2KW5

Solution NMR Structure of the Slr1183 protein from Synechocystis sp. PCC 6803, Northeast Structural Genomics Consortium Target SgR145


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

Re-refinement Note

A newer entry is available that reflects an alternative modeling of the original data: 2N47


Literature

Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples.

Lange, O.F.Rossi, P.Sgourakis, N.G.Song, Y.Lee, H.W.Aramini, J.M.Ertekin, A.Xiao, R.Acton, T.B.Montelione, G.T.Baker, D.

(2012) Proc Natl Acad Sci U S A 109: 10873-10878

  • DOI: https://doi.org/10.1073/pnas.1203013109
  • Primary Citation of Related Structures:  
    2KW5, 2KZN, 2LMD, 2LNU, 2LOK, 2LOY, 2MV0

  • PubMed Abstract: 

    We have developed an approach for determining NMR structures of proteins over 20 kDa that utilizes sparse distance restraints obtained using transverse relaxation optimized spectroscopy experiments on perdeuterated samples to guide RASREC Rosetta NMR structure calculations. The method was tested on 11 proteins ranging from 15 to 40 kDa, seven of which were previously unsolved. The RASREC Rosetta models were in good agreement with models obtained using traditional NMR methods with larger restraint sets. In five cases X-ray structures were determined or were available, allowing comparison of the accuracy of the Rosetta models and conventional NMR models. In all five cases, the Rosetta models were more similar to the X-ray structures over both the backbone and side-chain conformations than the "best effort" structures determined by conventional methods. The incorporation of sparse distance restraints into RASREC Rosetta allows routine determination of high-quality solution NMR structures for proteins up to 40 kDa, and should be broadly useful in structural biology.


  • Organizational Affiliation

    Biomolecular NMR and Munich Center for Integrated Protein Science, Department Chemie, Technische Universität München, 85747 Garching, Germany. oliver.lange@tum.de


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Slr1183 protein202Synechocystis sp. PCC 6803Mutation(s): 0 
Gene Names: slr1183
UniProt
Find proteins for P74712 (Synechocystis sp. (strain PCC 6803 / Kazusa))
Explore P74712 
Go to UniProtKB:  P74712
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP74712
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 

Revision History  (Full details and data files)

  • Version 1.0: 2010-04-21
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2012-06-27
    Changes: Database references
  • Version 1.3: 2012-07-18
    Changes: Database references