BMRB Entry 15627

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15627

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Title:
1H, 13C and 15N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis
Deposition date:
2008-01-18
Original release date:
2008-04-22
Authors:
Quinternet, Marc; Selme, Laure; Beaufils, Chrystel; Tsan, Pascale; Boschi-Muller, Sandrine; Averlant-Petit, Marie-Christine; Branlant, Guy; Cung, Manh-Thong
Citation:

Citation: Quinternet, Marc; Selme, Laure; Beaufils, Chrystel; Tsan, Pascale; Jacob, Christophe; Boschi-Muller, Sandrine; Averlant-Petit, Marie-Christine; Branlant, Guy; Cung, Manh-Thong. "1H, 13C, and 15N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis"  Biomol. NMR Assignments 2, 85-87 (2008).
PubMed: 19636931

Assembly members:

Assembly members:
nDsbD, polymer, 128 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Micrococcus meningitidis   Taxonomy ID: 487   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Neisseria meningitidis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETnDsbDC103S

Entity Sequences (FASTA):

Entity Sequences (FASTA):
nDsbD: MALDANDLLPPEKAFVPELA VADDGVNVRFRIADGYYMYQ AKIVGKTNPADLLGQPSFSK GEEKEDEFFGRQTVYHHEAQ VAFPYAKAVGEPYKLVLTYQ GSAEAGVCYPPVDTEFDIFG NGTYHPQT

Data sets:
Data typeCount
13C chemical shifts529
15N chemical shifts115
1H chemical shifts787

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1

Entities:

Entity 1, protein 128 residues - Formula weight is not available

1   METALALEUASPALAASNASPLEULEUPRO
2   PROGLULYSALAPHEVALPROGLULEUALA
3   VALALAASPASPGLYVALASNVALARGPHE
4   ARGILEALAASPGLYTYRTYRMETTYRGLN
5   ALALYSILEVALGLYLYSTHRASNPROALA
6   ASPLEULEUGLYGLNPROSERPHESERLYS
7   GLYGLUGLULYSGLUASPGLUPHEPHEGLY
8   ARGGLNTHRVALTYRHISHISGLUALAGLN
9   VALALAPHEPROTYRALALYSALAVALGLY
10   GLUPROTYRLYSLEUVALLEUTHRTYRGLN
11   GLYSERALAGLUALAGLYVALCYSTYRPRO
12   PROVALASPTHRGLUPHEASPILEPHEGLY
13   ASNGLYTHRTYRHISPROGLNTHR

Samples:

sample_1: nDsbD, [U-100% 13C; U-100% 15N], 0.5 mM; Potassium phosphate (KPi) 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 299 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

XEASY, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CAM08848 CAM10655 CAX49754 CBA05538 CBA06830
GB AAF41875 ABX73592 ADY95333 ADY99950 ADZ01187
PIR B81868
REF NP_274527 WP_002232751 WP_002234074 WP_002235976 WP_002238135
SP Q9JTL9 Q9JYM0
AlphaFold Q9JTL9 Q9JYM0

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