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Job DescriptionO05204
Confidence99.74%DateTue Jul 17 17:05:01 BST 2012
Rank126Aligned Residues121
% Identity31%Templated1vdca2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.50

  Insertion relative to template
  Deletion relative to template
  Catalytic residue from the CSA
 
Detailed help on interpreting your alignment


   318.320...... ...330.........340. ........350.........360.........370.........380.........390.
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Query Sequence  KLNIPGEEQ. . . . LINKGVAFCPHCDGP. . LFENKDVAVIGGGNSGVEAAIDLAGIVNHVTLFEFASELKADNVLQDRLR
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Template Sequence  RLSFVGSGEVLGGFWNRGISACAVCDGAAPIFRNKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAFRASKIMQQRAL
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BT
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BTTTS
TTSGGGTTS

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   118.120.........130.........140.........150.........160.........170.........180.........190.......
 
   392.......400.........410.. .......420.........430........
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Query Sequence  SLSNVDIKTNAKTTEVVGEDH. . . VTGIRYEDMNTGEEHLLNLDGIFVQI
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Template Sequence  SNPKIDVIWNSSVVEAYGDGERDVLGGLKVKNVVTGDVSDLKVSGLFFAI
Template Known Secondary structure  T
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SSSSSSSTTT


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   192.......200.........210.........220.........230.........240.
 
Download:Text version

No model constructed - rank, confidence too low




Phyre is for academic use only

Please cite: Protein structure prediction on the web: a case study using the Phyre server
Kelley LA and Sternberg MJE. Nature Protocols 4, 363 - 371 (2009) [pdf] [Import into BibTeX]
 
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Lawrence Kelley, Benjamin Jefferys 
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