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Job DescriptionP13033
Confidence97.31%DateThu Jan 5 11:33:29 GMT 2012
Rank287Aligned Residues116
% Identity9%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


   194.....200.........210.........220.........230....... ..240.........250.........260.........270..
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Query Sequence  FLDNEENWPLLLDALIPVANTCEMILMPACFGLADDKLWRWLNE. KLPCSLMLLPTLPPSVLGIRLQNQLQRQFVRQGGV
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Template Sequence  IPGIEHCISSNEAFYLPEPPRRVLTVGGGFISVEFAGIFNAYKPKDGQVTLCYRGEMILRGFDHTLREELTKQLTANGIQ
Template Known Secondary structure 
TTGGG
B
TT
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S
SS

TT
SSSSSSTTS
TT
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   170.........180.........190.........200.........210.........220.........230.........240.........
 
   273......280.........290.........300.........310.
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Query Sequence  WMPGDEVKKVTCKNGVVNEIWTRNHADIPLRPRFAVLAS
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Template Sequence  ILTKENPAKVELNADGSKSVTFESGK. . KMDFDLVMMAI
Template Known Secondary structure  S


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