File S1 - The Mode of Inhibitor Binding to Peptidyl-tRNA Hydrolase: Binding Studies and Structure Determination of Unbound and Bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii

Figure S1. Sequence alignments of peptidyl tRNA hydrolases (Pths) from Acinetobacter baumannii (AbPth) with Pseudomonas aeruginosa (PaPth) Escherichia coli (EcPth), Mycobacterium tuberculosis (MtPth) and Mycobacterium smegmatis (MsPth) whose crystal structures are known. The overall sequence identities vary from 58% to 39%. The flexible regions consisting of residues, Met1 - Leu6, Pro65 - Ser80, Gly111 - Leu118, Ile121 - Pro127, Pro139 - His148 and Pro181 - Ala193 are highlighted in grey. The probable residues involved in the catalysis are highlighted in yellow. The secondary structure elements α-helices (cylinders) and β-strands (arrows) are also indicated above the sequences. Figure S2. Showing results of polyacrylamide gel electrophoresis for AbPth. Lane A: molecular weight markers, 116.0 kDa - β-galactosidase, 66.2 kDa - bovine serum albumin, 45.0 kDa - ovalbumin, 35.0 kDa - lactate dehydrogenase, 25.0 kDa - ribonuclease, 18.4 kDa - β-lactoglobulin and 14.4 kDa - lysozyme; Lane B: purified protein, AbPth. Figure S3. Showing electron densities for the C-terminal segment, Pro181– Ala193 (A) |Fo–Fc| map at 2.5 σ cut off and (B) |2Fo–Fc| map at 1 σ cut off. Figure S4. Bindings of cytidine (A) and uridine (B) showing large conformational changes with side chains of Asn70, Asp98 and Asn116. The electron densities from the initial (Fo–Fc) map at 2.5 σ cut off. (DOC)