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Job DescriptionP06715
Confidence99.12%DateThu Jan 5 10:59:22 GMT 2012
Rank250Aligned Residues115
% Identity23%Templated1ebda2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.60

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


   146...150.........160.........170.........180.........190.........200.........210.........220.....
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Query Sequence  PDIPGVEYGIDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQL
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Template Sequence  PNFKFSNRILDSTGALNLGEVPKSLVVIGGGYIGIELGTAYANFGTKVTILEGAGEILSGFEKQMAAIIKKRLKKKGVEV
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   155....160.........170.........180.........190.........200.........210.........220.........230....
 
   226...230.........240......... 250.........260
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Query Sequence  HTNAIPKAVVKNTDGSLTLELEDG. . RSETVDCLIWA
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Template Sequence  VTNALAKGAEEREDGVTVTYEANGETKTIDADYVLVT
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   235....240.........250.........260.........270.
 
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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