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
18005 Chemical Shifts: 1 set
TBA Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins Download bibtex for citation iamge C Englbrecht, D Fessas, K Neugebauer, Konstantinos Tripsianes, M Machyna, M Sattler, T Madl, U Fischer
18006 Chemical Shifts: 1 set
TBA Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins Download bibtex for citation iamge C Englbrecht, D Fessas, K Neugebauer, Konstantinos Tripsianes, M Machyna, M Sattler, T Madl, U Fischer
18007 Chemical Shifts: 1 set
TBA Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins Download bibtex for citation iamge C Englbrecht, D Fessas, K Neugebauer, Konstantinos Tripsianes, M Machyna, M Sattler, T Madl, U Fischer
18008 Chemical Shifts: 1 set
TBA Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins Download bibtex for citation iamge C Englbrecht, D Fessas, K Neugebauer, Konstantinos Tripsianes, M Machyna, M Sattler, T Madl, U Fischer
4768 Chemical Shifts: 1 set
Structure of parvulin hPar14 NMR Solution Structure of hPar14 Reveals Similarity to the Peptidyl Prolyl cis/tans Isomerase Domain of the Mitotic Regulator hPin1 but Indicates a Different Functionality of the Protein Download bibtex for citation iamge Christine Rascher, Elena Sekerina, Gunter Fischer, Jens U Rahfeld, Jonathan Muller, Jorg Fanghanel, Peter Bayer