BMRB Entry 27435
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27435
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Title: NMR assignments of Decorator, a phage-cementing 15 KDa monomer PubMed: 30109462
Deposition date: 2018-03-28 Original release date: 2018-09-19
Authors: Newcomer, Rebecca; Belato, Helen; Teschke, Carolyn; Alexandrescu, Andrei
Citation: Newcomer, Rebecca; Belato, Helen; Teschke, Carolyn; Alexandrescu, Andrei. "NMR assignments for monomeric phage L decoration protein" Biomol. NMR Assignments 12, 339-343 (2018).
Assembly members:
Decorator, polymer, 137 residues, Formula weight is not available
Natural source: Common Name: Enterobacteria phage L Taxonomy ID: 45441 Superkingdom: Viruses Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Decorator: GSHMANPNFTPSWPLYKDAD
GVYVSALPIKAIKYANDGSA
NAEFDGPYADQYMSAQTVAV
FKPEVGGYLFRSQYGELLYM
SKTAFEANYTSASGSVANAE
TADKLSTARTITLTGAVTGS
ASFDGSANVTIETTSGS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 460 |
15N chemical shifts | 141 |
1H chemical shifts | 739 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Decorator monomer | 1 |
Entities:
Entity 1, Decorator monomer 137 residues - Formula weight is not available
The residues 'gsh' are an artifact of thrombin cleavage. The actual sequence of Dec begins with 'M...', with M being residue 1.
1 | GLY | SER | HIS | MET | ALA | ASN | PRO | ASN | PHE | THR | ||||
2 | PRO | SER | TRP | PRO | LEU | TYR | LYS | ASP | ALA | ASP | ||||
3 | GLY | VAL | TYR | VAL | SER | ALA | LEU | PRO | ILE | LYS | ||||
4 | ALA | ILE | LYS | TYR | ALA | ASN | ASP | GLY | SER | ALA | ||||
5 | ASN | ALA | GLU | PHE | ASP | GLY | PRO | TYR | ALA | ASP | ||||
6 | GLN | TYR | MET | SER | ALA | GLN | THR | VAL | ALA | VAL | ||||
7 | PHE | LYS | PRO | GLU | VAL | GLY | GLY | TYR | LEU | PHE | ||||
8 | ARG | SER | GLN | TYR | GLY | GLU | LEU | LEU | TYR | MET | ||||
9 | SER | LYS | THR | ALA | PHE | GLU | ALA | ASN | TYR | THR | ||||
10 | SER | ALA | SER | GLY | SER | VAL | ALA | ASN | ALA | GLU | ||||
11 | THR | ALA | ASP | LYS | LEU | SER | THR | ALA | ARG | THR | ||||
12 | ILE | THR | LEU | THR | GLY | ALA | VAL | THR | GLY | SER | ||||
13 | ALA | SER | PHE | ASP | GLY | SER | ALA | ASN | VAL | THR | ||||
14 | ILE | GLU | THR | THR | SER | GLY | SER |
Samples:
sample_1: sodium acetate 20 mM; sodium chloride 50 mM; EDTA 1 mM; Decorator, [U-100% 13C; U-100% 15N; U-80% 2H], 0.08 mM
sample_2: sodium acetate 40 mM; sodium chloride 100 mM; EDTA 2 mM; Decorator, [U-10% 13C; U-100% 15N], 1 mM
sample_3: sodium acetate 20 mM; sodium chloride 50 mM; EDTA 1 mM; Decorator, [U-100% 15N], 0.15 mM
sample_4: Decorator, [U-100% 13C; U-100% 15N; U-50% 2H], 0.2 mM; sodium acetate 20 mM; sodium chloride 50 mM; EDTA 1 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 4; pressure: 1 atm; temperature: 273 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D CCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_3 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_4 | isotropic | sample_conditions_1 |
Software:
Felix, Accelrys Software Inc. - processing
CcpNMR_Analysis, CCPN - chemical shift assignment, peak picking
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts