Small Angle Scattering Biological Data Bank SASBDB

SASBDB entries for UniProt ID:

SASDBU5 – Cyclopentadecanone monooxygenase, wild-type

UniProt ID: T2HVF7 (None-None) Cyclopentadecanone 1,2-monooxygenase

Cyclopentadecanone 1,2-monooxygenase experimental SAS data

Cyclopentadecanone 1,2-monooxygenase Kratky plot

Sample:	Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein
Buffer:	50 mM Tris 2 mM TCEP, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2013 Jan 27

The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure. Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM

R_g^Guinier	2.8	nm
D_max	10.4	nm
Volume^Porod	110	nm³

SASDBV5 – Cyclopentadecanone monooxygenase, NADP+, wild-type

UniProt ID: T2HVF7 (None-None) Cyclopentadecanone 1,2-monooxygenase

Sample:	Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein
Buffer:	50 mM Tris 2 mM TCEP 5 mM NADP+, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2

The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure. Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM

R_g^Guinier	2.7	nm
D_max	8.7	nm
Volume^Porod	120	nm³

SASDBW5 – Cyclopentadecanone monooxygenase, NADP+ and cyclopentadecanone, wild-type

UniProt ID: T2HVF7 (None-None) Cyclopentadecanone 1,2-monooxygenase

Sample:	Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein
Buffer:	50mM Tris 2mM TCEP 5mM NADP+ 1mM cyclopentadecanon, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2

The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure. Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM

R_g^Guinier	2.6	nm
D_max	9.0	nm
Volume^Porod	110	nm³

SASDBX5 – Cyclopentadecanone monooxygenase, NADP+ and ω-pentadecalactone, wild-type

UniProt ID: T2HVF7 (None-None) Cyclopentadecanone 1,2-monooxygenase

Sample:	Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein
Buffer:	50mM Tris mM TCEP 5mM NADP+ 1mM ω-pentadecalactone, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2

The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure. Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM

R_g^Guinier	2.6	nm
D_max	9.0	nm
Volume^Porod	100	nm³

SASDBY5 – C-terminal fragment (509-716) of the Methoprene-tolerant protein from Drosophila melanogaster

UniProt ID: Q9VYW2 (509-716) FI10506p

C-terminal fragment (509-716) of the Methoprene-tolerant protein from Drosophila melanogaster Rg histogram

Sample:	FI10506p monomer, 23 kDa Drosophila melanogaster protein
Buffer:	20mM Tris/HCl 150mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2015 Jul 21

Intrinsic Disorder of the C-Terminal Domain of Drosophila Methoprene-Tolerant Protein. PLoS One 11(9):e0162950 (2016)
Kolonko M, Ożga K, Hołubowicz R, Taube M, Kozak M, Ożyhar A, Greb-Markiewicz B

R_g^Guinier	5.1	nm
D_max	22.0	nm

SASDBZ5 – Enzyme I-Ntr (residues 170-424) in complex with NPr (residues 1-85)

UniProt ID: P0A9N0 (1-85) Phosphocarrier protein NPr

UniProt ID: P37177 (170-424) Phosphoenolpyruvate-protein phosphotransferase PtsP

Phosphocarrier protein NPrPhosphoenolpyruvate-protein phosphotransferase PtsP experimental SAS data

Sample:	Phosphocarrier protein NPr monomer, 9 kDa Escherichia coli protein Phosphoenolpyruvate-protein phosphotransferase PtsP monomer, 28 kDa Escherichia coli protein
Buffer:	10 mM Tris 150 mM NaCl 0.5 mM EDTA, pH: 7.5
Experiment:	SAXS data collected at Rigaku BioSAXS-1000, NIDDK, NIH on 2015 Jan 30

Structure of the NPr:EIN^Ntr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems. Structure 24(12):2127-2137 (2016)
Strickland M, Stanley AM, Wang G, Botos I, Schwieters CD, Buchanan SK, Peterkofsky A, Tjandra N

R_g^Guinier	2.3	nm
D_max	8.2	nm
Volume^Porod	52	nm³

SASDB86 – apo-BRD4

UniProt ID: O60885 (1-477) Bromodomain-containing protein 4

Bromodomain-containing protein 4 experimental SAS data

Sample:	Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer:	20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment:	SAXS data collected at BM29, ESRF on 2014 Sep 12

Potent and selective bivalent inhibitors of BET bromodomains. Nat Chem Biol 12(12):1097-1104 (2016)
Waring MJ, Chen H, Rabow AA, Walker G, Bobby R, Boiko S, Bradbury RH, Callis R, Clark E, Dale I, Daniels DL, Dulak A, Flavell L, Holdgate G, Jowitt TA, Kikhney A, McAlister M, Méndez J, Ogg D, Patel J, Petteruti P, Robb GR, Robers MB, Saif S, Stratton N, Svergun DI, Wang W, Whittaker D, Wilson DM, Yao Y

R_g^Guinier	7.0	nm
D_max	27.0	nm

SASDB96 – Compound 1:BRD4 (1:1)

UniProt ID: O60885 (1-477) Bromodomain-containing protein 4

Sample:	Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer:	20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment:	SAXS data collected at BM29, ESRF on 2014 Sep 12

R_g^Guinier	6.2	nm
D_max	27.5	nm

SASDBA6 – Compound 1:BRD4 (2:1)

UniProt ID: O60885 (1-477) Bromodomain-containing protein 4

Sample:	Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer:	20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment:	SAXS data collected at BM29, ESRF on 2014 Sep 12

R_g^Guinier	6.3	nm
D_max	24.5	nm

SASDBB6 – Compound 6:BRD4 (1:1)

UniProt ID: O60885 (1-477) Bromodomain-containing protein 4

Sample:	Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer:	20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment:	SAXS data collected at BM29, ESRF on 2015 Feb 8

R_g^Guinier	5.1	nm
D_max	24.3	nm

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