BMRB Entry 16325

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16325
MolProbity Validation Chart

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Title:
Chemical shift assignments of the second domain of the listeria protein Lin2157, Northeast Structural Genomics Consortium target Lkr136b
Deposition date:
2009-05-29
Original release date:
2009-06-11
Authors:
Wang, Xu; Hamilton, Keith; Xiao, Rong; Lee, Dan; Ciccosanti, Colleen; Nair, R.; Rost, B.; Acton, T.; Swapna, G.; Everett, John; Montelione, Gaetano; Prestegard, James
Citation:

Citation: Wang, Xu; Montelione, Gaetano; Prestegard, James. "Solution Structure of Lkr136b"  .

Assembly members:

Assembly members:
lkr136b, polymer, 100 residues, 11058 Da.

Natural source:

Natural source:   Common Name: Listeria innocua   Taxonomy ID: 1642   Superkingdom: Bacteria   Kingdom: Firmicutes   Genus/species: Listeria innocua

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET121

Entity Sequences (FASTA):

Entity Sequences (FASTA):
lkr136b: MVKVTYDGVYVLSVKEDVPA AGILHAGDLITEIDGQSFKS SQEFIDYIHSKKVGDTVKIK YKHGNKNEEASIKLTAIDKK GTPGIGITLVDDLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts395
15N chemical shifts92
1H chemical shifts520
residual dipolar couplings71

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1lkr136b1

Entities:

Entity 1, lkr136b 100 residues - 11058 Da.

residues L93 to H100 are part of a His tag

1   METVALLYSVALTHRTYRASPGLYVALTYR
2   VALLEUSERVALLYSGLUASPVALPROALA
3   ALAGLYILELEUHISALAGLYASPLEUILE
4   THRGLUILEASPGLYGLNSERPHELYSSER
5   SERGLNGLUPHEILEASPTYRILEHISSER
6   LYSLYSVALGLYASPTHRVALLYSILELYS
7   TYRLYSHISGLYASNLYSASNGLUGLUALA
8   SERILELYSLEUTHRALAILEASPLYSLYS
9   GLYTHRPROGLYILEGLYILETHRLEUVAL
10   ASPASPLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: lkr136b, [U-100% 13C; U-100% 15N], 1.18 mM; DTT 10 mM; sodium azide 0.02%; sodium chloride 200 mM; sodium acetate 20 mM; calcium chloride 5 mM; H2O 90%; D2O 10%

sample_2: lkr136b, [U-100% 13C; U-100% 15N], 1.18 mM; pentaethylene glycol monododecyl ether 4%; sodium chloride 200 mM; sodium azide 0.02%; DTT 10 mM; sodium acetate 20 mM; calcium chloride 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D HSQC/TROSYsample_1isotropicsample_conditions_1
2D HSQC/TROSYsample_2anisotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

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

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAC97387
GB EFR93256 EHN62540 KJR55152 KJR55498
REF WP_003767762 WP_003769606 WP_010991039 WP_033532865

Download HSQC peak lists in one of the following formats:
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