BMRB Entry 27742

Name: hSmad2 MH1 domain
Published: 2019-09-23

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27742

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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:

hSmad2 MH1 domain

Deposition date:

2018-12-24

Original release date:

2019-09-23

Authors:

Macias, Maria; Martin, Pau; Aragon, Eric; Ruiz, Lidia

Citation:

Citation: Aragon, Eric; Wang, Qiong; Zou, Yilong; Morgani, Sophie; Ruiz, Lidia; Kaczmarska, Zuzanna; Su, Jie; Torner, Carles; Tian, Lin; Hu, Jing; Shu, Weiping; Agrawal, Saloni; Gomes, Tiago; Marquez, Jose; Hadjantonakis, Anna-Katerina; Macias, Maria; Massague, Joan. "Structural basis for distinct roles of SMAD2 and SMAD3 in FOXH1 pioneer-directed TGF-beta signaling" Genes Dev. 33, 1506-1524 (2019).
PubMed: 31582430

Assembly members:

Assembly members:
smad2, polymer, 180 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: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
smad2: MSSILPFTPPVVKRLLGWKK SAGGSGGAGGGEQNGQEEKW CEKAVKSLVKKLKKTGRLDE LEKAITTQNCNTKCVTIPST CSEIWGLSTPNTIDQWDTTG LYSFSEQTRSLDGRLQVSHR KGLPHVIYCRLWRWPDLHSH HELKAIENCEYAFNLKKDEV CVNPYHYQRVETPVLPPVLV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	276
15N chemical shifts	128
1H chemical shifts	128

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	smad2	1

Entities:

Entity 1, smad2 180 residues - Formula weight is not available

1	MET	SER	SER	ILE	LEU	PRO	PHE	THR	PRO	PRO
2	VAL	VAL	LYS	ARG	LEU	LEU	GLY	TRP	LYS	LYS
3	SER	ALA	GLY	GLY	SER	GLY	GLY	ALA	GLY	GLY
4	GLY	GLU	GLN	ASN	GLY	GLN	GLU	GLU	LYS	TRP
5	CYS	GLU	LYS	ALA	VAL	LYS	SER	LEU	VAL	LYS
6	LYS	LEU	LYS	LYS	THR	GLY	ARG	LEU	ASP	GLU
7	LEU	GLU	LYS	ALA	ILE	THR	THR	GLN	ASN	CYS
8	ASN	THR	LYS	CYS	VAL	THR	ILE	PRO	SER	THR
9	CYS	SER	GLU	ILE	TRP	GLY	LEU	SER	THR	PRO
10	ASN	THR	ILE	ASP	GLN	TRP	ASP	THR	THR	GLY
11	LEU	TYR	SER	PHE	SER	GLU	GLN	THR	ARG	SER
12	LEU	ASP	GLY	ARG	LEU	GLN	VAL	SER	HIS	ARG
13	LYS	GLY	LEU	PRO	HIS	VAL	ILE	TYR	CYS	ARG
14	LEU	TRP	ARG	TRP	PRO	ASP	LEU	HIS	SER	HIS
15	HIS	GLU	LEU	LYS	ALA	ILE	GLU	ASN	CYS	GLU
16	TYR	ALA	PHE	ASN	LEU	LYS	LYS	ASP	GLU	VAL
17	CYS	VAL	ASN	PRO	TYR	HIS	TYR	GLN	ARG	VAL
18	GLU	THR	PRO	VAL	LEU	PRO	PRO	VAL	LEU	VAL

Samples:

sample_1: smad2, [U-100% 13C; U-100% 15N; U-80% 2H], 300 mM; MES 20 mM; sodium chloride 80 mM

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

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

TOPSPIN, Bruker Biospin - collection

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

UNP	Q15796-1
AlphaFold	Q15796

1	MET	SER	SER	ILE	LEU	PRO	PHE	THR	PRO	PRO
2	VAL	VAL	LYS	ARG	LEU	LEU	GLY	TRP	LYS	LYS
3	SER	ALA	GLY	GLY	SER	GLY	GLY	ALA	GLY	GLY
4	GLY	GLU	GLN	ASN	GLY	GLN	GLU	GLU	LYS	TRP
5	CYS	GLU	LYS	ALA	VAL	LYS	SER	LEU	VAL	LYS
6	LYS	LEU	LYS	LYS	THR	GLY	ARG	LEU	ASP	GLU
7	LEU	GLU	LYS	ALA	ILE	THR	THR	GLN	ASN	CYS
8	ASN	THR	LYS	CYS	VAL	THR	ILE	PRO	SER	THR
9	CYS	SER	GLU	ILE	TRP	GLY	LEU	SER	THR	PRO
10	ASN	THR	ILE	ASP	GLN	TRP	ASP	THR	THR	GLY
11	LEU	TYR	SER	PHE	SER	GLU	GLN	THR	ARG	SER
12	LEU	ASP	GLY	ARG	LEU	GLN	VAL	SER	HIS	ARG
13	LYS	GLY	LEU	PRO	HIS	VAL	ILE	TYR	CYS	ARG
14	LEU	TRP	ARG	TRP	PRO	ASP	LEU	HIS	SER	HIS
15	HIS	GLU	LEU	LYS	ALA	ILE	GLU	ASN	CYS	GLU
16	TYR	ALA	PHE	ASN	LEU	LYS	LYS	ASP	GLU	VAL
17	CYS	VAL	ASN	PRO	TYR	HIS	TYR	GLN	ARG	VAL
18	GLU	THR	PRO	VAL	LEU	PRO	PRO	VAL	LEU	VAL

1	MET	SER	SER	ILE	LEU	PRO	PHE	THR	PRO	PRO
2	VAL	VAL	LYS	ARG	LEU	LEU	GLY	TRP	LYS	LYS
3	SER	ALA	GLY	GLY	SER	GLY	GLY	ALA	GLY	GLY
4	GLY	GLU	GLN	ASN	GLY	GLN	GLU	GLU	LYS	TRP
5	CYS	GLU	LYS	ALA	VAL	LYS	SER	LEU	VAL	LYS
6	LYS	LEU	LYS	LYS	THR	GLY	ARG	LEU	ASP	GLU
7	LEU	GLU	LYS	ALA	ILE	THR	THR	GLN	ASN	CYS
8	ASN	THR	LYS	CYS	VAL	THR	ILE	PRO	SER	THR
9	CYS	SER	GLU	ILE	TRP	GLY	LEU	SER	THR	PRO
10	ASN	THR	ILE	ASP	GLN	TRP	ASP	THR	THR	GLY
11	LEU	TYR	SER	PHE	SER	GLU	GLN	THR	ARG	SER
12	LEU	ASP	GLY	ARG	LEU	GLN	VAL	SER	HIS	ARG
13	LYS	GLY	LEU	PRO	HIS	VAL	ILE	TYR	CYS	ARG
14	LEU	TRP	ARG	TRP	PRO	ASP	LEU	HIS	SER	HIS
15	HIS	GLU	LEU	LYS	ALA	ILE	GLU	ASN	CYS	GLU
16	TYR	ALA	PHE	ASN	LEU	LYS	LYS	ASP	GLU	VAL
17	CYS	VAL	ASN	PRO	TYR	HIS	TYR	GLN	ARG	VAL
18	GLU	THR	PRO	VAL	LEU	PRO	PRO	VAL	LEU	VAL