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Job DescriptionP37596
Confidence98.91%DateThu Jan 5 11:55:42 GMT 2012
Rank217Aligned Residues115
% Identity20%Templated1onfa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.60

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


   116...120.........130.........140.........150.........160.........170.........180.........190.....
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Query Sequence  VPGRELMLTLNSQQEYRACETQLRDARRVLIVGGGLIGSELAMDFCRAGKAVTLIDNAASILASLMPPEVSSRLQHRLTE
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Template Sequence  FPPVKGIENTISSDEFFNIKE. . . . SKKIGIVGSGYIAVELINVIKRLGIDSYIFARGNRIL. RKFDESVINVLENDMKK
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TTGGG
TT


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   154.....160.........170.... .....180.........190.........200.........210. ........220........
 
   196...200.........210... ......220...... ...230.....
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Query Sequence  MGVHLLLKSQLQGLEKTD. SGIQATLDRQRNI. EVDAVIAAT
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Template Sequence  NNINIVTFADVVEIKKVSDKNLSIHLSDGRIYEHFDHVIYCV
Template Known Secondary structure  TT

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SSTT
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   229230.........240.........250.........260.........270
 
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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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