BMRB Entry 36805

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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/BMR36805
MolProbity Validation Chart

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Title:
Structure of the transmembrane domain dimer of human IL-7R V253G mutant
Deposition date:
2025-10-27
Original release date:
2026-06-07
Authors:
Wang, Q.; Cai, T.; Chou, J.
Citation:

Citation: Wang, Q.; Cai, T.; Chou, J.. "Structure of the transmembrane domain dimer of the IL-7R V253G mutant"  .

Assembly members:

Assembly members:
Interleukin-7 receptor subunit alpha, polymer, 62 residues, 3427.169 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):
Interleukin-7 receptor subunit alpha: GEKDPILLTISILSFFSGAL LVILAHVLWKK

Data sets:
Data typeCount
13C chemical shifts57
15N chemical shifts28
1H chemical shifts28

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1_11
2entity_1_21

Entities:

Entity 1, entity_1_1 62 residues - 3427.169 Da.

1   GLYGLULYSASPPROILELEULEUTHRILE
2   SERILELEUSERPHEPHESERGLYALALEU
3   LEUVALILELEUALAHISVALLEUTRPLYS
4   LYS

Samples:

sample_5: The transmembrane domain of the IL-7R-V253G dimer, [U-100% 13C; U-100% 15N; U-85% 2H], 0.6 ± 0.05 mM; DHPC 150 ± 5 mM; POPC 60 ± 5 mM; MES 25 ± 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_6: Transmembrane domain of the IL-7R V253G mutant, [U-13C; U-15N], 0.6 ± 0.05 mM; Deuterated DHPC, [U-2H], 150 ± 5 mM; Deuterated POPC, [U-2H], 60 ± 5 mM; MES 25 ± 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_7: Transmembrane domain of the IL-7R V253G mutant, [U-13C; U-15N; U-2H], 0.4 ± 0.05 mM; Deuterated DHPC, [U-2H], 150 ± 5 mM; Deuterated POPC, [U-2H], 60 ± 5 mM; MES 25 ± 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_3: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 306 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY-HSQCsample_5isotropicsample_conditions_3
2D 1H-13C HSQCsample_6isotropicsample_conditions_3
3D TROSY HNCAsample_5isotropicsample_conditions_3
3D TROSY HN(CO)CAsample_5isotropicsample_conditions_3
3D TROSY HNCOsample_5isotropicsample_conditions_3
3D 1H-13C NOESYsample_6isotropicsample_conditions_3
3D 1H-15N NOESY-TROSYsample_6isotropicsample_conditions_3
3D 1H-15N NOESY-TROSYsample_7isotropicsample_conditions_3

Software:

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

TALOS+, Shen, Delaglio, Cornilescu, Bax - data analysis

XEASY, Bartels et al. - chemical shift assignment

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

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 900 MHz

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