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Entry ID Original Release date Data summary Entry Title Citation Title Authors
25987 2017-05-08 Chemical Shifts: 1 set
Solution structure of the T119M variant of transthyretin in its monomeric state Structure of Monomeric Transthyretin Carrying the Clinically Important T119M Mutation. Download bibtex for citation iamge Javier Oroz, Jin Hae Kim, Markus Zweckstetter
25986 2017-02-16 Chemical Shifts: 1 set
Solution structure of the F87M/L110M variant of transthyretin in the monomeric state Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90 Download bibtex for citation iamge Bliss J Chang, Javier Oroz, Jin Hae H Kim, Markus Zweckstetter
25142 2015-09-14 Chemical Shifts: 1 set
Solution structure of Hox homeodomain Structural insight into the interaction between the Hox and HMGB1 and understanding of the HMGB1-enhancing effect of Hox-DNA binding Download bibtex for citation iamge Bong-Jin Lee, Chinar Pathak, Hae-Kap Cheong, Hyun-Hwi Kim, Jung-Hwa Han, Sung Jean Park
19707 2014-09-16 Chemical Shifts: 1 set
Solution structure of the extracellular sensor domain of DraK histidine kinase Mechanism of the pH-Induced Conformational Change in the Sensor Domain of the DraK Histidine Kinase via the E83, E105, and E107 Residues Download bibtex for citation iamge Eun-Gyeong Lee, Eunha Hwang, Eun-Hee Kim, Hae-Kap Cheong, Hyo-Jeong Kim, Jae-Kyoung Lee, Jin-Wan Park, Jun-Goo Jee, Kwon-Joo Yeo, Ohsuk Kwon, Sang-Yoon Kim, Young-Soo Hong
18992 2014-02-14 Chemical Shifts: 1 set
Backbone resonance assignment of [2Fe-2S]-ferredoxin in its reduced state [2Fe-2S]-Ferredoxin Binds Directly to Cysteine Desulfurase and Supplies an Electron for Iron-Sulfur Cluster Assembly but Is Displaced by the Scaffold Protein or Bacterial Frataxin. Download bibtex for citation iamge Andrew T Troupis, Jin Hae Kim, John L Markley, Nichole M Reinen, Ronnie O Frederick
18991 2014-02-14 Chemical Shifts: 1 set
Backbone resonance assignment of [2Fe-2S]-ferredoxin in its oxidized state [2Fe-2S]-Ferredoxin Binds Directly to Cysteine Desulfurase and Supplies an Electron for Iron-Sulfur Cluster Assembly but Is Displaced by the Scaffold Protein or Bacterial Frataxin. Download bibtex for citation iamge Andrew T Troupis, Jin Hae Kim, John L Markley, Nichole M Reinen, Ronnie O Frederick
18381 2012-09-14 Chemical Shifts: 1 set
The backbone chemical shifts of IscU complexed with HscA Specialized Hsp70 Chaperone (HscA) Binds Preferentially to the Disordered Form, whereas J-protein (HscB) Binds Preferentially to the Structured Form of the Iron-Sulfur Cluster Scaffold Protein (IscU). Download bibtex for citation iamge Darius C-F Chow, Jin Hae Kim, John L Markley, Marco Tonelli, Ronnie O Frederick
18362 2012-09-14 Chemical Shifts: 1 set
Heteronuclear NOE Values: 1 set
T1 Relaxation Values: 1 set
T2 Relaxation Values: 1 set
The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(S107A) Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli. Download bibtex for citation iamge Jin Hae Kim, John L Markley, Marco Tonelli, Taewook Kim
18360 2012-09-14 Chemical Shifts: 1 set
Heteronuclear NOE Values: 1 set
T1 Relaxation Values: 1 set
T2 Relaxation Values: 1 set
The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(E111A) Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli. Download bibtex for citation iamge Jin Hae Kim, John L Markley, Marco Tonelli, Taewook Kim
18361 2012-09-14 Chemical Shifts: 1 set
Heteronuclear NOE Values: 1 set
T1 Relaxation Values: 1 set
T2 Relaxation Values: 1 set
The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(N90A) Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli. Download bibtex for citation iamge Jin Hae Kim, John L Markley, Marco Tonelli, Taewook Kim
18359 2012-09-14 Chemical Shifts: 1 set
Heteronuclear NOE Values: 1 set
T1 Relaxation Values: 1 set
T2 Relaxation Values: 1 set
The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(D39V) Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli. Download bibtex for citation iamge Jin Hae Kim, John L Markley, Marco Tonelli, Taewook Kim
