BMRB Entry 50595
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50595
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Title: Backbone and aliphatic side chain of Gamma mini-lid R133A PubMed: 33761093
Deposition date: 2020-11-26 Original release date: 2021-06-30
Authors: Mahdi, Sam; Bezsonova, Irina; Beuning, Penny; Korzhnev, Dmitry
Citation: Mahdi, Sam; Bezsonova, Irina; Beuning, Penny; Korzhnev, Dmitry. "NMR resonance assignments for the nucleotide binding domains of the E. coli clamp loader complex Gamma subunit" Biomol. NMR Assign. 15, 281-285 (2021).
Assembly members:
entity_1, polymer, 243 residues, 26764.61 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETDuet
Entity Sequences (FASTA):
entity_1: SMSYQVLARKWRPQTFADVV
GQEHVLTALANGLSLGRIHH
AYLFSGTRGVGKTSIARLLA
KGLNCETGITATPCGVCDNC
REIEQGRFVDLIEIDAASRT
KVEDTRDLLDNVQYAPARGR
FKVYLIDEVHMLSAHSFNAL
LKTLEEPPEHVKFLLATTDP
QKLPVTILSRCLQFHLKALD
VEQIRHQLEHILNEEHIAHE
PRALQLLARAAEGSLRDALS
LTDQAIASGDGQVSTQAVSA
MLG
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 870 |
| 15N chemical shifts | 214 |
| 1H chemical shifts | 1156 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Gamma Mini-Lid R133A | 1 |
Entities:
Entity 1, Gamma Mini-Lid R133A 243 residues - 26764.61 Da.
Sequence is mutated form of Wild Type (R133A)
| 1 | SER | MET | SER | TYR | GLN | VAL | LEU | ALA | ARG | LYS | ||||
| 2 | TRP | ARG | PRO | GLN | THR | PHE | ALA | ASP | VAL | VAL | ||||
| 3 | GLY | GLN | GLU | HIS | VAL | LEU | THR | ALA | LEU | ALA | ||||
| 4 | ASN | GLY | LEU | SER | LEU | GLY | ARG | ILE | HIS | HIS | ||||
| 5 | ALA | TYR | LEU | PHE | SER | GLY | THR | ARG | GLY | VAL | ||||
| 6 | GLY | LYS | THR | SER | ILE | ALA | ARG | LEU | LEU | ALA | ||||
| 7 | LYS | GLY | LEU | ASN | CYS | GLU | THR | GLY | ILE | THR | ||||
| 8 | ALA | THR | PRO | CYS | GLY | VAL | CYS | ASP | ASN | CYS | ||||
| 9 | ARG | GLU | ILE | GLU | GLN | GLY | ARG | PHE | VAL | ASP | ||||
| 10 | LEU | ILE | GLU | ILE | ASP | ALA | ALA | SER | ARG | THR | ||||
| 11 | LYS | VAL | GLU | ASP | THR | ARG | ASP | LEU | LEU | ASP | ||||
| 12 | ASN | VAL | GLN | TYR | ALA | PRO | ALA | ARG | GLY | ARG | ||||
| 13 | PHE | LYS | VAL | TYR | LEU | ILE | ASP | GLU | VAL | HIS | ||||
| 14 | MET | LEU | SER | ALA | HIS | SER | PHE | ASN | ALA | LEU | ||||
| 15 | LEU | LYS | THR | LEU | GLU | GLU | PRO | PRO | GLU | HIS | ||||
| 16 | VAL | LYS | PHE | LEU | LEU | ALA | THR | THR | ASP | PRO | ||||
| 17 | GLN | LYS | LEU | PRO | VAL | THR | ILE | LEU | SER | ARG | ||||
| 18 | CYS | LEU | GLN | PHE | HIS | LEU | LYS | ALA | LEU | ASP | ||||
| 19 | VAL | GLU | GLN | ILE | ARG | HIS | GLN | LEU | GLU | HIS | ||||
| 20 | ILE | LEU | ASN | GLU | GLU | HIS | ILE | ALA | HIS | GLU | ||||
| 21 | PRO | ARG | ALA | LEU | GLN | LEU | LEU | ALA | ARG | ALA | ||||
| 22 | ALA | GLU | GLY | SER | LEU | ARG | ASP | ALA | LEU | SER | ||||
| 23 | LEU | THR | ASP | GLN | ALA | ILE | ALA | SER | GLY | ASP | ||||
| 24 | GLY | GLN | VAL | SER | THR | GLN | ALA | VAL | SER | ALA | ||||
| 25 | MET | LEU | GLY |
Samples:
sample_1: Gamma Mini-Lid R133A, [U-100% 13C; U-100% 15N], 0.6 mM; PO4 50 mM; NaCl 100 mM; DTT 10 mM; NaN3 2 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe - processing
NMRFAM-SPARKY - chemical shift assignment, data analysis
TALOS-N - data analysis
NMR spectrometers:
- Varian VNMRS 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts