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Job DescriptionP39406
Confidence73.08%DateThu Jan 5 12:00:42 GMT 2012
Rank414Aligned Residues105
% Identity12%Templated1ojua1
SCOP infoNAD(P)-binding Rossmann-fold domains NAD(P)-binding Rossmann-fold domains LDH N-terminal domain-like
Resolution2.79

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


   198.200....... ..210.........220.........230.... .....240.........250.........260.........270.
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Query Sequence  GKVLDVGCGA. . GVLSVAFARHSPKIRLTLCDVSAPAVE. . . . ASRATLAANGVEGEVFASNVFSEVKGRFDMIISNPPF
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Template Sequence  MKLGFVGAGRVGSTSAFTCLLNLDVDEIALVDIAEDLAVGEAMDLAHAAAGIDKYPKIVGGADYS. LLKGSEIIVVTAGL
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   22.......30.........40.........50.........60.........70.........80...... ...90.........100
 
   272...... .280.........290.........300....
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Query Sequence  HDGMQTS. . . . . . . . LDAAQTLIRGAVRHLNSGGELRIVAN
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Template Sequence  ARKPGMTRLDLAHKNAGIIKDIAKKIVE. NAPESKILVVTN
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   101........110.........120........ .130.........140
 
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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