BMRB Entry 25810
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25810
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Title: NMR structure of the N-domain of troponin C bound to the switch region of troponin I and the covalent levosimendan analog i9.
Deposition date: 2015-09-14 Original release date: 2016-07-20
Authors: Pineda Sanabria, Sandra; Sykes, Brian; Robertson, Ian
Citation: Pineda Sanabria, Sandra; Robertson, Ian; Sun, Yin-Biao; Irving, Malcolm; Sykes, Brian. "Troponin C with covalently bound levosimendan analog i9 enhances contraction in cardiac muscle fibers" Not known ., .-..
Assembly members:
entity_1, polymer, 141 residues, 1702.936 Da.
entity_CA, non-polymer, 40.078 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MHHHHHHGGLVPRGSMDDIY
KAAVEQLTEEQKNEFKAAFD
IFVLGAEDGSISTKELGKVM
RMLGQNPTPEELQEMIDEVD
EDGSGTVDFDEFLVMMVRXM
KDDSENLYFQGRRVRISADA
MMQALLGARAKESLDLRAHL
K
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 352 |
| 15N chemical shifts | 116 |
| 19F chemical shifts | 2 |
| 1H chemical shifts | 675 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | CALCIUM ION | 2 |
Entities:
Entity 1, entity_1 141 residues - 1702.936 Da.
MHHHHHHGGLVPRGSMDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGSISTKELGKVMRMLGQNPTPEELQEMIDEVD EDGSGTVDFDEFLVMMVR(4J4)MKDDSENLYFQGRRVRISADAMMQALLGARAKESLDLRAHLK Residues 1 to 7 are the His tag (Auth_seq_ID -15 to -9). Residues 8 to 15 are the thrombin cleavage site (Auth_seq_ID -8 to -1). Residues 16 to 104 are the N-domain of troponin C residues 1-89 (Auth_seq_ID 1 to 89). Residues 105 to 111 are the TEV cleavage site (Auth_seq_ID 90 to 96). Residues 112 to 141 are residues 144-173 of troponin I (Auth_seq_ID 97 to 126).
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | GLY | GLY | LEU | ||||
| 2 | VAL | PRO | ARG | GLY | SER | MET | ASP | ASP | ILE | TYR | ||||
| 3 | LYS | ALA | ALA | VAL | GLU | GLN | LEU | THR | GLU | GLU | ||||
| 4 | GLN | LYS | ASN | GLU | PHE | LYS | ALA | ALA | PHE | ASP | ||||
| 5 | ILE | PHE | VAL | LEU | GLY | ALA | GLU | ASP | GLY | SER | ||||
| 6 | ILE | SER | THR | LYS | GLU | LEU | GLY | LYS | VAL | MET | ||||
| 7 | ARG | MET | LEU | GLY | GLN | ASN | PRO | THR | PRO | GLU | ||||
| 8 | GLU | LEU | GLN | GLU | MET | ILE | ASP | GLU | VAL | ASP | ||||
| 9 | GLU | ASP | GLY | SER | GLY | THR | VAL | ASP | PHE | ASP | ||||
| 10 | GLU | PHE | LEU | VAL | MET | MET | VAL | ARG | 4J4 | MET | ||||
| 11 | LYS | ASP | ASP | SER | GLU | ASN | LEU | TYR | PHE | GLN | ||||
| 12 | GLY | ARG | ARG | VAL | ARG | ILE | SER | ALA | ASP | ALA | ||||
| 13 | MET | MET | GLN | ALA | LEU | LEU | GLY | ALA | ARG | ALA | ||||
| 14 | LYS | GLU | SER | LEU | ASP | LEU | ARG | ALA | HIS | LEU | ||||
| 15 | LYS |
Entity 2, CALCIUM ION - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: entity_1, [U-15N], 0.65 mM; entity_2, [U-15N], 0.65 mM; potassium chloride 100 mM; imidazole 10 mM; calcium chloride 2 mM; DSS, [U-99% 2H], 0.25 mM
sample_2: entity_1, [U-13C; U-15N], 0.65 mM; entity_2, [U-13C; U-15N], 0.65 mM; potassium chloride 100 mM; imidazole 10 mM; calcium chloride 2 mM; DSS, [U-99% 2H], 0.25 mM
sample_3: entity_1, [U-13C; U-15N], 0.65 mM; entity_2, [U-13C; U-15N], 0.65 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; calcium chloride 2 mM; DSS, [U-99% 2H], 0.25 mM
sample_conditions_1: pH: 6.9; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
| gnoesyChsqc_CNfilt | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY CN filtered | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-19F HMQC | sample_3 | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis
TALOS, Cornilescu, Delaglio and Bax - Prediction of phi and psi dihedral angles
X-PLOR_NIH v2.35, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
PRODRG, A. W. Sch ttelkopf and D. M. F. van Aalten - Generation of topology and parameter files for non-standard aminoacid Ci9
NMR spectrometers:
- 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