BMRB Entry 34022

Title:
Structure of PfIMP2 (Immune Mapped Protein 2 from Plasmodium falciparum) - an antigenic protein
Deposition date:
2016-07-06
Original release date:
2016-12-05
Authors:
Benjamin, S.; Matthews, S.
Citation:

Citation: Jia, Y.; Benjamin, S.; Liu, Q.; Xu, Y.; Dogga, S.; Liu, J.; Matthews, S.; Soldati-Favre, D.; Benjamin, S.; Williams, F.; Kerry, L.; Matthews, S.. "Toxoplasma gondii immune mapped protein 1 is anchored to the inner leaflet of the plasma membrane and adopts a novel protein fold."  Biochim. Biophys. Acta 1865, 208-219 (2016).
PubMed: 27888074

Assembly members:

Assembly members:
entity_1, polymer, 156 residues, 17607.484 Da.

Natural source:

Natural source:   Common Name: Plasmodium falciparum   Taxonomy ID: 36329   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium falciparum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'   Vector: pNIC-ZB

Data sets:
Data typeCount
13C chemical shifts693
15N chemical shifts145
1H chemical shifts1087

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 156 residues - 17607.484 Da.

1   GLUGLULYSGLYALATYRLEUVALPHEASP
2   ASNALASERASNGLYTHRLEUPHEILEVAL
3   TRPLYSLYSGLULYSVALGLUASNALALEU
4   METPHEILELYSPROTHRLYSGLUVALPRO
5   GLUPHELYSPHEVALASNARGASNGLYLYS
6   ASNGLULEUILEARGASNLEUGLNSERASP
7   LYSLYSLEUPHETYRSERGLYILECYSGLN
8   PHEVALLYSGLUALALYSASPILELYSGLY
9   LYSLEUTHRLEULEUGLNHISPHEASPSER
10   SERPHEPROILELYSVALASPLEUTYRPHE
11   LEULYSGLYSERLYSVALMETPROLEUASN
12   THRGLYGLUPROPHEVALVALGLNASPILE
13   ASPALAMETSERVALLEUPROLYSGLYSER
14   SERSERLEULYSVALLYSTHRMETALALYS
15   ASPMETPHEVALSERARGGLYASNTHRGLU
16   GLYALASERILESERPHE

Samples:

sample_1: DTT 1 mM; HEPES 50 mM; PfIMP2, [U-13C; U-15N], 1.5 mM; sodium azide 0.02%; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; 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(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

Analysis, CCPN - peak picking

CNS, Brunger A. T. et.al. - refinement

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker AvanceII 600 MHz
  • Bruker AvanceII 800 MHz

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