1B4C

SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 21 
  • Conformers Submitted: 21 
  • Selection Criteria: SEE MAIN REFERENCE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta).

Drohat, A.C.Tjandra, N.Baldisseri, D.M.Weber, D.J.

(1999) Protein Sci 8: 800-809

  • DOI: https://doi.org/10.1110/ps.8.4.800
  • Primary Citation of Related Structures:  
    1B4C

  • PubMed Abstract: 

    The relative orientations of adjacent structural elements without many well-defined NOE contacts between them are typically poorly defined in NMR structures. For apo-S100B(betabeta) and the structurally homologous protein calcyclin, the solution structures determined by conventional NMR exhibited considerable differences and made it impossible to draw unambiguous conclusions regarding the Ca2+-induced conformational change required for target protein binding. The structure of rat apo-S100B(betabeta) was recalculated using a large number of constraints derived from dipolar couplings that were measured in a dilute liquid crystalline phase. The dipolar couplings orient bond vectors relative to a single-axis system, and thereby remove much of the uncertainty in NOE-based structures. The structure of apo-S100B(betabeta) indicates a minimal change in the first, pseudo-EF-hand Ca2+ binding site, but a large reorientation of helix 3 in the second, classical EF-hand upon Ca2+ binding.


  • Organizational Affiliation

    Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore 21201, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (S-100 PROTEIN, BETA CHAIN)
A, B
92Rattus norvegicusMutation(s): 0 
Gene Names: S100BETA FROM RATTUS NORVEGICUS (RAT)
UniProt
Find proteins for P04631 (Rattus norvegicus)
Explore P04631 
Go to UniProtKB:  P04631
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP04631
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 21 
  • Conformers Submitted: 21 
  • Selection Criteria: SEE MAIN REFERENCE 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-12-30
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-16
    Changes: Database references, Derived calculations, Experimental preparation