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 19233

Title: 1H, 13C, 15N assignments for P. yoelii Merozoite Surface Protein 1   PubMed: 24403012

Deposition date: 2013-05-08 Original release date: 2015-09-02

Authors: Curd, Rachel; Birdsall, Berry; Kadekoppala, Madhusudan; Ogun, Solabomi; Kelly, Geoff; Holder, Anthony

Citation: Curd, Rachel; Birdsall, Berry; Kadekoppala, Madhusudan; Ogun, Solabomi; Kelly, Geoff; Holder, Anthony. "The structure of Plasmodium yoelii merozoite surface protein 119, antibody specificity and implications for malaria vaccine design"  Open Biol. 4, 130091-130091 (2014).

Assembly members:
MSP1, polymer, 99 residues, Formula weight is not available

Natural source:   Common Name: apicomplexans   Taxonomy ID: 5861   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium Yoelii

Experimental source:   Production method: recombinant technology   Host organism: Pichia pastoris   Vector: pPICK9K

Entity Sequences (FASTA):
MSP1: GVDPKHVCVDTRDIPKNAGC FRDDDGTEEWRCLLGYKKGE GNTCVENNNPTCDINNGGCD PTASCQNAESTENSKKIICT CKEPTPNAYYEGVFCSSSS

Data sets:
Data typeCount
13C chemical shifts382
15N chemical shifts108
1H chemical shifts618

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MSP11

Entities:

Entity 1, MSP1 99 residues - Formula weight is not available

1   GLYVALASPPROLYSHISVALCYSVALASP
2   THRARGASPILEPROLYSASNALAGLYCYS
3   PHEARGASPASPASPGLYTHRGLUGLUTRP
4   ARGCYSLEULEUGLYTYRLYSLYSGLYGLU
5   GLYASNTHRCYSVALGLUASNASNASNPRO
6   THRCYSASPILEASNASNGLYGLYCYSASP
7   PROTHRALASERCYSGLNASNALAGLUSER
8   THRGLUASNSERLYSLYSILEILECYSTHR
9   CYSLYSGLUPROTHRPROASNALATYRTYR
10   GLUGLYVALPHECYSSERSERSERSER

Samples:

sample_1: MSP1, [U-99% 13C; U-99% 15N], 1.0 mM; potassium chloride 50.0 mM; potassium phosphate 25.0 mM; H2O 95%; D2O 5%

sample_conditions_1: pH*: 6.5; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

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