SASBDB entries for UniProt ID:

SASDEF4 – Tryparedoxin K102E, reduced state

UniProt ID: O77404 (None-None) Tryparedoxin K102E
Tryparedoxin K102E experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tryparedoxin K102E monomer, 16 kDa Trypanosoma brucei brucei protein
Buffer: 10 mM HEPES pH 7.5, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 31
Inhibitor-induced dimerization of an essential oxidoreductase from African Trypanosomes. Angew Chem Int Ed Engl (2019)
Wagner A, Le TA, Brennich M, Klein P, Bader N, Diehl E, Paszek D, Weickhmann AK, Dirdjaja N, Krauth-Siegel RL, Engels B, Opatz T, Schindelin H, Hellmich UA
RgGuinier 1.6 nm
Dmax 6.0 nm
VolumePorod 29 nm3

SASDEG4 – Tryparedoxin K102E, oxidized state

UniProt ID: O77404 (None-None) Tryparedoxin K102E
Tryparedoxin K102E experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tryparedoxin K102E monomer, 16 kDa Trypanosoma brucei brucei protein
Buffer: 10 mM HEPES pH 7.5, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 31
Inhibitor-induced dimerization of an essential oxidoreductase from African Trypanosomes. Angew Chem Int Ed Engl (2019)
Wagner A, Le TA, Brennich M, Klein P, Bader N, Diehl E, Paszek D, Weickhmann AK, Dirdjaja N, Krauth-Siegel RL, Engels B, Opatz T, Schindelin H, Hellmich UA
RgGuinier 1.6 nm
Dmax 4.3 nm
VolumePorod 26 nm3

SASDEH4 – Tryparedoxin K102E, in the presence of inhibitor CFT (2-(chloromethyl)-5-(4-fluorophenyl)thieno[2,3-d]pyrimidin-4(3H)-one)

UniProt ID: O77404 (None-None) Tryparedoxin K102E
Tryparedoxin K102E experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tryparedoxin K102E, 16 kDa Trypanosoma brucei brucei protein
Buffer: 10 mM HEPES pH 7.5, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 31
Inhibitor-induced dimerization of an essential oxidoreductase from African Trypanosomes. Angew Chem Int Ed Engl (2019)
Wagner A, Le TA, Brennich M, Klein P, Bader N, Diehl E, Paszek D, Weickhmann AK, Dirdjaja N, Krauth-Siegel RL, Engels B, Opatz T, Schindelin H, Hellmich UA
RgGuinier 1.8 nm
Dmax 6.2 nm
VolumePorod 37 nm3

SASDEM4 – HrpG/HrpV/HrpJ gatekeeper complex from Erwinia amylovora

UniProt ID: D4HVP1 (None-None) Type III secretion protein HrpG

UniProt ID: D4HVP4 (None-None) Type III secretion protein HrpV

UniProt ID: D4HVM8 (None-None) Hypersensitivity response secretion protein HrpJ
Type III secretion protein HrpGType III secretion protein HrpVHypersensitivity response secretion protein HrpJ experimental SAS data
CORAL model
Sample: Type III secretion protein HrpG, 19 kDa Erwinia amylovora protein
Type III secretion protein HrpV, 13 kDa Erwinia amylovora protein
Hypersensitivity response secretion protein HrpJ, 42 kDa Erwinia amylovora protein
Buffer: 20mM Tris-Cl, pH 8.0, 100mM NaCl, 2mM DTT, 0.5mM EDTA, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Apr 3
Migration of Type III Secretion System Transcriptional Regulators Links Gene Expression to Secretion. MBio 9(4) (2018)
Charova SN, Gazi AD, Mylonas E, Pozidis C, Sabarit B, Anagnostou D, Psatha K, Aivaliotis M, Beuzon CR, Panopoulos NJ, Kokkinidis M
RgGuinier 4.0 nm
Dmax 16.0 nm

