SASBDB entries for UniProt ID:

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

SASDBE4 – Plakin domain of Human desmoplakin

UniProt ID: P15924 (180-1025) Plakin domain of Human Desmoplakin
Plakin domain of Human Desmoplakin experimental SAS data
Plakin domain of Human desmoplakin Rg histogram
Sample: Plakin domain of Human Desmoplakin monomer, 99 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 7.5 nm
Dmax 35.0 nm
VolumePorod 136 nm3

SASDBK4 – The 1:1:3:1 crRNA:Cas6f:Cas7fv:Cas5fv CRISPR/Cas Type I-F short Cascade complex

UniProt ID: (None-None) short-crRNA: CRISPR/Cas Type I-F Cascade component

UniProt ID: A4Y6G3 (1-183) Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)

UniProt ID: A4Y6G1 (1-315) Trimeric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)

UniProt ID: A4Y6G2 (1-336) Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822)
short-crRNA: CRISPR/Cas Type I-F Cascade componentCas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)Trimeric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) experimental SAS data
DAMMIF model
Sample: Short-crRNA: CRISPR/Cas Type I-F Cascade component monomer, 14 kDa Shewanella putrefaciens RNA
Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family) monomer, 21 kDa Shewanella putrefaciens protein
Trimeric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821) trimer, 112 kDa Shewanella putrefaciens protein
Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) monomer, 38 kDa Shewanella putrefaciens protein
Buffer: 50 mM HEPES 150 mM NaCl 1mM DTT 1mM EDTA, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Jun 27
Modulating the Cascade architecture of a minimal Type I-F CRISPR-Cas system. Nucleic Acids Res 44(12):5872-82 (2016)
Gleditzsch D, Müller-Esparza H, Pausch P, Sharma K, Dwarakanath S, Urlaub H, Bange G, Randau L
RgGuinier 4.1 nm
Dmax 14.2 nm

SASDBL4 – The 1:1:6:1 crRNA:Cas6f:Cas7fv:Cas5fv CRISPR/Cas Type I-F wild-type Cascade complex

UniProt ID: A4Y6G3 (1-183) Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)

UniProt ID: A4Y6G2 (1-336) Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822)

UniProt ID: A4Y6G1 (1-315) Hexameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)

UniProt ID: (None-None) wildtype-crRNA: CRISPR/Cas Type I-F Cascade component
Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822)Hexameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)wildtype-crRNA: CRISPR/Cas Type I-F Cascade component experimental SAS data
DAMMIF model
Sample: Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family) monomer, 21 kDa Shewanella putrefaciens protein
Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) monomer, 38 kDa Shewanella putrefaciens protein
Hexameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821) hexamer, 223 kDa Shewanella putrefaciens protein
Wildtype-crRNA: CRISPR/Cas Type I-F Cascade component monomer, 19 kDa RNA
Buffer: 50 mM HEPES 150 mM NaCl 1mM DTT 1mM EDTA, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Jun 27
Modulating the Cascade architecture of a minimal Type I-F CRISPR-Cas system. Nucleic Acids Res 44(12):5872-82 (2016)
Gleditzsch D, Müller-Esparza H, Pausch P, Sharma K, Dwarakanath S, Urlaub H, Bange G, Randau L
RgGuinier 5.4 nm
Dmax 18.4 nm