SASBDB entries for UniProt ID:

SASDCH6 – GGDEF domain from Marinobacter aquaeolei diguanylate cyclase complexed with c-di-GMP - Northeast Structural Genomics Consortium Target MqR89a

UniProt ID: A1U3W3 (None-None) Diguanylate cyclase
Diguanylate cyclase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Diguanylate cyclase monomer, 20 kDa Marinobacter hydrocarbonoclasticus protein
Buffer: 5 mM DTT 100 mM NaCl 10 mM Tris-HCl 0.02 % NaN3, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2010 Feb 12
Small angle X-ray scattering as a complementary tool for high-throughput structural studies. Biopolymers 95(8):517-30 (2011)
Grant TD, Luft JR, Wolfley JR, Tsuruta H, Martel A, Montelione GT, Snell EH
RgGuinier 1.9 nm
Dmax 6.6 nm
VolumePorod 32 nm3

SASDCJ6 – MmoQ Response regulator (fragment 20-298) from Methylococcus capsulatus str. Bath, Northeast Structural Genomics Consortium Target McR175G

UniProt ID: Q7WZ31 (None-None) MmoQ
MmoQ experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: MmoQ monomer, 32 kDa Methylococcus capsulatus protein
Buffer: 5 mM DTT 100 mM NaCl 10 mM Tris-HCl 0.02 % NaN3, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2010 Feb 12
Small angle X-ray scattering as a complementary tool for high-throughput structural studies. Biopolymers 95(8):517-30 (2011)
Grant TD, Luft JR, Wolfley JR, Tsuruta H, Martel A, Montelione GT, Snell EH
RgGuinier 2.3 nm
Dmax 8.2 nm
VolumePorod 62 nm3

SASDCK6 – Sheath tail protein (DSY3957) from Desulfitobacterium hafniense, Northeast Structural Genomics Consortium Target DhR18

UniProt ID: Q24QE6 (None-None) Uncharacterized protein
Uncharacterized protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Uncharacterized protein monomer, 48 kDa Desulfitobacterium hafniense protein
Buffer: 5 mM DTT 100 mM NaCl 10 mM Tris-HCl 0.02 % NaN3, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2010 Feb 12
Small angle X-ray scattering as a complementary tool for high-throughput structural studies. Biopolymers 95(8):517-30 (2011)
Grant TD, Luft JR, Wolfley JR, Tsuruta H, Martel A, Montelione GT, Snell EH
RgGuinier 2.8 nm
Dmax 9.9 nm
VolumePorod 66 nm3

SASDCL6 – Lys63-linked dimer ubiquitin

UniProt ID: P0CG48 (305-379) Polyubiquitin-C
Polyubiquitin-C experimental SAS data
Polyubiquitin-C Kratky plot
Sample: Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
Buffer: 100mM NaCl, 10mM sodium acetate, pH: 6
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2016 Mar 24
Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition. Elife 4 (2015)
Liu Z, Gong Z, Jiang WX, Yang J, Zhu WK, Guo DC, Zhang WP, Liu ML, Tang C
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 24 nm3

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

UniProt ID: O95398-3 (2-881) Rap guanine nucleotide exchange factor 3
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

SASDCR6 – Rap guanine nucleotide exchange factor 3 (isoform3) - binary form with cAMP

UniProt ID: O95398-3 (2-881) Rap guanine nucleotide exchange factor 3 (dimer)
Rap guanine nucleotide exchange factor 3 (dimer) experimental SAS data
CORAL model
Sample: Rap guanine nucleotide exchange factor 3 (dimer) dimer, 200 kDa Homo sapiens protein
Buffer: 1mM EDTA, 10mM DTT, 500mM NaCl, 1mM cAMP, and 10mM Tris, pH: 9
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2012 Jan 30
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 5.3 nm
Dmax 15.7 nm
VolumePorod 415 nm3

SASDCS6 – Rap guanine nucleotide exchange factor 3 (isoform3) bound to RAS related protein 1b - with cAMP

