BMRB Entry 16057
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16057
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Lhuillier, Sophie; Gallopin, Matthieu; Gilquin, Bernard; Brasiles, Sandrine; Lancelot, Nathalie; Letellier, Guillaume; Gilles, Mathilde; Dethan, Guillaume; Orlova, Elena; Couprie, Joel; Tavares, Paulo; Zinn-Justin, Sophie. "Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism for viral DNA gating" Proc. Natl. Acad. Sci. U.S.A. 106, 8507-8512 (2009).
PubMed: 19433794
Assembly members:
gp15, polymer, 99 residues, 11270.051 Da.
Natural source: Common Name: Bacteriophage SPP1 Taxonomy ID: 10724 Superkingdom: Viruses Kingdom: not available Genus/species: Bacteriophage SPP1
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pLysS
Entity Sequences (FASTA):
gp15: QRVKRLLSITNDKHDEYLTE
MVPLLVEFAKDECHNPFIDK
DGNESIPSGVLIFVAKAAQF
YMTNAGLTGRSMDTVSYNFA
TEIPSTILKKLNPYRKMAR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 382 |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 666 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 99 residues - 11270.051 Da.
| 1 | GLN | ARG | VAL | LYS | ARG | LEU | LEU | SER | ILE | THR | ||||
| 2 | ASN | ASP | LYS | HIS | ASP | GLU | TYR | LEU | THR | GLU | ||||
| 3 | MET | VAL | PRO | LEU | LEU | VAL | GLU | PHE | ALA | LYS | ||||
| 4 | ASP | GLU | CYS | HIS | ASN | PRO | PHE | ILE | ASP | LYS | ||||
| 5 | ASP | GLY | ASN | GLU | SER | ILE | PRO | SER | GLY | VAL | ||||
| 6 | LEU | ILE | PHE | VAL | ALA | LYS | ALA | ALA | GLN | PHE | ||||
| 7 | TYR | MET | THR | ASN | ALA | GLY | LEU | THR | GLY | ARG | ||||
| 8 | SER | MET | ASP | THR | VAL | SER | TYR | ASN | PHE | ALA | ||||
| 9 | THR | GLU | ILE | PRO | SER | THR | ILE | LEU | LYS | LYS | ||||
| 10 | LEU | ASN | PRO | TYR | ARG | LYS | MET | ALA | ARG |
Samples:
sample_1: gp15, [U-100% 15N], 0.5 mM
sample_2: gp15, [U-100% 13C; U-100% 15N], 0.5 mM
sample_conditions_1: ionic strength: 0.3 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D H-D exchange | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N nOe transfer | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.113, Goddard - data analysis, peak picking
NMR spectrometers:
- Bruker Avance 2 600 MHz
- Bruker Avance 2 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks