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Job DescriptionP13035
Confidence97.45%DateThu Jan 5 11:33:30 GMT 2012
Rank285Aligned Residues109
% Identity26%Templated1nhpa1
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.00

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


   6...10.........20...... ...30.........40.........50.........60.........70.........80...
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Query Sequence  LIVIGGGINGAGIAADAAGRG. . LSVLMLEAQDLACATSSASSKLIHGGLRYLEHYEFRLVSEALAEREVLLKMAPHIAF
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Template Sequence  VIVLGSSHGGYEAVEELLNLHPDAEIQWYEKGDFISFLSAGMQLYLEGKVKDVNSVRYMTGEKMESR. . . . . . . . . . . . .
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   3......10.........20.........30.........40.........50.........60.........
 
   84.....90.........100.........110.........120.........130.........140.........150.........160...
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Query Sequence  PMRFRLPHRPHLRPAWMIRIGLFMYDHLGKRTSLPGSTGLRFGANSVLKPEIKRGFEYSDCWVDDARLVLANAQMVVRKG
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   70
 
   164.....170.........180.........190.........200........
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Query Sequence  GEVLTRTRATSARRENGLWIVEAEDIDTGKKYSWQARGLVNATGP
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Template Sequence  VNVFSNTEITAIQPKEHQVTVKD. . LVSGEERVENYDKLIISPGA
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   71........80.........90... ......100.........110...
 
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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