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Entry ID	Original Release date	Data summary	Entry Title	Citation Title	Authors
19155	2014-04-14	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	2007-03-22	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	2000-06-15	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	1999-08-12	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	1999-08-12	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	2000-03-08	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	1999-06-14	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	1999-06-14	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	1999-06-14	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