BMRB Entry 34459

Title:
P. falciparum essential light chain, N-terminal domain
Deposition date:
2019-11-25
Original release date:
2020-10-23
Authors:
Weininger, U.; Pazicky, S.; Loew, C.
Citation:

Citation: Pazicky, S.; Dhamotharan, K.; Kaszuba, K.; Mertens, H.; Gilberger, T.; Svergun, D.; Kosinski, J.; Weininger, U.; Loew, C.. "Structural role of essential light chains in the apicomplexan glideosome"  Commun. Biol. 3, 568-568 (2020).
PubMed: 33051581

Assembly members:

Assembly members:
entity_1, polymer, 74 residues, 8934.129 Da.

Natural source:

Natural source:   Common Name: Plasmodium falciparum 3D7   Taxonomy ID: 36329   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium falciparum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21   Vector: pNIC28_Bsa4

Entity Sequences (FASTA):

Data typeCount
13C chemical shifts290
15N chemical shifts81
1H chemical shifts566

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 74 residues - 8934.129 Da.

1   METALASERASPMETGLUGLULYSPHEARG
2   GLUALAPHEILELEUPHESERSERCYSSER
3   ASPHISILEGLUMETTYRLYSPHEPHEGLU
4   LEUMETASNSERPHEGLYILEILELEUTHR
5   ASNASPGLULYSALAALALEUPROASNASP
6   ILEASNMETASPTYRTRPLEUASNPHEALA
7   LYSLYSHISTYRASNTYRGLUGLNPROPHE
8   LYSHISILEASN

Samples:

sample_1: ELC 1-74, [U-99% 13C; U-99% 15N], 1.0 mM; Tris 50 mM; NaCl 20 mM; TCEP 0.5 mM

sample_2: ELC 1-74, 1-13C1 glucose, 1.0 mM; Tris 50 mM; NaCl 20 mM; TCEP 0.5 mM

sample_3: ELC 1-74, 2-13C1 glucose, 1.0 mM; Tris 50 mM; NaCl 20 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 70 mM; pH: 7.0; pressure: 1 bar; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D HCCH-TOCSY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker AVANCE II 800 MHz
  • Bruker AVANCE III 600 MHz

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