BMRB Entry 26985

Title:
1H, 13C and 15N resonance assignments of SmpB from Mycobacterium tuberculosis
Deposition date:
2016-12-23
Original release date:
2017-04-26
Authors:
Yang, Juanjuan; Lin, Donghai; Liu, Yindi
Citation:

Citation: Yang, Juanjuan; Liu, Yindi; Liu, Zhao; Meng, Chun; Lin, Donghai. "Backbone and side-chain resonance assignments for the tmRNA-binding protein, SmpB, from Mycobacterium tuberculosis"  Biomol. NMR Assign. ., .-. (2017).
PubMed: 28258549

Assembly members:

Assembly members:
SmpB, polymer, 151 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28(a)

Data sets:
Data typeCount
13C chemical shifts502
15N chemical shifts130
1H chemical shifts854

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SmpB1

Entities:

Entity 1, SmpB 151 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METSERSERARGGLYGLYARGGLNILEVAL
4   ALASERASNARGLYSALAARGHISASNTYR
5   SERILEILEGLUVALPHEGLUALAGLYVAL
6   ALALEUGLNGLYTHRGLUVALLYSSERLEU
7   ARGGLUGLYGLNALASERLEUALAASPSER
8   PHEALATHRILEASPASPGLYGLUVALTRP
9   LEUARGASNALAHISILEPROGLUTYRARG
10   HISGLYSERTRPTHRASNHISGLUPROARG
11   ARGASNARGLYSLEULEULEUHISARGARG
12   GLNILEASPTHRLEUVALGLYLYSILEARG
13   GLUGLYASNPHEALALEUVALPROLEUSER
14   LEUTYRPHEALAGLUGLYLYSVALLYSVAL
15   GLULEUALALEUALAARGGLYLYSGLNALA
16   ARG

Samples:

sample_1: SmpB, [U-100% 13C; U-100% 15N], 1.0 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AMX 850 MHz

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