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Job DescriptionP09158
Confidence88.48%DateThu Jan 5 11:02:05 GMT 2012
Rank478Aligned Residues87
% Identity11%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


   71........80.........90.........100........ .110.........120.........130.........140..
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Query Sequence  PLLAHGHAKHVLIIGGGDGAMLREVTRHKNVESITMVE. . . . . . . . IDAGVVSFCRQYLPNHNAGSYDDPRFKLVIDDGV
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Template Sequence  FFALPALPERVAVVGAGYIGVELGGVINGLGAKTHLFEMFDAPLPSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNTD
Template Known Secondary structure 
SS

S

STT

SSSSSSTTS
S

S


TT
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   160.........170.........180.........190.........200.........210.........220.........230.........
 
   143......150 .......
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Query Sequence  NFVNQTSQ. . . . . TFDVIIS
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Template Sequence  GSLTLELEDGRSETVDCLIW
Template Known Secondary structure  S
TTS
S
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   240.........250.........
 
Download:Text version

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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