BMRB Entry 50525
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50525
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Title: transmembrane domain of PD-L1 PubMed: 34429434
Deposition date: 2020-10-21 Original release date: 2021-10-22
Authors: Maorong, Wen; Yunlei, Cao; Bo, Ouyang
Citation: Wen, Maorong; Cao, Yunlei; Wu, Bin; Xiao, Taoran; Cao, Ruiyu; Wang, Qian; Liu, Xiwei; Xue, Hongjuan; Yu, Yang; Lin, Jialing; Xu, Chenqi; Xu, Jie; OuYang, Bo. "PD-L1 degradation is regulated by electrostatic membrane association of its cytoplasmic domain" Nat. Commun. 12, 5106-5106 (2021).
Assembly members:
entity_1, polymer, 59 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
entity_1: AHPPNERTHLVILGAILLAL
GVALTFIFRLRKGRLLDVKK
SGIQDTNSKKQSDTHLEET
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 196 |
15N chemical shifts | 55 |
1H chemical shifts | 374 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PD-L1-TM monomer | 1 |
Entities:
Entity 1, PD-L1-TM monomer 59 residues - Formula weight is not available
1 | ALA | HIS | PRO | PRO | ASN | GLU | ARG | THR | HIS | LEU | ||||
2 | VAL | ILE | LEU | GLY | ALA | ILE | LEU | LEU | ALA | LEU | ||||
3 | GLY | VAL | ALA | LEU | THR | PHE | ILE | PHE | ARG | LEU | ||||
4 | ARG | LYS | GLY | ARG | LEU | LEU | ASP | VAL | LYS | LYS | ||||
5 | SER | GLY | ILE | GLN | ASP | THR | ASN | SER | LYS | LYS | ||||
6 | GLN | SER | ASP | THR | HIS | LEU | GLU | GLU | THR |
Samples:
sample_1: entity_1, [U-13C; U-15N], 0.5 mM; MES 25 mM; DMPC 30 mM; DHPC 60 mM
sample_2: entity_1, [U-13C; U-15N], 0.5 mM; MES 25 mM; DMPC, [U-2H], 30 mM; DHPC, [U-2H], 60 mM
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 310 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | 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 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4.0.2 - collection
NMRPipe v8.9 - processing
XEASY - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts