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Job DescriptionP25534
Confidence98.70%DateThu Jan 5 11:42:01 GMT 2012
Rank116Aligned Residues163
% Identity11%Templated2gv8a1
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.10

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


   2.......10.........20.........30........ .40.........50.........60.........70.........80
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Query Sequence  SVIIVGGGMAGATLALAISRLSHGALPVHLIEATAPE. SHAHPGFDGRAIALAAGTCQQLARIGVWQSLADCATAITTVH
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Template Sequence  KIAIIGAGPSGLVTAKALLAEK. AFDQVTLFERRGSPGGVWNYTSTLSNKLPVPSTNPILTTEPIVGPAALPVYPSPLYR
Template Known Secondary structure 

STTT.

S
SSSSSSTT
S

S


S


SS


TT




B

SSS

B





T
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   8.10.........20......... 30.........40.........50.........60.........70.........80......
 
   81........90.........100.........110.........120.........130.........140.........150. ...
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Query Sequence  VSDRGHAGFVTLAAEDYQLAALGQVVELHNVGQRLFALLRKAPGVTLHCPDRVANVARTQSHVEVTLESGE. . . . . . TLT
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Template Sequence  DLQTNTPIELXGYCDQSFKPQTLQFPHRHTIQEYQRIYAQPL. LPFIKLATDVLDIEKKDGSWVVTYKGTKAGSPISKDI
Template Known Secondary structure  T
B
SS
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TT



TT

SS
BGGG.GGG
STTSSTT

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   87..90.........100.........110.........120........ .130.........140.........150.........160.....
 
   155....160......
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Query Sequence  GRVLVAADGTHS
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Template Sequence  FDAVSICNGHYE
Template Known Secondary structure  S


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   166...170.......
 
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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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