BMRB Entry 16113

Title:
H, 13C, and 15N Chemical Shift Assignments of Protein yppE from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR213
Deposition date:
2009-01-09
Original release date:
2009-03-02
Authors:
Liu, Gaohua; SINGARAPU, Kiran; Parish, David; Eletsky, Alexandre; Xu, Duanxiang; HO, Chi Kent; Fang, Yinyi; CUNNINGHAM, Kellie; MA, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Liu, Gaohua; Singarapu, Kiran; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Protein yppE from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR213"  .

Assembly members:

Assembly members:
yppe, polymer, 131 residues, Formula weight is not available

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 21-23C

Data sets:
Data typeCount
13C chemical shifts388
15N chemical shifts101
1H chemical shifts814

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1yppe1

Entities:

Entity 1, yppe 131 residues - Formula weight is not available

1   METLEUSERGLNTHRLEULEUGLUMETTHR
2   GLUGLNMETILEGLUVALALAGLULYSGLY
3   ALAASPARGTYRGLNGLUGLYLYSASNSER
4   ASNHISSERTYRASPPHEPHEGLUTHRILE
5   LYSPROALAVALGLUGLUASNASPGLULEU
6   ALAALAARGTRPALAGLUGLYALALEUGLU
7   LEUILELYSVALARGARGPROLYSTYRVAL
8   HISLYSGLUGLNILEGLUALAVALLYSASP
9   ASNPHELEUGLULEUVALLEUGLNSERTYR
10   VALHISHISILEHISLYSLYSARGPHELYS
11   ASPILETHRGLUSERVALLEUTYRTHRLEU
12   HISALAVALLYSASPGLUILEALAARGGLU
13   ASPSERARGLEUGLUHISHISHISHISHIS
14   HIS

Samples:

sample_1: yppe 0.94 mM; DTT 10 mM; Arginine 50 mM; Bis-Tris pH 6.5 50 mM; DSS 50 uM; NaN3 0.02%; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESYsample_1isotropicsample_conditions_1
GFT (4,3)D HNNCABCAsample_1isotropicsample_conditions_1
GFT (4,3)D CABCA(CO)NHNsample_1isotropicsample_conditions_1
GFT (4,3) HCCHsample_1isotropicsample_conditions_1
HNCACBsample_1isotropicsample_conditions_1
HABCONHsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

AutoStruct, Huang, Tejero, Powers and Montelione - data analysis, refinement

XEASY, Bartels et al. - data analysis, peak picking, refinement

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

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAI85724 BAM52709 BAM58284 GAK79397
EMBL CAB14144 CCU58728 CEI57439 CEJ77864 CJT23466
GB AAB38463 ADV92956 AEP91245 AFQ58175 AGA23534
REF NP_390109 WP_003246080 WP_015483369 WP_015714151 WP_017696991
SP P50833
AlphaFold P50833

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