sequence alignment of P. aeruginosa GluRS with homologs. The protein sequences were downloaded from the National Center for Biotechnology Information (NCBI). Ec, E. coli; Pa, P. aeruginosa; Tel, T. elongatus; Tth, T. thermophilus. Accession numbers for GluRS protein sequences of E. coli, P. aeruginosa, T. elongatus, and T. thermophilus are P04805, Q9XCL6, 2CFO_B, and Q72LI9, respectively. Sequence alignments were performed using Vector NTI Advance (TM) 11.0 (Invitrogen). Identical amino acid residues are white on black, and similar residues are white on gray. The positions of the HIGH and KMSKS motifs are indicated. Amino acid residues that interact with Glu (*), ATP (▲ for productive mode, △ for nonproductive mode), and tRNA (●) are indicated. The amino acid residues Arg358 and Thr444 (Tth numbering) are indicated (★).