Return to main results Retrieve Phyre Job Id

Job DescriptionP13033
Confidence97.31%DateThu Jan 5 11:33:29 GMT 2012
Rank288Aligned Residues98
% Identity10%Templated1gesa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.74

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


   209210.........220.........230.........240.........250.... .....260.........270.........280......
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Query Sequence  IPVANTCEMILMPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVL. . GIRLQNQLQRQFVRQGGVWMPGDEVKKVTCKN
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Template Sequence  LPALPERVAVVGAGYIGVELGGVING. . . . LGAKTHLFEMFDAPLPSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNT
Template Known Secondary structure 
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S....TT

SSSSSSTTS
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   163......170.........180........ .190.........200.........210.........220.........230........
 
   287..290.........300.........310..
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Query Sequence  GVVNEIWTRNHADIPLRPRFAVLASG
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Template Sequence  DGSLTLELEDGR. . SETVDCLIWAIG
Template Known Secondary structure  TS
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   239240.........250 .........260..
 
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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