BMRB Entry 27574

Name: human TGF-b2
Published: 2019-01-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27574

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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:

human TGF-b2

Deposition date:

2018-08-11

Original release date:

2019-01-02

Authors:

Henen, Morkos; Mahlawat, Pardeep; Ilangovan, Udayar; Hinck, Andrew

Citation:

Citation: Henen, Morkos; Mahlawat, Pardeep; Zwieb, Christian; Kodali, Ravi; Hanna, Ramsey; Krzysiak, Troy; Ilangovan, Udayar; Cano, Kristin; Hinck, Garrett; Vonberg, Morkos; McCabe, Megan; Hinck, Andrew. "TGF-b2 uses the concave surface of its extended finger region to bind betaglycan's ZP domain via three residues specific to TGF-b and Inhibin-a" J. Biol. Chem. 294, 3065-3080 (2019).
PubMed: 30598510

Assembly members:

Assembly members:
TGF-b2, polymer, 112 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: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TGF-b2: ALDAAYCFRNVQDNCCLRPL YIDFKRDLGWKWIHEPKGYN ANFCAGACPYLWSSDTQHSK VLSLYNTINPEASASPCCVS QDLEPLTILYYIGKTPKIEQ LSNMIVKSCKCS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	383
15N chemical shifts	92
1H chemical shifts	499

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TGF-b2, chain 1	1
2	TGF-b2, chain 2	1

Entities:

Entity 1, TGF-b2, chain 1 112 residues - Formula weight is not available

The sequence provided is that of the monomer, though the protein found in the NMR tube is a covalent (disulfide) linked homodimer. There is a single Arg to Lys substitution at position 60.

1

ALA

LEU

ASP

ALA

TYR

CYS

PHE

ARG

ASN

2

VAL

GLN

ASP

ASN

CYS

LEU

ARG

PRO

LEU

3

TYR

ILE

ASP

PHE

LYS

ARG

ASP

LEU

GLY

TRP

4

LYS

TRP

ILE

HIS

GLU

PRO

LYS

GLY

TYR

ASN

5

ALA

ASN

PHE

CYS

ALA

GLY

ALA

CYS

PRO

TYR

6

LEU

TRP

SER

ASP

THR

GLN

HIS

SER

LYS

7

VAL

LEU

SER

LEU

TYR

ASN

THR

ILE

ASN

PRO

8

GLU

ALA

SER

ALA

SER

PRO

CYS

VAL

SER

9

GLN

ASP

LEU

GLU

PRO

LEU

THR

ILE

LEU

TYR

10

TYR

ILE

GLY

LYS

THR

PRO

LYS

ILE

GLU

GLN

11

LEU

SER

ASN

MET

ILE

VAL

LYS

SER

CYS

LYS

12

CYS

SER

Samples:

sample_1: TGF-b2, [U-98% 13C; U-98% 15N], 0.25 mM

sample_conditions_1: ionic strength: 0 M; pH: 2.7; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1

Software:

NMRView vJ, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

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

NMR spectrometers:

Bruker Avance 700 MHz