BMRB Entry 15698

Name: Solution Structure of the Apo C terminal domain of Lethocerus troponin C isoform F1
Published: 2010-02-01

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PDB ID: 2k2a
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15698
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution Structure of the Apo C terminal domain of Lethocerus troponin C isoform F1 PubMed: 20104876

Deposition date: 2008-03-29 Original release date: 2010-02-01

Authors: De Nicola, Gian; Kelly, Geoff; Bullard, Belinda; McCormick, John

Citation: De Nicola, Gian Felice; Martin, Stephen; Bullard, Belinda; Pastore, Annalisa. "Solution structure of the Apo C-terminal domain of the Lethocerus F1 troponin C isoform." Biochemistry 49, 1719-1726 (2010).

Assembly members:
Lethocerus F1 troponin C isoform, polymer, 70 residues, 7849.534 Da.

Natural source: Common Name: Lethocerus indicus Taxonomy ID: 212017 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Lethocerus indicus

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

Entity Sequences (FASTA):
Lethocerus F1 troponin C isoform: MQQELREAFRLYDKEGNGYI STDVMREILAELDETLSSED LDAMIDEIDADGSGTVDFEE FMGVMTGGDE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	198
15N chemical shifts	71
1H chemical shifts	447

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	1
3	entity_3	1
4	entity_4	1
5	entity_5	1
6	entity_6	1
7	entity_7	1
8	entity_8	1
9	entity_9	1
10	entity_10	1

Entities:

Entity 1, entity_1 70 residues - 7849.534 Da.

The entry numbering corresponds to the numbering in the natural protein without added tags. It starts from residue 89 of lethocerus TnC

1	MET	GLN	GLN	GLU	LEU	ARG	GLU	ALA	PHE	ARG
2	LEU	TYR	ASP	LYS	GLU	GLY	ASN	GLY	TYR	ILE
3	SER	THR	ASP	VAL	MET	ARG	GLU	ILE	LEU	ALA
4	GLU	LEU	ASP	GLU	THR	LEU	SER	SER	GLU	ASP
5	LEU	ASP	ALA	MET	ILE	ASP	GLU	ILE	ASP	ALA
6	ASP	GLY	SER	GLY	THR	VAL	ASP	PHE	GLU	GLU
7	PHE	MET	GLY	VAL	MET	THR	GLY	GLY	ASP	GLU

Samples:

sample_1: protein, [U-99% 15N], 0.4 mM; sodium chloride 100 mM; TRIS 20 mM

sample_2: protein, [U-99% 15N], 0.4 mM; sodium chloride 100 mM; TRIS 20 mM

sample_3: protein, [U-99% 13C; U-99% 15N], 0.4 mM; sodium chloride 100 mM; TRIS 20 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

ARIA v1.2, Linge, O, . - refinement, structure solution

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

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

VNMR, Varian - collection

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 600 MHz

Biological Magnetic Resonance Data Bank