BMRB Entry 11436
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11436
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Title: NMR Chemical Shift Assignments for E73A mutant of Ostrich egg white Lysozyme PubMed: 21859795
Deposition date: 2011-03-18 Original release date: 2011-09-01
Authors: Shinya, Shoko; Ohnuma, Takayuki; Kawamura, Shunsuke; Nishimura, Shigenori; Fukamizo, Tamo
Citation: Shinya, Shoko; Ohnuma, Takayuki; Kawamura, Shunsuke; Torikata, Takao; Nishimura, Shigenori; Katoh, Etsuko; Fukamizo, Tamo. "Interaction of a goose-type lysozyme with chitin oligosaccharides as determined by NMR spectroscopy" J. Biochem. 150, 569-577 (2011).
Assembly members:
E73A-OEL, polymer, 187 residues, Formula weight is not available
Natural source: Common Name: Ostrich Taxonomy ID: 8801 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Struthio Linnaeus
Experimental source: Production method: recombinant technology Host organism: Pichia pastoris
Entity Sequences (FASTA):
E73A-OEL: SRTGCYGDVNRVDTTGASCK
SAKPEKLNYCGVAASRKIAE
RDLQSMDRYKALIKKVGQKL
CVDPAVIAGIISRASHAGKA
LRNGWGDNGNGFGLMQVDRR
SHKPVGEWNGERHLMQGTEI
LISMIKAIQKKFPRWTKEQQ
LKGGISAYNAGPGNVRSYER
MDIGTTHDDYANDVVARAQY
YKQHGYX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 339 |
| 15N chemical shifts | 174 |
| 1H chemical shifts | 174 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | E73A mutant ofOstrich egg white lysozyme | 1 |
Entities:
Entity 1, E73A mutant ofOstrich egg white lysozyme 187 residues - Formula weight is not available
| 1 | SER | ARG | THR | GLY | CYS | TYR | GLY | ASP | VAL | ASN | ||||
| 2 | ARG | VAL | ASP | THR | THR | GLY | ALA | SER | CYS | LYS | ||||
| 3 | SER | ALA | LYS | PRO | GLU | LYS | LEU | ASN | TYR | CYS | ||||
| 4 | GLY | VAL | ALA | ALA | SER | ARG | LYS | ILE | ALA | GLU | ||||
| 5 | ARG | ASP | LEU | GLN | SER | MET | ASP | ARG | TYR | LYS | ||||
| 6 | ALA | LEU | ILE | LYS | LYS | VAL | GLY | GLN | LYS | LEU | ||||
| 7 | CYS | VAL | ASP | PRO | ALA | VAL | ILE | ALA | GLY | ILE | ||||
| 8 | ILE | SER | ARG | ALA | SER | HIS | ALA | GLY | LYS | ALA | ||||
| 9 | LEU | ARG | ASN | GLY | TRP | GLY | ASP | ASN | GLY | ASN | ||||
| 10 | GLY | PHE | GLY | LEU | MET | GLN | VAL | ASP | ARG | ARG | ||||
| 11 | SER | HIS | LYS | PRO | VAL | GLY | GLU | TRP | ASN | GLY | ||||
| 12 | GLU | ARG | HIS | LEU | MET | GLN | GLY | THR | GLU | ILE | ||||
| 13 | LEU | ILE | SER | MET | ILE | LYS | ALA | ILE | GLN | LYS | ||||
| 14 | LYS | PHE | PRO | ARG | TRP | THR | LYS | GLU | GLN | GLN | ||||
| 15 | LEU | LYS | GLY | GLY | ILE | SER | ALA | TYR | ASN | ALA | ||||
| 16 | GLY | PRO | GLY | ASN | VAL | ARG | SER | TYR | GLU | ARG | ||||
| 17 | MET | ASP | ILE | GLY | THR | THR | HIS | ASP | ASP | TYR | ||||
| 18 | ALA | ASN | ASP | VAL | VAL | ALA | ARG | ALA | GLN | TYR | ||||
| 19 | TYR | LYS | GLN | HIS | GLY | TYR | 205 |
Samples:
sample_1: E73A-OEL, [U-99% 13C; U-99% 15N], 0.4 mM; sodium acetate 50 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 5.0; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts