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Job DescriptionP37127
Confidence98.85%DateThu Jan 5 11:54:48 GMT 2012
Rank248Aligned Residues103
% Identity20%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


   464.....470.........480.........490.........500.........510........ .520.........530.........
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Query Sequence  INTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNARE. . . . EGANFEFNVQPVALELNEQGH
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Template Sequence  LPYCPGKTLVVGASYVALECAGFLAGIGL. DVTVMVR. SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAGT
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STT
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ST
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   186...190.........200.........210.... .....220. ........230.........240.........250.........260...
 
   540.........550.........560.........570.........580.
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Query Sequence  VCGIRFLRTRLGEPDAQGRRRPVPVEGSEFVMPADAVIMAFG
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Template Sequence  PGRLKVTAKS. . . . . . . . . . . . . TNSEETIEDEFNTVLLAVG
Template Known Secondary structure  T

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   264.....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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