BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15035

Title: 1H, and 15N Chemical Shift Assignments for the N-terminal domain of Myxococcus xantus CarA protein.

Authors: Jimenez, M. Angeles; Padmanabhan, S.; Gonzalez, Carlos; Perez-Marin, Mari; Elias-Arnanz, Montserrat; Murillo, Francisco; Rico, Manuel

Citation: Navarro-Aviles, G.; Jimenez, M. Angeles; Perez-Marin, Mari; Gonzalez, Carlos; Rico, Manuel; Murillo, Francisco; Elias-Arnanz, Montserrat; Padmanabhan, S.. "Structural basis for operator and anti-repressor recognition by Myxococcus xanthus CarA repressor"  Mol. Microbiol. 63, 980-994 (2007).

Assembly members:
h6CarA(Nter), polymer, 98 residues, Formula weight is not available

Natural source:   Common Name: Myxococcus xanthus   Taxonomy ID: 34   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Myxococcus xanthus

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

Entity Sequences (FASTA):
h6CarA(Nter): MGSSHHHHHHSSGLVPRGSH MTLRIRTIARMTGIREATLR AWERRYGFPRPLRSEGNNYR VYSREEVEAVRRVARLIQEE GLSVSEAIAQVKTEPPRE

Data sets:
Data typeCount
15N chemical shifts86
1H chemical shifts504

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1h6CarA(Nter1

Entities:

Entity 1, h6CarA(Nter 98 residues - Formula weight is not available

Residues -19 to 0 represent an N-terminal His tag used for purification.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METTHRLEUARGILEARGTHRILEALAARG
4   METTHRGLYILEARGGLUALATHRLEUARG
5   ALATRPGLUARGARGTYRGLYPHEPROARG
6   PROLEUARGSERGLUGLYASNASNTYRARG
7   VALTYRSERARGGLUGLUVALGLUALAVAL
8   ARGARGVALALAARGLEUILEGLNGLUGLU
9   GLYLEUSERVALSERGLUALAILEALAGLN
10   VALLYSTHRGLUPROPROARGGLU

Samples:

sample_1: h6CarA(Nter)0.5 – 1.0 mM; H2O 90%; D2O 10%; DSS0.1 – 0.5 mM; sodium chloride 100 mM; sodium phosphate 50 mM

sample_2: h6CarA(Nter)0.5 – 1.0 mM; D2O 100%; DSS0.1 – 0.5 mM; sodium chloride 100 mM; sodium phosphate 50 mM

sample_3: h6CarA(Nter), [U-100% 15N], 0.5 – 1.0 mM; H2O 90%; D2O 10%; DSS0.1 – 0.5 mM; sodium chloride 100 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 0.150 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-15N TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H COSYsample_2isotropicsample_conditions_1

Software:

SPARKY, T Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 15023
PDB 2JML
EMBL CAA79964
GB ABF89801
REF WP_011551024
SP Q50899