BMRB Entry 51086

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for Transforming Growth Factor Beta Receptor 1 (TbRI) as bound to Domain 2 of Heligmosomoides polygyrus protein Transforming Growth Factor Beta Mimic 1 (TGM-1 D2)
Deposition date:
2021-09-14
Original release date:
2021-09-18
Authors:
Mukundan, Ananya; Byeon, Chang-Hyeock
Citation:

Citation: Mukundan, Ananya; Byeon, Chang-Hyeock; Hinck, Cynthia; Cunningham, Kyle; Campion, Tiffany; Smyth, Danielle; Maizels, Rick; Hinck, Andrew. "Convergent evolution of a parasite-encoded complement control protein-scaffold to mimic binding of mammalian TGF-b to its receptors, TbRI and TbRII"  J. Biol. Chem. 298, 101994-101994 (2022).
PubMed: 35500648

Assembly members:

Assembly members:
entity_1, polymer, 85 residues, 9451 Da.
entity_2, polymer, 83 residues, 9296 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   Vector: pet32b

Data sets:
Data typeCount
13C chemical shifts209
15N chemical shifts67
1H chemical shifts67

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TbRI1
2TGM-D22

Entities:

Entity 1, TbRI 85 residues - 9451 Da.

Residues 31-115 of the human TGF-B type I receptor

1   ALATHRALALEUGLNCYSPHECYSHISLEU
2   CYSTHRLYSASPASNPHETHRCYSVALTHR
3   ASPGLYLEUCYSPHEVALSERVALTHRGLU
4   THRTHRASPLYSVALILEHISASNSERSER
5   CYSILEALAGLUILEASPLEUILEPROARG
6   ASPARGPROPHEVALCYSALAPROSERSER
7   LYSTHRGLYSERVALTHRTHRTHRTYRCYS
8   CYSASNGLNASPHISCYSASNLYSILEGLU
9   LEUPROTHRTHRVAL

Entity 2, TGM-D2 83 residues - 9296 Da.

The first two residues are part of a KpNI cut site

1   GLYTHRARGCYSSERPROLEUPROTHRASN
2   ASPTHRVALSERPHEGLUTYRLEULYSALA
3   THRVALASNPROGLYILEILEPHEASNILE
4   THRVALHISPROASPALASERGLYLYSTYR
5   PROGLULEUTHRTYRILELYSARGILECYS
6   LYSASNPHEPROTHRASPSERASNVALGLN
7   GLYHISILEILEGLYMETCYSTYRASNALA
8   GLUTRPGLNPHESERSERTHRPROTHRCYS
9   PROALASER

Samples:

sample_1: Transforming Growth Factor Beta Receptor 1 (TbRI), [U-98% 15N; U-95% 13C], 250 uM; TGM-1 D2 325 uM; D2O 5%; Na2HPO4 25 mM; NaCl 50 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

CcpNMR v2.4 - chemical shift assignment, chemical shift calculation

NMRFAM-SPARKY v1.2 - chemical shift assignment, chemical shift calculation

TOPSPIN v3.1 - collection

NMRPipe v2.6 - data analysis

PINE vI-PINE - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE II 800 MHz

Related Database Links:

NCBI NP_004603.1 MG099712

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