BMRB Entry 51391
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51391
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Title: NMR Evidence for the Conformational Change of Phage Protein gVp Upon Binding to ssDNA PubMed: 35746735
Deposition date: 2022-04-07 Original release date: 2022-07-05
Authors: Kedem, Smadar; Hassid, Roni Rene; Shamir, Yoav; Goldbourt, Amir
Citation: Kedem, Smadar; Hassid, Roni Rene; Shamir, Yoav; Goldbourt, Amir. "Conformational Changes in Ff Phage Protein gVp upon Complexation with Its Viral Single-Stranded DNA Revealed Using Magic-Angle Spinning Solid-State NMR" Viruses 14, 1264-1264 (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 | 405 |
| 15N chemical shifts | 92 |
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 from fd bacteriophage, [U-100% 13C; U-100% 15N], 200 ± 50 g/L; NaCl 200 mM; EDTA 1 mM; Tris-HCl 10 mM
sample_2: gVp from fd bacteriophage, [1,3-13C]-glycerol, 200 ± 50 g/L; NaCl 200 mM; EDTA 1 mM; Tris-HCl 10 mM
sample_conditions_1: pH: 7.4; temperature: 263 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D DARR5 | sample_1 | isotropic | sample_conditions_1 |
| 2D DARR15 | sample_1 | isotropic | sample_conditions_1 |
| 2D DARR100 | sample_1 | isotropic | sample_conditions_1 |
| 2D DARR250 | sample_1 | isotropic | sample_conditions_1 |
| 2D RFDR6 | sample_1 | isotropic | sample_conditions_1 |
| 2D INADEQUATE | sample_1 | isotropic | sample_conditions_1 |
| 3D NCOCX25 | sample_1 | isotropic | sample_conditions_1 |
| 3D NCACX25 | sample_1 | isotropic | sample_conditions_1 |
| 2D DARR5 | sample_2 | isotropic | sample_conditions_1 |
| 2D DARR15 | sample_2 | isotropic | sample_conditions_1 |
| 2D DARR100 | sample_2 | isotropic | sample_conditions_1 |
| 2D DARR300 | sample_2 | isotropic | sample_conditions_1 |
| 2D NCA | sample_2 | isotropic | sample_conditions_1 |
| 2D NCO | sample_2 | isotropic | sample_conditions_1 |
| 3D NCOCX100 | sample_2 | isotropic | sample_conditions_1 |
| 3D NCACX100 | sample_2 | isotropic | sample_conditions_1 |
| 2D CORD150 | sample_2 | isotropic | sample_conditions_1 |
| 2D CORD300 | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe vv9.3 - processing
NMR spectrometers:
- Bruker AVANCE III 600 MHz