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Job DescriptionP04391
Confidence78.70%DateThu Jan 5 10:58:15 GMT 2012
Rank240Aligned Residues110
% Identity10%Templated1llca1
SCOP infoNAD(P)-binding Rossmann-fold domains NAD(P)-binding Rossmann-fold domains LDH N-terminal domain-like
Resolution3.00

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


   155....160.........170.........180.. .......190.........200.........210 .........220.........
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Query Sequence  NEMTLVYAGDARNNMGNSMLEAAALTGL. . DLRLVAPQACWPEAALVTECRALAQQNG. . . GNITLTEDVAKGVEGADFI
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Template Sequence  DHQKVILVG. D. GAVGSSYAFAMVLQGIAQEIGI. . . . . VDIFKDKTKGDAIDLSNALPFTSPKKIYSAEYSDAKDADLV
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   1920....... . .30.........40.........50 .........60.........70.........80.........90.
 
   230.........240.........250.........260.........270..
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Query Sequence  YTDVWVSMGEAKEKWAERIALLREYQVNSKMMQLTGNPEVKFL
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Template Sequence  VITAGAPKQPGETRLDLVNKNLKILKSIVDPIVD. SGFNLIFL
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   95....100.........110.........120........ .130......
 
Download:Text 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]
 
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Lawrence Kelley, Benjamin Jefferys 
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