SASBDB entries for UniProt ID:

SASDBW3 – Human calumenin (sarco-endoplasmic reticulum calcium-sensing protein)

UniProt ID: O43852 (68-315) Human Calumenin
Human Calumenin experimental SAS data
Human Calumenin Kratky plot
Sample: Human Calumenin monomer, 29 kDa Homo sapiens protein
Buffer: 25 mM Na-HEPES, 25 mM NaCl, 2.5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Feb 12
Ca-Dependent Folding of Human Calumenin. PLoS One 11(3):e0151547 (2016)
Mazzorana M, Hussain R, Sorensen T
RgGuinier 2.3 nm
Dmax 6.5 nm
VolumePorod 49 nm3

SASDB54 – Leishmania braziliensis stress-induced protein sti1 (LbHop), full length construct

UniProt ID: A4H5F0 (1-547) Stress-induced protein sti1
Stress-induced protein sti1 experimental SAS data
DAMFILT model
Sample: Stress-induced protein sti1 monomer, 62 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris 100 mM NaCl 1 mM EDTA 1 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2016 Feb 21
Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Arch Biochem Biophys 600:12-22 (2016)
Batista FAH, Seraphim TV, Santos CA, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC
RgGuinier 4.5 nm
Dmax 18.0 nm
VolumePorod 94 nm3

SASDB64 – Leishmania braziliensis stress-induced protein sti1 (LbHop TPR2A-TPR2B-DP2 construct)

UniProt ID: A4H5F0 (171-547) Stress-induced protein sti1 (Hop TPR2A-TPR2B-DP2 construct)
Stress-induced protein sti1 (Hop TPR2A-TPR2B-DP2 construct) experimental SAS data
DAMFILT model
Sample: Stress-induced protein sti1 (Hop TPR2A-TPR2B-DP2 construct) monomer, 44 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris 100 mM NaCl 1 mM EDTA 1 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2016 Feb 21
Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Arch Biochem Biophys 600:12-22 (2016)
Batista FAH, Seraphim TV, Santos CA, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 65 nm3

SASDB74 – CyaA Block I-V

UniProt ID: P0DKX7 (None-None) Adenylate cyclase toxin Block I-V
Adenylate cyclase toxin Block I-V experimental SAS data
DAMMIF model
Sample: Adenylate cyclase toxin Block I-V monomer, 70 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl 150 mM NaCl 10 mM CaCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. Mol Cell 62(1):47-62 (2016)
Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P
RgGuinier 5.6 nm
Dmax 17.2 nm
VolumePorod 275 nm3

SASDB84 – CyaA Block V

UniProt ID: P0DKX7 (None-None) Adenylate cyclase toxin Block V
Adenylate cyclase toxin Block V experimental SAS data
DAMMIF model
Sample: Adenylate cyclase toxin Block V monomer, 16 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl 150 mM NaCl 10 mM CaCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. Mol Cell 62(1):47-62 (2016)
Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P
RgGuinier 1.8 nm
Dmax 5.9 nm
VolumePorod 24 nm3

SASDB94 – Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis

UniProt ID: A0A1Z1SYD5 (64-243) C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein
C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein experimental SAS data
Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis Rg histogram
Sample: C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein monomer, 20 kDa Proteus mirabilis protein
Buffer: 25 mM HEPES 150mM NaCl 1mM DTT, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2012 Feb 29
A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance. Nat Commun 8:16065 (2017)
Furlong EJ, Lo AW, Kurth F, Premkumar L, Totsika M, Achard MES, Halili MA, Heras B, Whitten AE, Choudhury HG, Schembri MA, Martin JL
RgGuinier 3.7 nm
Dmax 10.5 nm
VolumePorod 92 nm3

SASDBA4 – Plakin domain fragment of Human plectin (central region spectrin repeats: SR3-SR4-SR5-SR6 and SH3)

UniProt ID: Q15149-2 (543-1006) Plakin domain fragment of Human plectin encompassing spectrin repeats SR3-SR4-SR5-SR6 and SH3
Plakin domain fragment of Human plectin encompassing spectrin repeats SR3-SR4-SR5-SR6 and SH3 experimental SAS data
DAMMIF model
Sample: Plakin domain fragment of Human plectin encompassing spectrin repeats SR3-SR4-SR5-SR6 and SH3 monomer, 53 kDa Homo sapiens protein
Buffer: 20 mM Sodium Phosphate 150 mM NaCl 5% glycerol 3 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 26
The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape. J Biol Chem 291(36):18643-62 (2016)
Ortega E, Manso JA, Buey RM, Carballido AM, Carabias A, Sonnenberg A, de Pereda JM
RgGuinier 5.1 nm
Dmax 21.0 nm
VolumePorod 91 nm3

SASDBB4 – Plakin domain fragment of Human plectin (C-terminal region spectrin repeats: SR7-SR8-SR9)

UniProt ID: Q15149-2 (1004-1372) Plakin domain fragment of Human plectin encompassing spectrin repeats SR7-SR8-SR9
Plakin domain fragment of Human plectin encompassing spectrin repeats SR7-SR8-SR9 experimental SAS data
DAMMIF model
Sample: Plakin domain fragment of Human plectin encompassing spectrin repeats SR7-SR8-SR9 monomer, 43 kDa Homo sapiens protein
Buffer: 20 mM Sodium Phosphate 150 mM NaCl 5% glycerol 3 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 26
The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape. J Biol Chem 291(36):18643-62 (2016)
Ortega E, Manso JA, Buey RM, Carballido AM, Carabias A, Sonnenberg A, de Pereda JM
RgGuinier 4.2 nm
Dmax 17.0 nm
VolumePorod 57 nm3

SASDBC4 – Plakin domain of Human plectin (spectrin repeats: SR3-SR9)

UniProt ID: Q15149-2 (543-1372) Plakin domain fragment of Human plectin encompassing spectrin repeats SR3-SR9
Plakin domain fragment of Human plectin encompassing spectrin repeats SR3-SR9 experimental SAS data
DAMMIF model
Sample: Plakin domain fragment of Human plectin encompassing spectrin repeats SR3-SR9 monomer, 96 kDa Homo sapiens protein
Buffer: 20 mM Sodium Phosphate 150 mM NaCl 5% glycerol 3 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Aug 13
The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape. J Biol Chem 291(36):18643-62 (2016)
Ortega E, Manso JA, Buey RM, Carballido AM, Carabias A, Sonnenberg A, de Pereda JM
RgGuinier 8.5 nm
Dmax 35.0 nm
VolumePorod 135 nm3

SASDBD4 – Plakin domain fragment of Human desmoplakin (C-terminal region spectrin repeats: SR7-SR8-SR9)

UniProt ID: P15924 (660-1025) Plakin domain fragment of Human Desmoplakin encompassing spectrin repeats SR7-SR8-SR9
Plakin domain fragment of Human Desmoplakin encompassing spectrin repeats SR7-SR8-SR9 experimental SAS data
DAMMIF model
Sample: Plakin domain fragment of Human Desmoplakin encompassing spectrin repeats SR7-SR8-SR9 monomer, 42 kDa Homo sapiens protein
Buffer: 20 mM Sodium Phosphate 150 mM NaCl 5% glycerol 3 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Sep 25
The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape. J Biol Chem 291(36):18643-62 (2016)
Ortega E, Manso JA, Buey RM, Carballido AM, Carabias A, Sonnenberg A, de Pereda JM
RgGuinier 4.4 nm
Dmax 17.5 nm
VolumePorod 69 nm3