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
26027 Chemical Shifts: 1 set
Chemical shift assignment of the natively disordered N-terminus (= NORS, residues 1-75) of M. tuberculosis protein kinase G (PknG) Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G Download bibtex for citation iamge Matthias Wittwer, Sonja A Dames
26028 Chemical Shifts: 1 set
Chemical shift assignment of residues 1-147 of M. tuberculosis protein kinase G (PknG) including the natively disordered N-terminus and the reduced, metal bound rubredoxin-like domain Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G Download bibtex for citation iamge Matthias Wittwer, Sonja A Dames
26029 Chemical Shifts: 1 set
Chemical shift assignment of the oxidized, unfolded rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG) Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G Download bibtex for citation iamge Matthias Wittwer, Sonja A Dames
26030 Chemical Shifts: 1 set
Chemical shift assignment of the reduced, metal bound rubredoxin-like domain (= RD, residues 74-147) of M. tuberculosis protein kinase G (PknG) Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G Download bibtex for citation iamge Matthias Wittwer, Sonja A Dames