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. Author manuscript; available in PMC: 2018 May 16.
Published in final edited form as: Org Biomol Chem. 2017 May 16;15(19):4096–4114. doi: 10.1039/c7ob00526a

Fig. 7.

Fig. 7

The bis-Thr pair in NMR structure, PDB entry, 2FIN. (a) The PDB entry contains 15 conformers, with a bis-Thr pair formed by residues Thr 78 and Thr 95. Over the 15 conformers of the protein, the two Thr residues display a range of χ torsion rotations. (b) An example of a polar bis-Thr conformation as seen in conformer 12 of the protein ensemble. In this example, the hydroxyl hydrogen atom of Thr 78 engages in a hydrogen bond (yellow dash) with the hydroxyl oxygen atom of Thr 95. (c) An example of a hydrophobic (or apolar) bis-Thr conformation as seen in conformer 1 of the protein ensemble. In this example, the methyl groups of Thr 78 and Thr 95 engage in a favorable hydrophobic contact (orange dash). Movie S1 shows the rotations observed for the 15 conformers in the PDB entry.