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 17009

Title: Sequence specific backbone assignment of the C-terminal domain of MqsA

Deposition date: 2010-06-19 Original release date: 2010-12-03

Authors: Brown, Breann; Grigoriu, Simina; Arruda, Jennifer; Page, Rebecca; Peti, Wolfgang

Citation: Brown, Breann; Wood, Thomas; Peti, Wolfgang; Page, Rebecca. "Structure of the Escherichia coli Antitoxin MqsA (YgiT/b3021) Bound to Its Gene Promoter Reveals Extensive Domain Rearrangements and the Specificity of Transcriptional Regulation."  J. Biol. Chem. 286, 2285-2296 (2011).

Assembly members:
mqsa_c, polymer, 73 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
mqsa_c: GHMASVNAETVAPEFIVKVR KKLSLTQKEASEIFGGGVNA FSRYEKGNAQPHPSTIKLLR VLDKHPELLNEIR

Data sets:
Data typeCount
13C chemical shifts288
15N chemical shifts65
1H chemical shifts65

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1mqsa cterm1

Entities:

Entity 1, mqsa cterm 73 residues - Formula weight is not available

GHM cloning artifacts; Alanine is residue 62 of MqsA

1   GLYHISMETALASERVALASNALAGLUTHR
2   VALALAPROGLUPHEILEVALLYSVALARG
3   LYSLYSLEUSERLEUTHRGLNLYSGLUALA
4   SERGLUILEPHEGLYGLYGLYVALASNALA
5   PHESERARGTYRGLULYSGLYASNALAGLN
6   PROHISPROSERTHRILELYSLEULEUARG
7   VALLEUASPLYSHISPROGLULEULEUASN
8   GLUILEARG

Samples:

sample_1: mqsa_c, [U-99% 15N], 0.5 mM; sodium chloride 50 mM; TRIS 10 mM; H2O 90%; D2O 10%

sample_2: mqsa_c, [U-99% 13C; U-99% 15N], 0.5 mM; sodium chloride 50 mM; TRIS 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 60 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

XEASY v1.8.2, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

BMRB 15446
PDB
DBJ BAE77077 BAJ44773 BAL39680
EMBL CAQ33360 CAR14662 CAR19632 CBJ02792 CCJ45634
GB AAA69189 AAC76057 ABV07432 ACA76352 ACB04106
REF NP_417493 WP_000650107 WP_001487520 WP_021572968 WP_044814339
SP Q46864

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