BMRB Entry 28102

Name: Resonance assignments of oxidized BpsDsbA
Published: 2021-07-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28102

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Resonance assignments of oxidized BpsDsbA

Deposition date:

2020-03-22

Original release date:

2021-07-16

Authors:

Mohanty, Biswaranjan; Nebl, Stefan; Scanlon, Martin

Citation:

Citation: Nebl, Stefan; Alwan, Wesam; Williams, Martin; Sharma, Gaurav; Taylor, Ashley; Doak, Bradley; Wilde, Karyn; McMahon, Roisin; Halili, Maria; Martin, Jennifer; Capuano, Ben; Fenwick, R Bryn; Mohanty, Biswaranjan; Scanlon, Martin. "NMR fragment screening reveals a novel small molecule binding site near the catalytic surface of the disulfide-dithiol oxidoreductase enzyme DsbA from Burkholderia pseudomallei" J. Biomol. NMR 74, 595-611 (2020).
PubMed: 32761504

Assembly members:

Assembly members:
BpsDsbA, polymer, 200 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Burkholderia pseudomallei Taxonomy ID: 28450 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia pseudomallei

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BpsDsbA: SNAAGFAQASPSAPVAGKDF EVMKSPQPVSAPAGKVEVIE FFWYGCPHCYEFEPTIEAWV KKQGDKIAFKRVPVAFRDDF VPHSKLFYALAALGVSEKVT PAVFNAIHKEKNYLLTPQAQ ADFLATQGVDKKKFLDAYNS FSVQGQVKQSAELLKNYNID GVPTIVVQGKYKTGPAYTNS LEGTAQVLDFLVKQVQDKKL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	780
15N chemical shifts	180
1H chemical shifts	991

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BpsDsbA monomer	1

Entities:

Entity 1, BpsDsbA monomer 200 residues - Formula weight is not available

1	SER	ASN	ALA	ALA	GLY	PHE	ALA	GLN	ALA	SER
2	PRO	SER	ALA	PRO	VAL	ALA	GLY	LYS	ASP	PHE
3	GLU	VAL	MET	LYS	SER	PRO	GLN	PRO	VAL	SER
4	ALA	PRO	ALA	GLY	LYS	VAL	GLU	VAL	ILE	GLU
5	PHE	PHE	TRP	TYR	GLY	CYS	PRO	HIS	CYS	TYR
6	GLU	PHE	GLU	PRO	THR	ILE	GLU	ALA	TRP	VAL
7	LYS	LYS	GLN	GLY	ASP	LYS	ILE	ALA	PHE	LYS
8	ARG	VAL	PRO	VAL	ALA	PHE	ARG	ASP	ASP	PHE
9	VAL	PRO	HIS	SER	LYS	LEU	PHE	TYR	ALA	LEU
10	ALA	ALA	LEU	GLY	VAL	SER	GLU	LYS	VAL	THR
11	PRO	ALA	VAL	PHE	ASN	ALA	ILE	HIS	LYS	GLU
12	LYS	ASN	TYR	LEU	LEU	THR	PRO	GLN	ALA	GLN
13	ALA	ASP	PHE	LEU	ALA	THR	GLN	GLY	VAL	ASP
14	LYS	LYS	LYS	PHE	LEU	ASP	ALA	TYR	ASN	SER
15	PHE	SER	VAL	GLN	GLY	GLN	VAL	LYS	GLN	SER
16	ALA	GLU	LEU	LEU	LYS	ASN	TYR	ASN	ILE	ASP
17	GLY	VAL	PRO	THR	ILE	VAL	VAL	GLN	GLY	LYS
18	TYR	LYS	THR	GLY	PRO	ALA	TYR	THR	ASN	SER
19	LEU	GLU	GLY	THR	ALA	GLN	VAL	LEU	ASP	PHE
20	LEU	VAL	LYS	GLN	VAL	GLN	ASP	LYS	LYS	LEU

Samples:

sample_1: BpsDsbA, [U-13C; U-15N], 0.6 mM; BpsDsbA, Fractional deuterated [U-13C; U-15N], 1 mM; HEPES 50 mM; NaCl 50 mM; NaN3 0.02%; EDTA 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D CHD2-C-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2 (pl7), Bruker Biospin - collection, data analysis, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

