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19 hits found for Kim

SASDBZ9 – Immunoglobulin domains 4,5,6,7 of Nucleoporin Pom152 (Pom152 Ig-4,5,6,7: amino acids 718-1148)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 49 kDa Saccharomyces cerevisiae (strain ... protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 4.3 nm
Dmax 15.4 nm
VolumePorod 67 nm3

SASDG56 – Inhibitor of apoptosis-stimulating protein of p53 (iASPP(621-828)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, extended

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitInhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) experimental SAS data
BILBOMD model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) monomer, 25 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Apr 25
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 3.4 nm
Dmax 12.4 nm
VolumePorod 132 nm3

SASDG66 – Inhibitor of apoptosis-stimulating protein of p53 (iASPP(621-828)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, compact

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitInhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) experimental SAS data
BILBOMD model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) monomer, 25 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Apr 25
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 3.0 nm
Dmax 10.9 nm
VolumePorod 116 nm3

SASDG76 – Inhibitor of apoptosis-stimulating protein of p53 (iASPP(608-828)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, compact

Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor)Serine/threonine-protein phosphatase PP1-alpha catalytic subunit experimental SAS data
BILBOMD model
Sample: Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) monomer, 25 kDa Homo sapiens protein
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 31
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 3.1 nm
Dmax 11.3 nm
VolumePorod 157 nm3

SASDG86 – Inhibitor of apoptosis-stimulating protein of p53 (iASPP(608-828)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, extended

Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor)Serine/threonine-protein phosphatase PP1-alpha catalytic subunit experimental SAS data
BILBOMD model
Sample: Inhibitor of apoptosis-stimulating protein of p53 (RelA-associated inhibitor) monomer, 25 kDa Homo sapiens protein
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 31
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 3.4 nm
Dmax 12.2 nm
VolumePorod 180 nm3

SASDG96 – Apoptosis-stimulating protein 2 of p53 (ASPP2(905-1128)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, compact

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitApoptosis-stimulating of p53 protein 2 experimental SAS data
BILBOMD model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Apoptosis-stimulating of p53 protein 2 monomer, 26 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 31
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 2.9 nm
Dmax 10.2 nm
VolumePorod 144 nm3

SASDGA6 – Apoptosis-stimulating protein 2 of p53 (ASPP2(905-1128)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, extended

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitApoptosis-stimulating of p53 protein 2 experimental SAS data
BILBOMD model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Apoptosis-stimulating of p53 protein 2 monomer, 26 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 31
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
...Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 3.3 nm
Dmax 11.7 nm
VolumePorod 172 nm3

SASDFD7 – Pseudomonas putida CBB5 NdmAB complex - static

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 127 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.5 nm
Dmax 12.3 nm

SASDFE7 – Pseudomonas putida CBB5 mCherry-NdmA/NdmB complex - static

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 207 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 5.4 nm
Dmax 13.8 nm

SASDFF7 – Pseudomonas putida CBB5 NdmA hexamer

Methylxanthine N1-demethylase NdmA experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA hexamer, 254 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.2 nm
Dmax 11.0 nm

SASDEF3 – Paenibacillus xanthan lyase (PXL) at 4 °C

Paenibacillus xanthan lyase experimental SAS data
Paenibacillus xanthan lyase Kratky plot
Sample: Paenibacillus xanthan lyase monomer, 113 kDa Paenibacillus sp-62047 protein
Buffer: 20 mM Tris,, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 15
Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity Cell Chemical Biology (2018)
Jensen P, Kadziola A, Comamala G, Segura D, Anderson L, Poulsen J, Rasmussen K, Agarwal S, Sainathan R, Monrad R, Svendsen A, Nielsen J, Lo Leggio L, Rand K
RgGuinier 3.7 nm
Dmax 13.1 nm
VolumePorod 137 nm3

SASDEG3 – Paenibacillus xanthan lyase (PXL) at 20 °C

Paenibacillus xanthan lyase experimental SAS data
Paenibacillus xanthan lyase Kratky plot
Sample: Paenibacillus xanthan lyase monomer, 113 kDa Paenibacillus sp-62047 protein
Buffer: 20 mM Tris,, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 15
Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity Cell Chemical Biology (2018)
Jensen P, Kadziola A, Comamala G, Segura D, Anderson L, Poulsen J, Rasmussen K, Agarwal S, Sainathan R, Monrad R, Svendsen A, Nielsen J, Lo Leggio L, Rand K
RgGuinier 3.8 nm
Dmax 13.8 nm
VolumePorod 134 nm3

SASDFG7 – Pseudomonas putida CBB5 NdmB hexamer

Methylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N3-demethylase NdmB hexamer, 258 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.3 nm
Dmax 12.2 nm

SASDFH7 – Pseudomonas putida CBB5 NdmAB complex

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 127 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 129 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2018 May 21
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 4.2 nm
Dmax 10.9 nm

SASDFJ7 – Pseudomonas putida CBB5 mCherry-NdmA/ECFP-NdmB complex - static

Methylxanthine N1-demethylase NdmAMethylxanthine N3-demethylase NdmB experimental SAS data
DAMMIF model
Sample: Methylxanthine N1-demethylase NdmA trimer, 207 kDa Pseudomonas putida protein
Methylxanthine N3-demethylase NdmB trimer, 208 kDa Pseudomonas putida protein
Buffer: 20 mM HEPES 150 mM NaCl 2 mM TCEP 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2018 Jul 27
Structural and Mechanistic Insights into Caffeine Degradation by the Bacterial N-Demethylase Complex. J Mol Biol 431(19):3647-3661 (2019)
Kim JH, Kim BH, Brooks S, Kang SY, Summers RM, Song HK
RgGuinier 5.6 nm
Dmax 19.1 nm

SASDBV9 – Immunoglobulin domain 4 of Nucleoporin Pom152 (Pom152 Ig-4: amino acids 718-820)

Nucleoporin POM152 experimental SAS data
MODELLER model
Sample: Nucleoporin POM152 monomer, 12 kDa Saccharomyces cerevisiae (strain ... protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 1.8 nm
Dmax 6.7 nm
VolumePorod 18 nm3

SASDBW9 – Immunoglobulin domains 4,5 of Nucleoporin Pom152 (Pom152 Ig-4,5: amino acids 718-920)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 24 kDa Saccharomyces cerevisiae (strain ... protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 2.7 nm
Dmax 9.4 nm
VolumePorod 23 nm3

SASDBX9 – Immunoglobulin domain 6 of Nucleoporin Pom152 (Pom152 Ig-6: amino acids 919-1020)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 12 kDa Saccharomyces cerevisiae (strain ... protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 2.8 nm
Dmax 7.9 nm
VolumePorod 57 nm3

SASDBY9 – Immunoglobulin domains 3,4 of Nucleoporin Pom152 (Pom152 Ig-3,4: amino acids 603-820)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 26 kDa Saccharomyces cerevisiae (strain ... protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
...Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 3.0 nm
Dmax 10.5 nm
VolumePorod 28 nm3