BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 25108

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25108

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Title: Backbone Chemical Shift Assignment for the pfPP1 phosphatase regulator pfI2 of Plasmodium falciparum

Deposition date: 2014-07-24 Original release date: 2014-08-26

Authors: Landrieu, Isabelle; Cantrelle, Francois-Xavier; Freville, Aline; Khalife, Jamal

Citation: Freville, Aline; Tellier, Geraldine; Vandomme, Audrey; Pierrot, Christine; Vicogne, Jerome; Cantrelle, Fran ois-Xavier; Martoriati, Alain; Cailliau-Maggio, Katia; Khalife, Jamal; Landrieu, Isabelle. "Identification of a Plasmodium falciparum inhibitor-2 motif involved in binding and regulation activity of the Protein Phosphatase type 1"  FEBS J. ., .-..

Assembly members:
PfI2, polymer, 155 residues, Formula weight is not available

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

Entity Sequences (FASTA):
PfI2: RGSHHHHHHGSMKKKVDKSV TKKTISWDEVTINEQDKERG SRMKILEPNTPFNFILMDSA SEDEASKYGDVKGSDEGQNN IADDLINKLNQLVEKQENKG VSNIDFKEKRKKHYNEYKML QKLRKSGTLDDIDEEYKPDN KDSNCDNSNMNESEE

Data sets:
Data typeCount
1H chemical shifts95
13C chemical shifts300
15N chemical shifts93

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PfI21

Entities:

Entity 1, PfI2 155 residues - Formula weight is not available

1   ARGGLYSERHISHISHISHISHISHISGLY
2   SERMETLYSLYSLYSVALASPLYSSERVAL
3   THRLYSLYSTHRILESERTRPASPGLUVAL
4   THRILEASNGLUGLNASPLYSGLUARGGLY
5   SERARGMETLYSILELEUGLUPROASNTHR
6   PROPHEASNPHEILELEUMETASPSERALA
7   SERGLUASPGLUALASERLYSTYRGLYASP
8   VALLYSGLYSERASPGLUGLYGLNASNASN
9   ILEALAASPASPLEUILEASNLYSLEUASN
10   GLNLEUVALGLULYSGLNGLUASNLYSGLY
11   VALSERASNILEASPPHELYSGLULYSARG
12   LYSLYSHISTYRASNGLUTYRLYSMETLEU
13   GLNLYSLEUARGLYSSERGLYTHRLEUASP
14   ASPILEASPGLUGLUTYRLYSPROASPASN
15   LYSASPSERASNCYSASPASNSERASNMET
16   ASNGLUSERGLUGLU

Samples:

sample_1: PfI2, [U-98% 15N], 0.05 – 0.1 mM; sodium phosphate 100 mM; sodium chloride 100 mM; EDTA 2.5 mM; DTT 10 mM; TSP 0.1 mM; D2O 5%; H2O 95%

sample_2: PfI2, [U-98% 13C; U-98% 15N], 0.05 – 0.2 mM; sodium phosphate 100 mM; sodium chloride 100 mM; EDTA 2.5 mM; DTT 10 mM; TSP 0.1 mM; D2O 5%; H2O 95%

sample_conditions_1: temperature: 298 K; pH: 6.7; pressure: 1 atm; ionic strength: 100 mM

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

TOPSPIN v2.1, Bruker Biospin - processing

Mars, Jung YS & Zweckstetter M - chemical shift assignment

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

plasmodb PF3D7_0320000
EMBL CAX64439 CDO62624
GB ETW20523 ETW38648 ETW45017 ETW51416 ETW52113
REF XP_002808630 XP_012761271

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