BMRB Entry 26772

Title:
Chemical shift assignments of PfEMP1 ATSCore - variant PFF0845c   PubMed: 28806784
Deposition date:
2016-04-01
Original release date:
2017-08-01
Authors:
Cutts, Erin; Vakonakis, Ioannis
Citation:

Citation: Cutts, Erin; Laasch, Niklas; Reiter, Dirk; Trenker, Raphael; Slater, Leanne; Stansfeld, Phillip; Vakonakis, Ioannis. "Structural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions"  PLoS Pathog. 13, e1006552-e1006552 (2017).

Assembly members:

Assembly members:
Core8, polymer, 83 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: pET16c

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: pET16c

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts242
15N chemical shifts80
1H chemical shifts80

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Core81

Entities:

Entity 1, Core8 83 residues - Formula weight is not available

Residues 1-5 represent a cloning artefact This domain construct excludes a large flexible linker present in the WT molecule

1   GLYPROLEUGLYSERTHRASNLYSPHETHR
2   ASPASNGLUTRPASNGLNLEULYSGLNASP
3   PHEILESERASNILESERGLNASNSERGLN
4   METASPLEUVALALALYSGLNTHRHISASN
5   ASPPROILEVALASNGLNILEASNLEUPHE
6   HISLYSTRPLEUASPARGHISARGASNMET
7   CYSGLUGLNTRPASPLYSASNLYSLYSGLU
8   GLULEULEUASPLYSLEUASNGLUGLUTRP
9   ASNLYSGLU

Samples:

sample_1: Core8, [U-99% 13C; U-99% 15N], 0.95 mM; sodium chloride 300 mM; sodium phosphate 20 mM; DTT 1 mM; DSS 0.05 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.34 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

CCPN_Analysis, Prof. Geerten Vuister - data analysis

NMR spectrometers:

  • Bruker Avance 750 MHz

Related Database Links:

UNP C6KT15

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