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Job DescriptionP11446
Confidence96.80%DateThu Jan 5 11:32:37 GMT 2012
Rank345Aligned Residues79
% Identity16%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


   3......10 .........20.........30.........40.........50.........60.........70.........
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Query Sequence  NTLIVGAS. . . GYAGAELVTYVNRHPHMNITALTVSAQSNDAGKLISDLHPQLKGIVDLPLQPMSDISEFSPGVDVVFLA
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Template Sequence  KIALVGASPKPERDANIVMKYLLEH. GYDVYPVNPKYEE. . . . . . . . . . . . . . . . . . VLGRKCYPSVLDIPDKIEVVDLF
Template Known Secondary structure  T

S
TTST.T

TT
S..................TT
BSSGGG
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S
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   24.....30.........40........ .50.........60. ........70.........80....
 
   80.........90.........100
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Query Sequence  TAHEVSHDLAPQFLEAGCVVF
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Template Sequence  VKPKLTMEYVEQAIKKGAKVV
Template Known Secondary structure  S
T
S
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   85....90.........100.....
 
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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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