BMRB Entry 30025

Title:
Solution structure of the BeF3-activated conformation of SdrG from Pseudomonas melonis Fr1
Deposition date:
2016-02-25
Original release date:
2016-07-13
Authors:
Campagne, S.; Vorholt, J.; Allain, F.H.-T.
Citation:

Citation: Campagne, Sebastien; Dintner, Sebastian; Gottschlich, Lisa; Thibault, Maxence; Bortfeld-Miller, Miriam; Kaczmarczyk, Andreas; Francez-Charlot, Anne; Allain, Frederic; Vorholt, Julia. "Role of the PFXFATG[G/Y] Motif in the Activation of SdrG, a Response Regulator Involved in the Alphaproteobacterial General Stress Response"  Structure 24, 1237-1247 (2016).
PubMed: 27396826

Assembly members:

Assembly members:
SdrG, polymer, 130 residues, 13892.781 Da.

Natural source:

Natural source:   Common Name: a-proteobacteria   Taxonomy ID: 1090317   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Sphingomonas Sphingomonas melonis

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts499
15N chemical shifts121
1H chemical shifts855

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 130 residues - 13892.781 Da.

1   METSERALALEUTHRGLNILELEUILEVAL
2   GLUASPGLUPROLEUILEALAMETMETLEU
3   GLUASPPHELEUGLUVALLEUASPLYSTHR
4   PROVALGLYTHRVALASPTHRVALALAGLY
5   ALALEUALAARGVALGLUASPGLYGLYILE
6   ASPALAALAILELEUASPVALASNLEUARG
7   GLYGLYGLULYSSERTHRPROVALALAGLU
8   ALALEUALAALAARGASPILEPROPHEVAL
9   PHEALATHRGLYGLYSERASPASPSERVAL
10   ASPSERARGPHEARGASPARGPROVALLEU
11   GLNLYSPROPHETHRMETASPGLYVALALA
12   LYSALALEUALAALALEULEUVALPROARG
13   GLYSERVALGLUHISHISHISHISHISHIS

Samples:

sample_1: BeF3-activated conformation of SdrG, [U-99% 13C; U-99% 15N], 1 mM; beryllium Chloride 5 mM; magnesium chloride 10 mM; sodium chloride 50 mM; sodium fluoride 30 mM; sodium phosphate 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 105 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
1D Hsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

AMBER12, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CARA v3.96, Keller and Wuthrich - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN v3.96, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 500 MHz
  • Bruker Avance 900 MHz

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