SASBDB entries for UniProt ID:

SASDP68 – Growth factor receptor-bound protein 2 (GRB2) - V123D mutant monomer

UniProt ID: P62993 (1-217) Growth factor receptor-bound protein 2 (V123D)
Growth factor receptor-bound protein 2 (V123D) experimental SAS data
PYMOL model
Sample: Growth factor receptor-bound protein 2 (V123D) monomer, 28 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Oct 31
GRB2 dimerization mediated by SH2 domain-swapping is critical for T cell signaling and cytokine production. Sci Rep 13(1):3505 (2023)
Sandouk A, Xu Z, Baruah S, Tremblay M, Hopkins JB, Chakravarthy S, Gakhar L, Schnicker NJ, Houtman JCD
RgGuinier 2.6 nm
Dmax 10.0 nm
VolumePorod 45 nm3

SASDP78 – Growth factor receptor-bound protein 2 (GRB2) - V122P/V123P mutant dimer

UniProt ID: P62993 (1-217) Growth factor receptor-bound protein 2 (V122P, V123P)
Growth factor receptor-bound protein 2 (V122P, V123P) experimental SAS data
PYMOL model
Sample: Growth factor receptor-bound protein 2 (V122P, V123P) dimer, 55 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Oct 31
GRB2 dimerization mediated by SH2 domain-swapping is critical for T cell signaling and cytokine production. Sci Rep 13(1):3505 (2023)
Sandouk A, Xu Z, Baruah S, Tremblay M, Hopkins JB, Chakravarthy S, Gakhar L, Schnicker NJ, Houtman JCD
RgGuinier 3.7 nm
Dmax 20.4 nm
VolumePorod 85 nm3

SASDP88 – N-terminal domain of S. cerevisiae eukaryotic initiation factor 4F subunit p150, eIF4G1 (Tif4631)

UniProt ID: P39935 (1-249) Eukaryotic initiation factor 4F subunit p150
Eukaryotic initiation factor 4F subunit p150 experimental SAS data
Eukaryotic initiation factor 4F subunit p150 Kratky plot
Sample: Eukaryotic initiation factor 4F subunit p150, 28 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 25 mM potassium phosphate, 25 mM NaCl, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Jul 14
eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. Front Mol Biosci 9:986121 (2022)
Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM
RgGuinier 5.2 nm
Dmax 19.0 nm
VolumePorod 137 nm3

SASDP98 – Human apo iron-sulfur cluster assembly 1 (ISCA1)

UniProt ID: Q9BUE6 (1-129) Iron-sulfur cluster assembly 1 homolog, mitochondrial
Iron-sulfur cluster assembly 1 homolog, mitochondrial experimental SAS data
DAMMIF model
Sample: Iron-sulfur cluster assembly 1 homolog, mitochondrial monomer, 14 kDa Homo sapiens protein
Buffer: 50 mM phosphate, 150 mM NaCl, 5 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 27
Structural plasticity of NFU1 upon interaction with binding partners: insights into the mitochondrial [4Fe-4S] cluster pathway Journal of Molecular Biology :168154 (2023)
Da Vela S, Saudino G, Lucarelli F, Banci L, Svergun D, Ciofi-Baffoni S
RgGuinier 1.9 nm
Dmax 6.8 nm
VolumePorod 25 nm3

SASDPA8 – Human apo NFU1 iron-sulfur cluster scaffold protein

UniProt ID: Q9UMS0 (59-254) NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (F118S, E168G)
NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (F118S, E168G) experimental SAS data
Human apo NFU1 iron-sulfur cluster scaffold protein Rg histogram
Sample: NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (F118S, E168G) monomer, 22 kDa Homo sapiens protein
Buffer: 50 mM phosphate, 150 mM NaCl, 5 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 27
Structural plasticity of NFU1 upon interaction with binding partners: insights into the mitochondrial [4Fe-4S] cluster pathway Journal of Molecular Biology :168154 (2023)
Da Vela S, Saudino G, Lucarelli F, Banci L, Svergun D, Ciofi-Baffoni S
RgGuinier 2.4 nm
Dmax 9.3 nm
VolumePorod 32 nm3

