| Entry ID | 
            Original Release date | 
            Data summary | 
            Entry Title | 
            Citation Title | 
            Authors | 
                    
    
    
        | 17268 | 
        2013-07-01 | 
        Chemical Shifts: 1 set   | 
        Solution Structures of Oxidized and Reduced Thioredoxin C from M. tb | 
        
Solution structures of Mycobacterium tuberculosis thioredoxin C and models of intact thioredoxin system suggest new approaches to inhibitor and drug design            
                 
            
         | 
        Andrew L Olson, Daniel S Sem, Sheng Cai, Terrence S Neumann |         
    
    
        | 17242 | 
        2013-07-01 | 
        Chemical Shifts: 1 set   | 
        Solution Structures of Oxidized and Reduced Thioredoxin C from M. tb | 
        
Solution structures of Mycobacterium tuberculosis thioredoxin C and models of intact thioredoxin system suggest new approaches to inhibitor and drug design            
                 
            
         | 
        Andrew L Olson, Daniel S Sem, Sheng Cai, Terrence S Neumann |         
    
    
        | 17098 | 
        2010-11-10 | 
        Kinetic Rates: 1 set   | 
        Cofactor fingerprinting with STD NMR to characterize proteins of unknown function: identification of a rare cCMP cofactor preference | 
        
Cofactor fingerprinting with STD NMR to characterize proteins of unknown function: identification of a rare cCMP cofactor preference            
                 
            
         | 
        Daniel S Sem, Huili Yao |         
    
    
        | 4033 | 
        1999-10-10 | 
        Chemical Shifts: 1 set   | 
        NMR Spectroscopic Studies of the DNA Binding Domain of the Monomer-Binding Nuclear Orphan Receptor, Human ERR2. The Carboxy-Terminal Extension to the Zinc-Finger Region is Unstructured in the Free Form of the Protein. | 
        
NMR Spectroscopic Studies of the DNA-Binding Domain of the    Monomer-Binding Nuclear Orphan Receptor, Human ERR2. The Carboxy    Terminal Extension to the Zinc-Finger Region is Unstructured in    the Free Form of the Protein.            
                 
            
         | 
        Daniel Sem, Danilo Casimiro, Joan Provencal, Peter Wright, Ronald Evans, Steven Kliewer |         
    
    
        | 4034 | 
        2001-02-17 | 
        Chemical Shifts: 1 set   | 
        NMR Spectroscopic Studies of the DNA Binding Domain of the Monomer-Binding Nuclear Orphan Receptor, Human ERR2. The Carboxy-Terminal Extension to the Zinc-Finger Region is Unstructured in the Free Form of the Protein. | 
        
NMR Spectroscopic Studies of the DNA-Binding Domain of the Monomer-Binding Nuclear Orphan Receptor, Human ERR2. The Carboxy Terminal Extension to the Zinc-Finger Region is Unstructured in the Free Form of the Protein.            
                 
            
         | 
        Daniel Sem, Danilo Casimiro, Joan Provencal, Peter Wright, Ronald Evans, Steven Kliewer |