BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19427

Title: The solution structure of the C-terminal domain of BldD from Streptomyces coelicolor   PubMed: 24356916

Deposition date: 2013-08-14 Original release date: 2013-11-26

Authors: Kim, Jeong-Mok; Won, Hyung-Sik; Kang, Sa-Ouk

Citation: Kim, Jeong-Mok; Won, Hyung-Sik; Kang, Sa-Ouk. "The C-terminal domain of the transcriptional regulator BldD from Streptomyces coelicolor A3(2) constitutes a novel fold of winged-helix domains."  Proteins ., .-. (2013).

Assembly members:
BldD-CTD, polymer, 89 residues, 9853.219 Da.

Natural source:   Common Name: high GC Gram+   Taxonomy ID: 1902   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces coelicolor

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

Entity Sequences (FASTA):
BldD-CTD: MEPPPKLVLDLERLATVPAE KAGPLQRYAATIQSQRGDYN GKVLSIRQDDLRTLAVIYDQ SPSVLTEQLISWGVLDADAR RAVASHDEL

Data sets:
Data typeCount
13C chemical shifts368
15N chemical shifts88
1H chemical shifts609

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1BldD-CTD1

Entities:

Entity 1, BldD-CTD 89 residues - 9853.219 Da.

1   METGLUPROPROPROLYSLEUVALLEUASP
2   LEUGLUARGLEUALATHRVALPROALAGLU
3   LYSALAGLYPROLEUGLNARGTYRALAALA
4   THRILEGLNSERGLNARGGLYASPTYRASN
5   GLYLYSVALLEUSERILEARGGLNASPASP
6   LEUARGTHRLEUALAVALILETYRASPGLN
7   SERPROSERVALLEUTHRGLUGLNLEUILE
8   SERTRPGLYVALLEUASPALAASPALAARG
9   ARGALAVALALASERHISASPGLULEU

Samples:

sample_1: BldD-CTD, [U-99% 13C; U-98% 15N], 2 mM; sodium phosphate 40 mM; sodium chloride 150 mM; sodium azide 0.005%; H2O 93%; D2O 7%

Conditions_for_BldD-CTD: ionic strength: 190 mM; pH: 6.8; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicConditions_for_BldD-CTD
2D 1H-13C HSQCsample_1isotropicConditions_for_BldD-CTD
2D 1H-13C HSQC aliphaticsample_1isotropicConditions_for_BldD-CTD
3D HNCACBsample_1isotropicConditions_for_BldD-CTD
3D HN(CO)CACBsample_1isotropicConditions_for_BldD-CTD
3D HNCOsample_1isotropicConditions_for_BldD-CTD
3D HCCH-TOCSYsample_1isotropicConditions_for_BldD-CTD
3D HCCH-COSYsample_1isotropicConditions_for_BldD-CTD
3D 1H-15N TOCSYsample_1isotropicConditions_for_BldD-CTD
3D 1H-15N NOESYsample_1isotropicConditions_for_BldD-CTD
3D 1H-13C NOESYsample_1isotropicConditions_for_BldD-CTD

Software:

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ GAP50531
EMBL CAB93369 CQR65077
GB AAC38279 AEY88188 AGF62344 AIJ16957 AIR97221
REF NP_625769 WP_003977337 WP_003988955 WP_004990661 WP_006131213

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts