BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 28058

Title: NMR assignment of self-processing module of FrpC protein of Neisseria meningitidis loaded with calcium ions   PubMed: 32184239

Deposition date: 2020-01-02 Original release date: 2020-02-20

Authors: Kuban, Vojtech; Zidek, Lukas; Macek, Pavel; Hritz, Jozef; Bumba, Ladislav; M., Faldyna; K., Nedbalcova; K., Nechvatalova

Citation: Kuban, V.; Macek, P.; Hritz, J.; Nechvatalova, K.; Nedbalcova, K.; Faldyna, M.; Zidek, L.; Bumba, L.. "Structural basis of Ca 2+ -dependent self-processing activity of repeat-in-toxin proteins"  mBio 11, e00226-20-e00226-20 (2020).

Assembly members:
SPM, polymer, 179 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 Da.

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

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

Entity Sequences (FASTA):
SPM: PLALDLDGDGIETVATKGFS GSLFDHNRDGIRTATGWVSA DDGLLVRDLNGNGIIDNGAE LFGDNTKLADGSFAKHGYAA LAELDSNGDNIINAADAAFQ SLRVWQDLNQDGISQANELR TLEELGIQSLDLAYKDVNKN LGNGNTLAQQGSYTKTNGTT AKMGDLLLAADNLHSRFLE

Data typeCount
13C chemical shifts608
15N chemical shifts162
1H chemical shifts974
T1 relaxation values124
T2 relaxation values124
heteronuclear NOE values124

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SPM1
2CA2

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

Entity 2, CA - Ca - 40.078 Da.

1   CA

Samples:

sample_1: SPM, [U-100% 13C; U-100% 15N], 0.4 mM; TRIS 5 mM; sodium chloride 50 mM; sodium azide 0.1%; Calcium chloride 10 mM

sample_conditions_1: ionic strength: 65 mM; pH: 7.4; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D R2 15N,1H correlationsample_1isotropicsample_conditions_1
2D R1 15N,1H correlationsample_1isotropicsample_conditions_1
2D NOE 15N,1H correlationsample_1isotropicsample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment, peak picking

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

TOPSPIN v3.2, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 850 MHz
  • Bruker Avance 950 MHz

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