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Job DescriptionP04036
Confidence97.68%DateThu Jan 5 10:58:10 GMT 2012
Rank258Aligned Residues129
% Identity9%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


   7..10.........20.........30.........40.........50.........60.........70.........80. ...
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Query Sequence  RVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGELAGAGKTGVTVQSSLDAVKDDFDVFIDFTR. . PEG
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Template Sequence  QFAVIGL. GRFGGSIVKELHRMGH. . EVLAVDINEEKVNAYASYATHAVIANATEENELLSLGIRNFEYVIVAIGANIQA
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.STT
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TTTT
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TT
TTTGGG
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   8.10.... .....20.........30 .........40.........50.........60.........70.........80....
 
   85....90.........100.........110.........120.........130.........140.
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Query Sequence  TLNHLAFCRQHGKGMVIGTTGFDEAGKQAIRDAAADIAIVFAANFSVGVNVMLKLLE
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Template Sequence  STLTTLLLKELDIPNIWVKA. QNYYHHKVLEKI. . GADRIIHPEKDMGVKIAQSLSD
Template Known Secondary structure  TT
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   85....90.........100.... .....110...... ...120.........130........
 
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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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