BMRB Entry 30965
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30965
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title: cTnC-TnI chimera complexed with A1 PubMed: 35349258
Deposition date: 2021-11-19 Original release date: 2022-03-30
Authors: Poppe, L.; Hartman, J.; Romero, A.; Reagan, J.
Citation: Poppe, L.; Hartman, J.; Romero, A.; Reagan, J.. "Structural and Thermodynamic Model for the Activation of Cardiac Troponin" Biochemistry 61, 741-748 (2022).
Assembly members:
entity_1, polymer, 129 residues, 14222.121 Da.
entity_BQ6, non-polymer, 446.495 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 BL21(DE3)
Entity Sequences (FASTA):
entity_1: GDDIYKAAVEQLTEEQKNEF
KAAFDIFVLGAEDGCISTKE
LGKVMRMLGQNPTPEELQEM
IDEVDEDGSGTVDFDEFLVM
MVRCMKDDSKGAGAGVRISA
DAMMQALLGARAKESLDLRA
HLKQVKKED
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 556 |
| 15N chemical shifts | 133 |
| 1H chemical shifts | 914 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | unit_2 | 2 |
Entities:
Entity 1, unit_1 129 residues - 14222.121 Da.
| 1 | GLY | 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 | LYS | ||||
| 10 | GLY | ALA | GLY | ALA | GLY | VAL | ARG | ILE | SER | ALA | ||||
| 11 | ASP | ALA | MET | MET | GLN | ALA | LEU | LEU | GLY | ALA | ||||
| 12 | ARG | ALA | LYS | GLU | SER | LEU | ASP | LEU | ARG | ALA | ||||
| 13 | HIS | LEU | LYS | GLN | VAL | LYS | LYS | GLU | ASP |
Entity 2, unit_2 - C21 H23 F N4 O4 S - 446.495 Da.
| 1 | BQ6 |
Samples:
sample_1: cTnC-TnI chimera, [U-13C; U-15N], 1 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| CBCANH | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin v3.0, Bruker-Biospin - processing
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
XEASY v1.5.5, Bartels et al. - peak picking
CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
NMR spectrometers:
- Bruker AVANCE III HD 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts