1RYK

Solution NMR Structure Protein yjbJ from Escherichia coli. Northeast Structural Genomics Consortium Target ET93; Ontario Centre for Structural Proteomics target EC0298_1_69;


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

An NMR approach to structural proteomics.

Pineda-Lucena, A.Liao, J.Wu, B.Yee, A.Cort, J.R.Kennedy, M.A.Edwards, A.M.Arrowsmith, C.H.

(2002) Proteins 47: 572-574

  • DOI: https://doi.org/10.1073/pnas.042684599
  • Primary Citation of Related Structures:  
    1JCU, 1JDQ, 1JE3, 1JRM, 1JW2, 1JW3, 1RYJ, 1RYK

  • PubMed Abstract: 

    The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMR. Although there was variability among proteomes, overall 20% of these proteins were found to be readily amenable to NMR structure determination. NMR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins.


  • Organizational Affiliation

    Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, ON, Canada M5G 1L7.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Protein yjbJ69Escherichia coliMutation(s): 0 
Gene Names: YJBJB4045Z5644ECS5028SF4160S3571
UniProt
Find proteins for P68206 (Escherichia coli (strain K12))
Explore P68206 
Go to UniProtKB:  P68206
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP68206
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-02-24
    Type: Initial release
  • Version 1.1: 2008-04-29
    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