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Job DescriptionP00393
Confidence99.64%DateThu Jan 5 10:56:36 GMT 2012
Rank106Aligned Residues121
% Identity27%Templated1xhca2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.35

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


   125....130.........140.........150.........160.........170.........180.........190.........200....
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Query Sequence  TSNDFNTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANLGANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYKGL
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Template Sequence  RAREPQIKGK. EYLLTLRTIFDADRIKESIENS. . . . . . . . . . . . . GEAIIIGGGFIGLELAGNLAE. . . . . . . . . . . . .
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SBTG.GG


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   104.....110... ......120.........130..... ....140.........150......
 
   205....210.........220.........230.........240.........250.........260.........270......
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Query Sequence  TNEALNVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEGGLHTKDGEYIEADLMVWAAGI
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Template Sequence  . . AGYHVKLIHRGAMFLG. LDEELSNMIKDMLEETGVKFFLNSELLEANEEGV. LTNSGFIEGKVKICAIGI
Template Known Secondary structure  ..TT

SSS

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   157..160.........170.. .......180.........190.........200...... ...210.........220....
 
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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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