1XHS

Solution NMR Structure of Protein ytfP from Escherichia coli. Northeast Structural Genomics Consortium Target ER111.

Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 56 
  • Conformers Submitted: 10 
  • Selection Criteria: LOWEST ENERGY 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Solution NMR structure of Escherichia coli ytfP expands the structural coverage of the UPF0131 protein domain family.

Aramini, J.M., Huang, Y.J., Swapna, G.V., Cort, J.R., Rajan, P.K., Xiao, R., Shastry, R., Acton, T.B., Liu, J., Rost, B., Kennedy, M.A., Montelione, G.T.

(2007) Proteins 68: 789-795

  • DOI: https://doi.org/10.1002/prot.21450
  • Primary Citation of Related Structures:  
    1XHS
    • Organizational Affiliation: 

    Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854, USA. jma@cabm.rutgers.edu


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hypothetical UPF0131 protein ytfP121Escherichia coliMutation(s): 0 
Gene Names: ytfP
UniProt
Find proteins for P0AE48 (Escherichia coli (strain K12))
Explore P0AE48 
Go to UniProtKB:  P0AE48
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0AE48
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 56 
  • Conformers Submitted: 10 
  • Selection Criteria: LOWEST ENERGY 

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-01-04
    Type: Initial release
  • Version 1.1: 2007-10-23
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Data collection, Database references, Derived calculations, Refinement description