BMRB Entry 17999

Title:
Chemical Shift Assignments from PfEMP1: Full-length
Deposition date:
2011-10-16
Original release date:
2012-01-18
Authors:
Vakonakis, Ioannis
Citation:

Citation: Mayer, Christina; Slater, Leanne; Erat, Michele; Konrat, Robert; Vakonakis, Ioannis. "Structural Analysis of the Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) Intracellular Domain Reveals a Conserved Interaction Epitope."  J. Biol. Chem. 287, 7182-7189 (2012).
PubMed: 22249178

Assembly members:

Assembly members:
ATS-FL, polymer, 403 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: malaria parasite P. falciparum   Taxonomy ID: 5833   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium falciparum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16-3c

Data sets:
Data typeCount
13C chemical shifts935
15N chemical shifts312
1H chemical shifts636

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ATS-FL1

Entities:

Entity 1, ATS-FL 403 residues - Formula weight is not available

Residues -10 to -1 represent a cloning artefact. Remaining sequence is the cytoplasmic domain of PfEMP1

1   GLYPROLEUGLYSERPROGLYILEPROGLY
2   LYSLYSLYSPROLYSSERPROVALASPLEU
3   ILEARGVALLEUASPILEHISLYSGLYASP
4   TYRGLYMETPROTHRLEULYSSERLYSASN
5   ARGTYRILEPROTYRALASERASPTHRTYR
6   LYSGLYLYSTHRTYRILETYRMETGLUGLY
7   ASPSERASPSERGLYHISTYRTYRGLUASP
8   THRTHRASPILETHRSERSERGLUSERGLU
9   TYRGLUGLUMETASPILEASNASPILETYR
10   VALPROASPSERPROLYSTYRLYSTHRLEU
11   ILEGLUVALVALLEUGLUPROSERLYSARG
12   ASPTHRPROSERSERASPALAPROMETASN
13   LYSPHETHRASPASPGLUTRPASNGLNLEU
14   LYSGLNASPPHEILESERGLYILELEUGLU
15   ASNGLUGLNLYSASPLEUPROLYSASNASN
16   ILESERGLYASNTHRPROMETASNTHRGLN
17   PROASNTHRLEUTYRPHEASNLYSPROGLU
18   GLULYSPROPHEILETHRSERILEHISASP
19   ARGASPLEUTYRSERGLYGLUGLUILEASN
20   TYRASNILEASNMETSERTHRASNSERMET
21   ASPASPTHRSERTYRVALSERASNASNVAL
22   TYRSERGLYILEASPLEUILEASNASPTHR
23   LEUSERGLYASNGLNHISILEASPILETYR
24   ASPGLUVALLEULYSARGLYSGLUASNGLU
25   LEUPHEGLYTHRASNTYRLYSLYSASNTHR
26   SERASNASNASNVALALALYSLEUTHRASN
27   SERASPPROILEMETASNGLNLEUASPLEU
28   LEUHISLYSTRPLEUASPARGHISARGASP
29   METCYSGLULYSTRPLYSSERLYSGLUASP
30   ILELEUHISLYSLEUASNGLUGLNTRPASN
31   LYSASPASNASPGLYGLYASNVALPROILE
32   ASPASNARGSERLEUASNTHRASPVALTRP
33   ILEGLUILEASPMETASPASPPROLYSGLY
34   LYSLYSGLUPHESERASNMETASPTHRILE
35   LEUASPASPILEGLUASPASPILETYRTYR
36   ASPVALASNASPASPGLUASNPROSERVAL
37   ASPASNILEPROMETASPHISASNLYSVAL
38   ASPVALPROLYSLYSVALHISVALGLUMET
39   LYSILELEUASNASNTHRSERASNGLYSER
40   LEUGLUPROGLUPHEPROILESERASPVAL
41   TRPASNILE

Samples:

sample_1: ATS-FL, [U-99% 13C; U-99% 15N], 0.2-0.5 mM; NaCl 50 mM; Na2HPO4 20 mM; NaN3 0.01%; DSS 0.1 mM

sample_conditions_1: ionic strength: 0.11 M; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAHBsample_1isotropicsample_conditions_1
3D HACACOsample_1isotropicsample_conditions_1
3D HACA(CO)Nsample_1isotropicsample_conditions_1

Software:

Omega Spectrometer Operating Software vBeta 6.03b2, Ge/Bruker - collection

NMRPipe v2.4 Rev 2006.095.11.35, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PIPP v4.3.7, Garrett - data analysis

NMR spectrometers:

  • GE OMEGA PSG 600 MHz

Related Database Links:

EMBL CAD51362
REF XP_001349513

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