SASBDB entries for UniProt ID:

SASDCX5 – Monomeric Sortilin at pH 5.5

UniProt ID: Q6PHU5 (None-None) Sortilin 1 A464E alias Neurotensin-receptor 3 A464E
Sortilin 1 A464E alias Neurotensin-receptor 3 A464E experimental SAS data
DAMMIF model
Sample: Sortilin 1 A464E alias Neurotensin-receptor 3 A464E monomer, 76 kDa Mus musculus protein
Buffer: 25 mM MES pH 5.5, 150 mM NaCl, pH: 5.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Apr 17
Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release. Nat Commun 8(1):1708 (2017)
Leloup N, Lössl P, Meijer DH, Brennich M, Heck AJR, Thies-Weesie DME, Janssen BJC
RgGuinier 3.4 nm
Dmax 10.0 nm
VolumePorod 217 nm3

SASDCY5 – Dimeric Sortilin at pH 5.5

UniProt ID: Q6PHU5 (None-None) Sortilin, also: Neurotensin-receptor 3
Sortilin, also: Neurotensin-receptor 3 experimental SAS data
CORAL model
Sample: Sortilin, also: Neurotensin-receptor 3 dimer, 153 kDa Mus musculus protein
Buffer: 25 mM MES pH 5.5, 150 mM NaCl, pH: 5.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Apr 17
Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release. Nat Commun 8(1):1708 (2017)
Leloup N, Lössl P, Meijer DH, Brennich M, Heck AJR, Thies-Weesie DME, Janssen BJC
RgGuinier 3.9 nm
Dmax 11.0 nm
VolumePorod 336 nm3

SASDCZ5 – Monomeric Sortilin at pH 7.4

UniProt ID: Q6PHU5 (None-None) Sortilin 1 A464E alias Neurotensin-receptor 3 A464E
Sortilin 1 A464E alias Neurotensin-receptor 3 A464E experimental SAS data
CORAL model
Sample: Sortilin 1 A464E alias Neurotensin-receptor 3 A464E monomer, 76 kDa Mus musculus protein
Buffer: 25 mM HEPES pH 7.4, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Apr 17
Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release. Nat Commun 8(1):1708 (2017)
Leloup N, Lössl P, Meijer DH, Brennich M, Heck AJR, Thies-Weesie DME, Janssen BJC
RgGuinier 3.3 nm
Dmax 10.5 nm
VolumePorod 217 nm3

SASDC26 – DH-PH - Dbl-homology domain (DH) and Pleckstrin-homology (PH) of Bcr-Abl tyrosine kinase p210

UniProt ID: P11274 (None-None) BCR-ABL p210 fusion protein (DH-PH)
BCR-ABL p210 fusion protein (DH-PH) experimental SAS data
DH-PH - Dbl-homology domain (DH) and Pleckstrin-homology (PH) of Bcr-Abl tyrosine kinase p210 Rg histogram
Sample: BCR-ABL p210 fusion protein (DH-PH) monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, 5% Glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Oct 13
Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase. Nat Commun 8(1):2101 (2017)
Reckel S, Gehin C, Tardivon D, Georgeon S, Kükenshöner T, Löhr F, Koide A, Buchner L, Panjkovich A, Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Güntert P, Dötsch V, Koide S, Gavin AC, Hantschel O
RgGuinier 3.2 nm
Dmax 11.1 nm
VolumePorod 69 nm3

SASDC36 – DH - Dbl-homology domain of Bcr-Abl tyrosine kinase p210

UniProt ID: P11274 (None-None) BCR-ABL p210 fusion protein
BCR-ABL p210 fusion protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: BCR-ABL p210 fusion protein monomer, 25 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, 5% Glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Oct 13
Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase. Nat Commun 8(1):2101 (2017)
Reckel S, Gehin C, Tardivon D, Georgeon S, Kükenshöner T, Löhr F, Koide A, Buchner L, Panjkovich A, Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Güntert P, Dötsch V, Koide S, Gavin AC, Hantschel O
RgGuinier 2.1 nm
Dmax 7.3 nm
VolumePorod 38 nm3

