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Job DescriptionP35340
Confidence98.75%DateWed Jan 25 15:20:51 GMT 2012
Rank276Aligned Residues107
% Identity20%Templated1gv4a2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.0

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


   337..340.........350.........360.........370....... ..380.........390... ......400......
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Query Sequence  YRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGI. . . . VEHVTLLEFAPEMKAD. . . . . . QVLQDKLRSLKNV
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Template Sequence  TLFRKIGDFRALEKISREVKSITVIGGGFLGSELACALGRKSQASGIEVIQLFPEKGNMGKILPQYLSNWTMEKVKREGV
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STT
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   281........290.........300.........310.........320.........330.........340.........350.........360
 
   407..410.........420.........430.........440.........
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Query Sequence  DIILNAQTTEVKGDGSKVVGLEYRDRVSGDIHNIELAGIFVQI
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Template Sequence  KVMPNAIVQSVGVSGGRLL. . . . . . IKLKDGRKVETDHIVTAV
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   361........370......... 380.........390.......
 
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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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