BMRB Entry 26548

Title:
Solid-state NMR sequential assignments of the N-terminal domain of HpDnaB helicase
Deposition date:
2015-03-24
Original release date:
2015-08-24
Authors:
Wiegand, Thomas; Gardiennet, Carole; Meier, Beat; Bockmann, Anja; Cadalbert, Riccardo; Lacabanne, Denis; Kunert, Britta; Guentert, Peter; Terradot, Laurent; Ravotti, Francesco
Citation:

Citation: Wiegand, Thomas; Gardiennet, Carole; Ravotti, Francesco; Cadalbert, Riccardo; Lacabanne, Denis; Kunert, Britta; Guentert, Peter; Terradot, Laurent; Bockmann, Anja; Meier, Beat. "Solid-state NMR sequential assignments of the N-terminal domain of HpDnaB helicase"  Biomol. NMR Assign. 10, 13-23 (2016).
PubMed: 26280528

Assembly members:

Assembly members:
HpDnaB_Nter, polymer, 159 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: H. pylori   Taxonomy ID: 210   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Helicobacter pylori

Experimental source:

Experimental source:   Production method: purified from the natural source   Host organism: Helicobacter pylori   Vector: pET151

Data sets:
Data typeCount
13C chemical shifts499
15N chemical shifts112

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HpDnaB_Nter_chainA1
2HpDnaB_Nter_chainB1

Entities:

Entity 1, HpDnaB_Nter_chainA 159 residues - Formula weight is not available

1   GLYILEASPPROPHETHRMETASPHISLEU
2   LYSHISLEUGLNGLNLEUGLNASNILEGLU
3   ARGILEVALLEUSERGLYILEVALLEUALA
4   ASNHISLYSILEGLUGLUVALHISSERVAL
5   LEUGLUPROSERASPPHETYRTYRPROPRO
6   ASNGLYLEUPHEPHEGLUILEALALEULYS
7   LEUHISGLUGLUASPCYSPROILEASPGLU
8   ASNPHEILEARGGLNLYSMETPROLYSASP
9   LYSGLNILELYSGLUGLUASPLEUVALALA
10   ILEPHEALAALASERPROILEASPASNILE
11   GLUALATYRVALGLUGLUILELYSASNALA
12   SERILELYSARGLYSLEUPHEGLYLEUALA
13   ASNTHRILEARGGLUGLNALALEUGLUSER
14   ALAGLNLYSSERSERASPILELEUGLYALA
15   VALGLUARGGLUVALTYRALALEULEUASN
16   GLYSERTHRILEGLUGLYPHEARGASN

Samples:

sample_1: HpDnaB_Nter, [U-100% 13C; U-100% 15N], 23.5 mg/mL; TRIS-HCl 50 mM; NaCl 100 mM; HEPES 100 mM; sodium azide 0.1%; glycerol 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 13C-13C DARR 10mssample_1isotropicsample_conditions_1
2D 13C-13C DARR 20mssample_1isotropicsample_conditions_1
2D 13C-13C DARR 50mssample_1isotropicsample_conditions_1
2D 13C-13C DARR 200mssample_1isotropicsample_conditions_1
2D 15N-13C NCAsample_1isotropicsample_conditions_1
3D 15N-13C-13C NCACBsample_1isotropicsample_conditions_1
3D 15N-13C-13C NCACXsample_1isotropicsample_conditions_1
3D 15N-13C-13C NCAOCXsample_1isotropicsample_conditions_1
3D 13C-15N-13C CANCOsample_1isotropicsample_conditions_1
3D 15N-13C-13C NcoCACBsample_1isotropicsample_conditions_1
3D 15N-13C-13C CANcoCAsample_1isotropicsample_conditions_1
3D 15N-13C-13C NCaCBCXsample_1isotropicsample_conditions_1
3D 13C-13C-13C CCCsample_1isotropicsample_conditions_1

Software:

TOPSPIN_v._3.2, Bruker Biospin - data analysis, processing

CCPN_v._2.4.1, Fogh et al. - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 850 MHz