Journal of Biomolecular NMR

, Volume 24, Issue 4, pp 277–289 | Cite as

Structure determination of a pseudotripeptide zinc complex with the COSMOS-NMR force field and DFT methods

  • Raiker WitterEmail author
  • Lydia Seyfart
  • Georg Greiner
  • Siegmund Reissmann
  • Jennie Weston
  • Ernst Anders
  • Ulrich Sternberg


A His-X-His pseudotripeptide zinc complex (X is a N-alkyl glycine derivative) similar to the catalytic center of the carbonic anhydrase was computer designed and experimentally synthesized. Using 2D-NMR techniques, all proton, carbon chemical shifts and nuclear overhauser effect signals were assigned. The three-dimensional structure of the complex was determined with the COSMOS (computer simulation of molecular structures) force field by applying 13C bond polarization theory chemical shift pseudo forces and restrictions for NOE distances. From molecular dynamics, simulated annealing simulations and geometry optimizations, the three best force field structures were taken for a final investigation by density functional theory calculations.

carboanhydrase carbonic anhydrase geometry optimization molecular dynamics peptide pseudo forces restrictions simulated annealing structure determination zinc complex 


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Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Raiker Witter
    • 1
    Email author
  • Lydia Seyfart
    • 2
  • Georg Greiner
    • 2
  • Siegmund Reissmann
    • 2
  • Jennie Weston
    • 3
  • Ernst Anders
    • 3
  • Ulrich Sternberg
    • 1
  1. 1.PAF / IOQ / HFFriedrich-Schiller-Universität JenaJenaGermany
  2. 2.Institute of Biochemistry and BiophysicsFriedrich-Schiller-Universität JenaJenaGermany
  3. 3.Institute of Organic Chemistry and Macromolecular ChemistryFriedrich-Schiller-Universität JenaJenaGermany

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