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Job DescriptionP35340
Confidence99.16%DateWed Jan 25 15:20:51 GMT 2012
Rank205Aligned Residues115
% Identity17%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


   332.......340.........350.........360.........370.........380.........390... ......400.......
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Query Sequence  PGEDQYRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKAD. . . . QVLQDKLRSLKNVD
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Template Sequence  PGDKEYCI. . . . SSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIK
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   171....... .180.........190.........200.........210.........220.........230.........240......
 
   408.410.........420... ......430.........440.........450
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Query Sequence  IILNAQTTEVKGDGSK. . . VVGLEYRDRVSGDIHNIELAGIFVQIG
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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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