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Job DescriptionP06715
Confidence98.91%DateThu Jan 5 10:59:22 GMT 2012
Rank272Aligned Residues109
% Identity20%Templated1v59a2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.20

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


   152.......160.........170.........180.........190.........200.........210.........220.........230.
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Query Sequence  EYGIDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIP
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Template Sequence  EKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTKV
Template Known Secondary structure  SS
TT
SS

S

STT

SSSSSSSSS
TT

S
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   168.170.........180.........190.........200.........210.........220.........230.........240.......
 
   232.......240..... ....250.........260
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Query Sequence  KAVVKNTDGSLTLE. . . . . . LEDGRSETVDCLIWA
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Template Sequence  ISAKRNDDKNVVEIVVEDTKTNKQENLEAEVLLVA
Template Known Secondary structure  TTTTTTTTS
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   248.250.........260.........270.........280..
 
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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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