BMRB Entry 50389
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50389
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Title: Backbone Assignments of the Rec3 domain of CRISPR-Cas9 for S. pyogenes PubMed: 32935194
Deposition date: 2020-07-13 Original release date: 2020-09-17
Authors: Skeens, Erin; East, Kyle; Lisi, George
Citation: Skeens, Erin; East, Kyle; Lisi, George. "1H, 13C, 15N backbone resonance assignment of the recognition lobe subdomain 3 (Rec3) from Streptococcus pyogenes CRISPR-Cas9" Biomol. NMR Assignments 15, 25-28 (2021).
Assembly members:
entity_1, polymer, 218 residues, Formula weight is not available
Natural source: Common Name: Streptococcus pyogenes Taxonomy ID: 1314 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus pyogenes
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
entity_1: SNFDKNLPNEKVLPKHSLLY
EYFTVYNELTKVKYVTEGMR
KPAFLSGEQKKAIVDLLFKT
NRKVTVKQLKEDYFKKIECF
DSVEISGVEDRFNASLGTYH
DLLKIIKDKDFLDNEENEDI
LEDIVLTLTLFEDREMIEER
LKTYAHLFDDKVMKQLKRRR
YTGWGRLSRKLINGIRDKQS
GKTILDFLKSDGFANRNFMQ
LIHDDSLTFKEDIQKAQV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 583 |
| 15N chemical shifts | 200 |
| 1H chemical shifts | 200 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | spyRec3 | 1 |
Entities:
Entity 1, spyRec3 218 residues - Formula weight is not available
| 1 | SER | ASN | PHE | ASP | LYS | ASN | LEU | PRO | ASN | GLU | ||||
| 2 | LYS | VAL | LEU | PRO | LYS | HIS | SER | LEU | LEU | TYR | ||||
| 3 | GLU | TYR | PHE | THR | VAL | TYR | ASN | GLU | LEU | THR | ||||
| 4 | LYS | VAL | LYS | TYR | VAL | THR | GLU | GLY | MET | ARG | ||||
| 5 | LYS | PRO | ALA | PHE | LEU | SER | GLY | GLU | GLN | LYS | ||||
| 6 | LYS | ALA | ILE | VAL | ASP | LEU | LEU | PHE | LYS | THR | ||||
| 7 | ASN | ARG | LYS | VAL | THR | VAL | LYS | GLN | LEU | LYS | ||||
| 8 | GLU | ASP | TYR | PHE | LYS | LYS | ILE | GLU | CYS | PHE | ||||
| 9 | ASP | SER | VAL | GLU | ILE | SER | GLY | VAL | GLU | ASP | ||||
| 10 | ARG | PHE | ASN | ALA | SER | LEU | GLY | THR | TYR | HIS | ||||
| 11 | ASP | LEU | LEU | LYS | ILE | ILE | LYS | ASP | LYS | ASP | ||||
| 12 | PHE | LEU | ASP | ASN | GLU | GLU | ASN | GLU | ASP | ILE | ||||
| 13 | LEU | GLU | ASP | ILE | VAL | LEU | THR | LEU | THR | LEU | ||||
| 14 | PHE | GLU | ASP | ARG | GLU | MET | ILE | GLU | GLU | ARG | ||||
| 15 | LEU | LYS | THR | TYR | ALA | HIS | LEU | PHE | ASP | ASP | ||||
| 16 | LYS | VAL | MET | LYS | GLN | LEU | LYS | ARG | ARG | ARG | ||||
| 17 | TYR | THR | GLY | TRP | GLY | ARG | LEU | SER | ARG | LYS | ||||
| 18 | LEU | ILE | ASN | GLY | ILE | ARG | ASP | LYS | GLN | SER | ||||
| 19 | GLY | LYS | THR | ILE | LEU | ASP | PHE | LEU | LYS | SER | ||||
| 20 | ASP | GLY | PHE | ALA | ASN | ARG | ASN | PHE | MET | GLN | ||||
| 21 | LEU | ILE | HIS | ASP | ASP | SER | LEU | THR | PHE | LYS | ||||
| 22 | GLU | ASP | ILE | GLN | LYS | ALA | GLN | VAL |
Samples:
sample_1: spyRec3, [U-13C; U-15N; U-2H], 1.2 mM; potassium chloride 80 mM; HEPES 20 mM
sample_conditions_1: ionic strength: 80 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA - chemical shift assignment
NMRPipe - processing
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts