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Job DescriptionP00350
Confidence97.05%DateThu Jan 5 10:56:33 GMT 2012
Rank327Aligned Residues102
% Identity13%Templated2d59a1
SCOP infoNAD(P)-binding Rossmann-fold domains NAD(P)-binding Rossmann-fold domains CoA-binding domain
Resolution1.65

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


   5....10. ........20.........30.........40.........50.........60.........70.........80
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Query Sequence  QIGVVGM. . . . AVMGRNLALNIESRGYTVSIFNRSREKTEEVIAENPGKKLVPYYTVKEFVESLETPRRILLMVKAGAGT
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Template Sequence  KIALVGASPKPERDANIVMKYLLEHGYDVYPVNPK. . . . . . . . . . . . YEEVLGRKCYPSVLDIPDKIEVVDLFVK. PKLT
Template Known Secondary structure  T

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TTSTT

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STT
BSSGGG
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   24.....30.........40.........50........ .60.........70.........80...... ...90
 
   81........90.........100.........110.........120....
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Query Sequence  DAAIDSLKPYLDKGDIIIDGGNTFFQDTIRRNRELSAEGFNFIG
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Template Sequence  MEYVEQAIKK. GAKVVWFQYNTYN. . . . REASKKADEAGLIIVA
Template Known Secondary structure  .T
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   91........100 .........110... ......120.........
 
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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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