Return to main results Retrieve Phyre Job Id

Job DescriptionP0A6P7
Confidence98.51%DateThu Jan 5 11:03:39 GMT 2012
Rank265Aligned Residues130
% Identity18%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


   65....70.........80.........90.........100.........110.........120.........130......... 140...
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Query Sequence  INLFEVADGKRLVDLPGYGYAEVPEEMKRKWQRALGEYLEKRQSLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIA. VLVL
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Template Sequence  VEYDTPTRHYAHVDCPG. . . . . . . . . . . . . HADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVF
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   67..70.........80... ......90.........100.........110.........120.........130...
 
   144.....150.........160........ .170.........180........ .190.........200.......
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Query Sequence  LTKADKLASGARKAQLNMVREAVLA. . . . FNGDVQVETFSSLKKQGVDK. . . . . . . . LRQKLDTWFSEMQPVEETQ
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Template Sequence  LNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKP
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   134.....140.........150.........160.........170.........180.........190.........200.........
 
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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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