BMRB Entry 16330

Title:
1H, 15N and 13C chemical shift assignments for the reduced form of the DsbA oxidoreductase from Staphylococcus aureus
Deposition date:
2009-06-03
Original release date:
2009-12-11
Authors:
Williams, Martin; Chalmers, David; Martin, Jennifer; Scanlon, Martin
Citation:

Citation: Williams, Martin; Chalmers, David; Martin, Jennifer; Scanlon, Martin. "Backbone and side chain 1H, 15N and 13C assignments for the oxidised and reduced forms of the oxidoreductase protein DsbA from Staphylococcus aureus."  Biomol. NMR Assignments 4, 25-28 (2010).
PubMed: 19936968

Assembly members:

Assembly members:
SaDsbA_Oxidoreductase, polymer, 186 residues, 21635 Da.

Natural source:

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts498
15N chemical shifts158
1H chemical shifts158

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DsbA monomer1

Entities:

Entity 1, DsbA monomer 186 residues - 21635 Da.

1   METALASERALATHRTHRSERSERLYSASN
2   GLYLYSPROLEUVALVALVALTYRGLYASP
3   TYRLYSCYSPROTYRCYSLYSGLULEUASP
4   GLULYSVALMETPROLYSLEUARGLYSASN
5   TYRILEASPASNHISLYSVALGLUTYRGLN
6   PHEVALASNLEUALAPHELEUGLYLYSASP
7   SERILEVALGLYSERARGALASERHISALA
8   VALLEUMETTYRALAPROLYSSERPHELEU
9   ASPPHEGLNLYSGLNLEUPHEALAALAGLN
10   GLNASPGLUASNLYSGLUTRPLEUTHRLYS
11   GLULEULEUASPLYSHISILELYSGLNLEU
12   HISLEUASPLYSGLUTHRGLUASNLYSILE
13   ILELYSASPTYRLYSTHRLYSASPSERLYS
14   SERTRPLYSALAALAGLULYSASPLYSLYS
15   ILEALALYSASPASNHISILELYSTHRTHR
16   PROTHRALAPHEILEASNGLYGLULYSVAL
17   GLUASPPROTYRASPTYRGLUSERTYRGLU
18   LYSLEULEULYSASPLYSILELYSLEUGLU
19   HISHISHISHISHISHIS

Samples:

sample_1: SaDsbA Oxidoreductase, [U-95% 13C; U-90% 15N], 0.24 ± 0.04 mM; HEPES 10 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 10 mM; pH: 6.8; pressure: 1 atm; temperature: 318 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NH-TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY v3.113, Goddard - chemical shift assignment, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16329
PDB
DBJ BAB43499 BAB58571 BAB96196 BAF68580 BAF79276
EMBL CAG41479 CAG44113 CAI81978 CAQ50840 CBI50404
GB AAG41993 AAW37232 ABD21498 ABD31702 ABQ50211
REF WP_000162799 WP_000162803 WP_000162804 WP_000162805 WP_000162807

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