1kum: Difference between revisions

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[[Image:1kum.png|left|200px]]
[[Image:1kum.png|left|200px]]


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===GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE===
===GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE===


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{{ABSTRACT_PUBMED_8683599}}
{{ABSTRACT_PUBMED_8683599}}


==About this Structure==
==About this Structure==
1KUM is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUM OCA].  
[[1kum]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUM OCA].  


==Reference==
==Reference==
<ref group="xtra">PMID:8683599</ref><references group="xtra"/>
<ref group="xtra">PMID:008683599</ref><ref group="xtra">PMID:011734033</ref><references group="xtra"/>
[[Category: Aspergillus niger]]
[[Category: Aspergillus niger]]
[[Category: Glucan 1,4-alpha-glucosidase]]
[[Category: Glucan 1,4-alpha-glucosidase]]
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Starch binding domain]]
[[Category: Starch binding domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 07:39:34 2009''

Revision as of 23:06, 5 December 2012

File:1kum.png

Template:STRUCTURE 1kum

GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN, NMR, MINIMIZED AVERAGE STRUCTUREGLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

Template:ABSTRACT PUBMED 8683599

About this StructureAbout this Structure

1kum is a 1 chain structure with sequence from Aspergillus niger. Full experimental information is available from OCA.

ReferenceReference

[xtra 1][xtra 2]

  1. Sorimachi K, Jacks AJ, Le Gal-Coeffet MF, Williamson G, Archer DB, Williamson MP. Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy. J Mol Biol. 1996 Jun 28;259(5):970-87. PMID:8683599 doi:http://dx.doi.org/10.1006/jmbi.1996.0374
  2. Sharman GJ, Griffiths-Jones SR, Jourdan M, Searle MS. Effects of amino acid phi,psi propensities and secondary structure interactions in modulating H alpha chemical shifts in peptide and protein beta-sheet. J Am Chem Soc. 2001 Dec 12;123(49):12318-24. PMID:11734033

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