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Job DescriptionP35340
Confidence99.55%DateWed Jan 25 15:20:51 GMT 2012
Rank157Aligned Residues112
% Identity19%Templated1w4xa1
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.7

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


   211........220.........230.........240... ..... .250.........260.. .....
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Query Sequence  DAYDVLIVGSGPAGAAAAIYSARKGIRTGLMGE. . RFGGQ. . . . . . . . . . ILDTVDIENYISVP. . . . . . . . . . . KTEGQ
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Template Sequence  EEVDVLVVGAGFSGLYALYRLRELGRSVHVIETAGDVGGVWYWNRYPGARCDIESIEYCYSFSEEVLQEWNWTERYASQP
Template Known Secondary structure  S

STT


SSSSS
T


TT
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TTTSS

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B
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   15....20.........30.........40.........50.........60.........70.........80.........90....
 
   268.270.........280... ......290.........300.........310.........320...
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Query Sequence  KLAGALKVHVDEYDVD. . VIDSQSASKLIPAAVEGGLHQIETASGAVLKARSIIVATG
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Template Sequence  EILRYINFVADKFDLRSGITFHTTVTAAAF. DEATNTWTVDTNHGDRIRARYLIMASG
Template Known Secondary structure  TTGGGG
S

.TTTTTT




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   95....100.........110.........120.... .....130.........140.........150.
 
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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