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Job DescriptionP15640
Confidence93.49%DateWed Jan 25 15:20:39 GMT 2012
Rank206Aligned Residues108
% Identity15%Templated1oi7a1
SCOP infoNAD(P)-binding Rossmann-fold domains NAD(P)-binding Rossmann-fold domains CoA-binding domain
Resolution1.23

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


   2.......10.........20.........30.........40.........50.........60.........70.........80.
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Query Sequence  KVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPALQNVAIGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGVV
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Template Sequence  RVLVQGITGREGQFHTKQMLTYGTKIVAGVTPGKGGMEVLGVPVY. . . . . . . DTVKEAVAHHEVDASIIFVPAPAAADAA
Template Known Secondary structure  TTTST

TT
TT
TT.......SSS

S


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   910.........20.........30.........40.........50... ......60.........70.........80.
 
   82.......90.........100.........110.......
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Query Sequence  DTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHKI
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Template Sequence  LEAAHAGIPLIVLITEGIPTL. DMVRAVEEIKALGS
Template Known Secondary structure  TT
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.T
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   82.......90.........100.. .......110......
 
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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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