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Job DescriptionP08201
Confidence99.34%DateThu Jan 5 11:00:55 GMT 2012
Rank162Aligned Residues113
% Identity16%Templated1aoga2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.30

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


   124.....130.........140.........150.........160...... ...170.........180.........190.........200
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Query Sequence  QDCFVYRTIEDLNAIESCARRSKRGAVVGGGLLGLEAAGALKN. . . LGIETHVIEFAPMLMAEQLDQMGGEQLRRKIESM
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Template Sequence  PGIEHCISSNEAFYLPEP. . . PRRVLTVGGGFISVEFAGIFNAYKPKDGQVTLCYRGEMILRG. FDHTLREELTKQLTAN
Template Known Secondary structure  TTGGG
B
TT
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S
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TT
SSSSSSTT.S
T
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   171........180........ .190.........200.........210.........220.........230 .........240......
 
   201........210.........220.........230.........240.
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Query Sequence  GVRVHTSKNTLEIVQEGVEARKTMRFADGSELEVDFIVFST
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Template Sequence  GIQILTKENPAKVELNADGSKS. VTFESGKKMDFDLVMMAI
Template Known Secondary structure  T
S


TTS
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   247..250.........260........ .270.........280......
 
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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