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 28052

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28052
MolProbity Validation Chart

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Title: 1H, 13C, and 15N chemical shift assignments of the C. diphtheriae methionine sulfoxide reductase B   PubMed: 31992594

Deposition date: 2019-11-29 Original release date: 2020-01-30

Authors: Tossounian, Maria-Armineh; Messens, Joris; Volkov, Alexander

Citation: Tossounian, Maria-Armineh; Khanh Truong, Anh-Co; Buts, Lieven; Wahni, Khadija; Mourenza, Alvaro; Leermakers, Martine; Vertommen, Didier; Mateos, Luis Mariano; Volkov, Alexander; Messens, Joris. "Methionine sulfoxide reductase B from Corynebacterium diphtheriae catalyzes sulfoxide reduction via an intramolecular disulfide cascade"  J. Biol. Chem. 295, 3664-3677 (2020).

Assembly members:
MsrB, polymer, 136 residues, Formula weight is not available
ZINC ION, non-polymer, 65.409 Da.

Natural source:   Common Name: Corynebacterium diphtheriae   Taxonomy ID: 1717   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Corynebacterium diphtheriae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b(+)

Entity Sequences (FASTA):
MsrB: MTNFKLITDTEWRQRLSSEE YRVLREAGTEAPHTGEYTNT TTEGIYSCRACGTELFRSTE KFNSHCGWPSFFSPLAGDKV IERTDTSHGMVRTEVICANC ESHLGHVFAGEGYDTPTDLR YCINSVCLTLIPAEES

Data sets:
Data typeCount
13C chemical shifts488
15N chemical shifts121
1H chemical shifts746

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1MsrB1
2Zinc2

Entities:

Entity 1, MsrB 136 residues - Formula weight is not available

1   METTHRASNPHELYSLEUILETHRASPTHR
2   GLUTRPARGGLNARGLEUSERSERGLUGLU
3   TYRARGVALLEUARGGLUALAGLYTHRGLU
4   ALAPROHISTHRGLYGLUTYRTHRASNTHR
5   THRTHRGLUGLYILETYRSERCYSARGALA
6   CYSGLYTHRGLULEUPHEARGSERTHRGLU
7   LYSPHEASNSERHISCYSGLYTRPPROSER
8   PHEPHESERPROLEUALAGLYASPLYSVAL
9   ILEGLUARGTHRASPTHRSERHISGLYMET
10   VALARGTHRGLUVALILECYSALAASNCYS
11   GLUSERHISLEUGLYHISVALPHEALAGLY
12   GLUGLYTYRASPTHRPROTHRASPLEUARG
13   TYRCYSILEASNSERVALCYSLEUTHRLEU
14   ILEPROALAGLUGLUSER

Entity 2, Zinc - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: MsrB, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 2 mM; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 165 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

CCPN, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

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