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Job DescriptionP33650
Confidence98.50%DateThu Jan 5 11:52:32 GMT 2012
Rank251Aligned Residues116
% Identity22%Templatec2hdnJ_
PDB info PDB header:translationChain: J: PDB Molecule:elongation factor ef-tu; PDBTitle: trypsin-modified elongation factor tu in complex with2 tetracycline at 2.8 angstrom resolution
Resolution2.80 Å

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


   35....40.........50.........60.........70.........80.........90........ .100.........110..
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Query Sequence  GVTVERKEGQFSTTDHQVTLVDLPGTYSLTTISSQTSLDEQIACHYILSGDADLLINVVDASNL. . ERNLYLTLQLLELG
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Template Sequence  GITINTSHVEYDTPTRHYAHVDCPGH. . . . . . . . . . . . ADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVG
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   5960.........70.........80.... .....90.........100.........110.........120......
 
   113. .....120.........130.........140. ........150.........160..
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Query Sequence  IP. CIVALNMLDIAEKQNIRIEIDALSARL. . . . . . . . . GCPVIPLVSTRGRGIEALKLA
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Template Sequence  VPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEA
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   127..130.........140.........150.........160.........170.........180......
 
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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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