SASBDB entries for UniProt ID:

SASDBN3 – Highly similar to Actin cross-linking family protein 7 (ACF7) Y259D mutant Homo Sapiens

UniProt ID: Q6ZSD7 (1-400) cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Y259D mutant
cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Y259D mutant experimental SAS data
cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Y259D mutant Kratky plot
Sample: CDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Y259D mutant monomer, 46 kDa Homo sapiens protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Nov 7
In vivo epidermal migration requires focal adhesion targeting of ACF7. Nat Commun 7:11692 (2016)
Yue J, Zhang Y, Liang WG, Gou X, Lee P, Liu H, Lyu W, Tang WJ, Chen SY, Yang F, Liang H, Wu X
RgGuinier 3.4 nm
Dmax 13.5 nm
VolumePorod 55 nm3

SASDBQ3 – Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164)

UniProt ID: T2B9R0 (1-164) Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164)
Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164) experimental SAS data
DAMMIF model
Sample: Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164) monomer, 18 kDa Middle East respiratory … protein
Buffer: 10 mM HEPES 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2015 Oct 5
Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering. Acta Crystallogr D Struct Biol 72(Pt 2):192-202 (2016)
Papageorgiou N, Lichière J, Baklouti A, Ferron F, Sévajol M, Canard B, Coutard B
RgGuinier 2.0 nm
Dmax 8.0 nm
VolumePorod 28 nm3

SASDBR3 – Wild type RNF8 complexed with Ubc13 (C87K, K92A mutant): conjugated to Ubiquitin

UniProt ID: O76064 (345-485) E3 ubiquitin-protein ligase RNF8

UniProt ID: P61088 (1-152) Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)

UniProt ID: P0CG48 (1-76) Polyubiquitin-C
E3 ubiquitin-protein ligase RNF8Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)Polyubiquitin-C experimental SAS data
MES-FOXS model
Sample: E3 ubiquitin-protein ligase RNF8 dimer, 35 kDa Homo sapiens protein
Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A) dimer, 36 kDa Homo sapiens protein
Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl 0.01 mM ZnSO4 1 mM DTT, pH: 6.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Sep 8
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. J Biol Chem 291(18):9396-410 (2016)
Hodge CD, Ismail IH, Edwards RA, Hura GL, Xiao AT, Tainer JA, Hendzel MJ, Glover JN
RgGuinier 4.5 nm
Dmax 18.9 nm
VolumePorod 119 nm3

SASDBS3 – Wild type RNF8 complexed with Ubc13 (C87K, K92A mutant) and Mms2: conjugated to Ubiquitin

UniProt ID: O76064 (345-485) E3 ubiquitin-protein ligase RNF8

UniProt ID: P61088 (1-152) Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)

UniProt ID: P0CG48 (1-76) Polyubiquitin-C

UniProt ID: Q15819 (1-145) Ubiquitin-conjugating enzyme E2 variant 2
E3 ubiquitin-protein ligase RNF8Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)Polyubiquitin-CUbiquitin-conjugating enzyme E2 variant 2 experimental SAS data
MES-FOXS model
Sample: E3 ubiquitin-protein ligase RNF8 dimer, 35 kDa Homo sapiens protein
Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A) dimer, 36 kDa Homo sapiens protein
Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
Ubiquitin-conjugating enzyme E2 variant 2 dimer, 34 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl 0.01 mM ZnSO4 1 mM DTT, pH: 6.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Sep 8
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. J Biol Chem 291(18):9396-410 (2016)
Hodge CD, Ismail IH, Edwards RA, Hura GL, Xiao AT, Tainer JA, Hendzel MJ, Glover JN
RgGuinier 5.4 nm
Dmax 23.8 nm
VolumePorod 214 nm3

SASDBT3 – RNF8 (L451D mutant) complexed with Ubc13 (C87K, K92A mutant): conjugated to Ubiquitin

UniProt ID: P61088 (1-152) Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)

