BMRB Entry 19719

Title:
Resonance assignments of the PHIST domain of P. falciparum protein PFI1780w   PubMed: 24983468
Deposition date:
2014-01-07
Original release date:
2016-05-24
Authors:
Vakonakis, Ioannis
Citation:

Citation: Oberli, Alexander; Slater, Leanne; Cutts, Erin; Brand, Francoise; Mundwiler-Pachlatko, Esther; Rusch, Sebastian; Masik, Martin; Erat, Michele; Beck, Hans-Peter; Vakonakis, Ioannis. "A Plasmodium falciparum PHIST protein binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surface"  FASEB J. 28, 4420-4433 (2014).

Assembly members:

Assembly members:
PFI1780w, polymer, 155 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:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6P-2

Experimental source:

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6P-2

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts148
1H chemical shifts414

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PHIST1

Entities:

Entity 1, PHIST 155 residues - Formula weight is not available

Residues 1-5 represent a cloning artefact

1   GLYPROLEUGLYSERTYRTHRALAGLUGLU
2   ILEASNGLUMETILEASNSERSERASNGLU
3   PHEILEASNARGASNASPMETASNILEILE
4   PHESERTYRVALHISGLUSERGLUARGGLU
5   LYSPHELYSLYSVALGLUGLUASNILEPHE
6   LYSPHEILEGLNSERILEVALGLUTHRTYR
7   LYSILEPROASPGLUTYRLYSMETARGLYS
8   PHELYSPHEALAHISPHEGLUMETGLNGLY
9   TYRALALEULYSGLNGLULYSPHELEULEU
10   GLUTYRALAPHELEUSERLEUASNGLYLYS
11   LEUCYSGLUARGLYSLYSPHELYSGLUVAL
12   LEUGLUTYRVALLYSARGGLUTRPILEGLU
13   PHEARGLYSSERMETPHEASPVALTRPLYS
14   GLULYSLEUALASERGLUPHEARGGLUHIS
15   GLYGLUMETLEUASNGLNLYSARGLYSLEU
16   LYSGLNHISGLULEU

Samples:

sample_1: PFI1780w, [U-99% 13C; U-99% 15N], 0.2 mM; D2O 5 % v/v; H2O 95 % v/v; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 0.02 % w/v; DTT 2 mM; DSS 0.1 mM

sample_conditions_1: ionic strength: 110 mM; pH: 7; pressure: 1 atm; temperature: 310.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

PIPP, Garrett - data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UNP Q8I2F2

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