BMRB Entry 34459

Name: P. falciparum essential light chain, N-terminal domain
Published: 2020-10-23

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34459

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: P. falciparum essential light chain, N-terminal domain PubMed: 33051581

Deposition date: 2019-11-25 Original release date: 2020-10-23

Authors: Weininger, U.; Pazicky, S.; Loew, C.

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).

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

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

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

Entity Sequences (FASTA):
entity_1: MASDMEEKFREAFILFSSCS DHIEMYKFFELMNSFGIILT NDEKAALPNDINMDYWLNFA KKHYNYEQPFKHIN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	290
15N chemical shifts	81
1H chemical shifts	566

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 74 residues - 8934.129 Da.

1

MET

ALA

SER

ASP

MET

GLU

LYS

PHE

ARG

2

GLU

ALA

PHE

ILE

LEU

PHE

SER

CYS

SER

3

ASP

HIS

ILE

GLU

MET

TYR

LYS

PHE

GLU

4

LEU

MET

ASN

SER

PHE

GLY

ILE

LEU

THR

5

ASN

ASP

GLU

LYS

ALA

LEU

PRO

ASN

ASP

6

ILE

ASN

MET

ASP

TYR

TRP

LEU

ASN

PHE

ALA

7

LYS

HIS

TYR

ASN

TYR

GLU

GLN

PRO

PHE

8

LYS

HIS

ILE

ASN

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_1	isotropic	sample_conditions_1
2D HCCH-TOCSY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_3	isotropic	sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts