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. 2011 Jun 15;6(6):e20950. doi: 10.1371/journal.pone.0020950

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Wang et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) Cartoon representation of the overall structure of rBTI. Different structural elements are shown in different colors, and the disulfide bridge is indicated. (B) A view of the hydrogen-bonding network and the hydrophobic core in rBTI. rBTI is shown in a cartoon presentation in green. Residues involved in hydrogen-bonding network and hydrophobic core are shown as ball-and-stick models. The grey sphere indicates a water molecule. Hydrogen bonds are indicated by black dashes and hydrophobic interactions are indicated by dotted clouds. (C) Overview of the structure of rBTI-trypsin complexes within an asymmetric unit. rBTIs are shown in yellow and magenta; trypsins are shown in green and cyan. The calcium ions in trypsin are shown as light-blue spheres. (D) Superposition of trypsin-bound rBTI and free rBTI. The binding loop of trypsin-bound rBTI (cyan) is shifted by a small distance from that of free rBTI (grey). The RMSD value calculated by superposition of trypsin-bound rBTI's and free rBTI's binding loops is 0.26 Å.