Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2018 Apr 26;8:6614. doi: 10.1038/s41598-018-24688-2

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Inter-protomer interfaces of three StI W111C homodimer structural models stabilized by a disulfide bridge between Cys 111 during molecular dynamics. All homodimer models were achieved after 100 ns of the trajectory (A) model_14 (31a_32b_1bsr), (B) model_25 (32a_31b11ba), and (C) model_63 (90a_90b_1grg). The different elements of secondary structure are shown in red (helixes), blue (sheets) and gray (loops and unordered structures). Tryptophan residues (green), except W147 in model_14, and disulfide bridge (yellow) are also high-lighted. Tryptophan and amino acid residues involved in the protein-protein interaction are labeling. Tables inserted (right) summarize the hydrogen bounds established for more than 30 ns of the dynamics (>30% of the simulation time). Images were produced with the Pymol v1.7.6.6 software for Windows¹⁰⁷.