BMRB Entry 19977
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19977
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Title: Solution structure human HCN2 CNBD in the cAMP-unbound state
Deposition date: 2014-05-16 Original release date: 2014-09-02
Authors: Saponaro, Andrea; Pauleta, Sofia; Cantini, Francesca; Matzapetakis, Manolis; Hammann, Christian; Banci, Lucia; Thiel, Gerard; Santoro, Bina; Moroni, Anna
Citation: Saponaro, Andrea; Pauleta, Sofia; Cantini, Francesca; Matzapetakis, Manolis; Hammann, Christian; Banci, Lucia; Thiel, Gerard; Santoro, Bina; Moroni, Anna. "Structural basis for the mutual antagonism of cAMP and TRIP8b in regulating HCN channel function" Not known ., .-..
Assembly members:
entity, polymer, 158 residues, 15918.672 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):
entity: GPSSPMELNGPLREEIVNFN
CRKLVASMPLFANADPNFVT
AMLTKLKFEVFQPGDYIIRE
GTIGKKMYFIQHGVVSVLTK
GNKEMKLSDGSYFGEICLLT
RGRRTASVRADTYCRLYSLS
VDNFNEVLEEYPMMRRAFET
VAIDRLDRIGKKNSILLH
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 1113 |
| 13C chemical shifts | 624 |
| 15N chemical shifts | 149 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | human HCN2 CNBD | 1 |
Entities:
Entity 1, human HCN2 CNBD 158 residues - 15918.672 Da.
Residues 515-520 represent a non-native affinity tag Residues 521-533 are unstructured and were omitted for simplicity
| 1 | GLY | PRO | SER | SER | PRO | MET | GLU | LEU | ASN | GLY | ||||
| 2 | PRO | LEU | ARG | GLU | GLU | ILE | VAL | ASN | PHE | ASN | ||||
| 3 | CYS | ARG | LYS | LEU | VAL | ALA | SER | MET | PRO | LEU | ||||
| 4 | PHE | ALA | ASN | ALA | ASP | PRO | ASN | PHE | VAL | THR | ||||
| 5 | ALA | MET | LEU | THR | LYS | LEU | LYS | PHE | GLU | VAL | ||||
| 6 | PHE | GLN | PRO | GLY | ASP | TYR | ILE | ILE | ARG | GLU | ||||
| 7 | GLY | THR | ILE | GLY | LYS | LYS | MET | TYR | PHE | ILE | ||||
| 8 | GLN | HIS | GLY | VAL | VAL | SER | VAL | LEU | THR | LYS | ||||
| 9 | GLY | ASN | LYS | GLU | MET | LYS | LEU | SER | ASP | GLY | ||||
| 10 | SER | TYR | PHE | GLY | GLU | ILE | CYS | LEU | LEU | THR | ||||
| 11 | ARG | GLY | ARG | ARG | THR | ALA | SER | VAL | ARG | ALA | ||||
| 12 | ASP | THR | TYR | CYS | ARG | LEU | TYR | SER | LEU | SER | ||||
| 13 | VAL | ASP | ASN | PHE | ASN | GLU | VAL | LEU | GLU | GLU | ||||
| 14 | TYR | PRO | MET | MET | ARG | ARG | ALA | PHE | GLU | THR | ||||
| 15 | VAL | ALA | ILE | ASP | ARG | LEU | ASP | ARG | ILE | GLY | ||||
| 16 | LYS | LYS | ASN | SER | ILE | LEU | LEU | HIS |
Samples:
sample_1: entity, [U-15N], 1 mM; potassium phosphate 20 mM; potassium chloride 150 mM
sample_2: entity, [U-13C; U-15N], 1 mM; potassium phosphate 20 mM; potassium chloride 150 mM
sample_3: entity 1 mM; potassium phosphate 20 mM; potassium chloride 150 mM
sample_conditions_1: temperature: 298 K; pH: 7.0; pressure: 1 atm; ionic strength: 170 mM
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 CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CARA v1.8, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER v12, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
CING, Geerten Vuister, Jurgen F. Doreleijers and Alan Wilter Sousa da Silva - structure validation
PSVS, Bhattacharya and Montelione - structure validation
CANDID, Herrmann, Guntert and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
- Bruker Avance 900 MHz
Related Database Links:
| PDB | |
| DBJ | BAD32628 BAI44633 BAI45607 |
| EMBL | CAA12406 CAB42602 CAB42630 |
| GB | AAC28444 AAC39760 AAC40125 AAF62174 AAI18002 |
| REF | NP_001185 NP_032252 NP_446136 XP_002193445 XP_002689207 |
| SP | O88703 Q9JKA9 Q9UL51 |
| TPG | DAA27526 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts