BMRB Entry 25495
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25495
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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: 2015-02-20 Original release date: 2015-06-01
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:
cNTnC, polymer, 89 residues, 10070.361 Da.
cTnIA162H, polymer, 27 residues, 3072.655 Da.
entity_CA, non-polymer, 40.078 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
cNTnC: MDDIYKAAVEQLTEEQKNEF
KAAFDIFVLGAEDGCISTKE
LGKVMRMLGQNPTPEELQEM
IDEVDEDGSGTVDFDEFLVM
MVRCMKDDS
cTnIA162H: RRVRISADAMMQALLGARHK
ESLDLRA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 239 |
| 15N chemical shifts | 83 |
| 1H chemical shifts | 731 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
| 3 | entity_3 | 3 |
Entities:
Entity 1, entity_1 89 residues - 10070.361 Da.
| 1 | MET | ASP | ASP | ILE | TYR | LYS | ALA | ALA | VAL | GLU | ||||
| 2 | GLN | LEU | THR | GLU | GLU | GLN | LYS | ASN | GLU | PHE | ||||
| 3 | LYS | ALA | ALA | PHE | ASP | ILE | PHE | VAL | LEU | GLY | ||||
| 4 | ALA | GLU | ASP | GLY | CYS | ILE | SER | THR | LYS | GLU | ||||
| 5 | LEU | GLY | LYS | VAL | MET | ARG | MET | LEU | GLY | GLN | ||||
| 6 | ASN | PRO | THR | PRO | GLU | GLU | LEU | GLN | GLU | MET | ||||
| 7 | ILE | ASP | GLU | VAL | ASP | GLU | ASP | GLY | SER | GLY | ||||
| 8 | THR | VAL | ASP | PHE | ASP | GLU | PHE | LEU | VAL | MET | ||||
| 9 | MET | VAL | ARG | CYS | MET | LYS | ASP | ASP | SER |
Entity 2, entity_2 27 residues - 3072.655 Da.
| 1 | ARG | ARG | VAL | ARG | ILE | SER | ALA | ASP | ALA | MET | ||||
| 2 | MET | GLN | ALA | LEU | LEU | GLY | ALA | ARG | HIS | LYS | ||||
| 3 | GLU | SER | LEU | ASP | LEU | ARG | ALA |
Entity 3, entity_3 - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: cNTnC, [U-15N], 0.9 mM; cTnIA162H 3.6 mM; Calcium 10 mM; imidazole 10 mM; DSS, [U-2H], 0.25 mM; DTT 10 mM; Potassium chloride 100 mM
sample_2: cNTnC, [U-13C; U-15N], 0.9 mM; cTnIA162H 3.6 mM; Calcium 10 mM; imidazole 10 mM; DSS, [U-2H], 0.25 mM; DTT 10 mM; Potassium chloride 100 mM
sample_3: cNTnC, [U-13C; U-15N], 0.9 mM; cTnIA162H 3.6 mM; Calcium 10 mM; imidazole 10 mM; DSS, [U-2H], 0.25 mM; DTT 10 mM; Potassium chloride 100 mM
sample_4: cNTnC, [U-15N], 0.9 mM; cTnIA162H 3.6 mM; Calcium 10 mM; imidazole 10 mM; DSS, [U-2H], 0.25 mM; DTT 10 mM; Potassium chloride 100 mM
sample_conditions_1: ionic strength: 0.12 M; pH: 6.1; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | sample_4 | isotropic | sample_conditions_1 |
| 13C-15N filtered TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 13C-15N filtered NOESY | sample_3 | isotropic | sample_conditions_1 |
| Chmqcnoesy-Cfilt | sample_3 | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRViewJ v8.2.33, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
X-PLOR_NIH v2.35, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
PSVS v1.5, Bhattacharya and Montelione - validation
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts