BMRB Entry 26552

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for Plasmodium falciparum Immune Mapped Protein 1 (PfIMP1)
Deposition date:
2015-04-08
Original release date:
2016-01-06
Authors:
Williams, Felix; Kerry, Louise
Citation:

Citation: Benjamin, Stefi; Williams, Felix; Kerry, Louise; Matthews, Stephen. "NMR assignment of the immune mapped protein 1 (IMP1) homologue from Plasmodium falciparum"  Biomol. NMR Assignments 9, 393-395 (2015).
PubMed: 25947350

Assembly members:

Assembly members:
PfIMP1, polymer, 181 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28-NTH

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
1PfIMP1 monomer1

Entities:

Entity 1, PfIMP1 monomer 181 residues - Formula weight is not available

1   METHISHISHISHISHISHISSERSERGLY
2   VALASPLEUGLYTHRGLUASNLEUTYRPHE
3   GLNSERMETMETSERGLUGLULYSGLYALA
4   TYRLEUVALPHEASPASNALASERASNGLY
5   THRLEUPHEILEVALTRPLYSLYSGLULYS
6   VALGLUASNALALEUMETPHEILELYSPRO
7   THRLYSGLUVALPROGLUPHELYSPHEVAL
8   ASNARGASNGLYLYSASNGLULEUILEARG
9   ASNLEUGLNSERASPLYSLYSLEUPHETYR
10   SERGLYILECYSGLNPHEVALLYSGLUALA
11   LYSASPILELYSGLYLYSLEUTHRLEULEU
12   GLNHISPHEASPSERSERPHEPROILELYS
13   VALASPLEUTYRPHELEULYSGLYSERLYS
14   VALMETPROLEUASNTHRGLYGLUPROPHE
15   VALVALGLNASPILEASPALAMETSERVAL
16   LEUPROLYSGLYSERSERSERLEULYSVAL
17   LYSTHRMETALALYSASPMETPHEVALSER
18   ARGGLYASNTHRGLUGLYALASERILESER
19   PHE

Samples:

sample_1: PfIMP1, [U-100% 13C; U-100% 15N], 1.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 250 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 HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRView, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

NCBI XP_001349200

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