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Job DescriptionP27306
Confidence98.30%DateThu Jan 5 11:43:55 GMT 2012
Rank303Aligned Residues114
% Identity18%Templated1mo9a2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.65

  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  DFTHPRIYDSDSIL. SMHHEP. RHVLIYGAGVIGCEYASIFRGMDVKVDLINTRDRLLAFLDQEMSDSLSYHFWNSGVVI
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Template Sequence  GVNAKGVFDHATLVEELDYEPGSTVVVVGGSKTAVEYGCFFNATGRRTVMLVRTEPLKLIKDNETRAYVLDRMKEQGMEI
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   193......200.........210.........220.........230.........240.........250.........260.........270..
 
   235....240......... 250.........260.........270
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Query Sequence  RHNEEYEKIEGCDDG. . . . . VIMHLKSGKKLKADCLLYANG
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Template Sequence  ISGSNVTRIEEDANGRVQAVVAMTPNGEMRIETDFVFLGLG
Template Known Secondary structure  SS

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   273......280.........290.........300.........310...
 
Download:Text version

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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