BMRB Entry 16506

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16506

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Title:
Back bone chemical shift assignments of the acyl-intermediates of fatty acid synthesis pathway of P. falciparum
Deposition date:
2009-09-22
Original release date:
2010-03-01
Authors:
Upadhyay, Santosh; Misra, Ashish; Srivastava, Richa; Surolia, Namita; Surolia, Avadhesha; Sundd, Monica
Citation:

Citation: Upadhyay, Santosh Kumar; Misra, Ashish; Surolia, Namita; Surolia, Avadhesha; Sundd, Monica. "Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum."  Biomol. NMR Assignments 4, 83-85 (2010).
PubMed: 20182923

Assembly members:

Assembly members:
acyl_carrier_protein, polymer, 79 residues, Formula weight is not available
PNS, non-polymer, 358.348 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet

Entity Sequences (FASTA):

Entity Sequences (FASTA):
acyl_carrier_protein: LKSTFDDIKKIISKQLSVEE DKIQMNSNFTKDLGADSLDL VELIMALEEKFNVTISDQDA LKINTVQDAIDYIEKNNKQ

Data sets:
Data typeCount
13C chemical shifts136
15N chemical shifts71
1H chemical shifts71

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer1
2PNS2

Entities:

Entity 1, monomer 79 residues - Formula weight is not available

Residue 1-5 not visible

1   LEULYSSERTHRPHEASPASPILELYSLYS
2   ILEILESERLYSGLNLEUSERVALGLUGLU
3   ASPLYSILEGLNMETASNSERASNPHETHR
4   LYSASPLEUGLYALAASPSERLEUASPLEU
5   VALGLULEUILEMETALALEUGLUGLULYS
6   PHEASNVALTHRILESERASPGLNASPALA
7   LEULYSILEASNTHRVALGLNASPALAILE
8   ASPTYRILEGLULYSASNASNLYSGLN

Entity 2, PNS - C11 H23 N2 O7 P S - 358.348 Da.

1   PNS

Samples:

sample_1: protein 1 mM; DTT 2.0 mM; sodium chloride 100 mM; sodium phosphate 50 mM; sodium azide 0.5%; D2O 90%; H2O 10%

sample_conditions_1: pH: 6.5; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

SPARKY v3.113, Goddard - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Varian INOVA 500 MHz

Related Database Links:

BMRB 16529 16530 16531 16532 16533 16661
PDB
EMBL CDO62314
GB AAC63959 AAC71866 ETW20884 ETW27965 ETW39040
REF XP_001349595 XP_012760964

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