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Job DescriptionP13033
Confidence97.61%DateThu Jan 5 11:33:29 GMT 2012
Rank280Aligned Residues112
% Identity12%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


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Query Sequence  LDNEENWPLLLDALIPVANTCEMILMPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVL. . GIRLQNQLQRQFVRQGGV
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Template Sequence  IDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSR. . . . LGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLD
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   165....170.........180.........190.........200.... .....210.........220.........230.........240
 
   273......280.........290..... ....300.........310
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Query Sequence  WMPGDEVKKVTCKNGVVNEIWTR. . . . NHADIPLRPRFAVLA
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Template Sequence  FKLSTKVISAKRNDDKNVVEIVVEDTKTNKQENLEAEVLLVA
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   241........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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