User:David Canner/Sandbox good

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==Scene Transitions==
==Scene Transitions==
===Smooth Transitions===
===Smooth Transitions===
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<StructureSection load='1dq8' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])'>Anything in this section will appear adjacent to the 3D structure and will be scrollable.</StructureSection>
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<StructureSection load='1dq8' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])'>
Example from the page [[HMG-CoA Reductase]]:
Example from the page [[HMG-CoA Reductase]]:
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Compared with:
Compared with:
The HMG binding pocket is the site of catalysis in HMGR. <scene name='HMG-CoA_Reductase/1dqa_cis_loop2/3'> The“cis-loop” that bends over the top of HMG </scene> is a critical structural element of this binding site. Residues <scene name='HMG-CoA_Reductase/1dqa_e_and_d/3'>E559 and D767</scene> and are positioned in the active site as is <scene name='HMG-CoA_Reductase/1dqa_k691/3'>K691 which is only 2.7 angstroms from the HMG O2 carbonyl oxygen</scene>. Etc…
The HMG binding pocket is the site of catalysis in HMGR. <scene name='HMG-CoA_Reductase/1dqa_cis_loop2/3'> The“cis-loop” that bends over the top of HMG </scene> is a critical structural element of this binding site. Residues <scene name='HMG-CoA_Reductase/1dqa_e_and_d/3'>E559 and D767</scene> and are positioned in the active site as is <scene name='HMG-CoA_Reductase/1dqa_k691/3'>K691 which is only 2.7 angstroms from the HMG O2 carbonyl oxygen</scene>. Etc…
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</StructureSection>

Revision as of 08:33, 21 November 2010

How to make excellent scenes:

This is a list of tips and tricks to develop effective scenes for your pages.

Tip #1: When developing a series of scenes illustrating related parts of a protein, use the “transition options” to create smooth transitions void of peculiar zoom-outs, etc.

Scene Transitions

Smooth Transitions

Structure of HMG-CoA reductase (PDB entry 1dq8)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

David Canner

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