BMRB Entry 25034

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25034

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Amide 1H and 15N chemical shift assignments and 15N relaxation parameters of the troponin C-troponin I hybrid proteins cChimera
Deposition date:
2014-06-20
Original release date:
2014-09-18
Authors:
Pineda Sanabria, Sandra; Sykes, Brian; Julien, Olivier
Citation:

Citation: Pineda-Sanabria, Sandra; Julien, Olivier; Sykes, Brian. "Versatile cardiac troponin chimera for muscle protein structural biology and drug discovery."  ACS Chem. Biol. 9, 2121-2130 (2014).
PubMed: 25010113

Assembly members:

Assembly members:
cChimera, polymer, 141 residues, 15937 Da.
entity_CA, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cChimera: MHHHHHHGGENLYFQGMDDI YKAAVEQLTEEQKNEFKAAF DIFVLGAEDGSISTKELGKV MRMLGQNPTPEELQEMIDEV DEDGSGTVDFDEFLVMMVRC MKDDSLVPPGSRRVRISADA MMQALLGARAKESLDLRAHL K

Data typeCount
1H chemical shifts183
15N chemical shifts95
heteronuclear NOE values183
T1 relaxation values181
T2 relaxation values182

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cChimera1
2CALCIUM ION2

Entities:

Entity 1, cChimera 141 residues - 15937 Da.

Residues -15 to -8 correspond to the His tag. Residues -7 to -1 correspond to the TEV cleavage site. Residues 1 to 89 correspond to residues 1 to 89 of cNTnC. Residues 90 to 95 correspond to the thrombin cleavage site. Residues 144 to 173 correspond to 144 to 173 of cTnI.

1   METHISHISHISHISHISHISGLYGLYGLU
2   ASNLEUTYRPHEGLNGLYMETASPASPILE
3   TYRLYSALAALAVALGLUGLNLEUTHRGLU
4   GLUGLNLYSASNGLUPHELYSALAALAPHE
5   ASPILEPHEVALLEUGLYALAGLUASPGLY
6   SERILESERTHRLYSGLULEUGLYLYSVAL
7   METARGMETLEUGLYGLNASNPROTHRPRO
8   GLUGLULEUGLNGLUMETILEASPGLUVAL
9   ASPGLUASPGLYSERGLYTHRVALASPPHE
10   ASPGLUPHELEUVALMETMETVALARGCYS
11   METLYSASPASPSERLEUVALPROPROGLY
12   SERARGARGVALARGILESERALAASPALA
13   METMETGLNALALEULEUGLYALAARGALA
14   LYSGLUSERLEUASPLEUARGALAHISLEU
15   LYS

Entity 2, CALCIUM ION - Ca - 40.078 Da.

1   CA

Samples:

sample_1: cChimera, [U-100% 15N], 0.5 – 0.8 mM; Ca2+ 2 mM; DTT 10 mM; potassium chloride 100 mM; imidazole 10 mM; D2O 5%

sample_conditions_1: temperature: 273 K; pH: 6.9; pressure: 1 atm; ionic strength: 0.1 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRView v8.2.33, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

VNMRJ, Varian - collection

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

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15385 15388 15400 15427 16190 16752 17103 19789 25120 25495 25797
PDB
DBJ BAA02369 BAG36483
EMBL CAA30736 CAG46663 CAG46683
GB AAA36772 AAA37492 AAA37493 AAA48654 AAB91994
PIR S07450 TPHUCC
PRF 1403394A 1510257A 750650A
REF NP_001029277 NP_001029523 NP_001123715 NP_001272501 NP_001291793
SP P02591 P05936 P09860 P19123 P63315
TPG DAA16908
AlphaFold P02591 P05936 P09860 P19123 P63315

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