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Job DescriptionP06715
Confidence98.74%DateThu Jan 5 10:59:22 GMT 2012
Rank287Aligned Residues113
% Identity32%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


   149150. ........160.........170.........180.........190.........200.........210.........220.......
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Query Sequence  PGV. EYGIDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHT
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Template Sequence  PGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR. SILLRGFDQDMANKIGEHMEEHGIKFIR
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   171........180.........190.........200.........210.........220. ........230.........240.........
 
   228.230.........240...... ...250.........260..
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Query Sequence  NAIPKAVVKNTDGSLTLEL. . . . . . . . EDGRSETVDCLIWAIG
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Template Sequence  QFVPTKIEQIEAGTPGRLKVTAKSTNSEETIEDEFNTVLLAVG
Template Known Secondary structure  S

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