BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 25511

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25511

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Structure and dynamics of the acidosis-resistant a162H mutant of the switch region of troponin I bound to the regulatory domain of troponin C   PubMed: 25996354

Deposition date: 2015-03-03 Original release date: 2016-06-30

Authors: Pineda Sanabria, Sandra; Robertson, Ian; Sykes, Brian

Citation: Pineda Sanabria, Sandra; Robertson, Ian; Sykes, Brian. "Structure and Dynamics of the Acidosis-Resistant A162H Mutant of the Switch Region of Troponin I Bound to the Regulatory Domain of Troponin C"  Biochemistry 54, 3583-3593 (2015).

Assembly members:
cChimeraX-A162H, polymer, 141 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 Da.

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

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

Entity Sequences (FASTA):
cChimeraX-A162H: MHHHHHHGGLVPRGSMDDIY KAAVEQLTEEQKNEFKAAFD IFVLGAEDGSISTKELGKVM RMLGQNPTPEELQEMIDEVD EDGSGTVDFDEFLVMMVRCM KDDSENLYFQGRRVRISADA MMQALLGARHKESLDLRAHL K

Data sets:
Data typeCount
15N chemical shifts91
1H chemical shifts91
T1 relaxation values176
T2 relaxation values168

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cChimeraX-A162H1
2CALCIUM ION2

Entities:

Entity 1, cChimeraX-A162H 141 residues - Formula weight is not available

Residues -15 to -7 correspond to the His tag. Residues -6 to -1 correspond to the thrombin cleavage site. Residues 1 to 89 correspond to residues 1 to 89 of cNTnC. Residues 90 to 96 correspond to the thrombin cleavage site. Residues 144 to 173 correspond to 144 to 173 of cTnI.

1   METHISHISHISHISHISHISGLYGLYLEU
2   VALPROARGGLYSERMETASPASPILETYR
3   LYSALAALAVALGLUGLNLEUTHRGLUGLU
4   GLNLYSASNGLUPHELYSALAALAPHEASP
5   ILEPHEVALLEUGLYALAGLUASPGLYSER
6   ILESERTHRLYSGLULEUGLYLYSVALMET
7   ARGMETLEUGLYGLNASNPROTHRPROGLU
8   GLULEUGLNGLUMETILEASPGLUVALASP
9   GLUASPGLYSERGLYTHRVALASPPHEASP
10   GLUPHELEUVALMETMETVALARGCYSMET
11   LYSASPASPSERGLUASNLEUTYRPHEGLN
12   GLYARGARGVALARGILESERALAASPALA
13   METMETGLNALALEULEUGLYALAARGHIS
14   LYSGLUSERLEUASPLEUARGALAHISLEU
15   LYS

Entity 2, CALCIUM ION - Ca - 40.078 Da.

1   CA

Samples:

sample_1: cChimeraX-A162H, [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: ionic strength: 0.12 M; pH: 7.4; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 0.12 M; pH: 6.4; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2

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 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts