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Job DescriptionP13033
Confidence96.92%DateThu Jan 5 11:33:29 GMT 2012
Rank295Aligned Residues113
% Identity10%Templated1gera2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.86

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


   194.....200.........210.........220.........230.........240.........250.... .....260.........270.
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Query Sequence  FLDNEENWPLLLDALIPVANTCEMILMPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVL. . GIRLQNQLQRQFVRQGG
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Template Sequence  IPGVEYGIDSDGFFALPALPERVAVVGAGYIAVELAGVINGL. . . . GAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGP
Template Known Secondary structure 
TTGGGSB
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   148.150.........160.........170.........180......... 190.........200.........210.........220...
 
   272.......280.........290.........300.........310..
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Query Sequence  VWMPGDEVKKVTCKNGVVNEIWTRNHADIPLRPRFAVLASG
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Template Sequence  QLHTNAIPKAVVKNTDGSLTLELEDG. . RSETVDCLIWAIG
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   224.....230.........240......... 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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Lawrence Kelley, Benjamin Jefferys 
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