BMRB Entry 15388

Title:
Solution Structure of F153W cardiac troponin C
Deposition date:
2007-07-18
Original release date:
2008-03-13
Authors:
Wang, Xu; Mercier, Pascal; Letourneau, Paul-Jean; Sykes, Brian
Citation:

Citation: Wang, Xu; Mercier, Pascal; Letourneau, Paul-Jean; Sykes, Brian. "Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies"  Protein Sci. 14, 2447-2460 (2005).
PubMed: 16131667

Assembly members:

Assembly members:
F153W, polymer, 161 residues, 18428.521 Da.
CA, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-21

Data sets:
Data typeCount
13C chemical shifts509
15N chemical shifts154
1H chemical shifts956

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1F153W cTnC1
2Calcium2

Entities:

Entity 1, F153W cTnC 161 residues - 18428.521 Da.

This protein is a version of cardiac troponin C with F153 mutated to W

1   METASPASPILETYRLYSALAALAVALGLU
2   GLNLEUTHRGLUGLUGLNLYSASNGLUPHE
3   LYSALAALAPHEASPILEPHEVALLEUGLY
4   ALAGLUASPGLYSERILESERTHRLYSGLU
5   LEUGLYLYSVALMETARGMETLEUGLYGLN
6   ASNPROTHRPROGLUGLULEUGLNGLUMET
7   ILEASPGLUVALASPGLUASPGLYSERGLY
8   THRVALASPPHEASPGLUPHELEUVALMET
9   METVALARGSERMETLYSASPASPSERLYS
10   GLYLYSSERGLUGLUGLULEUSERASPLEU
11   PHEARGMETPHEASPLYSASNALAASPGLY
12   TYRILEASPLEUASPGLULEULYSILEMET
13   LEUGLNALATHRGLYGLUTHRILETHRGLU
14   ASPASPILEGLUGLULEUMETLYSASPGLY
15   ASPLYSASNASNASPGLYARGILEASPTYR
16   ASPGLUTRPLEUGLUPHEMETLYSGLYVAL
17   GLU

Entity 2, Calcium - Ca - 40.078 Da.

1   CA

Samples:

sample_1: F153W 1.0 ± 0.2 mM; Calcium 10 ± 1 mM; potassium chloride 100 ± 10 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15385 15400 15427 16190 17103 19789 25034 25035 25120 25495 25797
PDB
DBJ BAG36483
EMBL CAA30736 CAG46663 CAG46683
GB AAA36772 AAA37492 AAA37493 AAB91994 AAH30244
PIR TPHUCC
PRF 1510257A 750650A
REF NP_001029277 NP_001029523 NP_001123715 NP_001272501 NP_003271
SP P02591 P19123 P63315 P63316 P63317
TPG DAA16908
AlphaFold P63315 P02591 P19123 P63316 P63317

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