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 15698

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

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:
Data typeCount
13C chemical shifts198
15N chemical shifts71
1H chemical shifts447

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21
3entity_31
4entity_41
5entity_51
6entity_61
7entity_71
8entity_81
9entity_91
10entity_101

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   METGLNGLNGLULEUARGGLUALAPHEARG
2   LEUTYRASPLYSGLUGLYASNGLYTYRILE
3   SERTHRASPVALMETARGGLUILELEUALA
4   GLULEUASPGLUTHRLEUSERSERGLUASP
5   LEUASPALAMETILEASPGLUILEASPALA
6   ASPGLYSERGLYTHRVALASPPHEGLUGLU
7   PHEMETGLYVALMETTHRGLYGLYASPGLU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_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

Related Database Links:

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