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Job DescriptionP33221
Confidence97.39%DateWed Jan 25 15:20:50 GMT 2012
Rank123Aligned Residues110
% Identity19%Templated2hmva1
SCOP infoNAD(P)-binding Rossmann-fold domains NAD(P)-binding Rossmann-fold domains Potassium channel NAD-binding domain
Resolution2.20

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


   13......20.........30.........40...... ...50.........60.........70.........80.........90
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Query Sequence  TRVMLLGSGELGKEVAIECQRLGVEVIAVDRYAD. . APAMHVAHRSHVINMLDGDALRRVVELEKPHYIVPEIEAIATDM
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Template Sequence  KQFAVIGLGRFGGSIVKELHRMGHEVLAVDINEEKVNAYASYATHAVIANATEENELLSLGIRNFEYVIVAIGANIQAST
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STT


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TTTT
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TT
TTTGGG
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   7..10.........20.........30.........40.........50.........60.........70.........80......
 
   91........100.........110.........120.......
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Query Sequence  LIQLEEEGLNVVPCARATKLTMNREGIRRLAAEELQL
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Template Sequence  LTTLLLKE. . . LDIPNIWVKAQNYYHHKV. . LEKIGA
Template Known Secondary structure  ...TT
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   87..90.... .....100.........110.. ......
 
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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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