BMRB Entry 28102

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

Data sets:
Data typeCount
13C chemical shifts780
15N chemical shifts180
1H chemical shifts991

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1BpsDsbA monomer1

Entities:

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

1   SERASNALAALAGLYPHEALAGLNALASER
2   PROSERALAPROVALALAGLYLYSASPPHE
3   GLUVALMETLYSSERPROGLNPROVALSER
4   ALAPROALAGLYLYSVALGLUVALILEGLU
5   PHEPHETRPTYRGLYCYSPROHISCYSTYR
6   GLUPHEGLUPROTHRILEGLUALATRPVAL
7   LYSLYSGLNGLYASPLYSILEALAPHELYS
8   ARGVALPROVALALAPHEARGASPASPPHE
9   VALPROHISSERLYSLEUPHETYRALALEU
10   ALAALALEUGLYVALSERGLULYSVALTHR
11   PROALAVALPHEASNALAILEHISLYSGLU
12   LYSASNTYRLEULEUTHRPROGLNALAGLN
13   ALAASPPHELEUALATHRGLNGLYVALASP
14   LYSLYSLYSPHELEUASPALATYRASNSER
15   PHESERVALGLNGLYGLNVALLYSGLNSER
16   ALAGLULEULEULYSASNTYRASNILEASP
17   GLYVALPROTHRILEVALVALGLNGLYLYS
18   TYRLYSTHRGLYPROALATYRTHRASNSER
19   LEUGLUGLYTHRALAGLNVALLEUASPPHE
20   LEUVALLYSGLNVALGLNASPLYSLYSLEU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D CHD2-C-TOCSYsample_1isotropicsample_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