SASBDB entries for UniProt ID:

SASDAF8 – Human Filamin A Ig-like domains 20-21 truncation (2151-2329)

UniProt ID: P21333 (2151-2329) Human Filamin A Ig-like domains 20-21
Human Filamin A Ig-like domains 20-21 experimental SAS data
Human Filamin A Ig-like domains 20-21 Kratky plot
Sample: Human Filamin A Ig-like domains 20-21 monomer, 19 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 2.4 nm
Dmax 8.5 nm
VolumePorod 29 nm3

SASDAG8 – Human Filamin A Ig-like domains 20-21* truncation (2141-2329) in complex with migfilin peptide

UniProt ID: P21333 (2141-2329) Human Filamin A Ig-like domains 20-21*/migfilin peptide complex
Human Filamin A Ig-like domains 20-21*/migfilin peptide complex experimental SAS data
Human Filamin A Ig-like domains 20-21*/migfilin peptide complex Kratky plot
Sample: Human Filamin A Ig-like domains 20-21*/migfilin peptide complex monomer, 23 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 2.4 nm
Dmax 8.2 nm
VolumePorod 33 nm3

SASDAH8 – Human Filamin A Ig-like domains 20-21* truncation (2141-2329)

UniProt ID: P21333 (2141-2329) Human Filamin A Ig-like domains 20-21*
Human Filamin A Ig-like domains 20-21* experimental SAS data
DAMMIF model
Sample: Human Filamin A Ig-like domains 20-21* monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 1.9 nm
Dmax 6.8 nm
VolumePorod 32 nm3

SASDAM8 – MHV-68 LANA

UniProt ID: O41974 (124-316) Latency-associated nuclear antigen
Latency-associated nuclear antigen experimental SAS data
MHV-68 LANA Rg histogram
Sample: Latency-associated nuclear antigen tetramer, 87 kDa Murid herpesvirus 4 protein
Buffer: 25 mM Na/K Phosphate, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Apr 27
KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Res 43(20):10039-54 (2015)
Ponnusamy R, Petoukhov MV, Correia B, Custodio TF, Juillard F, Tan M, Pires de Miranda M, Carrondo MA, Simas JP, Kaye KM, Svergun DI, McVey CE
RgGuinier 4.2 nm
Dmax 16.0 nm
VolumePorod 117 nm3

SASDAQ8 – kLANA mutant dimer-tetramer mixture

UniProt ID: Q9QR71 (1008-1150) ORF73 tetramer

UniProt ID: Q9QR71 (1008-1150) ORF73 dimer
ORF73 tetramerORF73 dimer experimental SAS data
NONE model
Sample: ORF73 tetramer tetramer, 63 kDa Human herpesvirus 8 protein
ORF73 dimer dimer, 32 kDa Human herpesvirus 8 protein
Buffer: 25 mM Na/K Phosphate, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Jun 21
KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Res 43(20):10039-54 (2015)
Ponnusamy R, Petoukhov MV, Correia B, Custodio TF, Juillard F, Tan M, Pires de Miranda M, Carrondo MA, Simas JP, Kaye KM, Svergun DI, McVey CE
RgGuinier 2.4 nm
Dmax 9.5 nm
VolumePorod 50 nm3

SASDAR8 – mLANA 124-316 mLBS1-2 8:1 complex

UniProt ID: (None-None) MHV-68 TR DNA

UniProt ID: O41974 (124-316) Latency-associated nuclear antigen
MHV-68 TR DNALatency-associated nuclear antigen experimental SAS data
CRYSOL model
Sample: MHV-68 TR DNA monomer, 30 kDa unidentified herpesvirus DNA
Latency-associated nuclear antigen octamer, 269 kDa Murid herpesvirus 4 protein
Buffer: 25 mM Na/K Phosphate, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Apr 27
KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Res 43(20):10039-54 (2015)
Ponnusamy R, Petoukhov MV, Correia B, Custodio TF, Juillard F, Tan M, Pires de Miranda M, Carrondo MA, Simas JP, Kaye KM, Svergun DI, McVey CE
RgGuinier 5.8 nm
Dmax 20.0 nm
VolumePorod 475 nm3

