BMRB Entry 27743

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

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27743

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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-beta 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, 149 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 LEKAITTQNCNTKCVTIPRS LDGRLQVSHRKGLPHVIYCR LWRWPDLHSHHELKAIENCE YAFNLKKDEVCVNPYHYQRV ETPVLPPSS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	250
15N chemical shifts	120
1H chemical shifts	120

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 149 residues - Formula weight is not available

This is an isoform lacking a 30aa exon. Sequence numbering is done as in the reference isoform. This is why the assignment skips residues 79 to 108.

1

MET

SER

ILE

LEU

PRO

PHE

THR

PRO

2

VAL

LYS

ARG

LEU

GLY

TRP

LYS

3

SER

ALA

GLY

SER

GLY

ALA

GLY

4

GLY

GLU

GLN

ASN

GLY

GLN

GLU

LYS

TRP

5

CYS

GLU

LYS

ALA

VAL

LYS

SER

LEU

VAL

LYS

6

LYS

LEU

LYS

THR

GLY

ARG

LEU

ASP

GLU

7

LEU

GLU

LYS

ALA

ILE

THR

GLN

ASN

CYS

8

ASN

THR

LYS

CYS

VAL

THR

ILE

PRO

ARG

SER

9

LEU

ASP

GLY

ARG

LEU

GLN

VAL

SER

HIS

ARG

10

LYS

GLY

LEU

PRO

HIS

VAL

ILE

TYR

CYS

ARG

11

LEU

TRP

ARG

TRP

PRO

ASP

LEU

HIS

SER

HIS

12

HIS

GLU

LEU

LYS

ALA

ILE

GLU

ASN

CYS

GLU

13

TYR

ALA

PHE

ASN

LEU

LYS

ASP

GLU

VAL

14

CYS

VAL

ASN

PRO

TYR

HIS

TYR

GLN

ARG

VAL

15

GLU

THR

PRO

VAL

LEU

PRO

SER

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	Q15796-2
AlphaFold	Q15796