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.
|
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
|
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
|
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
|
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.
|
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.
|
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).
|
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.
|
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.
|
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.
|
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.
|
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.
|
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
|
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
|
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
|
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.
|
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.
|
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.
|
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.
|
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.
|
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.
|
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
|
Byong-Seok Choi, Chaejoon Cheong, Chulhyun Lee, Eun-Hee Kim, Hae-Kap Cheong, Jin-Young Park, Sunghoon Kim, Youngsoo Kim |