SASBDB entries for UniProt ID:

SASDBR2 – Contactin-associated protein-like 2 (Caspr2) extracellular domains 1-1261.

UniProt ID: Q9UHC6 (1-1261) Contactin-associated protein-like 2 extracellular domains (1-1261)

Contactin-associated protein-like 2 extracellular domains (1-1261) experimental SAS data
DAMMIN model
Sample: Contactin-associated protein-like 2 extracellular domains (1-1261) monomer, 140 kDa Homo sapiens protein
Buffer: 10 mM HEPES 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2010 Oct 4
Structural Characterization of the Extracellular Domain of CASPR2 and Insights into Its Association with the Novel Ligand Contactin1. J Biol Chem 291(11):5788-802 (2016)
Rubio-Marrero EN, Vincelli G, Jeffries CM, Shaikh TR, Pakos IS, Ranaivoson FM, von Daake S, Demeler B, De Jaco A, Perkins G, Ellisman MH, Trewhella J, Comoletti D
RgGuinier 4.4 nm
Dmax 14.5 nm
VolumePorod 282 nm3

SASDBS2 – Recombinant Tn antigen-binding lectin from Vatairea macrocarpa

UniProt ID: P81371 (None-None) Recombinant Tn antigen-binding lectin

Recombinant Tn antigen-binding lectin experimental SAS data
CORAL model
Sample: Recombinant Tn antigen-binding lectin tetramer, 105 kDa Vatairea macrocarpa protein
Buffer: 100 mM sodium phosphate 150 mM NaCl 5% (v/v) glycerol, pH: 5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 11
Structural characterization of a Vatairea macrocarpa lectin in complex with a tumor-associated antigen: A new tool for cancer research. Int J Biochem Cell Biol 72:27-39 (2016)
Sousa BL, Silva-Filho JC, Kumar P, Graewert MA, Pereira RI, Cunha RMS, Nascimento KS, Bezerra GA, Delatorre P, Djinovic-Carugo K, Nagano CS, Gruber K, Cavada BS
RgGuinier 3.2 nm
Dmax 9.5 nm
VolumePorod 168 nm3

SASDBT2 – Ankyrin repeat domains from human Tankyrase-2 (489-649)

UniProt ID: Q9H2K2 (489-649) Ankyrin repeat domains from Tankyrase 2

Ankyrin repeat domains from Tankyrase 2 experimental SAS data
Ankyrin repeat domains from Tankyrase 2 Kratky plot
Sample: Ankyrin repeat domains from Tankyrase 2 monomer, 18 kDa Homo sapiens protein
Buffer: 50 mM HEPES 100mM NaCl 1mM TCEP, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Dec 4
Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Structure 24(2):252-60 (2016)
Fetics S, Thureau A, Campanacci V, Aumont-Nicaise M, Dang I, Gautreau A, Pérez J, Cherfils J
RgGuinier 1.8 nm
Dmax 6.3 nm
VolumePorod 24 nm3

SASDBU2 – Human Arpin (isoform 1)

UniProt ID: Q7Z6K5 (None-None) Human Arpin

Human Arpin experimental SAS data
Human Arpin Kratky plot
Sample: Human Arpin monomer, 25 kDa Homo sapiens protein
Buffer: 50 mM HEPES 100mM NaCl 1mM TCEP, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Dec 4
Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Structure 24(2):252-60 (2016)
Fetics S, Thureau A, Campanacci V, Aumont-Nicaise M, Dang I, Gautreau A, Pérez J, Cherfils J
RgGuinier 2.6 nm
Dmax 13.2 nm
VolumePorod 47 nm3

SASDBV2 – Zebrafish Arpin

UniProt ID: Q1LWJ6 (None-None) Zebrafish (Danio rerio) Arpin

Zebrafish (Danio rerio) Arpin experimental SAS data
Zebrafish (Danio rerio) Arpin Kratky plot
Sample: Zebrafish (Danio rerio) Arpin monomer, 25 kDa Danio rerio protein
Buffer: 50 mM HEPES 100mM NaCl 1mM TCEP, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Dec 4
Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Structure 24(2):252-60 (2016)
Fetics S, Thureau A, Campanacci V, Aumont-Nicaise M, Dang I, Gautreau A, Pérez J, Cherfils J
RgGuinier 2.7 nm
Dmax 13.8 nm
VolumePorod 47 nm3

SASDBW2 – Zebrafish (Danio rerio) Arpin truncated C-terminal mutant (delta-C 16).

UniProt ID: Q1LWJ6 (1-210) Zebrafish (Danio rerio) Arpin truncated C-terminal mutant (delta-C 16).

Zebrafish (Danio rerio) Arpin truncated C-terminal mutant (delta-C 16). experimental SAS data
Zebrafish (Danio rerio) Arpin truncated C-terminal mutant (delta-C 16). Kratky plot
Sample: Zebrafish (Danio rerio) Arpin truncated C-terminal mutant (delta-C 16). monomer, 24 kDa Danio rerio protein
Buffer: 50 mM HEPES 100mM NaCl 1mM TCEP, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Dec 4
Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope. Structure 24(2):252-60 (2016)
Fetics S, Thureau A, Campanacci V, Aumont-Nicaise M, Dang I, Gautreau A, Pérez J, Cherfils J
RgGuinier 2.2 nm
Dmax 11.3 nm
VolumePorod 37 nm3

SASDBY2 – Inorganic pyrophosphatase (PPase) from E. coli

UniProt ID: P0A7A9 (None-None) Inorganic pyrophosphatase (PPase) from E. coli

Inorganic pyrophosphatase (PPase) from E. coli experimental SAS data
DAMMIN model
Sample: Inorganic pyrophosphatase (PPase) from E. coli hexamer, 117 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 30
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 3.0 nm
Dmax 9.0 nm
VolumePorod 166 nm3

SASDBZ2 – Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli

UniProt ID: A0A0K4BP99 (None-None) Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli

Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli experimental SAS data
DAMMIN model
Sample: Class I fructose-1,6-bisphosphate aldolase (FbaB) from E. coli decamer, 381 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 30
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.4 nm
Dmax 12.7 nm
VolumePorod 484 nm3

SASDB23 – 5-keto-4-deoxyuronate isomerase (KduI) from E. coli

UniProt ID: Q46938 (None-None) 5-keto-4-deoxyuronate isomerase (KduI) from E. coli

5-keto-4-deoxyuronate isomerase (KduI) from E. coli experimental SAS data
NONE model
Sample: 5-keto-4-deoxyuronate isomerase (KduI) from E. coli None, Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 20
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.5 nm

SASDB33 – Glutamate decarboxylase alpha (GadA) from E. coli

UniProt ID: P69908 (None-None) Glutamate decarboxylase alpha (GadA) from E. coli

Glutamate decarboxylase alpha (GadA) from E. coli experimental SAS data
SASREF MX model
Sample: Glutamate decarboxylase alpha (GadA) from E. coli monomer, 53 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 20
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.8 nm
VolumePorod 410 nm3