SASDPB8 – Human apo iron-sulfur cluster assembly 1/NFU1 iron-sulfur cluster scaffold protein complex (ISCA1-NFU1)

UniProt ID: Q9BUE6 (1-129) Iron-sulfur cluster assembly 1 homolog, mitochondrial

UniProt ID: Q9UMS0 (59-254) NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (F118S, E168G)
Iron-sulfur cluster assembly 1 homolog, mitochondrialNFU1 iron-sulfur cluster scaffold homolog, mitochondrial (F118S, E168G) experimental SAS data
DAMMIF model
Sample: Iron-sulfur cluster assembly 1 homolog, mitochondrial monomer, 14 kDa Homo sapiens protein
NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (F118S, E168G) monomer, 22 kDa Homo sapiens protein
Buffer: 50 mM phosphate, 150 mM NaCl, 5 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 27
Structural plasticity of NFU1 upon interaction with binding partners: insights into the mitochondrial [4Fe-4S] cluster pathway Journal of Molecular Biology :168154 (2023)
Da Vela S, Saudino G, Lucarelli F, Banci L, Svergun D, Ciofi-Baffoni S
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 43 nm3

SASDPC8 – Human apo iron-sulfur cluster assembly 1/iron-sulfur cluster assembly 2 complex (ISCA1-ISCA2)

UniProt ID: Q9BUE6 (1-129) Iron-sulfur cluster assembly 1 homolog, mitochondrial

UniProt ID: Q86U28 (44-154) Iron-sulfur cluster assembly 2 homolog, mitochondrial
Iron-sulfur cluster assembly 1 homolog, mitochondrialIron-sulfur cluster assembly 2 homolog, mitochondrial experimental SAS data
DAMMIF model
Sample: Iron-sulfur cluster assembly 1 homolog, mitochondrial monomer, 14 kDa Homo sapiens protein
Iron-sulfur cluster assembly 2 homolog, mitochondrial monomer, 13 kDa Homo sapiens protein
Buffer: 50 mM phosphate, 150 mM NaCl, 5 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 27
Structural plasticity of NFU1 upon interaction with binding partners: insights into the mitochondrial [4Fe-4S] cluster pathway Journal of Molecular Biology :168154 (2023)
Da Vela S, Saudino G, Lucarelli F, Banci L, Svergun D, Ciofi-Baffoni S
RgGuinier 2.4 nm
Dmax 7.8 nm
VolumePorod 43 nm3

SASDPD8 – Human apo iron-sulfur cluster assembly 1/iron-sulfur cluster assembly 2/NFU1 iron-sulfur cluster scaffold protein complex (ISCA1-ISCA2-NFU1)

UniProt ID: Q9BUE6 (1-129) Iron-sulfur cluster assembly 1 homolog, mitochondrial

UniProt ID: Q9UMS0 (59-254) NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (F118S, E168G)

UniProt ID: Q86U28 (44-154) Iron-sulfur cluster assembly 2 homolog, mitochondrial
Iron-sulfur cluster assembly 1 homolog, mitochondrialNFU1 iron-sulfur cluster scaffold homolog, mitochondrial (F118S, E168G)Iron-sulfur cluster assembly 2 homolog, mitochondrial experimental SAS data
CORAL model
Sample: Iron-sulfur cluster assembly 1 homolog, mitochondrial monomer, 14 kDa Homo sapiens protein
NFU1 iron-sulfur cluster scaffold homolog, mitochondrial (F118S, E168G) monomer, 22 kDa Homo sapiens protein
Iron-sulfur cluster assembly 2 homolog, mitochondrial monomer, 13 kDa Homo sapiens protein
Buffer: 50 mM phosphate, 150 mM NaCl, 5 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Mar 27
Structural plasticity of NFU1 upon interaction with binding partners: insights into the mitochondrial [4Fe-4S] cluster pathway Journal of Molecular Biology :168154 (2023)
Da Vela S, Saudino G, Lucarelli F, Banci L, Svergun D, Ciofi-Baffoni S
RgGuinier 3.2 nm
Dmax 11.7 nm
VolumePorod 70 nm3

SASDPE8 – SMARCA2 bromodomain (isoform1):Protac (ACBI1):VCB (VHL-elongin C-elongin B)

