SASBDB entries for UniProt ID:

SASDG95 – Phosphorylated resistance to inhibitors of cholinesterase 8 homolog A (Ric-8A, 1-491) and G protein complex

UniProt ID: B1H241 (1-491) Resistance to inhibitors of cholinesterase 8 homolog A

UniProt ID: P10824 (24-354) Guanine nucleotide-binding protein G(i) subunit alpha-1
Resistance to inhibitors of cholinesterase 8 homolog AGuanine nucleotide-binding protein G(i) subunit alpha-1 experimental SAS data
DAMMIF model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 56 kDa Rattus norvegicus protein
Guanine nucleotide-binding protein G(i) subunit alpha-1 monomer, 38 kDa Rattus norvegicus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jul 30
Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1 Nature Communications 11(1) (2020)
McClelland L, Zhang K, Mou T, Johnston J, Yates-Hansen C, Li S, Thomas C, Doukov T, Triest S, Wohlkonig A, Tall G, Steyaert J, Chiu W, Sprang S
RgGuinier 3.5 nm
Dmax 11.5 nm
VolumePorod 120 nm3

SASDGA5 – The C-terminal cell-surface signaling domain of the Pseudomonas capeferrum anti-sigma regulator PupR

UniProt ID: Q52209 (110-324) PupR protein
PupR protein experimental SAS data
MULTIFOXS model
Sample: PupR protein monomer, 24 kDa Pseudomonas putida protein
Buffer: 25 mM HEPES 400 mM LiCl 10% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2016 Mar 16
Structural basis of cell surface signaling by a conserved sigma regulator in Gram-negative bacteria. J Biol Chem (2020)
Jensen JL, Jernberg BD, Sinha S, Colbert CL
RgGuinier 2.2 nm
Dmax 7.5 nm
VolumePorod 49 nm3

SASDGB5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) bound to RRESEI peptide

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 3.0 nm
Dmax 13.1 nm
VolumePorod 32 nm3

SASDGC5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) bound to RRESEI peptide (diluted)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 5 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.6 nm
Dmax 12.4 nm
VolumePorod 32 nm3

SASDGD5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) bound to RRESEI peptide (Paused SEC)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.3 nm
Dmax 6.8 nm
VolumePorod 28 nm3

SASDGE5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 9.2 nm
VolumePorod 32 nm3

SASDGF5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) (diluted)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.5 nm
Dmax 9.5 nm
VolumePorod 32 nm3

SASDGG5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) (Paused SEC)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 6.4 nm
VolumePorod 31 nm3

SASDGH5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Sep 16
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.7 nm
Dmax 6.3 nm
VolumePorod 29 nm3

SASDGJ5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH) (diluted)

UniProt ID: P78352 (55-249) PDZ1-2 fragment of PSD-95/Disks large homolog 4
PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 16 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Sep 16
The dual PDZ domain from Postsynaptic density protein 95 forms a scaffold with peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 3.1 nm
Dmax 7.0 nm
VolumePorod 41 nm3