BMRB Entry 26726

Title:
Backbone 1H, 15N, and 13C resonance assignments of the Extracellular Adherence Protein Domain 4
Deposition date:
2016-01-08
Original release date:
2016-07-14
Authors:
Woehl, Jordan; Takahashi, Daisuke; Herrera, Alvaro; Geisbrecht, Brian; Prakash, Om
Citation:

Citation: Woehl, Jordan; Takahashi, Daisuke; Herrera, Alvaro; Geisbrecht, Brian; Prakash, Om. "1H, 15N, and 13C resonance assignments of Staphylococcus aureus extracellular adherence protein domain 4"  Biomol. NMR Assignments 10, 301-305 (2016).
PubMed: 27372920

Assembly members:

Assembly members:
Eap4, polymer, 98 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: firmicutes   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: pT7HMT

Data sets:
Data typeCount
13C chemical shifts181
15N chemical shifts92
1H chemical shifts92

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Domain 41

Entities:

Entity 1, Domain 4 98 residues - Formula weight is not available

1   GLYSERTHRVALPROTYRTHRILEALAVAL
2   ASNGLYTHRSERTHRPROILELEUSERLYS
3   LEULYSILESERASNLYSGLNLEUILESER
4   TYRLYSTYRLEUASNASPLYSVALLYSSER
5   VALLEULYSSERGLUARGGLYILESERASP
6   LEUASPLEULYSPHEALALYSGLNALALYS
7   TYRTHRVALTYRPHELYSASNGLYLYSLYS
8   GLNVALVALASNLEULYSSERASPILEPHE
9   THRPROASNLEUPHESERALALYSASPILE
10   LYSLYSILEASPILEASPVALLYS

Samples:

sample_1: Eap4, [U-99% 13C; U-99% 15N], 0.5 – 1.0 mM; sodium phosphate 50 mM; sodium azide 0.1%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

VNMRJ, Varian - collection

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

TALOS, Cornilescu, Delaglio and Bax - secondary structure prediction

NMR spectrometers:

  • Varian VNMR 500 MHz
  • Bruker Avance III 800 MHz

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