Sandbox kinemage: Difference between revisions
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1. Interact with the kinemage on the right, which shows the mainchain from a crystal structure of oxy-myoglobin refined at 1Å resolution, with color-coded balls for the non-C atoms (O red, N blue). In the overview, drag to rotate the molecule slowly back & forth, to see in 3D the arrangement of helices that enclose the heme group (in pink). Turn on sidechains and sc atoms. The central Fe atom (orange) of the heme has an O2 ligand bound on one side; what is the amino-acid type and the residue number of the sidechain ligand on the other side? [You can click on an atom in the sidechain and read its pointID at bottom left of the graphics window, or figure it out by the shape and atom types of the sidechain.] | 1. Interact with the kinemage on the right, which shows the mainchain from a crystal structure of oxy-myoglobin refined at 1Å resolution, with color-coded balls for the non-C atoms (O red, N blue). In the overview, drag to rotate the molecule slowly back & forth, to see in 3D the arrangement of helices that enclose the heme group (in pink). Turn on sidechains and sc atoms. The central Fe atom (orange) of the heme has an O2 ligand bound on one side; what is the amino-acid type and the residue number of the sidechain ligand on the other side? [You can click on an atom in the sidechain and read its pointID at bottom left of the graphics window, or figure it out by the shape and atom types of the sidechain.] | ||
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==Notes== | |||
This material is a fragment from '''BCH222 :: Structure of Biological Macromolecules 1st Graphics Assignment''', by David and Jane Richardson, copied here for testing purposes only. | |||