SASDEN4 – Protein tyrosine phosphatase SHP2

UniProt ID: Q06124-2 (1-529) Tyrosine-protein phosphatase non-receptor type 11
Tyrosine-protein phosphatase non-receptor type 11 experimental SAS data
ALLOSMOD model
Sample: Tyrosine-protein phosphatase non-receptor type 11 monomer, 61 kDa Homo sapiens protein
Buffer: 50 mM ADA, 2 mM TCEP, pH: 6.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2016 Mar 28
Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2. Nat Commun 9(1):4507 (2018)
Pádua RAP, Sun Y, Marko I, Pitsawong W, Stiller JB, Otten R, Kern D
RgGuinier 2.7 nm
Dmax 8.9 nm

SASDEP4 – Protein tyrosine phosphatase SHP2 with E76K activating mutation

UniProt ID: Q06124-2 (1-529) Tyrosine-protein phosphatase non-receptor type 11 E76K
Tyrosine-protein phosphatase non-receptor type 11 E76K experimental SAS data
ALLOSMOD model
Sample: Tyrosine-protein phosphatase non-receptor type 11 E76K monomer, 61 kDa Homo sapiens protein
Buffer: 50 mM ADA, 2 mM TCEP, pH: 6.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2016 Mar 28
Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2. Nat Commun 9(1):4507 (2018)
Pádua RAP, Sun Y, Marko I, Pitsawong W, Stiller JB, Otten R, Kern D
RgGuinier 2.9 nm
Dmax 9.5 nm

SASDES4 – ACA8 in stealth nanodisc (SANS, 100% D2O)

UniProt ID: None (None-None) Membrane scaffold protein 1D1 (deuterated, 75%)

UniProt ID: None (None-None) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)

UniProt ID: Q9LF79 (None-None) Calcium-transporting ATPase 8, plasma membrane-type
Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-type experimental SAS data
Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Calcium-transporting ATPase 8, plasma membrane-type Kratky plot
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl), 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 4.0 nm
Dmax 13.0 nm
VolumePorod 202 nm3

SASDET4 – ACA8 complex with Calmodulin (75% deuterated) in stealth nanodisc (SANS, 100% D2O)

UniProt ID: None (None-None) Membrane scaffold protein 1D1 (deuterated, 75%)

UniProt ID: None (None-None) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)

UniProt ID: Q9LF79 (None-None) Calcium-transporting ATPase 8, plasma membrane-type

UniProt ID: P59220 (None-None) Calmodulin-7 (deuterated 75%)
Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-typeCalmodulin-7 (deuterated 75%) experimental SAS data
ACA8 complex with Calmodulin (75% deuterated) in stealth nanodisc (SANS, 100% D2O) Rg histogram
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl), 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Calmodulin-7 (deuterated 75%) monomer, Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 4.3 nm
Dmax 15.0 nm
VolumePorod 217 nm3

SASDEU4 – ACA8 complex with Calmodulin (hydrogenated) in stealth nanodisc (SANS, 100% D2O)

UniProt ID: None (None-None) Membrane scaffold protein 1D1 (deuterated, 75%)

UniProt ID: None (None-None) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)

UniProt ID: Q9LF79 (None-None) Calcium-transporting ATPase 8, plasma membrane-type

UniProt ID: P59220 (None-None) Calmodulin-7
Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-typeCalmodulin-7 experimental SAS data
Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Calcium-transporting ATPase 8, plasma membrane-type Calmodulin-7 Kratky plot
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl), 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Calmodulin-7 monomer, Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 4.8 nm
Dmax 18.0 nm
VolumePorod 297 nm3

SASDEV4 – ACA8 protein (apo) in stealth nanodisc

UniProt ID: None (None-None) Membrane scaffold protein 1D1 (deuterated, 75%)

UniProt ID: None (None-None) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)

UniProt ID: Q9LF79 (None-None) Calcium-transporting ATPase 8, plasma membrane-type
Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-type experimental SAS data
Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Calcium-transporting ATPase 8, plasma membrane-type Kratky plot
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl), 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 8
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 5.3 nm
Dmax 20.0 nm
VolumePorod 626 nm3