SASBDB entries for UniProt ID:

SASDH83 – Chemically crossed linked complex between Rho GTPase-activating protein 22 (ARHGAP22) and the beta isoform of the 14-3-3 protein beta/alpha

UniProt ID: P31946 (1-246) 14-3-3 protein beta/alpha

UniProt ID: Q7Z5H3 (1-405) Rho GTPase-activating protein 22
14-3-3 protein beta/alphaRho GTPase-activating protein 22 experimental SAS data
CORAL model
Sample: 14-3-3 protein beta/alpha dimer, 58 kDa Homo sapiens protein
Rho GTPase-activating protein 22 monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 195 nm3

SASDHK3 – Braveheart RNA + Cellular nucleic acid-binding protein (CNBP)

UniProt ID: None (None-None) Braveheart RNA

UniProt ID: P62633 (1-177) Cellular nucleic acid-binding protein
Braveheart RNACellular nucleic acid-binding protein experimental SAS data
DAMMIN model
Sample: Braveheart RNA monomer, 205 kDa Homo sapiens RNA
Cellular nucleic acid-binding protein monomer, 22 kDa Homo sapiens protein
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 23
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 9.8 nm
Dmax 30.2 nm
VolumePorod 1660 nm3

SASDHL3 – Braveheart Fragment 1 + Cellular nucleic acid-binding protein (CNBP)

UniProt ID: P62633 (1-177) Cellular nucleic acid-binding protein

UniProt ID: None (None-None) Braveheart Fragment 1
Cellular nucleic acid-binding proteinBraveheart Fragment 1 experimental SAS data
DAMMIN model
Sample: Cellular nucleic acid-binding protein monomer, 22 kDa Homo sapiens protein
Braveheart Fragment 1 monomer, 116 kDa Homo sapiens RNA
Buffer: 50 mM HEPES-KOH, 100 mM KCl, 6 mM MgCl2, pH: 7.6
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Jun 23
Zinc-finger protein CNBP alters the 3-D structure of lncRNA Braveheart in solution Nature Communications 11(1) (2020)
Kim D, Thiel B, Mrozowich T, Hennelly S, Hofacker I, Patel T, Sanbonmatsu K
RgGuinier 8.2 nm
Dmax 27.0 nm
VolumePorod 455 nm3

SASDHY3 – KinA-Sda complex

UniProt ID: P16497 (383-606) Sporulation kinase A

UniProt ID: Q7WY62 (7-52) Sporulation inhibitor sda
Sporulation kinase ASporulation inhibitor sda experimental SAS data
SASREF model
Sample: Sporulation kinase A dimer, 51 kDa Bacillus subtilis protein
Sporulation inhibitor sda dimer, 11 kDa Bacillus subtilis protein
Buffer: 50mM Tris, 200mM NaCl, 150mM Imidazole, pH: 8.5
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Nov 16
The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. J Mol Biol 368(2):407-20 (2007)
Whitten AE, Jacques DA, Hammouda B, Hanley T, King GF, Guss JM, Trewhella J, Langley DB
RgGuinier 2.9 nm
Dmax 8.0 nm
VolumePorod 85 nm3

SASDHZ3 – Sporulation kinase A

UniProt ID: P16497 (383-606) Sporulation kinase A
Sporulation kinase A experimental SAS data
SASREF model
Sample: Sporulation kinase A dimer, 51 kDa Bacillus subtilis protein
Buffer: 50mM Tris, 200mM NaCl, 150mM Imidazole, pH: 8.5
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Mar 18
The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. J Mol Biol 368(2):407-20 (2007)
Whitten AE, Jacques DA, Hammouda B, Hanley T, King GF, Guss JM, Trewhella J, Langley DB
RgGuinier 2.9 nm
Dmax 9.5 nm
VolumePorod 76 nm3

