BMRB Entry 16922

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16922
MolProbity Validation Chart

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Title:
Backbone structure of the membrane domain of E. coli histidine kinase receptor KdpD
Deposition date:
2010-05-11
Original release date:
2010-06-15
Authors:
Maslennikov, Innokentiy; Klammt, Christian; Kefala, Georgia; Okamura, Mizuki; Esquivies, Luis; Kwiatkowski, Witek; Choe, Senyon
Citation:

Citation: Maslennikov, Innokentiy; Klammt, Christian; Hwang, Eunha; Kefala, Georgia; Okamura, Mizuki; Esquivies, Luis; Mors, Karsten; Glaubitz, Clemens; Kwiatkowski, Witek; Jeon, Young Ho; Choe, Senyon. "Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis."  Proc. Natl. Acad. Sci. U.S.A. 107, 10902-10907 (2010).
PubMed: 20498088

Assembly members:

Assembly members:
histidine kinase receptor KdpD, polymer, 107 residues, 11442.749 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: pIVEX2.3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
histidine kinase receptor KdpD: MVQIQGSVVAAALSAVITLI AMQWLMAFDAANLVMLYLLG VVVVALFYGRWPSVVATVIN VVSFDLFFIAPRGTLAVSDV QYLLTFAVMLTVGLVIGNLT AGVRYQA

Data sets:
Data typeCount
13C chemical shifts257
15N chemical shifts102
1H chemical shifts102

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1histidine kinase receptor KdpD1

Entities:

Entity 1, histidine kinase receptor KdpD 107 residues - 11442.749 Da.

1   METVALGLNILEGLNGLYSERVALVALALA
2   ALAALALEUSERALAVALILETHRLEUILE
3   ALAMETGLNTRPLEUMETALAPHEASPALA
4   ALAASNLEUVALMETLEUTYRLEULEUGLY
5   VALVALVALVALALALEUPHETYRGLYARG
6   TRPPROSERVALVALALATHRVALILEASN
7   VALVALSERPHEASPLEUPHEPHEILEALA
8   PROARGGLYTHRLEUALAVALSERASPVAL
9   GLNTYRLEULEUTHRPHEALAVALMETLEU
10   THRVALGLYLEUVALILEGLYASNLEUTHR
11   ALAGLYVALARGTYRGLNALA

Samples:

sample_1: DSS 0.5 mM; Mes-BisTris 20 mM; 1-myristoyl-2-hydroxy-sn-glycero-3-[phospho-rac-(1-glycerol)] 100 mM; histidine kinase receptor KdpD, [U-99% 13C; U-99% 15N], 0.3 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v1.0.6, Guntert, Mumenthaler and Wuthrich - structure solution

CARA v2K.2, Keller and Wuthrich - data analysis, peak picking

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAA35352 BAB34146 BAG76279 BAI24084 BAI29552
EMBL CAP75181 CAQ31160 CAQ97539 CAR06880 CAR11989
GB AAA24041 AAC73789 AAG55016 AAN79253 AAZ87404
REF NP_308750 NP_415223 WP_001295875 WP_001297245 WP_001298625
SP P21865
AlphaFold P21865

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