BMRB Entry 26530

Title:
NMR assignment of intrinsically disordered self-processing module of FrpC protein of Neisseria meningitidis
Deposition date:
2015-03-06
Original release date:
2015-12-04
Authors:
Kuban, Vojtech; Zidek, Lukas; Novacek, Jiri; Bumba, Ladislav
Citation:

Citation: Kuban, Vojtech; Novacek, Jiri; Bumba, Ladislav; Zidek, Lukas. "NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis"  Biomol NMR Assign. 9, 435-440 (2015).
PubMed: 26138689

Assembly members:

Assembly members:
Self-processing_module_of_FrpC, polymer, 179 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: b-proteobacteria   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: pET42b

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts154
1H chemical shifts608

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SPM1

Entities:

Entity 1, SPM 179 residues - Formula weight is not available

1   PROLEUALALEUASPLEUASPGLYASPGLY
2   ILEGLUTHRVALALATHRLYSGLYPHESER
3   GLYSERLEUPHEASPHISASNARGASPGLY
4   ILEARGTHRALATHRGLYTRPVALSERALA
5   ASPASPGLYLEULEUVALARGASPLEUASN
6   GLYASNGLYILEILEASPASNGLYALAGLU
7   LEUPHEGLYASPASNTHRLYSLEUALAASP
8   GLYSERPHEALALYSHISGLYTYRALAALA
9   LEUALAGLULEUASPSERASNGLYASPASN
10   ILEILEASNALAALAASPALAALAPHEGLN
11   SERLEUARGVALTRPGLNASPLEUASNGLN
12   ASPGLYILESERGLNALAASNGLULEUARG
13   THRLEUGLUGLULEUGLYILEGLNSERLEU
14   ASPLEUALATYRLYSASPVALASNLYSASN
15   LEUGLYASNGLYASNTHRLEUALAGLNGLN
16   GLYSERTYRTHRLYSTHRASNGLYTHRTHR
17   ALALYSMETGLYASPLEULEULEUALAALA
18   ASPASNLEUHISSERARGPHELEUGLU

Samples:

sample_1: Self-processing module of FrpC, [U-100% 13C; U-100% 15N], 0.35 mM; sodium chloride 50 mM; sodium azide 0.1 % v/v; TRIS 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 55 mM; pH: 7.4; pressure: 1 atm; temperature: 303.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
4D HCBCACONsample_1isotropicsample_conditions_1
4D HCBCANCOsample_1isotropicsample_conditions_1
5D HN(CA)CONHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - data analysis

TOPSPIN, Bruker Biospin - collection

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

MFT, W. Kozminski - processing

NMR spectrometers:

  • Bruker Avance 600 MHz

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