1EKY

MODEL STRUCTURE FROM NON-NOE BASED NMR STRUCTURE CALCULATION

Summary for 1EKY

• Entry DOI: 10.2210/pdb1eky/pdb
• Related: 1nbb
• Descriptor: CYTOCHROME C', PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• Functional Keywords: four helix bundle, oxygen storage-transport complex, oxygen storage/transport
• Biological source: Rhodobacter capsulatus
• Total number of polymer chains: 1
• Total formula weight: 13771.22

Authors

Hus, J.C.,Marion, D.,Blackledge, M. (deposition date: 2000-03-10, release date: 2000-03-17, Last modification date: 2024-05-22)

Primary citation

Hus, J.C.,Marion, D.,Blackledge, M.
De novo determination of protein structure by NMR using orientational and long-range order restraints.
J.Mol.Biol., 298:927-936, 2000

PubMed Abstract: Orientational and novel long-range order restraints available from paramagnetic systems have been used to determine the backbone solution structure of the cytochrome c' protein to atomic resolution in the complete absence of restraints derived from the nuclear Overhauser effect. By exploiting the complementary geometric dependence of paramagnetic pseudocontact shifts and the recently proposed Curie-dipolar cross correlated relaxation effect, in combination with orientational constraints derived from residual dipolar coupling, autorelaxation rate ratios and secondary structure constraints, it is possible to define uniquely the fold and refine the tertiary structure of the protein (0.73 A backbone rmsd for 82/129 amino acid residues) starting from random atomic Cartesian coordinates. The structure calculation protocol, developed using specific models to describe the novel constraint interactions, is robust, requiring no precise a priori estimation of the various interaction strengths, and provides unambiguous convergence based only on the value of the target function. Tensor eigenvalues and their component orientations are allowed to float freely, and are thus simultaneously determined, and found to converge, during the structure calculation.

PubMed: 10801359
DOI: 10.1006/jmbi.2000.3714

Experimental method

SOLUTION NMR