BMRB Entry 16689

Title:
Backbone and side chain 1H, 15N and 13C assignments for a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125
Deposition date:
2010-01-21
Original release date:
2010-05-18
Authors:
Collins, Tony; Matzapetakis, Manolis; Santos, Helena
Citation:

Citation: Collins, Tony; Matzapetakis, Manolis; Santos, Helena. "Backbone and side chain 1H, 15N and 13C assignments for a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125."  Biomol. NMR Assignments 4, 151-154 (2010).
PubMed: 20455034

Assembly members:

Assembly members:
PshDsbA, polymer, 187 residues, 20809.7 Da.

Natural source:

Natural source:   Common Name: Pseudoalteromonas haloplanktis   Taxonomy ID: 228   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Pseudoalteromonas haloplanktis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b(+)

Data sets:
Data typeCount
13C chemical shifts880
15N chemical shifts200
1H chemical shifts1376

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DsbA1

Entities:

Entity 1, DsbA 187 residues - 20809.7 Da.

This is the mature protein sequence after cleavage of the 20 aminoacid signal peptide

1   ALAASNPHEGLUVALGLYASNGLNTYRTHR
2   VALILEASPILEGLULYSSERTHRTHRPRO
3   GLNVALTHRGLUTYRPHESERPHETYRCYS
4   PROHISCYSPHELYSPHEGLUPROVALALA
5   HISALAILEGLUGLUASNLEUPROALAGLY
6   ALAVALPHEILELYSASNHISVALASNPHE
7   LEUGLYGLYVALSERPROGLNTHRGLNSER
8   ASNLEUSERLEUALATYRLEUVALALALYS
9   LYSHISGLYGLNALAASPTHRILETHRASP
10   LYSILEPHELYSSERILEHISVALGLNARG
11   ALAPROLEUTHRGLUILELYSASPLEULYS
12   LYSLEULEUASPILEASNGLYILESERSER
13   ASPTHRPHEASPGLNASPILEALASERMET
14   PROILEILEALAALAGLUGLNALAMETGLN
15   ASPLYSGLNASNLYSTYRSERLYSLEUGLY
16   ALALEUTHRGLYVALPROTHRPHEILEVAL
17   ASNASPLYSTYRLYSILEASNLEUASNTHR
18   ILELYSSERGLNGLUGLULEUASPGLULEU
19   VALSERPHELEULEUALALEU

Samples:

13C15N: PshDsbA, [U-13C; U-15N], 2 mM; MOPS 10 mM; sodium chloride 50 mM; EDTA 1 mM; sodium azide 0.1 mM; H2O 95%; D2O 5%

15N: PshDsbA, [U-15N], 1.5 mM; MOPS 10 mM; sodium chloride 50 mM; EDTA 1 mM; sodium azide 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 60 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15Nisotropicsample_conditions_1
2D 1H-13C HSQC13C15Nisotropicsample_conditions_1
2D 1H-1H TOCSY15Nisotropicsample_conditions_1
2D 1H-1H NOESY15Nisotropicsample_conditions_1
3D HNCO13C15Nisotropicsample_conditions_1
3D HCACO13C15Nisotropicsample_conditions_1
3D HNCA13C15Nisotropicsample_conditions_1
3D HN(CO)CA13C15Nisotropicsample_conditions_1
3D HBHA(CO)NH13C15Nisotropicsample_conditions_1
3D CBCA(CO)NH13C15Nisotropicsample_conditions_1
3D CBCANH13C15Nisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
3D 1H-15N TOCSY15Nisotropicsample_conditions_1
3D 1H-13C NOESY13C15Nisotropicsample_conditions_1
hbCBcgcdceHE13C15Nisotropicsample_conditions_1
hbCBcgcdHD13C15Nisotropicsample_conditions_1
3D HNHA15Nisotropicsample_conditions_1
3D HCCH-TOCSY13C15Nisotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - data analysis, peak picking

RCI, (Berjanskii and Wishart ) - random coil prediction

CSI, (Wishart and Sykes) - secondary structure prediction

Checkshift, (Ginzinger, Skočibu ić and Heun - chemical shift recalibration

NMR spectrometers:

  • Bruker Avance II+ 800 MHz

Related Database Links:

EMBL CAG25536 CAI85351
REF WP_011326965

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