BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19029

Title: 1H, 13C and 15N resonance assignments of K2A1: N-terminal repeat of the K2A domain of Plasmodium falciparum knob - associated histidine rich protein (KAHRP).   PubMed: 25726759

Authors: Ganguly, Akshay Kumar; Bhavesh, Neel Sarovar

Citation: Ganguly, Akshay Kumar; Ranjan, Priyatosh; Kumar, Ashutosh; Bhavesh, Neel Sarovar. "Dynamic association of PfEMP1 and KAHRP in knobs mediates cytoadherence during Plasmodium invasion"  Sci Rep. 5, 8617-8617 (2015).

Assembly members:
K2A1, polymer, 60 residues, 7028.7 Da.

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):
K2A1: MGKHHSSKKHEGNDGEGEKK KKSKKHKDHDGEKKKSKKHK DNEDAESVKSKKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts219
15N chemical shifts54
1H chemical shifts216

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1K2A11

Entities:

Entity 1, K2A1 60 residues - 7028.7 Da.

The core polypeptide represents the first of two tandem repeats present in the K2A region (5' repeat region) of the Plasmodium falciparum knob associated histidine rich protein. Residues H55 - H60 represent a non - native hexahistidine affinity tag. Residues M1, G2, L53 and E54 are derived from the vector pET28b in which the polypeptide is cloned.

1   METGLYLYSHISHISSERSERLYSLYSHIS
2   GLUGLYASNASPGLYGLUGLYGLULYSLYS
3   LYSLYSSERLYSLYSHISLYSASPHISASP
4   GLYGLULYSLYSLYSSERLYSLYSHISLYS
5   ASPASNGLUASPALAGLUSERVALLYSSER
6   LYSLYSLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: K2A1, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 6.2; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D NCOsample_1isotropicsample_conditions_1
2D CACOsample_1isotropicsample_conditions_1
3D C(CCCO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz

Related Database Links:

EMBL CAA68268 CAA68270
GB AAA29629 AAA29630 AAA29632 AAC71810 AAD23574
PRF 1407234A 1413318A 2206359A
REF XP_001349534
SP P05229 P06719 P09346 P13817