SASBDB entries for UniProt ID:

SASDJ27 – Collagenase H C-terminal non-catalytic segments Polycystic Kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr780Ser, His782Ser, Tyr796Ser and Tyr801Ser bound to triple helical collagen like-peptide

UniProt ID: None (None-None) Collagen like-peptide [GPRG(POG)13]

UniProt ID: Q46085 (811-1021) Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr780Ser, His782Ser, Tyr796Ser and Tyr801Ser)

Collagen like-peptide [GPRG(POG)13]Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr780Ser, His782Ser, Tyr796Ser and Tyr801Ser) experimental SAS data
DAMFILT model
Sample: Collagen like-peptide [GPRG(POG)13] trimer, 11 kDa protein
Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr780Ser, His782Ser, Tyr796Ser and Tyr801Ser) monomer, 23 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 5
Elucidating Collagen Degradation Synergy between Col G and Col H from Hathewaya (Clostridium) histolytica and Identifying novel structural features in HPT and REC domains from VarS histidine kinase in V. alginolyticus University of Arkansas PhD thesis 28030553 (2020)
Perry Caviness
RgGuinier 3.2 nm
Dmax 18.0 nm
VolumePorod 34 nm3

SASDJ37 – Collagenase H C-terminal non-catalytic segments Polycystic Kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) bound to triple helical collagen like-peptide

UniProt ID: Q46085 (811-1021) Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD))

UniProt ID: None (None-None) Collagen like-peptide [GPRG(POG)13]

Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD))Collagen like-peptide [GPRG(POG)13] experimental SAS data
DAMFILT model
Sample: Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD)) monomer, 23 kDa Hathewaya histolytica protein
Collagen like-peptide [GPRG(POG)13] trimer, 11 kDa protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 5
Elucidating Collagen Degradation Synergy between Col G and Col H from Hathewaya (Clostridium) histolytica and Identifying novel structural features in HPT and REC domains from VarS histidine kinase in V. alginolyticus University of Arkansas PhD thesis 28030553 (2020)
Perry Caviness
RgGuinier 3.3 nm
Dmax 18.0 nm
VolumePorod 35 nm3

SASDJ47 – Polyglutamine protein ataxin-3 (Q13)

UniProt ID: P54252 (1-361) Ataxin-3 (polyglutamine protein ataxin-3 (Q13))

Ataxin-3 (polyglutamine protein ataxin-3 (Q13)) experimental SAS data
Polyglutamine protein ataxin-3 (Q13) Rg histogram
Sample: Ataxin-3 (polyglutamine protein ataxin-3 (Q13)) monomer, 41 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate buffer, 2 mM TCEP, 5% glycerol, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 May 24
Capturing the Conformational Ensemble of the Mixed Folded Polyglutamine Protein Ataxin-3. Structure (2020)
Sicorello A, Różycki B, Konarev PV, Svergun DI, Pastore A
RgGuinier 4.0 nm
Dmax 14.1 nm
VolumePorod 79 nm3

SASDJL7 – Oxidised fimbrial BcfH protein

UniProt ID: A0A0H3N7J9 (28-281) Hypothetical exported protein

Hypothetical exported protein experimental SAS data
CORAL model
Sample: Hypothetical exported protein trimer, 83 kDa Salmonella typhimurium (strain … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 14
Salmonella enterica BcfH is a trimeric thioredoxin-like bifunctional enzyme with both thiol oxidase and disulfide isomerase activities. Antioxid Redox Signal (2021)
Subedi P, Paxman JJ, Wang G, Hor L, Hong Y, Verderosa AD, Whitten AE, Panjikar S, Santos-Martin CF, Martin JL, Totsika M, Heras B
RgGuinier 3.2 nm
Dmax 11.5 nm
VolumePorod 93 nm3

SASDJM7 – Iron-sulfur cluster assembly protein (IscU)

UniProt ID: Q8IKT4 (37-162) Iron-sulfur cluster assembly protein

Iron-sulfur cluster assembly protein experimental SAS data
DAMFILT model
Sample: Iron-sulfur cluster assembly protein trimer, 42 kDa Plasmodium falciparum (isolate … protein
Buffer: 50 mM Tris-Cl, 300 mM NaCl, 5% Glycerol, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2019 May 5
[Fe-S] cluster biogenesis and unusual assembly of the ISC scaffold complex in Plasmodium falciparum mitochondrion
Ravishankar Ramachandran
RgGuinier 5.4 nm
Dmax 11.1 nm
VolumePorod 177 nm3

