SASBDB entries for UniProt ID:

SASDTK8 – Heterogeneous nuclear ribonucleoprotein A1-A mutant (hnRNP A1-A(mut)) at 250 MPa

UniProt ID: P09651-2 (2-320) Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 34 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 3.6 nm

SASDTL8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 0.1 MPa

UniProt ID: P09651 (1-196) Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 25 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 2.8 nm

SASDTM8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 50 MPa

UniProt ID: P09651 (1-196) Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 25 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 3.0 nm

SASDTN8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 100 MPa

UniProt ID: P09651 (1-196) Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 25 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 3.2 nm

SASDTP8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 150 MPa

UniProt ID: P09651 (1-196) Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 25 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 2.9 nm

SASDTQ8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 200 MPa

UniProt ID: P09651 (1-196) Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 25 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 3.1 nm

SASDTR8 – UP1 domain mutant of heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) at 250 MPa

UniProt ID: P09651 (1-196) Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S )

Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) experimental SAS data
Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) Kratky plot
Sample: Heterogeneous nuclear ribonucleoprotein A1 (C43S/R75D/R88D/C175S ) monomer, 25 kDa Homo sapiens protein
Buffer: 100 mM HEPES, 350 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2023 Mar 1
Thermodynamic coupling of the tandem RRM domains of hnRNP A1 underlie its pleiotropic RNA binding functions. Sci Adv 10(28):eadk6580 (2024)
Levengood JD, Potoyan D, Penumutchu S, Kumar A, Zhou Q, Wang Y, Hansen AL, Kutluay S, Roche J, Tolbert BS
RgGuinier 3.2 nm

SASDTT8 – UvrB (UvrABC system protein B)

UniProt ID: P9WFC7 (22-719) UvrABC system protein B

UvrABC system protein B experimental SAS data
DAMFILT model
Sample: UvrABC system protein B dimer, 156 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 50 mM Tris pH-8, 200 mM NaCl, 2% glycerol, pH:
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2023 Jun 6
Inhibition of Mycobacterium tuberculosis UvrB by small molecules: Potent NER disruption and structural insights into dimer conformation. Int J Biol Macromol :147338 (2025)
Jahan F, Anand S, Kumar S, Pandey G, Siddiqi MI, Krishnan MY, Ramachandran R
RgGuinier 6.7 nm
Dmax 17.5 nm
VolumePorod 120 nm3

SASDTU8 – Complement C3* at 1.25 mg/mL (pH 6.0, 200 mM NaCl)

UniProt ID: P01024 (1-1663) Complement C3 (Δ668-671)

Complement C3 (Δ668-671) experimental SAS data
CORAL model
Sample: Complement C3 (Δ668-671) monomer, 187 kDa Homo sapiens protein
Buffer: 20 mM MES pH 6.0, 200 mM NaCl, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Nov 7
Cryo-EM analysis of complement C3 reveals a reversible major opening of the macroglobulin ring. Nat Struct Mol Biol (2025)
Gadeberg TAF, Jørgensen MH, Olesen HG, Lorentzen J, Harwood SL, Almeida AV, Fruergaard MU, Jensen RK, Kanis P, Pedersen H, Tranchant E, Petersen SV, Thøgersen IB, Kragelund BB, Lyons JA, Enghild JJ, Andersen GR
RgGuinier 5.4 nm
Dmax 21.8 nm
VolumePorod 357 nm3

SASDTV8 – Mouse Fc fragment of IgG binding protein

UniProt ID: E9Q9C6 (27-2583) Fc fragment of IgG binding protein

Fc fragment of IgG binding protein experimental SAS data
DAMMIN model
Sample: Fc fragment of IgG binding protein dimer, 552 kDa Mus musculus protein
Buffer: 25 mM HEPES, 100 mM NaCl, 10 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2020 Nov 20
The structure of FCGBP is formed as a disulfide-mediated homodimer between its C-terminal domains. FEBS J (2025)
Ehrencrona E, Gallego P, Trillo-Muyo S, Garcia-Bonete MJ, Recktenwald CV, Hansson GC, Johansson MEV
RgGuinier 10.0 nm
Dmax 42.0 nm
VolumePorod 1462 nm3