BMRB Entry 51085

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51085

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for Transforming Growth Factor Beta Receptor 2 (TbRII) as bound to Domain 3 of Heligmosomoides polygyrus protein Transforming Growth Factor Beta Mimic 1 (TGM-1 D3)
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, 123 residues, Formula weight is not available
entity_2, polymer, 90 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: pet32b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MVTDNAGAVKFPQLCKFCDV RFSTCDNQKSCMSNCSITSI CEKPQEVCVAVWRKNDENIT LETVCHDPKLPYHDFILEDA ASPKCIMKEKKKPGETFFMC SCSSDECNDNIIFSEEYNTS NPD
entity_2: GSGTGCPPLPDDGIVFYEYY GYAGDRHTVGPVVTKDSSGN YPSPTHARRRCRALSQEADP GEFVAICYKSGTTGESHWEY YKNIGKCPDP

Data sets:
Data typeCount
13C chemical shifts333
15N chemical shifts93
1H chemical shifts94

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TbRII1
2TGM-D32

Entities:

Entity 1, TbRII 123 residues - Formula weight is not available

1   METVALTHRASPASNALAGLYALAVALLYS
2   PHEPROGLNLEUCYSLYSPHECYSASPVAL
3   ARGPHESERTHRCYSASPASNGLNLYSSER
4   CYSMETSERASNCYSSERILETHRSERILE
5   CYSGLULYSPROGLNGLUVALCYSVALALA
6   VALTRPARGLYSASNASPGLUASNILETHR
7   LEUGLUTHRVALCYSHISASPPROLYSLEU
8   PROTYRHISASPPHEILELEUGLUASPALA
9   ALASERPROLYSCYSILEMETLYSGLULYS
10   LYSLYSPROGLYGLUTHRPHEPHEMETCYS
11   SERCYSSERSERASPGLUCYSASNASPASN
12   ILEILEPHESERGLUGLUTYRASNTHRSER
13   ASNPROASP

Entity 2, TGM-D3 90 residues - Formula weight is not available

The first two residues GS are part of a thrombin tag, the second two residues GT are part of a linker. The native protein starts from residue 5 'GCPP...' until 'CPDP'. The residue labeling starts from residue 173.

1   GLYSERGLYTHRGLYCYSPROPROLEUPRO
2   ASPASPGLYILEVALPHETYRGLUTYRTYR
3   GLYTYRALAGLYASPARGHISTHRVALGLY
4   PROVALVALTHRLYSASPSERSERGLYASN
5   TYRPROSERPROTHRHISALAARGARGARG
6   CYSARGALALEUSERGLNGLUALAASPPRO
7   GLYGLUPHEVALALAILECYSTYRLYSSER
8   GLYTHRTHRGLYGLUSERHISTRPGLUTYR
9   TYRLYSASNILEGLYLYSCYSPROASPPRO

Samples:

sample_1: Transforming Growth Factor Beta Receptor 2 (TbRII), [U-98% 15N; U-95% 13C], 250 uM; TGM-1 D3 325 uM; D2O 5%; Na2HPO4 25 mM; NaCl 50 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 310 K

Experiments:

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

Related Database Links:

NCBI AHI94913 MG099712

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