BMRB Entry 18598

Title:
Backbone resonance assignments for AgrA LytTR domain
Deposition date:
2012-07-17
Original release date:
2013-02-28
Authors:
Leonard, Paul; Sidote, David; Stock, Ann
Citation:

Citation: Leonard, Paul; Bezar, Ian; Sidote, David; Stock, Ann. "Identification of a hydrophobic cleft in the LytTR domain of AgrA as a locus for small molecule interactions that inhibit DNA binding."  Biochemistry 51, 10035-10043 (2012).
PubMed: 23181972

Assembly members:

Assembly members:
AgrAc, polymer, 103 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET9a

Data sets:
Data typeCount
13C chemical shifts302
15N chemical shifts100
1H chemical shifts100

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LytTR domain1

Entities:

Entity 1, LytTR domain 103 residues - Formula weight is not available

1   METASPASNSERVALGLUTHRILEGLULEU
2   LYSARGGLYSERASNSERVALTYRVALGLN
3   TYRASPASPILEMETPHEPHEGLUSERSER
4   THRLYSSERHISARGLEUILEALAHISLEU
5   ASPASNARGGLNILEGLUPHETYRGLYASN
6   LEULYSGLULEUSERGLNLEUASPASPARG
7   PHEPHEARGCYSHISASNSERPHEVALVAL
8   ASNARGHISASNILEGLUSERILEASPSER
9   LYSGLUARGILEVALTYRPHELYSASNLYS
10   GLUHISCYSTYRALASERVALARGASNVAL
11   LYSLYSILE

Samples:

sample_1: AgrAc, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 5.8; pressure: 1 atm; temperature: 293.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

VNMR, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ANALYSIS v2.0, CCPN - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

UNP P0A0I7
PDB
DBJ BAB43126 BAB58201 BAB95828 BAF68218 BAF78907
EMBL CAA36784 CAG41107 CAG43751 CAI81612 CAQ50464
GB AAA26597 AAW36991 ABB17358 ABB17371 ABB17378
REF WP_000688486 WP_000688487 WP_000688488 WP_000688490 WP_000688492
SP P0A0I5 P0A0I6 P0A0I7 Q5HEG2 Q6G7R8
AlphaFold P13131 P0A0I5 P0A0I6 P0A0I7 Q5HEG2 Q6G7R8

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