1	SER	ASN	ALA	ALA	GLY	PHE	ALA	GLN	ALA	SER
2	PRO	SER	ALA	PRO	VAL	ALA	GLY	LYS	ASP	PHE
3	GLU	VAL	MET	LYS	SER	PRO	GLN	PRO	VAL	SER
4	ALA	PRO	ALA	GLY	LYS	VAL	GLU	VAL	ILE	GLU
5	PHE	PHE	TRP	TYR	GLY	CYS	PRO	HIS	CYS	TYR
6	GLU	PHE	GLU	PRO	THR	ILE	GLU	ALA	TRP	VAL
7	LYS	LYS	GLN	GLY	ASP	LYS	ILE	ALA	PHE	LYS
8	ARG	VAL	PRO	VAL	ALA	PHE	ARG	ASP	ASP	PHE
9	VAL	PRO	HIS	SER	LYS	LEU	PHE	TYR	ALA	LEU
10	ALA	ALA	LEU	GLY	VAL	SER	GLU	LYS	VAL	THR
11	PRO	ALA	VAL	PHE	ASN	ALA	ILE	HIS	LYS	GLU
12	LYS	ASN	TYR	LEU	LEU	THR	PRO	GLN	ALA	GLN
13	ALA	ASP	PHE	LEU	ALA	THR	GLN	GLY	VAL	ASP
14	LYS	LYS	LYS	PHE	LEU	ASP	ALA	TYR	ASN	SER
15	PHE	SER	VAL	GLN	GLY	GLN	VAL	LYS	GLN	SER
16	ALA	GLU	LEU	LEU	LYS	ASN	TYR	ASN	ILE	ASP
17	GLY	VAL	PRO	THR	ILE	VAL	VAL	GLN	GLY	LYS
18	TYR	LYS	THR	GLY	PRO	ALA	TYR	THR	ASN	SER
19	LEU	GLU	GLY	THR	ALA	GLN	VAL	LEU	ASP	PHE
20	LEU	VAL	LYS	GLN	VAL	GLN	ASP	LYS	LYS	LEU

1	SER	ASN	ALA	ALA	GLY	PHE	ALA	GLN	ALA	SER
2	PRO	SER	ALA	PRO	VAL	ALA	GLY	LYS	ASP	PHE
3	GLU	VAL	MET	LYS	SER	PRO	GLN	PRO	VAL	SER
4	ALA	PRO	ALA	GLY	LYS	VAL	GLU	VAL	ILE	GLU
5	PHE	PHE	TRP	TYR	GLY	CYS	PRO	HIS	CYS	TYR
6	GLU	PHE	GLU	PRO	THR	ILE	GLU	ALA	TRP	VAL
7	LYS	LYS	GLN	GLY	ASP	LYS	ILE	ALA	PHE	LYS
8	ARG	VAL	PRO	VAL	ALA	PHE	ARG	ASP	ASP	PHE
9	VAL	PRO	HIS	SER	LYS	LEU	PHE	TYR	ALA	LEU
10	ALA	ALA	LEU	GLY	VAL	SER	GLU	LYS	VAL	THR
11	PRO	ALA	VAL	PHE	ASN	ALA	ILE	HIS	LYS	GLU
12	LYS	ASN	TYR	LEU	LEU	THR	PRO	GLN	ALA	GLN
13	ALA	ASP	PHE	LEU	ALA	THR	GLN	GLY	VAL	ASP
14	LYS	LYS	LYS	PHE	LEU	ASP	ALA	TYR	ASN	SER
15	PHE	SER	VAL	GLN	GLY	GLN	VAL	LYS	GLN	SER
16	ALA	GLU	LEU	LEU	LYS	ASN	TYR	ASN	ILE	ASP
17	GLY	VAL	PRO	THR	ILE	VAL	VAL	GLN	GLY	LYS
18	TYR	LYS	THR	GLY	PRO	ALA	TYR	THR	ASN	SER
19	LEU	GLU	GLY	THR	ALA	GLN	VAL	LEU	ASP	PHE
20	LEU	VAL	LYS	GLN	VAL	GLN	ASP	LYS	LYS	LEU

1	SER	ASN	ALA	ALA	GLY	PHE	ALA	GLN	ALA	SER
2	PRO	SER	ALA	PRO	VAL	ALA	GLY	LYS	ASP	PHE
3	GLU	VAL	MET	LYS	SER	PRO	GLN	PRO	VAL	SER
4	ALA	PRO	ALA	GLY	LYS	VAL	GLU	VAL	ILE	GLU
5	PHE	PHE	TRP	TYR	GLY	CYS	PRO	HIS	CYS	TYR
6	GLU	PHE	GLU	PRO	THR	ILE	GLU	ALA	TRP	VAL
7	LYS	LYS	GLN	GLY	ASP	LYS	ILE	ALA	PHE	LYS
8	ARG	VAL	PRO	VAL	ALA	PHE	ARG	ASP	ASP	PHE
9	VAL	PRO	HIS	SER	LYS	LEU	PHE	TYR	ALA	LEU
10	ALA	ALA	LEU	GLY	VAL	SER	GLU	LYS	VAL	THR
11	PRO	ALA	VAL	PHE	ASN	ALA	ILE	HIS	LYS	GLU
12	LYS	ASN	TYR	LEU	LEU	THR	PRO	GLN	ALA	GLN
13	ALA	ASP	PHE	LEU	ALA	THR	GLN	GLY	VAL	ASP
14	LYS	LYS	LYS	PHE	LEU	ASP	ALA	TYR	ASN	SER
15	PHE	SER	VAL	GLN	GLY	GLN	VAL	LYS	GLN	SER
16	ALA	GLU	LEU	LEU	LYS	ASN	TYR	ASN	ILE	ASP
17	GLY	VAL	PRO	THR	ILE	VAL	VAL	GLN	GLY	LYS
18	TYR	LYS	THR	GLY	PRO	ALA	TYR	THR	ASN	SER
19	LEU	GLU	GLY	THR	ALA	GLN	VAL	LEU	ASP	PHE
20	LEU	VAL	LYS	GLN	VAL	GLN	ASP	LYS	LYS	LEU