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Job DescriptionG5EE56
Confidence99.73%DateFri May 3 21:16:22 BST 2013
Rank383Aligned Residues106
% Identity28%Templated1pica_
SCOP infoSH2-like SH2 domain SH2 domain
ResolutionUNK

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


   128.130.........140.........150.........160.........170.........180.........190.........200.......
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Query Sequence  AKQQTIESEEWYAGKIPRNRAERLVLSSHLPKGTFLIREREADTREFALTIRDTDDQRNGGTVKHYKIKRLDHDQGYFIT
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Template Sequence  SPIPHHDEKTWNVGSSNRNKAENLLRGK. . RDGTFLVRES. SKQGCYACSVV. . . . . . VDGEVKHCVIN. KTATGYGFAE
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   2.......10.........20......... 30......... 40.........50 .........60. ........70.
 
   208.210.........220...... ...230.........240...
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Query Sequence  TRRTFRSLQELVRYYSDVP. . . . . DGLCCQLTFPAPRLAPT
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Template Sequence  PYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR
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   72.......80.........90.........100.........110..
 
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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