3d4w
From Proteopedia
(Difference between revisions)
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- | + | [[Image:3d4w.png|left|200px]] | |
- | The | + | <!-- |
+ | The line below this paragraph, containing "STRUCTURE_3d4w", creates the "Structure Box" on the page. | ||
+ | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
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+ | {{STRUCTURE_3d4w| PDB=3d4w | SCENE= }} | ||
- | + | ===Crystal structure of Staphylococcal nuclease variant Delta+PHS A109R at cryogenic temperature=== | |
- | Description: Crystal structure of Staphylococcal nuclease variant Delta+PHS A109R at cryogenic temperature | ||
- | + | <!-- | |
+ | The line below this paragraph, {{ABSTRACT_PUBMED_22080604}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 22080604 is the PubMed ID number. | ||
+ | --> | ||
+ | {{ABSTRACT_PUBMED_22080604}} | ||
+ | |||
+ | ==About this Structure== | ||
+ | [[3d4w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D4W OCA]. | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:022080604</ref><references group="xtra"/> | ||
+ | [[Category: Micrococcal nuclease]] | ||
+ | [[Category: Staphylococcus aureus]] | ||
+ | [[Category: Garcia-Moreno, E B.]] | ||
+ | [[Category: Harms, M J.]] | ||
+ | [[Category: Schlessman, J L.]] | ||
+ | [[Category: Endonuclease]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Hyperstable variant]] | ||
+ | [[Category: Internal arg]] | ||
+ | [[Category: Metal-binding]] | ||
+ | [[Category: Secreted]] | ||
+ | [[Category: Staphylococcal nuclease]] | ||
+ | [[Category: Zymogen]] |
Revision as of 05:23, 30 November 2011
Crystal structure of Staphylococcal nuclease variant Delta+PHS A109R at cryogenic temperature
Template:ABSTRACT PUBMED 22080604
About this Structure
3d4w is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
- Harms MJ, Schlessman JL, Sue GR, Garcia-Moreno E B. Arginine residues at internal positions in a protein are always charged. Proc Natl Acad Sci U S A. 2011 Nov 22;108(47):18954-9. Epub 2011 Nov 11. PMID:22080604 doi:10.1073/pnas.1104808108