BMRB Entry 19425
Click here to enlarge.
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/BMR19425
MolProbity Validation Chart
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: X-ray crystallography-solution NMR hybrid structure of mouse RyR2 domain A. PubMed: 23978697
Deposition date: 2013-08-13 Original release date: 2013-09-10
Authors: Amador, Fernando; Stathopulos, Peter; Seabrook, Genevieve; Ikura, Mitsuhiko
Citation: Amador, Fernando; Kimlicka, Lynn; Stathopulos, Peter; Gasmi-Seabrook, Genevieve; Maclennan, David; Van Petegem, Filip; Ikura, Mitsuhiko. "Type 2 Ryanodine Receptor Domain A Contains a Unique and Dynamic -Helix That Transitions to a -Strand in a Mutant Linked with a Heritable Cardiomyopathy." J. Mol. Biol. 425, 4034-4046 (2013).
Assembly members:
entity, polymer, 219 residues, 23049.213 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GSGSEIQFLRTDDEVVLQCT
ATIHKEQQKLCLAAEGFGNR
LCFLESTSNSKNVPPDLSIC
TFVLEQSLSVRALQEMLANT
VEKSEGQVDVEKWKFMMKTA
QGGGHRTLLYGHAILLRHSY
SGMYLCCLSTSRSSTDKLAF
DVGLQEDTTGEACWWTIHPA
SKQRSEGEKVRVGDDLILVS
VSSERYLHLSYGNSSWHVDA
AFQQTLWSVAPISSGSEAA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 541 |
| 15N chemical shifts | 185 |
| 1H chemical shifts | 185 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | mouse RyR2 domain A | 1 |
Entities:
Entity 1, mouse RyR2 domain A 219 residues - 23049.213 Da.
Residues 1-4 are a cloning artifact; residues 5-219 correspond to 10-224 of mouse RyR2 (E9Q401).
| 1 | GLY | SER | GLY | SER | GLU | ILE | GLN | PHE | LEU | ARG | ||||
| 2 | THR | ASP | ASP | GLU | VAL | VAL | LEU | GLN | CYS | THR | ||||
| 3 | ALA | THR | ILE | HIS | LYS | GLU | GLN | GLN | LYS | LEU | ||||
| 4 | CYS | LEU | ALA | ALA | GLU | GLY | PHE | GLY | ASN | ARG | ||||
| 5 | LEU | CYS | PHE | LEU | GLU | SER | THR | SER | ASN | SER | ||||
| 6 | LYS | ASN | VAL | PRO | PRO | ASP | LEU | SER | ILE | CYS | ||||
| 7 | THR | PHE | VAL | LEU | GLU | GLN | SER | LEU | SER | VAL | ||||
| 8 | ARG | ALA | LEU | GLN | GLU | MET | LEU | ALA | ASN | THR | ||||
| 9 | VAL | GLU | LYS | SER | GLU | GLY | GLN | VAL | ASP | VAL | ||||
| 10 | GLU | LYS | TRP | LYS | PHE | MET | MET | LYS | THR | ALA | ||||
| 11 | GLN | GLY | GLY | GLY | HIS | ARG | THR | LEU | LEU | TYR | ||||
| 12 | GLY | HIS | ALA | ILE | LEU | LEU | ARG | HIS | SER | TYR | ||||
| 13 | SER | GLY | MET | TYR | LEU | CYS | CYS | LEU | SER | THR | ||||
| 14 | SER | ARG | SER | SER | THR | ASP | LYS | LEU | ALA | PHE | ||||
| 15 | ASP | VAL | GLY | LEU | GLN | GLU | ASP | THR | THR | GLY | ||||
| 16 | GLU | ALA | CYS | TRP | TRP | THR | ILE | HIS | PRO | ALA | ||||
| 17 | SER | LYS | GLN | ARG | SER | GLU | GLY | GLU | LYS | VAL | ||||
| 18 | ARG | VAL | GLY | ASP | ASP | LEU | ILE | LEU | VAL | SER | ||||
| 19 | VAL | SER | SER | GLU | ARG | TYR | LEU | HIS | LEU | SER | ||||
| 20 | TYR | GLY | ASN | SER | SER | TRP | HIS | VAL | ASP | ALA | ||||
| 21 | ALA | PHE | GLN | GLN | THR | LEU | TRP | SER | VAL | ALA | ||||
| 22 | PRO | ILE | SER | SER | GLY | SER | GLU | ALA | ALA |
Samples:
sample_1: entity, [U-13C; U-15N; U-2H], 0.4 mM; sodium phosphate 20 mM; sodium chloride 300 mM; TCEP 2 mM; DTT 5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.328 M; pH: 7; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - chemical shift assignment, peak picking
TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation, data analysis, geometry optimization
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| UNP | E9Q401 |
| PDB | |
| EMBL | CAA66975 CAC18855 |
| GB | AAA31179 AAA93465 AAG34081 AAI67757 AAI72794 |
| PRF | 1617118A |
| REF | NP_001026 NP_001076226 NP_076357 XP_002808310 XP_002923703 |
| SP | E9Q401 P30957 Q92736 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts