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Job DescriptionP35340
Confidence98.95%DateWed Jan 25 15:20:51 GMT 2012
Rank246Aligned Residues111
% Identity21%Templated1gera2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.86

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


   330.........340.........350.........360.........370.........380.........390... ......400....
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Query Sequence  NVPGEDQYRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKAD. . . . . QVLQDKLRSLK
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Template Sequence  DIPGVEY. . . . . GIDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAE
Template Known Secondary structure 

TTGGG.....SB
T
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S

STT

SSSSS
TTS
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   147..150... ......160.........170.........180.........190.........200.........210.........220.
 
   405....410.........420.........430.........440.........450
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Query Sequence  NVDIILNAQTTEVKGDGSKVVGLEYRDRVSGDIHNIELAGIFVQIG
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Template Sequence  GPQLHTNAIPKAVVKNTDGSLTLEL. . . . . EDGRSETVDCLIWAIG
Template Known Secondary structure  S

S


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   222.......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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