SASBDB entries for UniProt ID:

SASDME5 – Leucine-rich repeat protein SHOC-2 bound to serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP1C) and Ras-related protein M-Ras

UniProt ID: Q9UQ13 (2-582) Leucine-rich repeat protein SHOC-2

UniProt ID: P36873 (1-323) Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

UniProt ID: O14807 (1-208) Ras-related protein M-Ras
Leucine-rich repeat protein SHOC-2Serine/threonine-protein phosphatase PP1-gamma catalytic subunitRas-related protein M-Ras experimental SAS data
BILBOMD model
Sample: Leucine-rich repeat protein SHOC-2 monomer, 65 kDa Homo sapiens protein
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit monomer, 37 kDa Homo sapiens protein
Ras-related protein M-Ras monomer, 24 kDa Homo sapiens protein
Buffer: 25 mM Tris pH 7.5, 100 mM NaCl, 1 mM TCEP, 1 mM MnCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 20
Structural basis for SHOC2 modulation of RAS signalling. Nature (2022)
Liau NPD, Johnson MC, Izadi S, Gerosa L, Hammel M, Bruning JM, Wendorff TJ, Phung W, Hymowitz SG, Sudhamsu J
RgGuinier 3.5 nm
Dmax 12.4 nm
VolumePorod 215 nm3

SASDMR5 – Tn3 family transposase (TnpA WT)

UniProt ID: M1QZ58 (1-987) TnpA transposase
TnpA transposase experimental SAS data
GASBOR model
Sample: TnpA transposase dimer, 234 kDa Bacillus thuringiensis serovar … protein
Buffer: 50 mM HEPES, 200 mM NaCl, 100 mM L-Arg HCL, pH: 7.9
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Nov 2
AFM-based force spectroscopy unravels stepwise formation of the DNA transposition complex in the widespread Tn3 family mobile genetic elements. Nucleic Acids Res (2023)
Fernandez M, Shkumatov AV, Liu Y, Stulemeijer C, Derclaye S, Efremov RG, Hallet B, Alsteens D
RgGuinier 4.6 nm
Dmax 16.0 nm
VolumePorod 480 nm3

SASDMS5 – Glutathione S-transferase/RNA recognition motif (RRM)-containing protein 4 fusion

UniProt ID: A0A0D1DWZ5 (4-792) RNA recognition motif (RRM)-containing protein 4
RNA recognition motif (RRM)-containing protein 4 experimental SAS data
Glutathione S-transferase/RNA recognition motif (RRM)-containing protein 4 fusion Rg histogram
Sample: RNA recognition motif (RRM)-containing protein 4 monomer, 111 kDa Ustilago maydis protein
Buffer: 20 mM Hepes, 200 mM NaCl, 1 mM βME, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2021 Apr 30
A MademoiseLLE domain binding platform links the key RNA transporter to endosomes PLOS Genetics 18(6):e1010269 (2022)
Devan S, Schott-Verdugo S, Müntjes K, Bismar L, Reiners J, Hachani E, Schmitt L, Höppner A, Smits S, Gohlke H, Feldbrügge M, Mitchell A
RgGuinier 8.8 nm
Dmax 30.7 nm
VolumePorod 587 nm3

SASDMT5 – N-terminal histidine tagged RNA recognition motif (RRM)-containing protein 4 NT4

UniProt ID: A0A0D1DWZ5 (421-792) RNA recognition motif (RRM)-containing protein 4 NT4
RNA recognition motif (RRM)-containing protein 4 NT4 experimental SAS data
N-terminal histidine tagged RNA recognition motif (RRM)-containing protein 4 NT4 Rg histogram
Sample: RNA recognition motif (RRM)-containing protein 4 NT4 monomer, 40 kDa Ustilago maydis protein
Buffer: 20 mM Hepes, 200 mM NaCl, 1 mM βME, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2021 Apr 30
A MademoiseLLE domain binding platform links the key RNA transporter to endosomes PLOS Genetics 18(6):e1010269 (2022)
Devan S, Schott-Verdugo S, Müntjes K, Bismar L, Reiners J, Hachani E, Schmitt L, Höppner A, Smits S, Gohlke H, Feldbrügge M, Mitchell A
RgGuinier 5.6 nm
Dmax 18.5 nm
VolumePorod 123 nm3

SASDMV5 – Kinesin superfamily protein 3 A/B and kinesin associated protein 3 (KAP)

