BMRB Entry 15529

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15529

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Title:
Back bone chemical shifts of B. subtillis protein YkuJ, Northeast Structural Genomics Consortium Target SR360.
Deposition date:
2007-10-17
Original release date:
2007-10-31
Authors:
Wang, Xu; Ho, Chi-Kent; Janjua, Haleema; Cunningham, Kellie; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Bansal, Sonal; Prestegard, James
Citation:

Citation: Wang, Xu; Bansal, Sonal; Jiang, Mei; Prestegard, James. "RDC-assisted modeling of symmetric protein homo-oligomers"  Protein. Sci. 17, 899-907 (2008).
PubMed: 18436958

Assembly members:

Assembly members:
SR360, polymer, 87 residues, 10320.8 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SR360: MSQLMGIITRLQSLQETAEA ANEPMQRYFEVNGEKICSVK YFEKNQTFELTVFQKGEKPN TYPFDNIDMVSIEIFELLQL EHHHHHH

Data sets:
Data typeCount
13C chemical shifts137
15N chemical shifts70
1H chemical shifts70
residual dipolar couplings111

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SR3601

Entities:

Entity 1, SR360 87 residues - 10320.8 Da.

Last 8 residues are part of the His tag

1   METSERGLNLEUMETGLYILEILETHRARG
2   LEUGLNSERLEUGLNGLUTHRALAGLUALA
3   ALAASNGLUPROMETGLNARGTYRPHEGLU
4   VALASNGLYGLULYSILECYSSERVALLYS
5   TYRPHEGLULYSASNGLNTHRPHEGLULEU
6   THRVALPHEGLNLYSGLYGLULYSPROASN
7   THRTYRPROPHEASPASNILEASPMETVAL
8   SERILEGLUILEPHEGLULEULEUGLNLEU
9   GLUHISHISHISHISHISHIS

Samples:

sample_1: SR360, [U-100% 13C; U-100% 15N], 1.2 ± 0.1 mM; D2O 5%; DTT 100 mM; MES 20 mM; sodium chloride 100 mM; Calcium Chloride 5 mM

sample_2: SR360, [5% 13C; U-100% 15N], 1.2 ± 0.1 mM; D2O 5%; DTT 100 mM; MES 20 mM; sodium chloride 100 mM; Calcium Chloride 5 mM; pentaethylene glycol monododecyl ether 0.04 v/v; Hexanol 0.006 v/v

sample_3: SR360, [5% 13C; U-100% 15N], 1.2 ± 0.1 mM; D2O 5%; DTT 100 mM; MES 20 mM; sodium chloride 100 mM; Calcium Chloride 5 mM; Pf1 phage 0.01 w/v

sample_conditions_1: ionic strength: 0.115 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D IPAP 1H,15N-HSQCsample_2anisotropicsample_conditions_1
2D IPAP 1H-15N HSQCsample_3anisotropicsample_conditions_1

Software:

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

REDCAT, Valafar,Losonszi,Prestegard - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

DBJ BAI85020 BAM52055 BAM57632 GAK78526
EMBL CAA10873 CAB13283 CBI42612 CCF04895 CCG49344
GB ABS73750 ADM37497 ADV96428 AEB24186 AEB63055
REF NP_389293 WP_003154613 WP_003218671 WP_010334055 WP_013352074
SP O34588
AlphaFold O34588

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