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 15075

Title: Merozoite surface protein 2 (MSP2) of Plasmodium falciparum: expression, structure and amyloid formation of the conserved N-terminal domain   PubMed: 17516503

Authors: Low, Andrew; Chandrashekaran, Indu; Adda, Christopher; Yao, Shenggan; Sabo, Jennifer; Zhang, Xuecheng; Soetopo, Alfreda; Anders, Robin; Norton, Raymond

Citation: Low, Andrew; Chandrashekaran, Indu; Adda, Christopher; Yao, Shenggan; Sabo, Jennifer; Zhang, Xuecheng; Soetopo, Alfreda; Anders, Robin; Norton, Raymond. "Merozoite surface protein 2 of Plasmodium falciparum: expression, structure, dynamics, and fibril formation of the conserved N-terminal domain"  Biopolymers 87, 12-22 (2007).

Assembly members:
1-25MSP2, polymer, 28 residues, 3228 Da.

Natural source:   Common Name: Escherichia coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
1-25MSP2: GSMIKNESKYSNTFINNAYN MSIRRSMA

Data sets:
Data typeCount
15N chemical shifts30
1H chemical shifts166
coupling constants11

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
11-25MSP21

Entities:

Entity 1, 1-25MSP2 28 residues - 3228 Da.

Residues -3 to -1 are from the cleavage site. Residues 1 to 25 are the N-terminal region of MSP2

1   GLYSERMETILELYSASNGLUSERLYSTYR
2   SERASNTHRPHEILEASNASNALATYRASN
3   METSERILEARGARGSERMETALA

Samples:

sample_1: 1-25MSP2, [U-15N], 1.2 mM; D2O 5%; Acetic Acid 10 mM

sample_conditions_1: ionic strength: 10 mM; pH: 3.4; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - Data collection, Data processing

XEASY v1.3, Bartels et al. - Peak assignments

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 15590 25202
PDB
EMBL CAA37829 CAA37830 CAA53701 CAA53946 CAA60699
GB AAA19735 AAA19737 AAA19738 AAA19739 AAA19740
PIR B45632 C39112
PRF 2023165A 2023165B
REF XP_001349578
SP P19260 P19599 P50496 P50497 P50498