UniProt ID: Q61771 (475-747) Kinesin-like protein KIF3B

UniProt ID: P70188 (1-693) Kinesin-associated protein 3

UniProt ID: P28741 (481-701) Kinesin-like protein KIF3A
Kinesin-like protein KIF3BKinesin-associated protein 3Kinesin-like protein KIF3A experimental SAS data
DAMMIF model
Sample: Kinesin-like protein KIF3B monomer, 32 kDa Mus musculus protein
Kinesin-associated protein 3 monomer, 81 kDa Mus musculus protein
Kinesin-like protein KIF3A monomer, 28 kDa Mus musculus protein
Buffer: 20 mM Tris-HCl, 200 mM NaCl, 5% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BL-15A2, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2020 Jun 24
The two-step cargo recognition mechanism of heterotrimeric kinesin. EMBO Rep :e56864 (2023)
Jiang X, Ogawa T, Yonezawa K, Shimizu N, Ichinose S, Uchihashi T, Nagaike W, Moriya T, Adachi N, Kawasaki M, Dohmae N, Senda T, Hirokawa N
RgGuinier 5.8 nm
Dmax 27.0 nm
VolumePorod 557 nm3

SASDMW5 – Kinesin superfamily protein 3 A/B and kinesin associated protein 3 (KAP) with APC ARM

UniProt ID: Q61315 (338-1010) Adenomatous polyposis coli protein (N-terminal ARM domain)

UniProt ID: P28741 (481-701) Kinesin-like protein KIF3A

UniProt ID: Q61771 (475-747) Kinesin-like protein KIF3B

UniProt ID: P70188 (1-692) Kinesin-associated protein 3
Adenomatous polyposis coli protein (N-terminal ARM domain)Kinesin-like protein KIF3AKinesin-like protein KIF3BKinesin-associated protein 3 experimental SAS data
DAMMIF model
Sample: Adenomatous polyposis coli protein (N-terminal ARM domain) monomer, 75 kDa Mus musculus protein
Kinesin-like protein KIF3A monomer, 28 kDa Mus musculus protein
Kinesin-like protein KIF3B monomer, 32 kDa Mus musculus protein
Kinesin-associated protein 3 monomer, 81 kDa Mus musculus protein
Buffer: 25 mM Tris-HCl, 200 mM NaCl, 1 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2020 Nov 17
The two-step cargo recognition mechanism of heterotrimeric kinesin. EMBO Rep :e56864 (2023)
Jiang X, Ogawa T, Yonezawa K, Shimizu N, Ichinose S, Uchihashi T, Nagaike W, Moriya T, Adachi N, Kawasaki M, Dohmae N, Senda T, Hirokawa N
RgGuinier 5.4 nm
Dmax 19.5 nm
VolumePorod 763 nm3

SASDMX5 – Zea mays beta-amylase (ZmBAM7) short

UniProt ID: B6SVZ0 (69-567) Beta-amylase
Beta-amylase experimental SAS data
Beta-amylase Kratky plot
Sample: Beta-amylase tetramer, 231 kDa Zea mays protein
Buffer: 50 mM HEPES, 25 mM NaCl, and 0.2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 7
The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2 Acta Crystallographica Section D Structural Biology 78(5) (2022)
Ravenburg C, Riney M, Monroe J, Berndsen C
RgGuinier 5.3 nm
Dmax 16.3 nm
VolumePorod 615 nm3

SASDMY5 – Truncated Zea mays beta-amylase (ZmBAM7) short

UniProt ID: B6SVZ0 (69-567) Beta-amylase
Beta-amylase experimental SAS data
Beta-amylase Kratky plot
Sample: Beta-amylase tetramer, 231 kDa Zea mays protein
Buffer: 50 mM HEPES, 25 mM NaCl, and 0.2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 7
The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2 Acta Crystallographica Section D Structural Biology 78(5) (2022)
Ravenburg C, Riney M, Monroe J, Berndsen C
RgGuinier 5.1 nm
Dmax 13.9 nm
VolumePorod 467 nm3

SASDMZ5 – Arabidopsis thaliana beta-amylase 1

UniProt ID: Q9LIR6 (42-575) Beta-amylase 1, chloroplastic
Beta-amylase 1, chloroplastic experimental SAS data
YASARA model
Sample: Beta-amylase 1, chloroplastic monomer, 65 kDa Arabidopsis thaliana protein
Buffer: 50 mM MES, 100 mM NaCl, 1 mM DTT, pH: 6.7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 22
The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2 Acta Crystallographica Section D Structural Biology 78(5) (2022)
Ravenburg C, Riney M, Monroe J, Berndsen C
RgGuinier 2.6 nm
Dmax 9.8 nm
VolumePorod 88 nm3

SASDM26 – Sweet potato beta-amylase 5

UniProt ID: P10537 (2-499) Beta-amylase
Beta-amylase experimental SAS data
Beta-amylase Kratky plot
Sample: Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
Buffer: 20 mM HEPES, 150 mM NaCl, and 0.2 mM TCEP, pH: 7.3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 7
The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2 Acta Crystallographica Section D Structural Biology 78(5) (2022)
Ravenburg C, Riney M, Monroe J, Berndsen C
RgGuinier 4.4 nm
Dmax 14.1 nm
VolumePorod 296 nm3