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Job DescriptionP29351
Confidence99.81%DateWed Jul 10 14:09:17 BST 2013
Rank122Aligned Residues94
% Identity33%Templated1i3za_
SCOP infoSH2-like SH2 domain SH2 domain
Resolution2.15

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


   108.110.........120.........130.........140.........150.........160.......
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Query Sequence  ERWYHGHISGGQAESLLQAKGEPWTFLVRESLSQPGDFVLSVLNDQPKAGPGSPLRVTHI
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Template Sequence  LPYYHGCLTKRECEALLLKGGVDGNFLIRDSESVPGALCLCVSFKK. . . . . . . . . LVYSY
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   3......10.........20.........30.........40........ .50...
 
   168.170.. .......180. ........190.........200.........210....
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Query Sequence  KVMCE. GGRYTVGGS. . . . . ETFDSLTDLVEHFKKTGIEEASGAFVYLRQPYY
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Template Sequence  RIFREKHGYYRIETDAHTPRTIFPNLQELVSKYGKPGQ. . . . GLVVHLSNPIM
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   54.....60.........70.........80.........90. ........100..
 
Download:Text version FASTA 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]
 
© Structural Bioinformatics Group, Imperial College, London
Lawrence Kelley, Benjamin Jefferys 
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