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 17266

Title: Solution structure of the C-terminal domain of SilB from Cupriavidus metallidurans   PubMed: 21299248

Authors: Bersch, Beate; Derfoufi, Kheiro-Mouna; Vandenbussche, Guy

Citation: Bersch, Beate; Derfoufi, Kheiro-Mouna; De Angelis, Fabien; Auquier, Vanessa; Ngonlong Ekende, Elisabeth; Mergeay, Max; Ruysschaert, Jean-Marie; Vandenbussche, Guy. "Structural and Metal Binding Characterization of the C-Terminal Metallochaperone Domain of Membrane Fusion Protein SilB from Cupriavidus metallidurans CH34."  Biochemistry 50, 2194-2204 (2011).

Assembly members:
SilB(440-521), polymer, 82 residues, 8540.854 Da.

Natural source:   Common Name: Cupriavidus metallidurans   Taxonomy ID: not available   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Cupriavidus metallidurans

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

Entity Sequences (FASTA):
SilB(440-521): GPEHRAVGRIQSIGERSLII AHEAIPSAQWGAMTMEFAAP PAGLPQGLKAGDRVAFSFRL DPHGMATLVTVAPQVQTAGA KP

Data sets:
Data typeCount
13C chemical shifts335
15N chemical shifts89
1H chemical shifts545
heteronuclear NOE values68
T1 relaxation values64
T2 relaxation values66

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SilB(440-521)1

Entities:

Entity 1, SilB(440-521) 82 residues - 8540.854 Da.

residues 440 to 521 in the unprocessed protein sequence have been renumbered from 1 to 82 in this pdb entry and associated data

1   GLYPROGLUHISARGALAVALGLYARGILE
2   GLNSERILEGLYGLUARGSERLEUILEILE
3   ALAHISGLUALAILEPROSERALAGLNTRP
4   GLYALAMETTHRMETGLUPHEALAALAPRO
5   PROALAGLYLEUPROGLNGLYLEULYSALA
6   GLYASPARGVALALAPHESERPHEARGLEU
7   ASPPROHISGLYMETALATHRLEUVALTHR
8   VALALAPROGLNVALGLNTHRALAGLYALA
9   LYSPRO

Samples:

sample_1: SilB(440-521), [U-100% 15N], 1 mM; MES 50 mM; H2O 90%; D2O 10%

sample_2: SilB(440-521), [U-100% 13C; U-100% 15N], 1 mM; MES 50 mM; H2O 90%; D2O 10%

sample_3: SilB(440-521), [U-100% 15N], 1 mM; MES 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(CO)CACBsample_2isotropicsample_conditions_1
3D-intraHNCAsample_2isotropicsample_conditions_1
3D-intraHN(CA)CBsample_2isotropicsample_conditions_1
2D 1H-15N HADAMACsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
T1 relaxationsample_1isotropicsample_conditions_1
T1rho relaxationsample_1isotropicsample_conditions_1
T2 relaxationsample_1isotropicsample_conditions_1
Heteronuclear NOEsample_1isotropicsample_conditions_1

Software:

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

VNMRJ, Varian - collection

NMRView, Johnson, One Moon Scientific - data analysis

BATCH, Lescop, Brutscher - chemical shift assignment

UNIO, Torsten Herrmann - chemical shift assignment, peak picking, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

CurveFit, AG Palmer - data analysis

TALOS, Cornilescu, Delaglio and Bax - determination of dihedral angles

NMR spectrometers:

  • Varian VNMRS 800 MHz
  • Varian VNMRS 600 MHz
  • Varian VNMRS 600 MHz

Related Database Links:

PDB
EMBL CAI11314
GB ABF12994 ELA00440
REF WP_008642712 WP_011229392 WP_017510653 YP_145665