BMRB Entry 16874
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16874
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Title: The solution structure of rat Lipocalin-type Prostaglandin D Synthase PubMed: 18590794
Deposition date: 2010-04-16 Original release date: 2010-05-17
Authors: Liu, Jiafu; Lin, Donghai
Citation: Liu, Jiafu; Guo, Chenyun; Yao, Yihe; Lin, Donghai. "The solution structure and dynamics of rat Lipocalin-Type Prostaglandin D Synthase" Biochimie 90, 1637-1646 (2008).
Assembly members:
rL-PGDS, polymer, 165 residues, Formula weight is not available
Natural source: Common Name: Norway rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
rL-PGDS: QGHDTVQPNFQQDKFLGRWY
SAGLASNSSWFREKKELLFM
CQTVVAPSTEGGLNLTSTFL
RKNQCETKVMVLQPAGVPGQ
YTYNSPHWGSFHSLSVVETD
YDEYAFLFSKGTKGPGQDFR
MATLYSRAQLLKEELKEKFI
TFSKDQGLTEEDIVFLPQPD
KCIQE
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 599 |
15N chemical shifts | 153 |
1H chemical shifts | 865 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | rat Lipocalin-Type Prostaglandin D Synthase | 1 |
Entities:
Entity 1, rat Lipocalin-Type Prostaglandin D Synthase 165 residues - Formula weight is not available
1 | GLN | GLY | HIS | ASP | THR | VAL | GLN | PRO | ASN | PHE | ||||
2 | GLN | GLN | ASP | LYS | PHE | LEU | GLY | ARG | TRP | TYR | ||||
3 | SER | ALA | GLY | LEU | ALA | SER | ASN | SER | SER | TRP | ||||
4 | PHE | ARG | GLU | LYS | LYS | GLU | LEU | LEU | PHE | MET | ||||
5 | CYS | GLN | THR | VAL | VAL | ALA | PRO | SER | THR | GLU | ||||
6 | GLY | GLY | LEU | ASN | LEU | THR | SER | THR | PHE | LEU | ||||
7 | ARG | LYS | ASN | GLN | CYS | GLU | THR | LYS | VAL | MET | ||||
8 | VAL | LEU | GLN | PRO | ALA | GLY | VAL | PRO | GLY | GLN | ||||
9 | TYR | THR | TYR | ASN | SER | PRO | HIS | TRP | GLY | SER | ||||
10 | PHE | HIS | SER | LEU | SER | VAL | VAL | GLU | THR | ASP | ||||
11 | TYR | ASP | GLU | TYR | ALA | PHE | LEU | PHE | SER | LYS | ||||
12 | GLY | THR | LYS | GLY | PRO | GLY | GLN | ASP | PHE | ARG | ||||
13 | MET | ALA | THR | LEU | TYR | SER | ARG | ALA | GLN | LEU | ||||
14 | LEU | LYS | GLU | GLU | LEU | LYS | GLU | LYS | PHE | ILE | ||||
15 | THR | PHE | SER | LYS | ASP | GLN | GLY | LEU | THR | GLU | ||||
16 | GLU | ASP | ILE | VAL | PHE | LEU | PRO | GLN | PRO | ASP | ||||
17 | LYS | CYS | ILE | GLN | GLU |
Samples:
sample_1: rL-PGDS, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%; sodium phosphate 15 mM; NaCl 150 mM
sample_conditions_1: ionic strength: 0.200 M; pH: 6.5; 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 C(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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- 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