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Job DescriptionO05204
Confidence99.11%DateTue Jul 17 17:05:01 BST 2012
Rank220Aligned Residues109
% Identity22%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


   321........330.........340.. .......350.........360.........370.........380.... ..
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Query Sequence  IPGEEQLINKGVAFCPHCDGPL. . . . . . . . FENKDVAVIGGGNSGVEAAIDLAGIVNHVTLFEFASELKADN. . . . . . VL
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Template Sequence  IPGKD. . . LDNIYLMRGRQWAIKLKQKTVDPEVNNVVVIGSGYIGIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDV
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TTTT...SBS


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STT
SSSSTTTTT

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   120.... .....130.........140.........150.........160.........170.........180.........190......
 
   387..390.........400.........410.........420.........430........
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Query Sequence  QDRLRSLSNVDIKTNAKTTEVVGEDHVTGIRYEDMNTGEEHLLNLDGIFVQI
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Template Sequence  LTEEMEANNITIATGETVERYEGDGRVQKV. . . . . . VTDKNAYDADLVVVAV
Template Known Secondary structure  TTTS


SSB

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   197..200.........210.........220...... ...230.........240..
 
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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