BMRB Entry 19707

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19707
MolProbity Validation Chart

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Title:
Solution structure of the extracellular sensor domain of DraK histidine kinase
Deposition date:
2013-12-25
Original release date:
2014-09-16
Authors:
Yeo, Kwon Joo; Cheong, Hae-Kap
Citation:

Citation: Yeo, Kwon-Joo; Hong, Young-Soo; Jee, Jun-Goo; Lee, Jae-Kyoung; Kim, Hyo-Jeong; Park, Jin-Wan; Kim, Eun-Hee; Hwang, Eunha; Kim, Sang-Yoon; Lee, Eun-Gyeong; Kwon, Ohsuk; Cheong, Hae-Kap. "Mechanism of the pH-Induced Conformational Change in the Sensor Domain of the DraK Histidine Kinase via the E83, E105, and E107 Residues"  PLoS One 9, e107168-e107168 (2014).
PubMed: 25203403

Assembly members:

Assembly members:
DraK, polymer, 90 residues, 9760.893 Da.

Natural source:

Natural source:   Common Name: High GC gram positive   Taxonomy ID: 1902   Superkingdom: Bacteria   Kingdom: Actinobacteria   Genus/species: Streptomyces coelicolor

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Streptomyces coelicolor   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DraK: GSETRTISSTAQERVDLEAV RLASIVDSRLIGTGSVDEDF LREQIRDARYAVIRIPGQPV VEVGTKPTGDVLQGRATGEE GETVLVEEPR

Data sets:
Data typeCount
1H chemical shifts619
13C chemical shifts361
15N chemical shifts93

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 90 residues - 9760.893 Da.

1   GLYSERGLUTHRARGTHRILESERSERTHR
2   ALAGLNGLUARGVALASPLEUGLUALAVAL
3   ARGLEUALASERILEVALASPSERARGLEU
4   ILEGLYTHRGLYSERVALASPGLUASPPHE
5   LEUARGGLUGLNILEARGASPALAARGTYR
6   ALAVALILEARGILEPROGLYGLNPROVAL
7   VALGLUVALGLYTHRLYSPROTHRGLYASP
8   VALLEUGLNGLYARGALATHRGLYGLUGLU
9   GLYGLUTHRVALLEUVALGLUGLUPROARG

Samples:

sample_1: DraK, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%; sodium acetate 10 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

PDB
EMBL CAB89434
GB AIJ15408 EFD68832 EOY48125 KKD15092
REF NP_627282 WP_003975749 WP_011028744

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