BMRB Entry 30799

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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/BMR30799
MolProbity Validation Chart

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Title:
Transmembrane structure of TNFR1
Deposition date:
2020-09-22
Original release date:
2020-09-28
Authors:
Zhao, L.; Chou, J.
Citation:

Citation: Zhao, L.; Fu, Q.; Pan, L.; Piai, A.; Chou, J.. "The Diversity and Similarity of Transmembrane Trimerization of TNF Receptors"  Front. Cell Dev. Biol. 8, 569684-569684 (2020).
PubMed: 33163490

Assembly members:

Assembly members:
entity_1, polymer, 30 residues, 3371.109 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GTTVLLPLVIFFGLALLSLL FIGLAYRYQR

Data sets:
Data typeCount
13C chemical shifts54
15N chemical shifts26
1H chemical shifts26

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21
3unit_31

Entities:

Entity 1, unit_1 30 residues - 3371.109 Da.

1   GLYTHRTHRVALLEULEUPROLEUVALILE
2   PHEPHEGLYLEUALALEULEUSERLEULEU
3   PHEILEGLYLEUALATYRARGTYRGLNARG

Samples:

sample_1: Protein, [U-100% 13C; U-100% 15N; U-80% 2H], 0.7 mM; sodium phosphate 20 mM; DMPC 50 mM; DHPC 100 mM

sample_2: Protein, [U-100% 13C; U-100% 15N], 0.7 mM; sodium phosphate 20 mM; DMPC 50 mM; DHPC 100 mM

sample_3: sodium phosphate 20 mM; DMPC 50 mM; DHPC 100 mM; Protein A, [U-100% 13C], 0.4 mM; Protein B, [U-100% 2H; U-100% 15N], 0.4 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY FOR METHYLSsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

XEASY, Bartels - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AVANCE 600 MHz
  • Bruker AVANCE 750 MHz
  • Bruker AVANCE 800 MHz

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