| Entry ID |
Data summary |
Entry Title |
Citation Title |
Authors |
| 19155 |
Chemical Shifts: 1 set
|
NMR Structure of CbpAN from Streptococcus pneumoniae |
Host Specification of Factor H Binding by Streptococcus pneumoniae
|
Aizhuo Liu, David Achila, Erik Martinez-Hackert, Honggao Yan, Rahul Banerjee, Yue Li |
| 6223 |
Chemical Shifts: 1 set
|
Sequential resonance assignment of yeast cytosine deaminase in complex with a transition state analogue |
Simultaneous NMR assignment of backbone and side chain amides in large proteins with IS-TROSY
|
Aizhuo Liu, Honggao Yan, L Yao, Yue Li |
| 4722 |
Chemical Shifts: 1 set
|
1H,13C and 15N resonance assignments of Aquifex aeolifex aeolicus shikimate kinase in complex with shikimate |
Letter to the Editor: 1H, 13C and 15N resonance assignments of Aquifex aeolicus shikimate kinase in complex with the substrate shikimate
|
Honggao Yan, Qin Liu, Yan Wu, Yue Li |
| 4300 |
Chemical Shifts: 1 set
|
1H , 13C, 15N Assigned Chemical Shifts for HPPK-AMPPCP Complex |
1H, 13C and 15N Resonance Assignments of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin Pyrophosphokinase and its Complex with MgAMPPCP
|
Genbin Shi, Honggao Yan, Jinhai Gao |
| 4299 |
Chemical Shifts: 1 set
|
1H, 13C and 15N Resonance Assignments of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin Pyrophosphokinase and its Complex with MgAMPPCP |
1H, 13C and 15N Resonance Assignments of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin Pyrophosphokinase and its Complex with MgAMPPCP
|
Genbin Shi, Honggao Yan, Jinhai Gao |
| 4186 |
Chemical Shifts: 1 set
|
NMR Solution Structure of Human Cellular Retinoic Acid Binding Protein-Type II |
NMR Solution Structure of type II Human Cellular Retinoic Acid Binding Protein: Implications for Ligand Binding
|
Frits Abildgaard, Honggao Yan, John L Markley, L Wang, Yue Li |
| 918 |
Chemical Shifts: 1 set
|
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine |
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine
|
Honggao Yan, Ming-Daw Tsai, Zhengtao Shi |
| 919 |
Chemical Shifts: 1 set
|
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine |
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine
|
Honggao Yan, Ming-Daw Tsai, Zhengtao Shi |
| 920 |
Chemical Shifts: 1 set
|
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine |
Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine
|
Honggao Yan, Ming-Daw Tsai, Zhengtao Shi |
