1vb9

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==About this Structure==
==About this Structure==
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1VB9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VB9 OCA].
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1VB9 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VB9 OCA].
==Reference==
==Reference==
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The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product., Mizuno M, Tonozuka T, Uechi A, Ohtaki A, Ichikawa K, Kamitori S, Nishikawa A, Sakano Y, Eur J Biochem. 2004 Jun;271(12):2530-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15182368 15182368]
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<ref group="xtra">PMID:15182368</ref><references group="xtra"/>
[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
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[[Category: Single protein]]
 
[[Category: Thermoactinomyces vulgaris]]
[[Category: Thermoactinomyces vulgaris]]
[[Category: Ichikawa, K.]]
[[Category: Ichikawa, K.]]
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[[Category: Gh family 13]]
[[Category: Gh family 13]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:06:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 08:41:00 2009''

Revision as of 06:41, 17 February 2009

Template:STRUCTURE 1vb9

Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product

Template:ABSTRACT PUBMED 15182368

About this Structure

1VB9 is a 2 chains structure of sequences from Thermoactinomyces vulgaris. Full crystallographic information is available from OCA.

Reference

  • Mizuno M, Tonozuka T, Uechi A, Ohtaki A, Ichikawa K, Kamitori S, Nishikawa A, Sakano Y. The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product. Eur J Biochem. 2004 Jun;271(12):2530-8. PMID:15182368 doi:10.1111/j.1432-1033.2004.04183.x

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