18288 2012-03-22 Chemical Shifts: 1 set
1H, 13C and 15N chemical shift assignments of Ninjurin1 ENT domain 1H, 13C and 15N chemical shift assignments of Ninjurin1 Extracellular N-terminal Domain. Download bibtex for citation iamge Bong-Jin Lee, Hae-Kap Cheong, In-Gyun Lee, Ji-Hun Kim, Ki-Young Lee, Kyu-Yeon Lee, Sun-Bok Jang
17844 2012-02-28 Chemical Shifts: 1 set
The assigned chemical shifts of disordered-IscU complexed with IscS Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase Download bibtex for citation iamge Jin Hae Kim, John L Markley, Marco Tonelli
17836 2012-02-28 Chemical Shifts: 1 set
The assigned chemical shifts for the disordered forms of apo-IscU Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase Download bibtex for citation iamge Jin Hae Kim, John L Markley, Tonelli Marco
17837 2012-02-28 Chemical Shifts: 1 set
The assigned chemical shifts for the structured forms of apo-IscU Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase Download bibtex for citation iamge Jin Hae Kim, John L Markley, Marco Tonelli
17282 2012-08-29 Chemical Shifts: 1 set
Heteronuclear NOE Values: 1 set
T1 Relaxation Values: 1 set
T2 Relaxation Values: 1 set
Residual Dipolar Couplings: 1 set
Solution Structure of apo-IscU(WT) Three-dimensional structure and determinants of stability of the iron-sulfur cluster scaffold protein IscU from Escherichia coli. Download bibtex for citation iamge Jin Hae Kim, John L Markley, Marco Tonelli, Taewook Kim
16603 2012-08-29 Chemical Shifts: 1 set
Residual Dipolar Couplings: 1 set
Solution Structure of apo-IscU Three-dimensional structure and determinants of stability of the iron-sulfur cluster scaffold protein IscU from Escherichia coli. Download bibtex for citation iamge Jin Hae Kim, John L Markley, Marco Tonelli, Taewook Kim
20098 2010-10-27 Chemical Shifts: 1 set
Effects of Peptoid Residue Substitutions on Structural Flexibility and Bacterial-Cell Selectivity of Piscidin 1 Structural flexibility and the positive charges are the key factors in bacterial cell selectivity and membrane penetration of peptoid-substituted analog of Piscidin 1. Download bibtex for citation iamge Jee-Young Lee, Jin-Kyoung Kim, Ki-Woong Jeong, Song Yub Shin, Soyoung Shin, Sung-Ah Lee, Yangmee Kim, Yong Hae Nan, Yong Sun Park
20095 2010-10-27 Chemical Shifts: 1 set
Effects of Peptoid Residue Substitutions on Structural Flexibility and Bacterial-Cell Selectivity of Piscidin 1 Structural flexibility and the positive charges are the key factors in bacterial cell selectivity and membrane penetration of peptoid-substituted analog of Piscidin 1. Download bibtex for citation iamge Jee-Young Lee, Jin-Kyoung Kim, Ki-Woong Jeong, Song Yub Shin, Soyoung Shin, Sung-Ah Lee, Yangmee Kim, Yong Hae Nan, Yong Sun Park
7432 2009-08-20 Chemical Shifts: 1 set
Heteronuclear NOE Values: 1 set
T1 Relaxation Values: 1 set
T2 Relaxation Values: 1 set
Structural characterization of IscU and its interaction with HscB Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB. Download bibtex for citation iamge Anna K Fuzery, Dennis T Ta, Jin Hae Kim, John L Markley, Larry E Vickery, Marco Tonelli, William M Westler
15967 2008-09-28 Chemical Shifts: 1 set
Structural characterization of IscU and its interaction with HscB Structure and Dynamics of the Iron-Sulfur Cluster Assembly Scaffold Protein IscU and Its Interaction with the Cochaperone HscB. Download bibtex for citation iamge Anna K Fuzery, Dennis T Ta, Jin Hae Kim, John L Markley, Larry E Vickery, Marco Tonelli, William M Westler
5699 2003-08-07 Chemical Shifts: 1 set
Structure of the N-terminal Extension of Human Aspartyl-tRNA Synthetase: Implications for its biological function Structure of the N-terminal Extension of Human Aspartyl-tRNA Synthetase: Implications for its Biological Function Download bibtex for citation iamge Byong-Seok Choi, Chaejoon Cheong, Chulhyun Lee, Eun-Hee Kim, Hae-Kap Cheong, Jin-Young Park, Sunghoon Kim, Youngsoo Kim