1gac: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "1gac" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
{{STRUCTURE_1gac| PDB=1gac | SCENE= }} | {{STRUCTURE_1gac| PDB=1gac | SCENE= }} | ||
===NMR structure of asymmetric homodimer of a82846b, a glycopeptide antibiotic, complexed with its cell wall pentapeptide fragment=== | ===NMR structure of asymmetric homodimer of a82846b, a glycopeptide antibiotic, complexed with its cell wall pentapeptide fragment=== | ||
{{ABSTRACT_PUBMED_7626632}} | {{ABSTRACT_PUBMED_7626632}} | ||
| Line 22: | Line 7: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:007626632</ref><references group="xtra"/> | <ref group="xtra">PMID:007626632</ref><references group="xtra"/><references/> | ||
[[Category: Kline, A D.]] | [[Category: Kline, A D.]] | ||
[[Category: Loncharich, R J.]] | [[Category: Loncharich, R J.]] | ||
Revision as of 10:42, 16 April 2014
NMR structure of asymmetric homodimer of a82846b, a glycopeptide antibiotic, complexed with its cell wall pentapeptide fragment
Template:ABSTRACT PUBMED 7626632
About this Structure
1gac is a 4 chain structure. Full experimental information is available from OCA.
Reference
- Prowse WG, Kline AD, Skelton MA, Loncharich RJ. Conformation of A82846B, a glycopeptide antibiotic, complexed with its cell wall fragment: an asymmetric homodimer determined using NMR spectroscopy. Biochemistry. 1995 Jul 25;34(29):9632-44. PMID:7626632