BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19707

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

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

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