SASDJN7 – Cysteine desulfurase, Iron-sulfur cluster assembly protein (IscS_IscU) complex

UniProt ID: Q8IKT4 (37-162) Iron-sulfur cluster assembly protein

UniProt ID: Q8IBI5 (104-553) Cysteine desulfurase, putative

Iron-sulfur cluster assembly proteinCysteine desulfurase, putative experimental SAS data
DAMMIF model
Sample: Iron-sulfur cluster assembly protein tetramer, 56 kDa Plasmodium falciparum (isolate … protein
Cysteine desulfurase, putative tetramer, 204 kDa Plasmodium falciparum (isolate … protein
Buffer: 50 mM Tris-Cl, 300 mM NaCl, 5% Glycerol, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2019 Sep 4
[Fe-S] cluster biogenesis and unusual assembly of the ISC scaffold complex in Plasmodium falciparum mitochondrion
Ravishankar Ramachandran
RgGuinier 6.4 nm
Dmax 17.6 nm
VolumePorod 1100 nm3

SASDJP7 – Cysteine desulfurase, Iron-sulfur cluster assembly protein, Protein ISD11 (IscS_IscU_Isd11) complex

UniProt ID: Q8IBI5 (104-553) Cysteine desulfurase, putative

UniProt ID: Q8IKT4 (37-162) Iron-sulfur cluster assembly protein

UniProt ID: Q8IEK7 (1-87) Protein ISD11

Cysteine desulfurase, putativeIron-sulfur cluster assembly proteinProtein ISD11 experimental SAS data
DAMMIF model
Sample: Cysteine desulfurase, putative tetramer, 204 kDa Plasmodium falciparum (isolate … protein
Iron-sulfur cluster assembly protein tetramer, 56 kDa Plasmodium falciparum (isolate … protein
Protein ISD11 tetramer, 43 kDa Plasmodium falciparum (isolate … protein
Buffer: 50 mM Tris-Cl, 300 mM NaCl, 5% Glycerol, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2019 Sep 19
[Fe-S] cluster biogenesis and unusual assembly of the ISC scaffold complex in Plasmodium falciparum mitochondrion
Ravishankar Ramachandran
RgGuinier 7.1 nm
Dmax 17.9 nm
VolumePorod 950 nm3

SASDJQ7 – Human Cathepsin X

UniProt ID: Q9UBR2 (62-303) Cathepsin Z

Cathepsin Z experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Cathepsin Z dimer, 54 kDa Homo sapiens protein
Buffer: 20 mM sodium acetate, 1 mM EDTA, pH: 5.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Dec 6
Human cathepsin X/Z is a biologically active homodimer. Biochim Biophys Acta Proteins Proteom :140567 (2020)
Dolenc I, Štefe I, Turk D, Taler-Verčič A, Turk B, Turk V, Stoka V
RgGuinier 2.6 nm
Dmax 6.5 nm
VolumePorod 89 nm3

SASDJR7 – Mouse cysteine sulphinic acid decarboxylase (CSAD)

UniProt ID: Q9DBE0 (1-493) Cysteine sulfinic acid decarboxylase

Cysteine sulfinic acid decarboxylase experimental SAS data
SREFLEX model
Sample: Cysteine sulfinic acid decarboxylase dimer, 117 kDa Mus musculus protein
Buffer: 20 mM HEPES, 200 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Feb 4
Structure and substrate specificity determinants of the taurine biosynthetic enzyme cysteine sulphinic acid decarboxylase. J Struct Biol :107674 (2020)
Mahootchi E, Raasakka A, Luan W, Muruganandam G, Loris R, Haavik J, Kursula P
RgGuinier 3.4 nm
Dmax 15.0 nm
VolumePorod 198 nm3

SASDJS7 – Phloem-associated RNA chaperone-like protein (PARCL) at pH 7.5

UniProt ID: Q9C7W1 (1-178) Filaggrin-like protein

Filaggrin-like protein experimental SAS data
Phloem-associated RNA chaperone-like protein (PARCL) at pH 7.5 Rg histogram
Sample: Filaggrin-like protein monomer, 20 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, 150 mM NaCl, 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Aug 22
Intrinsically disordered plant protein PARCL co-localizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD Journal of Biological Chemistry :102631 (2022)
Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries C, Svergun D, Betzel C, Morris R, Kragler F, Kehr J
RgGuinier 3.5 nm
Dmax 14.0 nm
VolumePorod 46 nm3