Browse by MODEL: Hybrid

SASDHX3 – Hyperstable de novo protein Super WA20 (SUWA)

Hyperstable de novo protein Super WA20 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Hyperstable de novo protein Super WA20 dimer, 25 kDa de novo protein protein
Buffer: 20 mM HEPES, 100 mM NaCl, 200 mM ArgHCl, 10% glycerol,, pH: 7.5
Experiment: SAXS data collected at BL-6A, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2016 Feb 26
Hyperstable De Novo Protein with a Dimeric Bisecting Topology. ACS Synth Biol (2020)
Kimura N, Mochizuki K, Umezawa K, Hecht MH, Arai R
RgGuinier 2.7 nm
Dmax 10.0 nm

SASDGS5 – MvaT (low salt data set)

MvaT(mutant) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: MvaT(mutant) dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 20 mM Bis-Tris 50 mM KCl, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins. Nucleic Acids Res (2020)
Qin L, Bdira FB, Sterckx YGJ, Volkov AN, Vreede J, Giachin G, van Schaik P, Ubbink M, Dame RT
RgGuinier 3.6 nm
Dmax 14.7 nm
VolumePorod 47 nm3

SASDGT5 – MvaT (high salt data set)

MvaT(mutant) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: MvaT(mutant) dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 20 mM Bis-Tris 300 mM KCl, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins. Nucleic Acids Res (2020)
Qin L, Bdira FB, Sterckx YGJ, Volkov AN, Vreede J, Giachin G, van Schaik P, Ubbink M, Dame RT
RgGuinier 3.8 nm
Dmax 15.8 nm
VolumePorod 50 nm3

SASDH44 – 3' Complex of XPA-DBD and RPA70AB

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

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

SASDHP7 – Haloalkane dehalogenase variant DhaA115 - monomeric fraction

Haloalkane dehalogenase variant DhaA115 -monomeric fraction experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Haloalkane dehalogenase variant DhaA115 -monomeric fraction monomer, 34 kDa Rhodococcus rhodochrous protein
Buffer: 50 mM potassium phosphate buffer (41 mM K₂HPO₄, 9mM KH₂PO₄), pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2019 Aug 22
Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst Chemical Science 11(41):11162-11178 (2020)
Markova K, Chmelova K, Marques S, Carpentier P, Bednar D, Damborsky J, Marek M
RgGuinier 1.9 nm
Dmax 6.0 nm
VolumePorod 41 nm3

SASDHQ7 – Haloalkane dehalogenase variant DhaA115 - dimeric fraction

Haloalkane dehalogenase variant DhaA115 - dimeric fraction experimental SAS data
CORAL model
Sample: Haloalkane dehalogenase variant DhaA115 - dimeric fraction dimer, 69 kDa Rhodococcus rhodochrous protein
Buffer: 50 mM potassium phosphate buffer (41 mM K₂HPO₄, 9mM KH₂PO₄), pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2019 Aug 22
Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst Chemical Science 11(41):11162-11178 (2020)
Markova K, Chmelova K, Marques S, Carpentier P, Bednar D, Damborsky J, Marek M
RgGuinier 2.9 nm
Dmax 8.9 nm
VolumePorod 78 nm3

SASDF29 – Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 4 - in complex with STAU1 binding site within the ADP-ribosylation factor1

Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 4ADP-ribosylation factor1 - short experimental SAS data
OTHER model
Sample: Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 4 monomer, 8 kDa Homo sapiens protein
ADP-ribosylation factor1 - short monomer, 11 kDa Homo sapiens RNA
Buffer: 50 mM potassium phosphate, 100 mM NaCl, 3.5 mM 2-mercaptoethanol, pH: 6.8
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2015 Dec 10
Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition. Nucleic Acids Res (2019)
Yadav DK, Zigáčková D, Zlobina M, Klumpler T, Beaumont C, Kubíčková M, Vaňáčová Š, Lukavsky PJ
RgGuinier 1.7 nm
Dmax 6.0 nm
VolumePorod 21 nm3

SASDF39 – Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4 - in complex with STAU1 binding site within the ADP-ribosylation factor1

ADP-ribosylation factor1 - shortDouble-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4 experimental SAS data
OTHER model
Sample: ADP-ribosylation factor1 - short monomer, 11 kDa Homo sapiens RNA
Double-stranded RNA-binding protein Staufen homolog 1 - RNA binding domain 3 and 4 monomer, 20 kDa Homo sapiens protein
Buffer: 50 mM sodium phosphate buffer, 300 mM NaCl, 500 mM imidazole, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2018 May 29
Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition. Nucleic Acids Res (2019)
Yadav DK, Zigáčková D, Zlobina M, Klumpler T, Beaumont C, Kubíčková M, Vaňáčová Š, Lukavsky PJ
RgGuinier 2.1 nm
Dmax 6.4 nm
VolumePorod 39 nm3

SASDCQ6 – Rap guanine nucleotide exchange factor 3 (isoform3) - apo form

Rap guanine nucleotide exchange factor 3 experimental SAS data
SWISSMODEL model
Sample: Rap guanine nucleotide exchange factor 3 monomer, 100 kDa Homo sapiens protein
Buffer: 1mM EDTA, 10mM DTT, 500mM NaCl, and 10mM Tris, pH: 9
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2012 Sep 7
Conformational States of Exchange Protein Directly Activated by cAMP (EPAC1) Revealed by Ensemble Modeling and Integrative Structural Biology. Cells 9(1) (2019)
White MA, Tsalkova T, Mei FC, Cheng X
RgGuinier 3.4 nm
Dmax 11.0 nm
VolumePorod 180 nm3