UniProt ID: P51531 (1373-1511) Probable global transcription activator SNF2L2 (isoform 1)

UniProt ID: P40337 (54-213) von Hippel-Lindau disease tumor suppressor

UniProt ID: Q15370 (1-104) Elongin-B

UniProt ID: Q15369 (17-112) Elongin-C

UniProt ID: None (None-None) ACBI1 protac
Probable global transcription activator SNF2L2 (isoform 1)von Hippel-Lindau disease tumor suppressorElongin-BElongin-CACBI1 protac experimental SAS data
Probable global transcription activator SNF2L2 (isoform 1) von Hippel-Lindau disease tumor suppressor Elongin-B Elongin-C ACBI1 protac Kratky plot
Sample: Probable global transcription activator SNF2L2 (isoform 1) monomer, 16 kDa Homo sapiens protein
Von Hippel-Lindau disease tumor suppressor monomer, 19 kDa Homo sapiens protein
Elongin-B monomer, 12 kDa Homo sapiens protein
Elongin-C monomer, 11 kDa Homo sapiens protein
ACBI1 protac monomer, 1 kDa
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, Département de Biochimie, Université de Montréal on 2021 Aug 11
Predicting the structural basis of targeted protein degradation by integrating molecular dynamics simulations with structural mass spectrometry. Nat Commun 13(1):5884 (2022)
Dixon T, MacPherson D, Mostofian B, Dauzhenka T, Lotz S, McGee D, Shechter S, Shrestha UR, Wiewiora R, McDargh ZA, Pei F, Pal R, Ribeiro JV, Wilkerson T, Sachdeva V, Gao N, Jain S, Sparks S, Li Y, Vinitsky A, Zhang X, Razavi AM, Kolossváry I, Imbriglio J, Evdokimov A, Bergeron L, Zhou W, Adhikari J, Ruprecht B, Dickson A, Xu H, Sherman W, Izaguirre JA
RgGuinier 3.3 nm
Dmax 12.5 nm
VolumePorod 83 nm3

SASDPF8 – SMARCA2 bromodomain (isoform2):Protac (ACBI1):VCB (VHL-elongin C-elongin B)

UniProt ID: P40337 (54-213) von Hippel-Lindau disease tumor suppressor

UniProt ID: Q15370 (1-104) Elongin-B

UniProt ID: Q15369 (17-112) Elongin-C

UniProt ID: None (None-None) ACBI1 protac

UniProt ID: P51531 (1373-1511) Probable global transcription activator SNF2L2 (isoform 2)
von Hippel-Lindau disease tumor suppressorElongin-BElongin-CACBI1 protacProbable global transcription activator SNF2L2 (isoform 2) experimental SAS data
von Hippel-Lindau disease tumor suppressor Elongin-B Elongin-C ACBI1 protac Probable global transcription activator SNF2L2 (isoform 2) Kratky plot
Sample: Von Hippel-Lindau disease tumor suppressor monomer, 19 kDa Homo sapiens protein
Elongin-B monomer, 12 kDa Homo sapiens protein
Elongin-C monomer, 11 kDa Homo sapiens protein
ACBI1 protac monomer, 1 kDa
Probable global transcription activator SNF2L2 (isoform 2) monomer, 14 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, Département de Biochimie, Université de Montréal on 2021 Aug 11
Predicting the structural basis of targeted protein degradation by integrating molecular dynamics simulations with structural mass spectrometry. Nat Commun 13(1):5884 (2022)
Dixon T, MacPherson D, Mostofian B, Dauzhenka T, Lotz S, McGee D, Shechter S, Shrestha UR, Wiewiora R, McDargh ZA, Pei F, Pal R, Ribeiro JV, Wilkerson T, Sachdeva V, Gao N, Jain S, Sparks S, Li Y, Vinitsky A, Zhang X, Razavi AM, Kolossváry I, Imbriglio J, Evdokimov A, Bergeron L, Zhou W, Adhikari J, Ruprecht B, Dickson A, Xu H, Sherman W, Izaguirre JA
RgGuinier 3.2 nm
Dmax 11.1 nm
VolumePorod 75 nm3