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Additional Supporting Information may be found in the online version of this article.

FilenameFormatSizeDescription
prot24302-sup-0001-suppfig1.pdf4214KFigure S1 Snapshots of wild type and mutants of single chain cylindrin at the beginning and end of 300 ns simulation.
prot24302-sup-0002-suppfig2.pdf727KFigure S2 Change in the hydrophobic contacts Cα-Cα distances between the pair of residue 4 from each strand in the dry interior of single chain cylindrin. Red for wild-type (WT-TR), magenta for V4GV8G, brown for V4AV8A, blue V2L, and green for VTL. The results are the averages of three independent 300 ns trajectories. Here, a stands for strand number and b for residue number in aStb-aStb designation of the Cα-Cα distance of the hydrophobic core residues Val4 in the wild type single chain cylindrin and mutants.
prot24302-sup-0003-suppfig3.pdf730KFigure S3 Comparison of the average salt bridge interactions distances between Lysn and Asp along the 300 ns simulation of the wild-type and its mutants of single chain cylindrin along the three out of register interfaces. Red for wild-type (WT-TR), magenta for V4GV8G, brown for V4AV8A, blue V2L, and green for VTL. The results are the average of three independent 300 ns simulations of each system. Here, a stands for strand number and b for residue number in aKb- aDb designation of the salt bridge distance of the wild type single chain cylindrin and mutants

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