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
Deposition date:
2020-10-21
Original release date:
2021-10-22
Authors:
Maorong, Wen; Yunlei, Cao; Bo, Ouyang
Citation:

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).
PubMed: 34429434

Assembly members:

Assembly members:
entity_1, polymer, 59 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AHPPNERTHLVILGAILLAL GVALTFIFRLRKGRLLDVKK SGIQDTNSKKQSDTHLEET

Data sets:
Data typeCount
13C chemical shifts196
15N chemical shifts55
1H chemical shifts374

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PD-L1-TM monomer1

Entities:

Entity 1, PD-L1-TM monomer 59 residues - Formula weight is not available

1   ALAHISPROPROASNGLUARGTHRHISLEU
2   VALILELEUGLYALAILELEULEUALALEU
3   GLYVALALALEUTHRPHEILEPHEARGLEU
4   ARGLYSGLYARGLEULEUASPVALLYSLYS
5   SERGLYILEGLNASPTHRASNSERLYSLYS
6   GLNSERASPTHRHISLEUGLUGLUTHR

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:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_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

Related Database Links:

UNP Q9NZQ7
AlphaFold Q9NUZ5

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks