BMRB Entry 17830

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17830

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Title:
1H, 13C and 15N Resonance Assignments for Oxidised and Reduced nDsbD fromm Escherichia coli
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).
PubMed: 21543317

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
nDsbD-red: MDTLFDAPGRSQFVPADQAF AFDFQQNQHDLNLTWQIKDG YYLYRKQIRITPEHAKIADV QLPQGVWHEDEFYGKSEIYR DRLTLPVTINQASAGATLTV TYQGCADAGFCYPPETKTVP LSEVVANNAAPQPVGLVPR

Data sets:
Data typeCount
13C chemical shifts489
15N chemical shifts122
1H chemical shifts763

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1nDsbD-red1

Entities:

Entity 1, nDsbD-red 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

Related Database Links:

BMRB 17831
PDB 1JPE 1JZD 1L6P 1VRS 1Z5Y 3PFU
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 P58162 Q0SXE3 Q0T9Q5 Q1R3C4

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