SASBDB entries for UniProt ID:

SASDNF6 – full-length MERS CoV N -protein complexed with 5-propoxy-1H-indole (P4-1 compound)

UniProt ID: K9N4V7 (1-411) Nucleoprotein

UniProt ID: None (None-None) 5-(Propoxy)-1H-indole
Nucleoprotein5-(Propoxy)-1H-indole experimental SAS data
CORAL model
Sample: Nucleoprotein dodecamer, 548 kDa Middle East respiratory … protein
5-(Propoxy)-1H-indole dodecamer, 2 kDa
Buffer: 50 mM Tris-HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at 23A, Taiwan Photon Source, NSRRC on 2019 Nov 22
Targeting the N-Terminus Domain of the Coronavirus Nucleocapsid Protein Induces Abnormal Oligomerization via Allosteric Modulation Frontiers in Molecular Biosciences 9 (2022)
Hsu J, Chen J, Lin S, Hong J, Chen Y, Jeng U, Luo S, Hou M
RgGuinier 6.4 nm
Dmax 22.0 nm
VolumePorod 896 nm3

SASDNG6 – full-length MERS CoV N-protein complexed with 5-Isopropoxy-1H-indole (P4-2 compound)

UniProt ID: K9N4V7 (1-411) Nucleoprotein

UniProt ID: None (None-None) 5-Isopropoxy-1H-indole
Nucleoprotein5-Isopropoxy-1H-indole experimental SAS data
CORAL model
Sample: Nucleoprotein dodecamer, 548 kDa Middle East respiratory … protein
5-Isopropoxy-1H-indole dodecamer, 2 kDa
Buffer: 50 mM Tris-HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at 23A, Taiwan Photon Source, NSRRC on 2019 Nov 22
Targeting the N-Terminus Domain of the Coronavirus Nucleocapsid Protein Induces Abnormal Oligomerization via Allosteric Modulation Frontiers in Molecular Biosciences 9 (2022)
Hsu J, Chen J, Lin S, Hong J, Chen Y, Jeng U, Luo S, Hou M
RgGuinier 6.4 nm
Dmax 22.2 nm
VolumePorod 911 nm3

SASDNH6 – full-length MERS CoV N-protein complexed with 5-(2-fluoroethoxy)-1H-indole (P4-3 compound)

UniProt ID: K9N4V7 (1-411) Nucleoprotein

UniProt ID: None (None-None) 5-(2-fluoroethoxy)-1H-indole
Nucleoprotein5-(2-fluoroethoxy)-1H-indole experimental SAS data
CORAL model
Sample: Nucleoprotein tetramer, 183 kDa Middle East respiratory … protein
5-(2-fluoroethoxy)-1H-indole tetramer, 1 kDa
Buffer: 50 mM Tris-HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at 23A, Taiwan Photon Source, NSRRC on 2019 Nov 26
Targeting the N-Terminus Domain of the Coronavirus Nucleocapsid Protein Induces Abnormal Oligomerization via Allosteric Modulation Frontiers in Molecular Biosciences 9 (2022)
Hsu J, Chen J, Lin S, Hong J, Chen Y, Jeng U, Luo S, Hou M
RgGuinier 5.7 nm
Dmax 19.1 nm
VolumePorod 477 nm3

SASDNJ6 – full-length MERS CoV N-protein complexed with 5-(2-methoxyethoxy)-1H-indole (P4-4 compound)

UniProt ID: K9N4V7 (1-411) Nucleoprotein

UniProt ID: None (None-None) 5-(2-methoxyethoxy)-1H-indole
Nucleoprotein5-(2-methoxyethoxy)-1H-indole experimental SAS data
CORAL model
Sample: Nucleoprotein tetramer, 183 kDa Middle East respiratory … protein
5-(2-methoxyethoxy)-1H-indole tetramer, 1 kDa
Buffer: 50 mM Tris-HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at 23A, Taiwan Photon Source, NSRRC on 2019 Nov 26
Targeting the N-Terminus Domain of the Coronavirus Nucleocapsid Protein Induces Abnormal Oligomerization via Allosteric Modulation Frontiers in Molecular Biosciences 9 (2022)
Hsu J, Chen J, Lin S, Hong J, Chen Y, Jeng U, Luo S, Hou M
RgGuinier 6.0 nm
Dmax 18.5 nm
VolumePorod 500 nm3

SASDNK6 – Retinoblastoma protein at 1 mg/ml

UniProt ID: None (None-None) Retinoblastoma-associated protein
Retinoblastoma-associated protein experimental SAS data
Retinoblastoma-associated protein Kratky plot
Sample: Retinoblastoma-associated protein monomer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 14
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 2.4 nm
Dmax 7.4 nm
VolumePorod 66 nm3

SASDNL6 – Retinoblastoma protein at 2 mg/ml

UniProt ID: None (None-None) Retinoblastoma-associated protein
Retinoblastoma-associated protein experimental SAS data
Retinoblastoma-associated protein Kratky plot
Sample: Retinoblastoma-associated protein monomer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 14
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 2.5 nm
Dmax 7.9 nm
VolumePorod 64 nm3

SASDNM6 – Retinoblastoma protein at 4 mg/ml

UniProt ID: None (None-None) Retinoblastoma-associated protein
Retinoblastoma-associated protein experimental SAS data
Retinoblastoma-associated protein Kratky plot
Sample: Retinoblastoma-associated protein monomer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 14
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 2.6 nm
Dmax 10.0 nm
VolumePorod 68 nm3

SASDNN6 – Early E1A protein at 4.2 mg/ml

UniProt ID: None (None-None) Early E1A protein
Early E1A protein experimental SAS data
Early E1A protein Kratky plot
Sample: Early E1A protein monomer, 13 kDa Human adenovirus C … protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Mar 24
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 4.0 nm

SASDNP6 – Early E1A protein at 5.6 mg/ml

UniProt ID: None (None-None) Early E1A protein
Early E1A protein experimental SAS data
Early E1A protein Kratky plot
Sample: Early E1A protein monomer, 13 kDa Human adenovirus C … protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Mar 24
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 4.2 nm

SASDNQ6 – Early E1A protein at 7.0 mg/ml

UniProt ID: None (None-None) Early E1A protein
Early E1A protein experimental SAS data
Early E1A protein Kratky plot
Sample: Early E1A protein monomer, 13 kDa Human adenovirus C … protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Mar 24
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 4.1 nm