UniProt ID: P0CG48 (1-76) Polyubiquitin-C

UniProt ID: O76064 (345-485) E3 ubiquitin-protein ligase RNF8 mutant (L451D)
Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)Polyubiquitin-CE3 ubiquitin-protein ligase RNF8 mutant (L451D) experimental SAS data
MES-FOXS model
Sample: Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A) dimer, 36 kDa Homo sapiens protein
Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
E3 ubiquitin-protein ligase RNF8 mutant (L451D) dimer, 35 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl 0.01 mM ZnSO4 1 mM DTT, pH: 6.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Sep 8
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. J Biol Chem 291(18):9396-410 (2016)
Hodge CD, Ismail IH, Edwards RA, Hura GL, Xiao AT, Tainer JA, Hendzel MJ, Glover JN
RgGuinier 4.3 nm
Dmax 18.9 nm
VolumePorod 111 nm3

SASDBU3 – RNF8 (L451D mutant) complexed with Ubc13 (C87K, K92A mutant) and Mms2: conjugated to Ubiquitin

UniProt ID: P61088 (1-152) Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)

UniProt ID: P0CG48 (1-76) Polyubiquitin-C

UniProt ID: Q15819 (1-145) Ubiquitin-conjugating enzyme E2 variant 2

UniProt ID: O76064 (345-485) E3 ubiquitin-protein ligase RNF8 mutant (L451D)
Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)Polyubiquitin-CUbiquitin-conjugating enzyme E2 variant 2E3 ubiquitin-protein ligase RNF8 mutant (L451D) experimental SAS data
MES-FOXS model
Sample: Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A) dimer, 36 kDa Homo sapiens protein
Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
Ubiquitin-conjugating enzyme E2 variant 2 dimer, 34 kDa Homo sapiens protein
E3 ubiquitin-protein ligase RNF8 mutant (L451D) dimer, 35 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl 0.01 mM ZnSO4 1 mM DTT, pH: 6.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Sep 8
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. J Biol Chem 291(18):9396-410 (2016)
Hodge CD, Ismail IH, Edwards RA, Hura GL, Xiao AT, Tainer JA, Hendzel MJ, Glover JN
RgGuinier 5.2 nm
Dmax 23.8 nm
VolumePorod 192 nm3

SASDBV3 – Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant)

UniProt ID: P11532 (1991-2694) Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47)
Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) experimental SAS data
GASBOR model
Sample: Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) monomer, 64 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol 5% acetonitrile, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Feb 5
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
Delalande O, Molza AE, Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, Le Rumeur E
RgGuinier 6.0 nm
Dmax 21.0 nm
VolumePorod 184 nm3

SASDBW3 – Human calumenin (sarco-endoplasmic reticulum calcium-sensing protein)

UniProt ID: O43852 (68-315) Human Calumenin
Human Calumenin experimental SAS data
Human Calumenin Kratky plot
Sample: Human Calumenin monomer, 29 kDa Homo sapiens protein
Buffer: 25 mM Na-HEPES, 25 mM NaCl, 2.5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Feb 12
Ca-Dependent Folding of Human Calumenin. PLoS One 11(3):e0151547 (2016)
Mazzorana M, Hussain R, Sorensen T
RgGuinier 2.3 nm
Dmax 6.5 nm
VolumePorod 49 nm3

SASDB54 – Leishmania braziliensis stress-induced protein sti1 (LbHop), full length construct

UniProt ID: A4H5F0 (1-547) Stress-induced protein sti1
Stress-induced protein sti1 experimental SAS data
DAMFILT model
Sample: Stress-induced protein sti1 monomer, 62 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris 100 mM NaCl 1 mM EDTA 1 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2016 Feb 21
Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Arch Biochem Biophys 600:12-22 (2016)
Batista FAH, Seraphim TV, Santos CA, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC
RgGuinier 4.5 nm
Dmax 18.0 nm
VolumePorod 94 nm3

SASDB64 – Leishmania braziliensis stress-induced protein sti1 (LbHop TPR2A-TPR2B-DP2 construct)

UniProt ID: A4H5F0 (171-547) Stress-induced protein sti1 (Hop TPR2A-TPR2B-DP2 construct)
Stress-induced protein sti1 (Hop TPR2A-TPR2B-DP2 construct) experimental SAS data
DAMFILT model
Sample: Stress-induced protein sti1 (Hop TPR2A-TPR2B-DP2 construct) monomer, 44 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris 100 mM NaCl 1 mM EDTA 1 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2016 Feb 21
Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Arch Biochem Biophys 600:12-22 (2016)
Batista FAH, Seraphim TV, Santos CA, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 65 nm3