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Job DescriptionP31450
Confidence90.41%DateThu Jan 5 11:47:41 GMT 2012
Rank483Aligned Residues76
% Identity11%Templated1d7ya2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.10

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


   2.......10.........20.........30.........40...... ...50.........60. ...
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Query Sequence  TKFSVVVAGGGSTFTPGIVLMLLANQDRFPLRALKFYDNDGARQE. . . . . VIAEACKVILKEKAP. . . . . . . . . . . . DIA
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Template Sequence  PQSRLLIVGGGVIGLELAATART. . . . . . AGVHVSLVETQPRLMSRAAPATLADFVARYHAAQGVDLRFERSVTGSVDGV
Template Known Secondary structure  TT


S......TT
SSSSTTTTTS
TTT
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TT
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   144.....150.........160...... ...170.........180.........190.........200.........210.......
 
   65....70.........80......
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Query Sequence  FSYTTDPEVAFSDVDFVMAHIR
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Template Sequence  VLLDDGTRI. . . AADMVVVGIG
Template Known Secondary structure  TTS
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   218.220...... ...230......
 
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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