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Job DescriptionP77650
Confidence99.41%DateThu Jan 5 12:31:22 GMT 2012
Rank168Aligned Residues120
% Identity35%Templated1d7ya2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.10

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


   115....120.........130.........140.........150.........160.........170.........180.........190....
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Query Sequence  LPLLDALGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQ
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Template Sequence  PTLQGATMP. VHTLRTLEDARRIQAGLRPQSRLLIVGGGVIGLELAATARTAGVHVSLVETQPRLMSRAAPATLADFVAR
Template Known Secondary structure  GGGTT
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   117..120..... ....130.........140.........150.........160.........170.........180.........190.....
 
   195....200.........210.........220.........230........
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Query Sequence  RHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIG
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Template Sequence  YHAAQGVDLRFERSVTGSVDGVV. . . LLDDGTRIAADMVVVGIG
Template Known Secondary structure  TTT
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   196...200.........210........ .220.........230......
 
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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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