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Job DescriptionP0A9B2
Confidence91.73%DateThu Jan 5 11:09:48 GMT 2012
Rank490Aligned Residues130
% Identity15%Templated1xhca1
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.35

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


   4.....10.........20.........30..... ....40.........50.........60.........70.......
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Query Sequence  KVGINGFGRIGRIVFRAAQKRSDIEIVAINDL. . . . . . LDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAE
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Template Sequence  KVVIVGNGPGGFELAKQLSQTYEVTVIDKEPVPYYSKPMLSHYIAGFIPRNRLFPYSLDWYRKRGIEIRLAEEAKLIDRG
Template Known Secondary structure 

STTTS
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   2.......10.........20.........30.........40.........50.........60.........70.........80.
 
   78.80.........90.........100.........110.........120.........130...
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Query Sequence  RDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKG
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Template Conservation               
 

 
 
                   
     
    


 
Template Sequence  RKVVITEKGEVPYDTLVLATGAPNVDLARRSGIHTGRGILIDDNFRTSAKDVYAIG
Template Known Secondary structure  TTSS

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   82.......90.........100.........110.........120.........130.......
 
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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