BMRB Entry 51083

Name: Backbone and Sidechain 1H, 13C, and 15N Chemical Shift Assignments for Domain 3 of Heligmosomoides polygyrus protein Transforming Growth Factor Beta Mimic 1 (TGM-1 D3)
Published: 2021-09-18

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PDB ID: 7sxb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51083
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone and Sidechain 1H, 13C, and 15N Chemical Shift Assignments for 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, 90 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Heligmosomoides polygyrus Taxonomy ID: 6339 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Heligmosomoides polygyrus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet32b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSGTGCPPLPDDGIVFYEYY GYAGDRHTVGPVVTKDSSGN YPSPTHARRRCRALSQEADP GEFVAICYKSGTTGESHWEY YKNIGKCPDP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	366
15N chemical shifts	95
1H chemical shifts	551

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TGM-1 D3	1

Entities:

Entity 1, TGM-1 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	GLY	SER	GLY	THR	GLY	CYS	PRO	PRO	LEU	PRO
2	ASP	ASP	GLY	ILE	VAL	PHE	TYR	GLU	TYR	TYR
3	GLY	TYR	ALA	GLY	ASP	ARG	HIS	THR	VAL	GLY
4	PRO	VAL	VAL	THR	LYS	ASP	SER	SER	GLY	ASN
5	TYR	PRO	SER	PRO	THR	HIS	ALA	ARG	ARG	ARG
6	CYS	ARG	ALA	LEU	SER	GLN	GLU	ALA	ASP	PRO
7	GLY	GLU	PHE	VAL	ALA	ILE	CYS	TYR	LYS	SER
8	GLY	THR	THR	GLY	GLU	SER	HIS	TRP	GLU	TYR
9	TYR	LYS	ASN	ILE	GLY	LYS	CYS	PRO	ASP	PRO

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_4	anisotropic	sample_conditions_2
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
2D CB(CGCDCD)HD	sample_1	isotropic	sample_conditions_1
1H 13C HSQC-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_4	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D CB(CGCDCD)HE	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCA(CO)N	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

BMRB Entry 51083

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	GLY	SER	GLY	THR	GLY	CYS	PRO	PRO	LEU	PRO
2	ASP	ASP	GLY	ILE	VAL	PHE	TYR	GLU	TYR	TYR
3	GLY	TYR	ALA	GLY	ASP	ARG	HIS	THR	VAL	GLY
4	PRO	VAL	VAL	THR	LYS	ASP	SER	SER	GLY	ASN
5	TYR	PRO	SER	PRO	THR	HIS	ALA	ARG	ARG	ARG
6	CYS	ARG	ALA	LEU	SER	GLN	GLU	ALA	ASP	PRO
7	GLY	GLU	PHE	VAL	ALA	ILE	CYS	TYR	LYS	SER
8	GLY	THR	THR	GLY	GLU	SER	HIS	TRP	GLU	TYR
9	TYR	LYS	ASN	ILE	GLY	LYS	CYS	PRO	ASP	PRO

1	GLY	SER	GLY	THR	GLY	CYS	PRO	PRO	LEU	PRO
2	ASP	ASP	GLY	ILE	VAL	PHE	TYR	GLU	TYR	TYR
3	GLY	TYR	ALA	GLY	ASP	ARG	HIS	THR	VAL	GLY
4	PRO	VAL	VAL	THR	LYS	ASP	SER	SER	GLY	ASN
5	TYR	PRO	SER	PRO	THR	HIS	ALA	ARG	ARG	ARG
6	CYS	ARG	ALA	LEU	SER	GLN	GLU	ALA	ASP	PRO
7	GLY	GLU	PHE	VAL	ALA	ILE	CYS	TYR	LYS	SER
8	GLY	THR	THR	GLY	GLU	SER	HIS	TRP	GLU	TYR
9	TYR	LYS	ASN	ILE	GLY	LYS	CYS	PRO	ASP	PRO

1	GLY	SER	GLY	THR	GLY	CYS	PRO	PRO	LEU	PRO
2	ASP	ASP	GLY	ILE	VAL	PHE	TYR	GLU	TYR	TYR
3	GLY	TYR	ALA	GLY	ASP	ARG	HIS	THR	VAL	GLY
4	PRO	VAL	VAL	THR	LYS	ASP	SER	SER	GLY	ASN
5	TYR	PRO	SER	PRO	THR	HIS	ALA	ARG	ARG	ARG
6	CYS	ARG	ALA	LEU	SER	GLN	GLU	ALA	ASP	PRO
7	GLY	GLU	PHE	VAL	ALA	ILE	CYS	TYR	LYS	SER
8	GLY	THR	THR	GLY	GLU	SER	HIS	TRP	GLU	TYR
9	TYR	LYS	ASN	ILE	GLY	LYS	CYS	PRO	ASP	PRO