BMRB Entry 16664
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16664
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Di Paolo, Alexandre; Duval, Valerie; Matagne, Andre; Redfield, Christina. "Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda." Biomol. NMR Assignments 4, 111-114 (2010).
PubMed: 20300891
Assembly members:
lambda_lysozyme, polymer, 158 residues, Formula weight is not available
Natural source: Common Name: Bacteriophage lambda Taxonomy ID: 10710 Superkingdom: Viruses Kingdom: not available Genus/species: Lambda-like viruses Enterobacteria phage lambda
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b
Entity Sequences (FASTA):
lambda_lysozyme: MVEINNQRKAFLDMLAWSEG
TDNGRQKTRNHGYDVIVGGE
LFTDYSDHPRKLVTLNPKLK
STGAGRYQLLSRWWDAYRKQ
LGLKDFSPKSQDAVALQQIK
ERGALPMIDRGDIRQAIDRC
SNIWASLPGAGYGQFEHKAD
SLIAKFKEAGGTVREIDV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 302 |
| 15N chemical shifts | 151 |
| 1H chemical shifts | 315 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | lambda lysozyme | 1 |
Entities:
Entity 1, lambda lysozyme 158 residues - Formula weight is not available
| 1 | MET | VAL | GLU | ILE | ASN | ASN | GLN | ARG | LYS | ALA | ||||
| 2 | PHE | LEU | ASP | MET | LEU | ALA | TRP | SER | GLU | GLY | ||||
| 3 | THR | ASP | ASN | GLY | ARG | GLN | LYS | THR | ARG | ASN | ||||
| 4 | HIS | GLY | TYR | ASP | VAL | ILE | VAL | GLY | GLY | GLU | ||||
| 5 | LEU | PHE | THR | ASP | TYR | SER | ASP | HIS | PRO | ARG | ||||
| 6 | LYS | LEU | VAL | THR | LEU | ASN | PRO | LYS | LEU | LYS | ||||
| 7 | SER | THR | GLY | ALA | GLY | ARG | TYR | GLN | LEU | LEU | ||||
| 8 | SER | ARG | TRP | TRP | ASP | ALA | TYR | ARG | LYS | GLN | ||||
| 9 | LEU | GLY | LEU | LYS | ASP | PHE | SER | PRO | LYS | SER | ||||
| 10 | GLN | ASP | ALA | VAL | ALA | LEU | GLN | GLN | ILE | LYS | ||||
| 11 | GLU | ARG | GLY | ALA | LEU | PRO | MET | ILE | ASP | ARG | ||||
| 12 | GLY | ASP | ILE | ARG | GLN | ALA | ILE | ASP | ARG | CYS | ||||
| 13 | SER | ASN | ILE | TRP | ALA | SER | LEU | PRO | GLY | ALA | ||||
| 14 | GLY | TYR | GLY | GLN | PHE | GLU | HIS | LYS | ALA | ASP | ||||
| 15 | SER | LEU | ILE | ALA | LYS | PHE | LYS | GLU | ALA | GLY | ||||
| 16 | GLY | THR | VAL | ARG | GLU | ILE | ASP | VAL |
Samples:
sample_1: lambda lysozyme, [U-98% 15N], 1 mM
sample_2: lambda lysozyme, [U-98% 13C; U-98% 15N], 1 mM
sample_conditions_1: ionic strength: 0 M; pH: 5.45; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D (H)C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
FELIX v2.3, Accelrys Software Inc. - processing
NMR spectrometers:
- home-built home-built 750 MHz
- home-built home-built 600 MHz
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks