BMRB Entry 17831

Title:
1H, 13C and 15N resonance assignments for oxidised and reduced nDsbD from Escherichia coli   PubMed: 21543317
Deposition date:
2011-08-04
Original release date:
2011-10-25
Authors:
Mavridou, Despoina; Stelzl, Lukas; Ferguson, Stuart; Redfield, Christina
Citation:

Citation: Mavridou, Despoina; Saridakis, Emmanuel; Kritsiligkou, Paraskevi; Goddard, Alan; Stevens, Julie; Ferguson, Stuart; Redfield, Christina. "Oxidation state-dependent protein-protein interactions in disulfide cascades."  J. Biol. Chem. 286, 24943-24956 (2011).

Assembly members:

Assembly members:
nDsbD-ox, polymer, 139 residues, 15604.5 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Experimental source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Data sets:
Data typeCount
13C chemical shifts475
15N chemical shifts119
1H chemical shifts746

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1nDsbD-ox1

Entities:

Entity 1, nDsbD-ox 139 residues - 15604.5 Da.

Residues L2-V132 of the native sequence have been deposited. This is the N-terminal periplasmic domain of a membrane protein. The N-terminal residues MDT are a result of the cloning process. Residues G133-R137 remain after thrombin cleavage of the affinity tag.

1   METASPTHRLEUPHEASPALAPROGLYARG
2   SERGLNPHEVALPROALAASPGLNALAPHE
3   ALAPHEASPPHEGLNGLNASNGLNHISASP
4   LEUASNLEUTHRTRPGLNILELYSASPGLY
5   TYRTYRLEUTYRARGLYSGLNILEARGILE
6   THRPROGLUHISALALYSILEALAASPVAL
7   GLNLEUPROGLNGLYVALTRPHISGLUASP
8   GLUPHETYRGLYLYSSERGLUILETYRARG
9   ASPARGLEUTHRLEUPROVALTHRILEASN
10   GLNALASERALAGLYALATHRLEUTHRVAL
11   THRTYRGLNGLYCYSALAASPALAGLYPHE
12   CYSTYRPROPROGLUTHRLYSTHRVALPRO
13   LEUSERGLUVALVALALAASNASNALAALA
14   PROGLNPROVALGLYLEUVALPROARG

Samples:

sample_1: nDsbD-ox, [U-98% 15N], 0.5 – 1.0 mM; H2O 95%; D2O 5%

sample_2: nDsbD-ox, [U-98% 13C; U-98% 15N], 0.5 – 1.0 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D 1H-15N HSQC-NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

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

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • home-built home-built using GE Omega software 750 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 17830
PDB
DBJ BAB38540 BAE78138 BAG66862 BAG79959 BAI28440
EMBL CAA54781 CAA85375 CAQ34485 CAR01112 CAR05872
GB AAA97035 AAC77096 AAG59335 AAN45708 AAN83640
REF NP_313144 NP_418559 NP_710001 WP_000068901 WP_000068902
SP P36655 P58162 Q0SXE3 Q0T9Q5 Q1R3C4
AlphaFold P36655

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