UniProt ID: O95398-3 (2-881) Rap guanine nucleotide exchange factor 3

UniProt ID: Q52L50 (1-167) RAS related protein 1b
Rap guanine nucleotide exchange factor 3RAS related protein 1b experimental SAS data
SWISSMODEL model
Sample: Rap guanine nucleotide exchange factor 3 monomer, 100 kDa Homo sapiens protein
RAS related protein 1b monomer, 18 kDa Mus musculus protein
Buffer: 1mM EDTA, 10mM DTT, 500mM NaCl, 1mM cAMP, and 10mM Tris, pH: 9
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2013 Apr 1
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 4.1 nm
Dmax 14.2 nm
VolumePorod 207 nm3

SASDCT6 – 12N12 nucleosome in 60% sucrose with ADP-BeF3

UniProt ID: (None-None) 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)

UniProt ID: P06897 (None-None) Histone H2A type 1

UniProt ID: P02281 (None-None) Histone H2B 1.1

UniProt ID: P84233 (1-136) Histone H3.2

UniProt ID: P62799 (None-None) Histone H4
169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)Histone H2A type 1Histone H2B 1.1Histone H3.2Histone H4 experimental SAS data
12N12 nucleosome in 60% sucrose with ADP-BeF3 Rg histogram
Sample: 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA) monomer, 52 kDa DNA
Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein
Histone H2B 1.1 monomer, 14 kDa Xenopus laevis protein
Histone H3.2 monomer, 15 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, ADP-BeF3 (0.5 mM ADP, 4 mM NaF, 0.6 mM BeCl2), pH: 7.8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 24
The ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome. Nucleic Acids Res 46(10):4978-4990 (2018)
Tokuda JM, Ren R, Levendosky RF, Tay RJ, Yan M, Pollack L, Bowman GD
RgGuinier 4.8 nm
Dmax 14.0 nm

SASDCU6 – Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose without any nucleotides added (Apo)

UniProt ID: P32657 (118-1274) Chromodomain-helicase-DNA-binding protein 1

UniProt ID: (None-None) 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)

UniProt ID: P06897 (None-None) Histone H2A type 1

UniProt ID: P02281 (None-None) Histone H2B 1.1

UniProt ID: P84233 (1-136) Histone H3.2

UniProt ID: P62799 (None-None) Histone H4
Chromodomain-helicase-DNA-binding protein 1169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)Histone H2A type 1Histone H2B 1.1Histone H3.2Histone H4 experimental SAS data
Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose without any nucleotides added (Apo) Rg histogram
Sample: Chromodomain-helicase-DNA-binding protein 1 dimer, 266 kDa Saccharomyces cerevisiae protein
169 bp DNA (145 bp Widom 601, flanked by 12bp DNA) monomer, 52 kDa DNA
Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein
Histone H2B 1.1 monomer, 14 kDa Xenopus laevis protein
Histone H3.2 monomer, 15 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, pH: 7.8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 24
The ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome. Nucleic Acids Res 46(10):4978-4990 (2018)
Tokuda JM, Ren R, Levendosky RF, Tay RJ, Yan M, Pollack L, Bowman GD
RgGuinier 5.2 nm
Dmax 12.8 nm

SASDCV6 – Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with ADP-BeF3

UniProt ID: P32657 (118-1274) Chromodomain-helicase-DNA-binding protein 1

UniProt ID: (None-None) 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)

UniProt ID: P06897 (None-None) Histone H2A type 1

UniProt ID: P02281 (None-None) Histone H2B 1.1

UniProt ID: P84233 (1-136) Histone H3.2

UniProt ID: P62799 (None-None) Histone H4
Chromodomain-helicase-DNA-binding protein 1169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)Histone H2A type 1Histone H2B 1.1Histone H3.2Histone H4 experimental SAS data
Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with ADP-BeF3 Rg histogram
Sample: Chromodomain-helicase-DNA-binding protein 1 dimer, 266 kDa Saccharomyces cerevisiae protein
169 bp DNA (145 bp Widom 601, flanked by 12bp DNA) monomer, 52 kDa DNA
Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein
Histone H2B 1.1 monomer, 14 kDa Xenopus laevis protein
Histone H3.2 monomer, 15 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, ADP-BeF3 (0.5 mM ADP, 4 mM NaF, 0.6 mM BeCl2), pH: 7.8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 24
The ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome. Nucleic Acids Res 46(10):4978-4990 (2018)
Tokuda JM, Ren R, Levendosky RF, Tay RJ, Yan M, Pollack L, Bowman GD
RgGuinier 5.3 nm
Dmax 16.5 nm