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 34292

Title: The CTD of HpDprA, a DNA binding Winged Helix domain which do not bind dsDNA   PubMed: 30771270

Deposition date: 2018-06-22 Original release date: 2019-04-22

Authors: Lisboa, J.; Celma, L.; Sanchez, D.; Marquis, M.; Andreani, J.; Guerois, R.; Ochsenbein, F.; Durand, D.; Marsin, S.; Cuniasse, P.; Radicella, J.; Quevillon-Cheruel, S.

Citation: Lisboa, J.; Celma, L.; Sanchez, D.; Marquis, M.; Andreani, J.; Guerois, R.; Ochsenbein, F.; Durand, D.; Marsin, S.; Cuniasse, P.; Radicella, J.; Quevillon-Cheruel, S.. "The C-terminal domain of HpDprA is a DNA-binding winged helix domain that does not bind double-stranded DNA."  FEBS J. 286, 1941-1958 (2019).

Assembly members:
entity_1, polymer, 59 residues, 7139.292 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
entity_1: MLKDYHLKEMPEMEDEFLEY CAKNPSYEEAYLKFGDKLLE YELLGKIKRINHIVVLAHH

Data sets:
Data typeCount
13C chemical shifts221
15N chemical shifts55
1H chemical shifts427

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 59 residues - 7139.292 Da.

1   METLEULYSASPTYRHISLEULYSGLUMET
2   PROGLUMETGLUASPGLUPHELEUGLUTYR
3   CYSALALYSASNPROSERTYRGLUGLUALA
4   TYRLEULYSPHEGLYASPLYSLEULEUGLU
5   TYRGLULEULEUGLYLYSILELYSARGILE
6   ASNHISILEVALVALLEUALAHISHIS

Samples:

sample_1: HpDprA CTD, [U-15N; U-13C], 128 uM; Phosphate Buffer (NH2PO4) 20 mM; NaCl 50 mM

sample_2: HpDprA CTD, [U-13C; U-15N], 128 uM; Phosphate Buffer (NH2PO4) 20 mM; NaCl 50 mM

sample_3: HpDprA CTD, [U-15N], 34 uM; Phosphate Buffer (NH2PO4) 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 5.6; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 5.6 pD; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_3
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - processing

SPARKY, Goddard - chemical shift assignment

CcpNMR, CCPN - data analysis

CANDID, Herrmann, Guntert and Wuthrich - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker DRX 600 MHz

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