BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 51296

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51296

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Title: 1H, 15N & 13C resonance assignment of the periplasmic domain of OutG, major pseudopilin from Dickeya dadantii type 2 secretion system   PubMed: 35482172

Deposition date: 2022-01-27 Original release date: 2022-05-02

Authors: Jacobsen, Theis; Dazzoni, Regine; Renault, Melvin; Bardiaux, Benjamin; Nilges, Michael; Shevchik, Vladimir; Izadi-Pruneyre, Nadia

Citation: Jacobsen, Theis; Dazzoni, Regine; Renault, Melvin; Bardiaux, Benjamin; Nilges, Michael; Shevchik, Vladimir; Izadi-Pruneyre, Nadia. "Secondary structure and 1 H, 15 N & 13 C resonance assignments of the periplasmic domain of OutG, major pseudopilin from Dickeya dadantii type II secretion system"  Biomol. NMR Assign. 16, 231-236 (2022).

Assembly members:
entity_1, polymer, 125 residues, Formula weight is not available

Natural source:   Common Name: Dickeya Dadantii   Taxonomy ID: 204038   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Dickeya Dadantii

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET20b(+)

Entity Sequences (FASTA):
entity_1: GMGMGNKEKADRQKAISDIV ALESALDMYKLDNSRYPTTE QGLGALVKKPTTPPEPRSYP QDGYIRRLPQDPWGAEYQLV SPGRHGKVDVFSYGPDGMPD TDDDIGNWNVGTSAHSNGSN GNGNP

Data sets:
Data typeCount
13C chemical shifts475
15N chemical shifts117
1H chemical shifts700

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OutG1

Entities:

Entity 1, OutG 125 residues - Formula weight is not available

The first glycine is left over form the TEV cleavage site and a MG motif from the cloning.

1   GLYMETGLYMETGLYASNLYSGLULYSALA
2   ASPARGGLNLYSALAILESERASPILEVAL
3   ALALEUGLUSERALALEUASPMETTYRLYS
4   LEUASPASNSERARGTYRPROTHRTHRGLU
5   GLNGLYLEUGLYALALEUVALLYSLYSPRO
6   THRTHRPROPROGLUPROARGSERTYRPRO
7   GLNASPGLYTYRILEARGARGLEUPROGLN
8   ASPPROTRPGLYALAGLUTYRGLNLEUVAL
9   SERPROGLYARGHISGLYLYSVALASPVAL
10   PHESERTYRGLYPROASPGLYMETPROASP
11   THRASPASPASPILEGLYASNTRPASNVAL
12   GLYTHRSERALAHISSERASNGLYSERASN
13   GLYASNGLYASNPRO

Samples:

sample_1: OutG, [U-13C; U-15N], 0.43 mM; HEPES 50 mM; NaCl 100 mM; CaCl2 5 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1

Software:

CcpNMR v2.5.1 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III HD 600 MHz
  • Bruker AVANCE NEO 800 MHz

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