BMRB Entry 26689

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26689

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
The chemical shifts (partial) of E. coli DnaC N-terminal domain
Deposition date:
2015-10-12
Original release date:
2021-07-27
Authors:
Nagata, Koji; Horita, Shoichiro; Katayama, Tsutomu; Ueda, Tadashi; Tanokura, Masaru
Citation:

Citation: Nagata, Koji; Okada, Akitoshi; Ohtsuka, Jun; Ohkuri, Takatoshi; Akama, Yusuke; Sakiyama, Yukari; Miyazaki, Erika; Horita, Shoichiro; Katayama, Tsutomu; Ueda, Tadashi; Tanokura, Masaru. "Crystal structure of the complex of the interaction domains of Escherichia coli DnaB helicase and DnaC helicase loader: structural basis implying a distortion-accumulation mechanism for the DnaB ring opening caused by DnaC binding"  J. Biochem. 167, 1-14 (2020).
PubMed: 31665315

Assembly members:

Assembly members:
DnaC_NTD, polymer, 52 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DnaC_NTD: MKNVGDLMQRLQKMMPAHIK PAFKTGEELLAWQKEQGAIR SAALERENRAMK

Data sets:
Data typeCount
13C chemical shifts193
15N chemical shifts50
1H chemical shifts301

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DnaC NTD1

Entities:

Entity 1, DnaC NTD 52 residues - Formula weight is not available

1   METLYSASNVALGLYASPLEUMETGLNARG
2   LEUGLNLYSMETMETPROALAHISILELYS
3   PROALAPHELYSTHRGLYGLUGLULEULEU
4   ALATRPGLNLYSGLUGLNGLYALAILEARG
5   SERALAALALEUGLUARGGLUASNARGALA
6   METLYS

Samples:

sample_1: DnaC NTD 0.5 mM; sodium phosphate 20 mM; sodium azide 0.02 % w/v; H2O 90 % v/v; D2O, [U-100% 2H], 10 % v/v

sample_2: DnaC NTD, [U-99% 15N], 0.5 mM; sodium phosphate 20 mM; sodium azide 0.02 % w/v; H2O 90 % v/v; D2O, [U-100% 2H], 10 % v/v

sample_3: DnaC NTD, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 20 mM; sodium azide 0.02 % w/v; H2O 90 % v/v; D2O, [U-100% 2H], 10 % v/v

sample_conditions_1: ionic strength: 0.12 M; pH: 6.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

VNMR, Varian - collection

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

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

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

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