SASDH24 – Calcium-Activated Chloride Channel Regulator 1 VWA domain

UniProt ID: A8K7I4 (302-476) Calcium-activated chloride channel regulator 1
Calcium-activated chloride channel regulator 1 experimental SAS data
DAMFILT model
Sample: Calcium-activated chloride channel regulator 1 monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Jun 6
Structural and Biophysical Analysis of the CLCA1 VWA Domain Suggests Mode of TMEM16A Engagement. Cell Rep 30(4):1141-1151.e3 (2020)
Berry KN, Brett TJ
RgGuinier 1.8 nm
Dmax 6.6 nm

SASDH34 – Calcium-Activated Chloride Channel Regulator 1 CAT-CYS-VWA domain construct

UniProt ID: A8K7I4 (22-477) Calcium-activated chloride channel regulator 1
Calcium-activated chloride channel regulator 1 experimental SAS data
DAMFILT model
Sample: Calcium-activated chloride channel regulator 1 monomer, 52 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Jun 6
Structural and Biophysical Analysis of the CLCA1 VWA Domain Suggests Mode of TMEM16A Engagement. Cell Rep 30(4):1141-1151.e3 (2020)
Berry KN, Brett TJ
RgGuinier 3.4 nm
Dmax 13.4 nm

SASDH44 – 3' Complex of XPA-DBD and RPA70AB

UniProt ID: P23025 (98-239) DNA repair protein complementing XP-A cells

UniProt ID: P27694 (183-420) Replication protein A 70 kDa DNA-binding subunit

UniProt ID: None (None-None) 3-prime Nucleotide Excision Repair Junction Model Substrate
DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunit3-prime Nucleotide Excision Repair Junction Model Substrate experimental SAS data
HADDOCK model
Sample: DNA repair protein complementing XP-A cells monomer, 17 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 27 kDa Homo sapiens protein
3-prime Nucleotide Excision Repair Junction Model Substrate monomer, 11 kDa DNA
Buffer: 20 mM Tris, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 17 Nov 2
A key interaction with RPA orients XPA in NER complexes. Nucleic Acids Res (2020)
Topolska-Woś AM, Sugitani N, Cordoba JJ, Le Meur KV, Le Meur RA, Kim HS, Yeo JE, Rosenberg D, Hammel M, Schärer OD, Chazin WJ
RgGuinier 3.1 nm
Dmax 9.7 nm
VolumePorod 103 nm3

SASDH54 – 5' Complex of XPA-DBD with RPA70AB

UniProt ID: P23025 (98-239) DNA repair protein complementing XP-A cells

UniProt ID: P27694 (183-420) Replication protein A 70 kDa DNA-binding subunit

UniProt ID: None (None-None) 5-prime Nucleotide Excision Repair Junction Model Substrate
DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunit5-prime Nucleotide Excision Repair Junction Model Substrate experimental SAS data
HADDOCK model
Sample: DNA repair protein complementing XP-A cells monomer, 17 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 27 kDa Homo sapiens protein
5-prime Nucleotide Excision Repair Junction Model Substrate monomer, 11 kDa DNA
Buffer: 20 mM Tris, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 4
A key interaction with RPA orients XPA in NER complexes. Nucleic Acids Res (2020)
Topolska-Woś AM, Sugitani N, Cordoba JJ, Le Meur KV, Le Meur RA, Kim HS, Yeo JE, Rosenberg D, Hammel M, Schärer OD, Chazin WJ
RgGuinier 2.9 nm
Dmax 97.0 nm
VolumePorod 87 nm3

SASDH64 – Plasmodium falciparum myosin essential light chain, N-terminal domain

UniProt ID: Q8IJM4 (1-74) Myosin essential light chain
Myosin essential light chain experimental SAS data
PYMOL model
Sample: Myosin essential light chain monomer, 9 kDa Plasmodium falciparum protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Oct 25
Structural role of essential light chains in the apicomplexan glideosome. Commun Biol 3(1):568 (2020)
Pazicky S, Dhamotharan K, Kaszuba K, Mertens HDT, Gilberger T, Svergun D, Kosinski J, Weininger U, Löw C
RgGuinier 1.4 nm
Dmax 4.3 nm
VolumePorod 12 nm3