SASDC46 – PH - Pleckstrin-homology domain of Bcr-Abl tyrosine kinase p210

UniProt ID: P11274 (None-None) BCR-ABL p210 fusion protein (PH domain)
BCR-ABL p210 fusion protein (PH domain) experimental SAS data
SREFLEX model
Sample: BCR-ABL p210 fusion protein (PH domain) monomer, 22 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, 5% Glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Nov 10
Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase. Nat Commun 8(1):2101 (2017)
Reckel S, Gehin C, Tardivon D, Georgeon S, Kükenshöner T, Löhr F, Koide A, Buchner L, Panjkovich A, Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Güntert P, Dötsch V, Koide S, Gavin AC, Hantschel O
RgGuinier 2.0 nm
Dmax 6.6 nm
VolumePorod 38 nm3

SASDC56 – Blue light receptor YtvA, dark/inactive state

UniProt ID: O34627 (2-261) pfyP - Blue light photoreceptor
pfyP - Blue light photoreceptor experimental SAS data
GASBOR model
Sample: PfyP - Blue light photoreceptor dimer, 58 kDa Bacillus subtilis protein
Buffer: PBS + 5 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Oct 24
The switch that does not flip: the blue-light receptor YtvA from Bacillus subtilis adopts an elongated dimer conformation independent of the activation state as revealed by a combined AUC and SAXS study. J Mol Biol 403(1):78-87 (2010)
Jurk M, Dorn M, Kikhney A, Svergun D, Gärtner W, Schmieder P
RgGuinier 3.2 nm
Dmax 10.1 nm
VolumePorod 75 nm3

SASDC66 – Blue light receptor YtvA, lit/active state

UniProt ID: O34627 (2-261) pfyP - Blue light photoreceptor
pfyP - Blue light photoreceptor experimental SAS data
GASBOR model
Sample: PfyP - Blue light photoreceptor dimer, 58 kDa Bacillus subtilis protein
Buffer: PBS + 5 mM DTT, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Oct 24
The switch that does not flip: the blue-light receptor YtvA from Bacillus subtilis adopts an elongated dimer conformation independent of the activation state as revealed by a combined AUC and SAXS study. J Mol Biol 403(1):78-87 (2010)
Jurk M, Dorn M, Kikhney A, Svergun D, Gärtner W, Schmieder P
RgGuinier 3.2 nm
Dmax 10.1 nm
VolumePorod 74 nm3

SASDC76 – Extracellular domain of human B-lymphocyte cell receptor CD22

UniProt ID: P20273 (None-None) CD22 extracellular domain
CD22 extracellular domain experimental SAS data
DAMMIF model
Sample: CD22 extracellular domain monomer, 90 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl, pH: 9
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2016 Apr 21
Molecular basis of human CD22 function and therapeutic targeting. Nat Commun 8(1):764 (2017)
Ereño-Orbea J, Sicard T, Cui H, Mazhab-Jafari MT, Benlekbir S, Guarné A, Rubinstein JL, Julien JP
RgGuinier 8.0 nm
Dmax 30.6 nm

SASDC86 – Extracellular domain of human B-lymphocyte cell receptor CD22 in complex with alpha 2,6 sialyllactose

UniProt ID: P20273 (None-None) CD22 extracellular domain

UniProt ID: (None-None) alpha(2,6)-Sialyllactose
CD22 extracellular domainalpha(2,6)-Sialyllactose experimental SAS data
DAMMIF model
Sample: CD22 extracellular domain monomer, 90 kDa Homo sapiens protein
Alpha(2,6)-Sialyllactose, 1 kDa
Buffer: 20 mM Tris 150 mM NaCl, pH: 9
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2016 Apr 21
Molecular basis of human CD22 function and therapeutic targeting. Nat Commun 8(1):764 (2017)
Ereño-Orbea J, Sicard T, Cui H, Mazhab-Jafari MT, Benlekbir S, Guarné A, Rubinstein JL, Julien JP
RgGuinier 8.1 nm
Dmax 29.8 nm