BMRB Entry 51284
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51284
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Title: Solid state NMR chemical shift assignment of the non-structural single-stranded DNA binding protein gVp from fd bacteriophage PubMed: 35460051
Deposition date: 2022-01-19 Original release date: 2022-04-04
Authors: Hassid, Roni Rene; Kedem, Smadar; Bachar-Beck, Meital; Shamir, Yoav; Goldbourt, Amir
Citation: Hassid, Roni Rene; Kedem, Smadar; Bachar-Beck, Meital; Shamir, Yoav; Goldbourt, Amir. "Solid state NMR chemical shift assignment of the non-structural single-stranded DNA binding protein gVp from fd bacteriophage" Biomol. NMR Assignments 16, 181-185 (2022).
Assembly members:
entity_1, polymer, 87 residues, Formula weight is not available
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: pET-30b
Entity Sequences (FASTA):
entity_1: MIKVEIKPSQAQFTTRSGVS
RQGKPYSLNEQLCYVDLGNE
YPVLVKITLDEGQPAYAPGL
YTVHLSSFKVGQFGSLMIDR
LRLVPAK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 350 |
| 15N chemical shifts | 93 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | gVp | 1 |
Entities:
Entity 1, gVp 87 residues - Formula weight is not available
| 1 | MET | ILE | LYS | VAL | GLU | ILE | LYS | PRO | SER | GLN | ||||
| 2 | ALA | GLN | PHE | THR | THR | ARG | SER | GLY | VAL | SER | ||||
| 3 | ARG | GLN | GLY | LYS | PRO | TYR | SER | LEU | ASN | GLU | ||||
| 4 | GLN | LEU | CYS | TYR | VAL | ASP | LEU | GLY | ASN | GLU | ||||
| 5 | TYR | PRO | VAL | LEU | VAL | LYS | ILE | THR | LEU | ASP | ||||
| 6 | GLU | GLY | GLN | PRO | ALA | TYR | ALA | PRO | GLY | LEU | ||||
| 7 | TYR | THR | VAL | HIS | LEU | SER | SER | PHE | LYS | VAL | ||||
| 8 | GLY | GLN | PHE | GLY | SER | LEU | MET | ILE | ASP | ARG | ||||
| 9 | LEU | ARG | LEU | VAL | PRO | ALA | LYS |
Samples:
sample_1: gVp, [U-100% 13C; U-100% 15N], 200 ± 50 g/L; NaCl 200 mM; EDTA 1 mM; Tris-HCl 10 mM
sample_conditions_1: temperature controller setting: 263 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D DARR5 | sample_1 | isotropic | sample_conditions_1 |
| 2D DARR25 | sample_1 | isotropic | sample_conditions_1 |
| 2D DARR100 | sample_1 | isotropic | sample_conditions_1 |
| 3D NCACX | sample_1 | isotropic | sample_conditions_1 |
| 3D NCOCX | sample_1 | isotropic | sample_conditions_1 |
| 2D NCA | sample_1 | isotropic | sample_conditions_1 |
| 2D NCO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe vv9.3 - processing
NMR spectrometers:
- Bruker AVANCE III 600 MHz