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Job DescriptionP77650
Confidence98.98%DateThu Jan 5 12:31:22 GMT 2012
Rank247Aligned Residues115
% Identity20%Templated1lpfa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.80

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


   123......130.........140.........150.........160.........170.........180.........190.........200..
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Query Sequence  ERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVR
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Template Sequence  PAPLSDDIIVDSTGALEFQAVPKKLGVIGAGVIGLELGSVWARLGAEVTVLEALDKFL. PAADEQIAKEALKVLTKQGLN
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TTT
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   159160.........170.........180.........190.........200.........210...... ...220.........230.......
 
   203......210...... ...220.........230........
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Query Sequence  ILLNNAIEHVVDGE. . . . KVELTLQSGETLQADVVIYGIG
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Template Sequence  IRLGARVTASEVKKKQVTVTFTDANGEQKETFDKLIVAVG
Template Known Secondary structure  TT


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   238.240.........250.........260.........270.......
 
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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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