SASBDB entries for UniProt ID:

SASDHW2 – The Legionella pneumophila type II secretion system substrate NttE

UniProt ID: A0A4Q5N6R9 (20-288) Uncharacterized protein

Uncharacterized protein experimental SAS data
GASBOR model
Sample: Uncharacterized protein dimer, 66 kDa Legionella pneumophila protein
Buffer: 20 mM Tris, 200 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Sep 18
Structure, Dynamics and Cellular Insight Into Novel Substrates of the Legionella pneumophila Type II Secretion System Frontiers in Molecular Biosciences 7 (2020)
Portlock T, Tyson J, Dantu S, Rehman S, White R, McIntire I, Sewell L, Richardson K, Shaw R, Pandini A, Cianciotto N, Garnett J
RgGuinier 2.9 nm
Dmax 9.4 nm
VolumePorod 114 nm3

SASDHX2 – Dehydrodolichyl diphosphate synthase complex subunit DHDDS

UniProt ID: Q86SQ9 (1-333) Dehydrodolichyl diphosphate synthase complex subunit DHDDS

Dehydrodolichyl diphosphate synthase complex subunit DHDDS experimental SAS data
MODELLER model
Sample: Dehydrodolichyl diphosphate synthase complex subunit DHDDS dimer, 78 kDa Homo sapiens protein
Buffer: Tris-HCl, 150 mM NaCl, 20 mM 2-mercaptoethanol and 0.02% Triton-X100, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 2
Structural Characterization of Full-Length Human Dehydrodolichyl Diphosphate Synthase Using an Integrative Computational and Experimental Approach. Biomolecules 9(11) (2019)
Lisnyansky Bar-El M, Lee SY, Ki AY, Kapelushnik N, Loewenstein A, Chung KY, Schneidman-Duhovny D, Giladi M, Newman H, Haitin Y
RgGuinier 3.2 nm
Dmax 13.0 nm
VolumePorod 122 nm3

SASDHY2 – Human APPL2 (DCC-interacting protein 13-beta)

UniProt ID: Q8NEU8 (1-384) Adaptor protein, phosphotyrosine interaction, pleckstrin homology domain, and leucine zipper-containing protein 2

Adaptor protein, phosphotyrosine interaction, pleckstrin homology domain, and leucine zipper-containing protein 2 experimental SAS data
BUNCH model
Sample: Adaptor protein, phosphotyrosine interaction, pleckstrin homology domain, and leucine zipper-containing protein 2 dimer, 87 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 1 mM DTT, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 7 Apr 20
Membrane curvature protein exhibits interdomain flexibility and binds a small GTPase. J Biol Chem 287(49):40996-1006 (2012)
King GJ, Stöckli J, Hu SH, Winnen B, Duprez WG, Meoli CC, Junutula JR, Jarrott RJ, James DE, Whitten AE, Martin JL
RgGuinier 5.1 nm
Dmax 18.0 nm
VolumePorod 140 nm3

SASDHZ2 – 14-3-3 protein beta isoform

UniProt ID: P31946 (1-246) 14-3-3 protein beta/alpha

14-3-3 protein beta/alpha experimental SAS data
BUNCH model
Sample: 14-3-3 protein beta/alpha dimer, 58 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 92 nm3

SASDH23 – Antigen 43 alpha domain

UniProt ID: None (53-551) Alpha domain of Ag43a

Alpha domain of Ag43a experimental SAS data
DAMMIN model
Sample: Alpha domain of Ag43a monomer, 49 kDa Escherichia coli protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2009 Nov 19
The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping. Proc Natl Acad Sci U S A 111(1):457-62 (2014)
Heras B, Totsika M, Peters KM, Paxman JJ, Gee CL, Jarrott RJ, Perugini MA, Whitten AE, Schembri MA
RgGuinier 3.6 nm
Dmax 12.2 nm
VolumePorod 62 nm3

SASDH33 – Rho GTPase-activating protein 22

UniProt ID: Q7Z5H3 (1-405) Rho GTPase-activating protein 22

Rho GTPase-activating protein 22 experimental SAS data
BUNCH model
Sample: Rho GTPase-activating protein 22 monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.2 nm
Dmax 12.0 nm
VolumePorod 88 nm3

SASDH43 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN)

UniProt ID: P11881 (1-604) N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 5 mM EGTA, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.2 nm
Dmax 10.0 nm
VolumePorod 135 nm3

SASDH53 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with calcium

UniProt ID: P11881 (1-604) N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 10 mM CaCl2, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.4 nm
Dmax 11.0 nm
VolumePorod 160 nm3

SASDH63 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with bound inositol 1,4,5-trisphosphate (IP3)

UniProt ID: P11881 (1-604) N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 5 mM EGTA, 0.25 mM IP3, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.1 nm
Dmax 8.8 nm
VolumePorod 115 nm3

SASDH73 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with bound inositol 1,4,5-trisphosphate (IP3) plus calcium

UniProt ID: P11881 (1-604) N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 10 mM CaCl2, 0.25 mM IP3, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.2 nm
Dmax 9.6 nm
VolumePorod 132 nm3