BMRB Entry 19707

Name: Solution structure of the extracellular sensor domain of DraK histidine kinase
Published: 2014-09-16

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PDB ID: 2mj6
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
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the extracellular sensor domain of DraK histidine kinase PubMed: 25203403

Deposition date: 2013-12-25 Original release date: 2014-09-16

Authors: Yeo, Kwon Joo; Cheong, Hae-Kap

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).

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

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

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

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	619
13C chemical shifts	361
15N chemical shifts	93

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 90 residues - 9760.893 Da.

1	GLY	SER	GLU	THR	ARG	THR	ILE	SER	SER	THR
2	ALA	GLN	GLU	ARG	VAL	ASP	LEU	GLU	ALA	VAL
3	ARG	LEU	ALA	SER	ILE	VAL	ASP	SER	ARG	LEU
4	ILE	GLY	THR	GLY	SER	VAL	ASP	GLU	ASP	PHE
5	LEU	ARG	GLU	GLN	ILE	ARG	ASP	ALA	ARG	TYR
6	ALA	VAL	ILE	ARG	ILE	PRO	GLY	GLN	PRO	VAL
7	VAL	GLU	VAL	GLY	THR	LYS	PRO	THR	GLY	ASP
8	VAL	LEU	GLN	GLY	ARG	ALA	THR	GLY	GLU	GLU
9	GLY	GLU	THR	VAL	LEU	VAL	GLU	GLU	PRO	ARG

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis

NMR spectrometers:

Bruker Avance 900 MHz

PDB	2MJ6
EMBL	CAB89434
GB	AIJ15408 EFD68832 EOY48125 KKD15092
REF	NP_627282 WP_003975749 WP_011028744

Biological Magnetic Resonance Data Bank