BMRB Entry 27540

Title:
1H, 15N, and 13C triple resonance assignments of innate immune evasion protein EapH2 from the S. aureus
Deposition date:
2018-07-12
Original release date:
2019-01-02
Authors:
Herrera, Alvaro; Dubey, Abhinav; Geisbrecht, Brian; Arthanari, Haribabu; Prakash, Om
Citation:

Citation: Herrera, Alvaro; Dubey, Abhinav; Geisbrecht, Brian; Arthanari, Haribabu; Prakash, Om. "Backbone resonance assignments of innate immune evasion protein EapH2 from the S. aureus."  Biomol. NMR Assign. 13, 219-222 (2019).
PubMed: 30729401

Assembly members:

Assembly members:
Extracellular_Adherence_Protein_Homolog_2, polymer, 117 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: pT7HMT

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts319
15N chemical shifts111
1H chemical shifts111

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EapH21

Entities:

Entity 1, EapH2 117 residues - Formula weight is not available

1   GLYSERTHRALAGLULYSASPLYSLEUPRO
2   ALATHRGLNLYSALALYSGLUMETGLNASN
3   VALPROTYRTHRILEALAVALASPGLYILE
4   METALAPHEASNGLNSERTYRLEUASNLEU
5   PROLYSASPSERGLNLEUSERTYRLEUASP
6   LEUGLYASNLYSVALLYSALALEULEUTYR
7   ASPGLUARGGLYVALTHRPROGLULYSILE
8   ARGASNALALYSSERALAVALTYRTHRILE
9   THRTRPLYSASPGLYSERLYSLYSGLUVAL
10   ASPLEULYSLYSASPSERTYRTHRALAASN
11   LEUPHEASPSERASNSERILELYSGLNILE
12   ASPILEASNVALLYSTHRLYS

Samples:

N15C13: Extracellular Adherence Protein Homolog 2, [U-99% 13C; U-99% 15N], 0.75 mM; sodium phosphate 50 mM

N15: Extracellular Adherence Protein Homolog 2, [U-99% 15N], 0.75 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCN15isotropicsample_conditions_1
3D HNCAN15C13isotropicsample_conditions_1
3D HN(CO)CAN15C13isotropicsample_conditions_1
3D HNCON15C13isotropicsample_conditions_1
3D HCACON15C13isotropicsample_conditions_1
3D HNCACBN15C13isotropicsample_conditions_1

Software:

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

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

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