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Job DescriptionP00393
Confidence99.25%DateThu Jan 5 10:56:36 GMT 2012
Rank157Aligned Residues91
% Identity34%Templated1lvla2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.45

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


   170.........180.........190.........200.........210.........220.........230.........240.........
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Query Sequence  KVNIAIVGGGATGVELSAELHNAVKQLHSYGYKGLTNEALNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMV
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Template Sequence  PQHLVVVGGGYIGLELGIAYRKL. . . . . . . . . . . . . . . GAQVSVVEARERILPTYDSELTAPVAESLKKLGIALHLGHSV
Template Known Secondary structure 
S

S...............T

SSSSSSTTS
T
TT
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   171........180.........190... ......200.........210.........220.........230.....
 
   250........ .260.........270.....
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Query Sequence  TSADEGGLH. . . . TKDGEYIEADLMVWAAG
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Template Sequence  EGYENGCLLANDGKGGQLRLEADRVLVAVG
Template Known Secondary structure  TT
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   236...240.........250.........260.....
 
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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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