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Job DescriptionP77650
Confidence99.39%DateThu Jan 5 12:31:22 GMT 2012
Rank171Aligned Residues121
% Identity21%Templated1nhpa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.00

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


   117..120.........130......... 140.........150.........160.........170.........180.........190....
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Query Sequence  LLDALGERCFTLRHAGDAARLRE. . VLQPERSVVIIGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQ
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Template Sequence  IPGKDLDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGSGYIGIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDVLTE
Template Known Secondary structure 
TTTTSBS


T
TT



STT
SSSSTTTTT

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   120.........130.........140.........150.........160.........170.........180.........190.........
 
   195....200.........210.........220.........230.......
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Query Sequence  RHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGI
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Template Sequence  EMEANNITIATGETVERYEGDGRVQKVVTDKNAYDADLVVVAV
Template Known Secondary structure  TTTS


SSB

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   200.........210.........220.........230.........240..
 
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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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