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Job DescriptionP39286
Confidence98.37%DateThu Jan 5 11:58:58 GMT 2012
Rank88Aligned Residues84
% Identity19%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


   120.........130.........140.........150.... .....160..... ....170.........180.. .......190.
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Query Sequence  AANIDQIVIVSAILPELSLNIIDRYLVACETLQIE. PIIVLNKIDLL. DDEGMAFVNEQMDIYRN. . . . . . IGYRVLMVS
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Template Sequence  AAQMDGAILVVAATDGPMPQTRE. HILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGS
Template Known Secondary structure  SS

SSTTT
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   95....100.........110....... ..120.........130.........140.........150.........160.........170...
 
   192.......200....
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Query Sequence  SHTQDGLKPLEEA
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Template Sequence  ALKALEGDAEWEA
Template Known Secondary structure  T
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   174.....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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