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Recent Citations
Rational HIV immunogen design to target specific germline B cell receptors. Jardine J, Julien JP et al. Science. 2013 May 10;340(6133):711-6.
Self-assembling cages from coiled-coil peptide modules. Fletcher JM, Harniman RL et al. Science. 2013 May 3;340(6132):595-9.
A conformational switch in HP1 releases auto-inhibition to drive heterochromatin assembly. Canzio D, Liao M et al. Nature. 2013 Apr 18;496(7445):377-81.
The bacterial DnaC helicase loader is a DnaB ring breaker. Arias-Palomo E, O'Shea VL et al. Cell. 2013 Apr 11;153(2):438-48.
The architecture of Tetrahymena telomerase holoenzyme. Jiang J, Miracco EJ et al. Nature. 2013 Apr 11;496(7444):187-92.
(Previously featured citations...)Chimera Search
Google™ SearchNews
April 18, 2013
A production release candidate (version 1.8) is now available; please try it and report any problems. See the release notes for changes relative to the previous release.
January 30, 2013
Chimera production release 1.7 is now available. See the release notes for new features since the 1.6 release series. Mac PowerPC and OS X 10.5 are no longer supported.
January 17, 2013
A production release candidate (version 1.7) is now available; please try it and report any problems. See the release notes for changes relative to the previous release. Mac PowerPC and OS X 10.5 are no longer supported.
(Previous news...)Upcoming Events
UCSF Chimera is a highly extensible program for interactive visualization and analysis of molecular structures and related data, including density maps, supramolecular assemblies, sequence alignments, docking results, trajectories, and conformational ensembles. High-quality images and animations can be generated. Chimera includes complete documentation and several tutorials, and can be downloaded free of charge for academic, government, non-profit, and personal use. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics, funded by the National Institutes of Health (NIGMS P41-GM103311).
Feature Highlight
Given two or more superimposed structures,
Match→Align creates a corresponding sequence alignment.
The user specifies a distance cutoff for residues allowed to be
in the same column of the output alignment.
In proteins, the distances are measured between α-carbons.
The method is independent of residue types and how the
structures were superimposed.
The figure shows a superposition from
MatchMaker
of five proteins from the
SCOP WD40 superfamily
and a corresponding sequence alignment from
Match→Align, automatically shown in
Multalign Viewer. In the sequence alignment,
light green and yellow boxes indicate strands and helices, while the
headers
RMSD and Conservation show spatial and sequence
conservation, respectively.
Gallery Sample
Large ribosomal RNA is shown with individual bases depicted using solvent excluded molecular surfaces. Bases A, C, G, U are colored red, yellow, green, and blue. The surfaces were made with the Chimera multiscale tool in combination with the nucleic acid blobs plug-in. The image was raytraced using POVray.
Protein Data Bank model 1s72.
(More samples...)