BMRB Entry 27532
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27532
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title: Backbone and side chain NMR assignments for the ribosome Binding Factor A (RbfA) from Staphylococcus aureus PubMed: 30225569
Deposition date: 2018-07-03 Original release date: 2018-10-03
Authors: Usachev, Konstantin; Blokhin, Dmitriy; Bikmullin, Aydar; Nurullina, Liliya; Validov, Shamil; Garaeva, Natalia; Klochkov, Vladimir; Aganov, Albert; Khusainov, Iskander; Yusupov, Marat
Citation: Blokhin, Dmitriy; Bikmullin, Aydar; Nurullina, Liliya; Garaeva, Natalia; Validov, Shamil; Klochkov, Vladimir; Aganov, Albert; Khusainov, Iskander; Yusupov, Marat; Usachev, Konstantin. "Backbone and side chain NMR assignments for the ribosome binding factor A (RbfA) from Staphylococcus aureus" Biomol. NMR Assignments 13, 27-30 (2019).
Assembly members:
RbfA, polymer, 118 residues, 13669.7691 Da.
Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
RbfA: GSSMRAERVGEQMKKELMDI
INNKVKDPRVGFITITDVVL
TNDLSQAKVFLTVLGNDKEV
ENTFKALDKAKGFIKSELGS
RMRLRIMPELMYEYDQSIEY
GNKIERMIQDLHKQDRVE
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 339 |
| 15N chemical shifts | 102 |
| 1H chemical shifts | 390 |
| coupling constants | 72 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RbfA | 1 |
Entities:
Entity 1, RbfA 118 residues - 13669.7691 Da.
| 1 | GLY | SER | SER | MET | ARG | ALA | GLU | ARG | VAL | GLY | ||||
| 2 | GLU | GLN | MET | LYS | LYS | GLU | LEU | MET | ASP | ILE | ||||
| 3 | ILE | ASN | ASN | LYS | VAL | LYS | ASP | PRO | ARG | VAL | ||||
| 4 | GLY | PHE | ILE | THR | ILE | THR | ASP | VAL | VAL | LEU | ||||
| 5 | THR | ASN | ASP | LEU | SER | GLN | ALA | LYS | VAL | PHE | ||||
| 6 | LEU | THR | VAL | LEU | GLY | ASN | ASP | LYS | GLU | VAL | ||||
| 7 | GLU | ASN | THR | PHE | LYS | ALA | LEU | ASP | LYS | ALA | ||||
| 8 | LYS | GLY | PHE | ILE | LYS | SER | GLU | LEU | GLY | SER | ||||
| 9 | ARG | MET | ARG | LEU | ARG | ILE | MET | PRO | GLU | LEU | ||||
| 10 | MET | TYR | GLU | TYR | ASP | GLN | SER | ILE | GLU | TYR | ||||
| 11 | GLY | ASN | LYS | ILE | GLU | ARG | MET | ILE | GLN | ASP | ||||
| 12 | LEU | HIS | LYS | GLN | ASP | ARG | VAL | GLU |
Samples:
sample_1: RbfA, [U-100% 13C; U-100% 15N], 0.9 mM; phosphate buffer 50 mM; NH4Cl 250 mM
CondSet1: ionic strength: 0.250 M; pH: 7.600; pressure: 1.000 atm; temperature: 308.000 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC/HMQC | sample_1 | isotropic | CondSet1 |
| 2D 1H-13C HSQC/HMQC | sample_1 | isotropic | CondSet1 |
| 2D 1H-13C HSQC/HMQC | sample_1 | isotropic | CondSet1 |
| 3D HNCA | sample_1 | isotropic | CondSet1 |
| 3D HNCACB | sample_1 | isotropic | CondSet1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | CondSet1 |
| 3D HNCO | sample_1 | isotropic | CondSet1 |
| HN(CA)CO (H[N[ca[CO]]]) | sample_1 | isotropic | CondSet1 |
| CC(CO)NH (HNco_C.relayed) | sample_1 | isotropic | CondSet1 |
| 3D H(CCO)NH | sample_1 | isotropic | CondSet1 |
| 3D HNHA | sample_1 | isotropic | CondSet1 |
Software:
CcpNmr_Analysis v2.4, CCPN - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts