Small Angle Scattering Biological Data Bank SASBDB

SASDRZ7 – Human wild-type nicotinamide phosphoribosyltransferase (NAMPT)

Nicotinamide phosphoribosyltransferase experimental SAS data

Nicotinamide phosphoribosyltransferase Kratky plot

Sample:	Nicotinamide phosphoribosyltransferase dimer, 114 kDa Homo sapiens protein
Buffer:	20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, pH: 8
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 May 20

Identification of structural determinants of nicotinamide phosphoribosyl transferase (NAMPT) activity and substrate selectivity. J Struct Biol :108004 (2023)
Houry D, Raasakka A, Ferrario E, Niere M, Bifulco E, Kursula P, Ziegler M

R_g^Guinier	3.3	nm
D_max	12.9	nm
Volume^Porod	181	nm³

SASDR28 – Human wild-type nicotinamide phosphoribosyltransferase (NAMPT) in the presence of nicotinamide

Sample:	Nicotinamide phosphoribosyltransferase dimer, 114 kDa Homo sapiens protein
Buffer:	20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM nicotinamide, pH: 8
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 May 20

R_g^Guinier	3.2	nm
D_max	12.8	nm
Volume^Porod	166	nm³

SASDR38 – Human wild-type nicotinamide phosphoribosyltransferase (NAMPT) in the presence of nicotinic acid

Sample:	Nicotinamide phosphoribosyltransferase dimer, 114 kDa Homo sapiens protein
Buffer:	20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM nicotinic acid, pH: 8
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 May 20

R_g^Guinier	3.3	nm
D_max	12.9	nm
Volume^Porod	180	nm³

SASDR48 – Human wild-type nicotinamide phosphoribosyltransferase (NAMPT) in the presence of phosphoribosyl pyrophosphate

Sample:	Nicotinamide phosphoribosyltransferase dimer, 114 kDa Homo sapiens protein
Buffer:	20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM phosphoribosyl pyrophosphate, pH: 8
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 May 20

R_g^Guinier	3.3	nm
D_max	12.9	nm
Volume^Porod	173	nm³

SASDR58 – Human nicotinamide phosphoribosyltransferase Δ42-51 loop mutant (NAMPT Δ42-51)

Nicotinamide phosphoribosyltransferase Δ42-51 experimental SAS data

Nicotinamide phosphoribosyltransferase Δ42-51 Kratky plot

Sample:	Nicotinamide phosphoribosyltransferase Δ42-51 dimer, 111 kDa Homo sapiens protein
Buffer:	20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, pH: 8
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 May 20

R_g^Guinier	3.2	nm
D_max	11.0	nm
Volume^Porod	159	nm³

SASDR68 – Human nicotinamide phosphoribosyltransferase Δ42-51 loop mutant (NAMPT Δ42-51) in the presence of nicotinamide

Sample:	Nicotinamide phosphoribosyltransferase Δ42-51 dimer, 111 kDa Homo sapiens protein
Buffer:	20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM nicotinamide, pH: 8
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 May 20

R_g^Guinier	3.2	nm
D_max	10.9	nm
Volume^Porod	151	nm³

SASDR78 – Human nicotinamide phosphoribosyltransferase Δ42-51 loop mutant (NAMPT Δ42-51) in the presence of nicotinic acid

Sample:	Nicotinamide phosphoribosyltransferase Δ42-51 dimer, 111 kDa Homo sapiens protein
Buffer:	20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM nicotinic acid, pH: 8
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 May 20

R_g^Guinier	3.3	nm
D_max	11.2	nm
Volume^Porod	152	nm³

SASDR88 – Human nicotinamide phosphoribosyltransferase Δ42-51 loop mutant (NAMPT Δ42-51) in the presence of phosphoribosyl pyrophosphate

Sample:	Nicotinamide phosphoribosyltransferase Δ42-51 dimer, 111 kDa Homo sapiens protein
Buffer:	20 mM Tris-HCl, 500 mM NaCl, 6 mM MgCl2, 5% (v/v) glycerol, 1 mM phosphoribosyl pyrophosphate, pH: 8
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2019 May 20

R_g^Guinier	3.2	nm
D_max	11.4	nm
Volume^Porod	154	nm³

SASDS36 – Human RAD51C-XRCC3 at pH 8 in the presence of ATP and vanadate, a phosphate mimic

Isoform 1 of DNA repair protein RAD51 homolog 3DNA repair protein XRCC3 experimental SAS data

Sample:	Isoform 1 of DNA repair protein RAD51 homolog 3 monomer, 40 kDa Homo sapiens protein DNA repair protein XRCC3 monomer, 38 kDa Homo sapiens protein
Buffer:	10 mM HEPES pH 8, 100 mM NaCl, 2.5 mM ATP, 2.5 mM MgCl2, and 0.1 mM Na3VO4, pH: 8
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 May 5

RAD51C-XRCC3 structure and cancer patient mutations define DNA replication roles Nature Communications 14(1) (2023)
Longo M, Roy S, Chen Y, Tomaszowski K, Arvai A, Pepper J, Boisvert R, Kunnimalaiyaan S, Keshvani C, Schild D, Bacolla A, Williams G, Tainer J, Schlacher K

R_g^Guinier	3.6	nm
D_max	14.0	nm
Volume^Porod	132	nm³

SASDJ26 – Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial-monomer

Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial experimental SAS data

Sample:	Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22, mitochondrial monomer, 70 kDa Saccharomyces cerevisiae protein
Buffer:	40 mM Tris pH 7.5, 500 mM NaCl, 5% glycerol, 2.5 mM DTT, pH: 7.5
Experiment:	SAXS data collected at B21, Diamond Light Source on 2017 May 1

Probable S-adenosyl-L-methionine-dependent RNA methyltransferase RSM22
Jahangir Alam

R_g^Guinier	3.8	nm
D_max	13.9	nm
Volume^Porod	160	nm³

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