SASDAS8 – kLANA 1008-1150 -- kLBS1-2 complex 8:2 (partially dissociated)

UniProt ID: (None-None) kLBS1-2 DNA

UniProt ID: Q9QR71 (1008-1150) ORF73 tetramer

UniProt ID: Q9QR71 (1008-1150) ORF73 octamer

UniProt ID: (None-None) kLBS1-2 DNA two monomers
kLBS1-2 DNAORF73 tetramerORF73 octamerkLBS1-2 DNA two monomers experimental SAS data
NONE model
Sample: KLBS1-2 DNA monomer, 24 kDa unidentified herpesvirus DNA
ORF73 tetramer tetramer, 63 kDa Human herpesvirus 8 protein
ORF73 octamer octamer, 126 kDa Human herpesvirus 8 protein
KLBS1-2 DNA two monomers dimer, 48 kDa unidentified herpesvirus RNA
Buffer: 25 mM Na/K Phosphate, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Apr 27
KSHV but not MHV-68 LANA induces a strong bend upon binding to terminal repeat viral DNA. Nucleic Acids Res 43(20):10039-54 (2015)
Ponnusamy R, Petoukhov MV, Correia B, Custodio TF, Juillard F, Tan M, Pires de Miranda M, Carrondo MA, Simas JP, Kaye KM, Svergun DI, McVey CE
RgGuinier 4.8 nm
Dmax 16.0 nm
VolumePorod 250 nm3

SASDAY8 – Human alphacoronavirus non-structural protein Nsp10 in the presence of Zn

UniProt ID: P0C6U2 (3934-4068) HCoV-229E Non-structural protein 10
HCoV-229E Non-structural protein 10 experimental SAS data
CORAL model
Sample: HCoV-229E Non-structural protein 10 monomer, 15 kDa Human coronavirus 229E protein
Buffer: 25 mM HEPES 280 mM NaCl 2 mM DTT 500 µM ZnCl2, pH: 7.6
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Sep 25
Human alphacoronavirus non-structural protein Nsp10
Sven Falke, Al Kikhney
RgGuinier 1.7 nm
Dmax 5.8 nm

SASDA39 – HCoV-229E Nsp10 in the absence of Zn

UniProt ID: P0C6U2 (3934-4068) HCoV-229E Non-structural protein 10
HCoV-229E Non-structural protein 10 experimental SAS data
CORAL model
Sample: HCoV-229E Non-structural protein 10 monomer, 15 kDa Human coronavirus 229E protein
Buffer: 25 mM HEPES 400 mM NaCl 1 mM EDTA 5% glycerol 40 mM NaH2PO4, pH: 7.9
Experiment: SAXS data collected at EMBL P12, PETRA III on 2011 Sep 8
Human alphacoronavirus non-structural protein Nsp10
Sven Falke, Al Kikhney
RgGuinier 1.9 nm
Dmax 6.9 nm

SASDA89 – Complex between ovine GM-CSF and GM-CSF/IL-2 inhibition factor

UniProt ID: Q9J5U5 (None-None) GM-CSF/IL-2 inhibition factor

UniProt ID: P28773 (18-144) Granulocyte-macrophage colony-stimulating factor
GM-CSF/IL-2 inhibition factorGranulocyte-macrophage colony-stimulating factor experimental SAS data
NONE model
Sample: GM-CSF/IL-2 inhibition factor tetramer, 120 kDa Orf virus protein
Granulocyte-macrophage colony-stimulating factor dimer, 29 kDa Ovis aries protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Sep 10
Structural basis of GM-CSF and IL-2 sequestration by the viral decoy receptor GIF. Nat Commun 7:13228 (2016)
Felix J, Kandiah E, De Munck S, Bloch Y, van Zundert GC, Pauwels K, Dansercoer A, Novanska K, Read RJ, Bonvin AM, Vergauwen B, Verstraete K, Gutsche I, Savvides SN
RgGuinier 3.8 nm
Dmax 12.4 nm
VolumePorod 231 nm3