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Job DescriptionP08201
Confidence99.49%DateThu Jan 5 11:00:55 GMT 2012
Rank144Aligned Residues116
% Identity21%Templated1onfa2
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


   115....120.........130.........140.........150.........160.........170.........180.........190....
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Query Sequence  IPPIKGSDTQDCFVYRTIEDLNAIESCARRSKRGAVVGGGLLGLEAAGALKNLGIETHVIEFAPMLMAEQLDQMGGEQLR
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Template Sequence  FPPVKGIEN. . TISSDEFFN. . . . . . . IKESKKIGIVGSGYIAVELINVIKRLGIDSYIFARGNRILRK. FDESVINVLE
Template Known Secondary structure 

S
TTGGG..
TT.......



S

STTT

SSSSS
TT.S
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   154.....160.. .......170. ........180.........190.........200.........210... ......220...
 
   195....200.........210.........220.........230... ......240.
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Query Sequence  RKIESMGVRVHTSKNTLEIVQEGVEARKTMRFADGSELE. VDFIVFST
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Template Sequence  NDMKKNNINIVTFADVVEIKKVSDKNLS. IHLSDGRIYEHFDHVIYCV
Template Known Secondary structure  TT

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SSTT
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   224.....230.........240.........250. ........260.........270
 
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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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