BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

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Entry ID Data summary Entry Title Citation Title Authors
34240 Chemical Shifts: 1 set
Protein environment affects the water-tryptophan binding mode. Molecular dynamics simulations of Engrailed homeodomain mutants Protein environment affects the water-tryptophan binding mode. MD, QM/MM, and NMR studies of engrailed homeodomain mutants. Download bibtex for citation iamge F Sebesta, J Kozelka, J V Burda, L Zidek, M Zachrdla, N Spackova, P Srb, S Jansen, Z Trosanova
11528 Chemical Shifts: 1 set
STRUCTURE OF METALLO-DNA IN SOLUTION The structure of metallo-DNA with consecutive T-Hg(II)-T base-pairs explains positive entropy for the metallo-base-pair formation Download bibtex for citation iamge A Ono, C Kojima, H Yamaguchi, I Okamoto, J Kondo, J Sebera, J V Burda, S Oda, T Dairaku, T Kawamura, T Komuro, V Sychrovsky, Y Kondo, Y Tanaka