BMRB Entry 36293
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36293
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: membrane-bound PD-L1-CD PubMed: 34429434
Deposition date: 2019-11-07 Original release date: 2021-08-02
Authors: Maorong, W.; Bin, W.; Bo, O.
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:
Programmed cell death 1 ligand 1, polymer, 33 residues, 3797.370 Da.
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
Entity Sequences (FASTA):
Programmed cell death 1 ligand 1: GPRLRKGRMMDVKKCGIQDT
NSKKQSDTHLEET
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 134 |
| 15N chemical shifts | 37 |
| 1H chemical shifts | 223 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 33 residues - 3797.370 Da.
| 1 | GLY | PRO | ARG | LEU | ARG | LYS | GLY | ARG | MET | MET | ||||
| 2 | ASP | VAL | LYS | LYS | CYS | GLY | ILE | GLN | ASP | THR | ||||
| 3 | ASN | SER | LYS | LYS | GLN | SER | ASP | THR | HIS | LEU | ||||
| 4 | GLU | GLU | THR |
Samples:
sample_1: PD-L1-CD, [U-13C; U-15N; U-2H], 0.5 mM; DHPC 85 mM; DMPG 60 mM; H2O 90%; D2O, [U-2H], 10%
sample_2: PD-L1-CD, [U-13C; U-15N], 0.5 mM; DHPC, [U-2H], 85 mM; DMPG, [U-2H], 60 mM; H2O 90%; D2O, [U-2H], 10%
sample_3: PD-L1-CD, [U-15N; U-2H], 0.5 mM; DHPC, [U-2H], 85 mM; POPG 60 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 20 mM; pH: 6.0; 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY for lipid NOE | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
Sparky, Goddard - chemical shift assignment, peak picking
TopSpin v3.5.5, Bruker Biospin - collection
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker AVANCE 600 MHz
- Varian DD2 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts