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Job DescriptionP13033
Confidence97.73%DateThu Jan 5 11:33:29 GMT 2012
Rank276Aligned Residues116
% Identity11%Templated1feca2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.70

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


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Query Sequence  DNEENWPLLLDALIPVANTCEMILMPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVL. GIRLQNQLQRQFVRQGGVWM
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Template Sequence  GDDLCITSNEAFYLDEAPKRALCVGGGYISIEFAGIFNAYKARGGQVDLAYRGDMILRGFDSELRKQLTEQLRANGINVR
Template Known Secondary structure 
GGG
B
TT
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S
SSS
TT
SSSSSSTTS
TT
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   170.........180.........190.........200.........210.........220.........230.........240.........
 
   275....280.........290.........300.........310...
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Query Sequence  PGDEVKKVTCKNGVVNEIWTRNHADIPLRPRFAVLASGS
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Template Sequence  THENPAKVTKNADGTRHVVFESGA. . EADYDVVMLAIGR
Template Known Secondary structure  T


TTS
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   250.........260.........270... ......280......
 
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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