5WOX

NMR solution structure of KanY protein (ms6282) using two 4D-spectra


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra.

Evangelidis, T.Nerli, S.Novacek, J.Brereton, A.E.Karplus, P.A.Dotas, R.R.Venditti, V.Sgourakis, N.G.Tripsianes, K.

(2018) Nat Commun 9: 384-384

  • DOI: https://doi.org/10.1038/s41467-017-02592-z
  • Primary Citation of Related Structures:  
    5WOT, 5WOX, 5WOY, 5WOZ

  • PubMed Abstract: 

    Automated methods for NMR structure determination of proteins are continuously becoming more robust. However, current methods addressing larger, more complex targets rely on analyzing 6-10 complementary spectra, suggesting the need for alternative approaches. Here, we describe 4D-CHAINS/autoNOE-Rosetta, a complete pipeline for NOE-driven structure determination of medium- to larger-sized proteins. The 4D-CHAINS algorithm analyzes two 4D spectra recorded using a single, fully protonated protein sample in an iterative ansatz where common NOEs between different spin systems supplement conventional through-bond connectivities to establish assignments of sidechain and backbone resonances at high levels of completeness and with a minimum error rate. The 4D-CHAINS assignments are then used to guide automated assignment of long-range NOEs and structure refinement in autoNOE-Rosetta. Our results on four targets ranging in size from 15.5 to 27.3 kDa illustrate that the structures of proteins can be determined accurately and in an unsupervised manner in a matter of days.


  • Organizational Affiliation

    CEITEC-Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, 62500, Czech Republic.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Uncharacterized protein145Mycolicibacterium smegmatis MC2 155Mutation(s): 0 
Gene Names: MSMEI_6117
UniProt
Find proteins for A0R5R3 (Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155))
Explore A0R5R3 
Go to UniProtKB:  A0R5R3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0R5R3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • 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: 2018-02-07
    Type: Initial release
  • Version 1.1: 2024-05-01
    Changes: Data collection, Database references