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. 2012 May 10;8(5):e1002502. doi: 10.1371/journal.pcbi.1002502

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Larrson 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) The RMSd from the crystal structure (without over all rotation and translation of the entire capsid) for the of the shell domain (average over the last 0.1 and all 60 proteins). (B) As A but after aligning each protein individually to the crystal structure. (C) The RMSf for the of the shell domain (average over the last 0.1 ). (D) The number of contacts to water molecules crossing the capsid shell. The secondary structure elements of the crystal structure are shown as gray (-strand) or checkered (-helix) regions.

Inline graphic — (A) The RMSd from the crystal structure (without over all rotation and translation of the entire capsid) for the of the shell domain (average over the last 0.1 and all 60 proteins). (B) As A but after aligning each protein individually to the crystal structure. (C) The RMSf for the of the shell domain (average over the last 0.1 ). (D) The number of contacts to water molecules crossing the capsid shell. The secondary structure elements of the crystal structure are shown as gray (-strand) or checkered (-helix) regions.