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Job DescriptionP35340
Confidence99.69%DateWed Jan 25 15:20:51 GMT 2012
Rank139Aligned Residues143
% Identity17%Templated1xhca1
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.35

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


   357..360.........370.........380.........390... ......400.........410.........
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Query Sequence  RVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKAD. . . . . . . . . . . . . . . . . QVLQDKLRSLKNVDIILNAQTTEVKG
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Template Sequence  KVVIVGNGPGGFELAKQLSQTY. EVTVIDKEPVPYYSKPMLSHYIAGFIPRNRLFPYSLDWYRKRGIEIRLAEEAKLIDR
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STTTS.
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STTTTSS
GGGG
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   2.......10.........20... ......30.........40.........50.........60.........70.........80
 
   420.........430.........440.........450.........460.........470.........480.........490... ...
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Query Sequence  DGSKVVGLEYRDRVSGDIHNIELAGIFVQIGLLPNTNWLEGAVERNRMGEIIIDAKCETNVKGVFAAGDCTTVP. . . YKQ
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Template Sequence  GRKVVI. . . . . . . . . TEKGEVPYDTLVLATGAPNVDLARRSGI. . HTGRGILIDDNFRTSAKDVYAIGDCAEYSGIIAGT
Template Known Secondary structure  TTT.........SS

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BSSS

TTSB
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GGGBTTB


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   81..... ...90.........100.........110.... .....120.........130.........140.........
 
   497..500.........510.
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Query Sequence  IIIATGEGAKASLSA
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Template Sequence  AKAAMEQARVLADIL
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   272.......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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