BMRB Entry 17768
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17768
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Title: Structure of bacteriophage SPP1 gp17 protein PubMed: 22072538
Deposition date: 2011-07-07 Original release date: 2012-05-09
Authors: Chagot, Benjamin; Auzat, Isabelle; Gallopin, Matthieu; Petitpas, Isabelle; Gilquin, Bernard; Tavares, Paulo; Zinn-Justin, Sophie
Citation: Chagot, Benjamin; Auzat, Isabelle; Gallopin, Matthieu; Petitpas, Isabelle; Gilquin, Bernard; Tavares, Paulo; Zinn-Justin, Sophie. "Solution structure of gp17 from the Siphoviridae bacteriophage SPP1: insights into its role in virion assembly." Proteins 80, 319-326 (2012).
Assembly members:
gp17, polymer, 139 residues, 15478.582 Da.
Natural source: Common Name: Bacteriophage SPP1 Taxonomy ID: 10724 Superkingdom: Viruses Kingdom: not available Genus/species: Lambda-like viruses Bacteriophage SPP1
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
gp17: QGLQTWKLASRALQKATVEN
LESYQPLMEMVNQVTESPGK
DDPYPYVVIGDQSSTPFETK
SSFGENITMDFHVWGGTTRA
EAQDISSRVLEALTYKPLMF
EGFTFVAKKLVLAQVITDTD
GVTKHGIIKVRFTINNNTG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 282 |
| 15N chemical shifts | 102 |
| 1H chemical shifts | 708 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | gp17 | 1 |
Entities:
Entity 1, gp17 139 residues - 15478.582 Da.
First four residues (QGLQ) and the two last (TG) are cloning artefacts
| 1 | GLN | GLY | LEU | GLN | THR | TRP | LYS | LEU | ALA | SER | ||||
| 2 | ARG | ALA | LEU | GLN | LYS | ALA | THR | VAL | GLU | ASN | ||||
| 3 | LEU | GLU | SER | TYR | GLN | PRO | LEU | MET | GLU | MET | ||||
| 4 | VAL | ASN | GLN | VAL | THR | GLU | SER | PRO | GLY | LYS | ||||
| 5 | ASP | ASP | PRO | TYR | PRO | TYR | VAL | VAL | ILE | GLY | ||||
| 6 | ASP | GLN | SER | SER | THR | PRO | PHE | GLU | THR | LYS | ||||
| 7 | SER | SER | PHE | GLY | GLU | ASN | ILE | THR | MET | ASP | ||||
| 8 | PHE | HIS | VAL | TRP | GLY | GLY | THR | THR | ARG | ALA | ||||
| 9 | GLU | ALA | GLN | ASP | ILE | SER | SER | ARG | VAL | LEU | ||||
| 10 | GLU | ALA | LEU | THR | TYR | LYS | PRO | LEU | MET | PHE | ||||
| 11 | GLU | GLY | PHE | THR | PHE | VAL | ALA | LYS | LYS | LEU | ||||
| 12 | VAL | LEU | ALA | GLN | VAL | ILE | THR | ASP | THR | ASP | ||||
| 13 | GLY | VAL | THR | LYS | HIS | GLY | ILE | ILE | LYS | VAL | ||||
| 14 | ARG | PHE | THR | ILE | ASN | ASN | ASN | THR | GLY |
Samples:
sample_1: gp17, [U-100% 13C; U-100% 15N], 0.3 mM; H2O 90%; D2O 10%; TRIS 50 mM; sodium chloride 50 mM
sample_2: gp17 0.3 mM; H2O 90%; D2O 10%; MES 50 mM; sodium chloride 500 mM
sample_3: gp17, [U-100% 13C; U-100% 15N], 0.6 mM; H2O 90%; D2O 10%; MES 50 mM; sodium chloride 500 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 0.5 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H COSY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_2 |
| T1 relaxation | sample_3 | isotropic | sample_conditions_2 |
| T2 relaxation | sample_3 | isotropic | sample_conditions_2 |
| heteronuclear NOE | sample_3 | isotropic | sample_conditions_2 |
Software:
TOPSPIN v1.3, Bruker Biospin - collection, processing
SPARKY v1.3, Goddard - chemical shift assignment
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker AMX 700 MHz
- Bruker AMX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts