BMRB Entry 15023

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15023
MolProbity Validation Chart

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Title:
1H, and 15N Chemical Shift Assignments for the N-terminal domain of Myxococcus xantus CarA protein.
Deposition date:
2006-11-13
Original release date:
2007-02-08
Authors:
Jimenez, M. Angeles; Padmanabhan, S.; Gonzalez, Carlos; Perez-Marin, Mari; Elias-Arnanz, Montserrat; Murillo, Francisco; Rico, Manuel
Citation:

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).
PubMed: 17233828

Assembly members:

Assembly members:
CarA(Nter), polymer, 81 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CarA(Nter): GSHMTLRIRTIARMTGIREA TLRAWERRYGFPRPLRSEGN NYRVYSREEVEAVRRVARLI QEEGLSVSEAIAQVKTEPPR E

Data sets:
Data typeCount
15N chemical shifts77
1H chemical shifts561

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1CarA(Nter1

Entities:

Entity 1, CarA(Nter 81 residues - Formula weight is not available

Residues -2 to 0 represent an N-terminal cloning tag.

1   GLYSERHISMETTHRLEUARGILEARGTHR
2   ILEALAARGMETTHRGLYILEARGGLUALA
3   THRLEUARGALATRPGLUARGARGTYRGLY
4   PHEPROARGPROLEUARGSERGLUGLYASN
5   ASNTYRARGVALTYRSERARGGLUGLUVAL
6   GLUALAVALARGARGVALALAARGLEUILE
7   GLNGLUGLUGLYLEUSERVALSERGLUALA
8   ILEALAGLNVALLYSTHRGLUPROPROARG
9   GLU

Samples:

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

sample_3: CarA(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 AV 600 MHz

Related Database Links:

BMRB 15035
PDB
EMBL CAA79964
GB ABF89801
REF WP_011551024
SP Q50899
AlphaFold Q50899

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