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Job DescriptionP77503
Confidence97.00%DateThu Jan 5 12:30:02 GMT 2012
Rank291Aligned Residues105
% Identity12%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


   11........20.........30.........40.........50...... ...60.........70.........80......
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Query Sequence  RVAIIGAGQVADKVHASYYCTRNDLELVAVCDSRLSQAQALAEKYG. . . . NASVWDDPQAMLLAVKPDVVSVCSPNRFHY
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Template Sequence  QFAVIGLGRFGGSI. VKELHRM. GHEVL. AVDINEEKVNAYASYATHAVIANATEENELLSLGIRNFEYVIVAIGANIQA
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S.T.T


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TTTT
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TTTGGG
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   8.10.........20. ....... .30... ......40.........50.........60.........70.........80....
 
   87..90.........100.........110........
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Query Sequence  EHTLMALEAGCHVMCEKPPAMTPEQAREMCDT
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Template Sequence  STLTTLLLKELDIPNIWVKAQNYYHHKVLEKI
Template Known Secondary structure  TT
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   85....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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