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Job DescriptionP13033
Confidence97.19%DateThu Jan 5 11:33:29 GMT 2012
Rank290Aligned Residues98
% Identity11%Templated1q1ra2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.91

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


   211........220.........230.........240.........250.... .....260.........270.........280.......
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Query Sequence  VANTCEMILMPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVL. . . GIRLQNQLQRQFVRQGGVWMPGDEVKKVTCKNG
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Template Sequence  IADNRLVVIGGGYIGLEVAATAIKA. . . . NMHVTLLDTAARVLERVTAPPVSAFYEHLHREAGVDIRTGTQVCGFEMSTD
Template Known Secondary structure 
TT


ST....T

SSSSTTTTTS
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TT
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   147..150.........160.........170. ........180.........190.........200.........210.........220..
 
   288.290.........300.........310..
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Query Sequence  VVNEIWTRNHADIPLRPRFAVLASG
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Template Sequence  QQKVTAVLCEDGTRLPADLVIAGIG
Template Known Secondary structure  T

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   223......230.........240.......
 
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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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