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Job DescriptionP00393
Confidence99.38%DateThu Jan 5 10:56:36 GMT 2012
Rank140Aligned Residues111
% Identity31%Templated1gesa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.74

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


   130.........140.........150.........160.........170.........180.........190.........200.........
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Query Sequence  NTPGVKENCIFLDNPHQARRFHQEMLNLFLKYSANLGANGKVNIAIVGGGATGVELSAELHNAVKQLHSYGYKGLTNEAL
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Template Sequence  DIPGVEY. . . . GIDSDGFFALPAL. . . . . . . . . . . . . . . . PERVAVVGAGYIGVELGGVINGL. . . . . . . . . . . . . . . GA
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TTGGG....SB

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ST...............T
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   147..150... ......160...... ...170.........180......... 190.
 
   210.........220.........230.........240.........250..... ....260.........270.....
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Query Sequence  NVTLVEAGERILPALPPRISAAAHNELTKLGVRVLTQTMVTSADEG. . . . . GLHTKDGEYIEADLMVWAAG
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Template Sequence  KTHLFEMFDAPLPSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNTDGSLTLELEDGRSETVDCLIWAIG
Template Known Secondary structure 
SSSSSSTTS
S

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TTS
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   192.......200.........210.........220.........230.........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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Lawrence Kelley, Benjamin Jefferys 
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