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Job DescriptionO05204
Confidence99.23%DateTue Jul 17 17:05:01 BST 2012
Rank194Aligned Residues114
% Identity18%Templated1h6va2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution3.0

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


   322.......330.........340.........350.........360.........370.........380... ......390.......
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Query Sequence  PGEEQLINKGVAFCPHCDGPLFENKDVAVIGGGNSGVEAAIDLAGIVNHVTLFEFASELKAD. . . . NVLQDRLRSLSNVD
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Template Sequence  PGDKEYC. . . . ISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIK
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   171...... ..180.........190.........200.........210.........220.........230.........240......
 
   398.400........ .410.........420.........430.........
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Query Sequence  IKTNAKTTEVV. . . . GEDHVTGIRYEDMNTGEEHLLNLDGIFVQIG
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Template Sequence  FIRQFVPTKIEQIEAGTPGRLKVTAKSTNSEETIEDEFNTVLLAVG
Template Known Secondary structure  S

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   247..250.........260.........270.........280.........290..
 
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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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