BMRB Entry 27548

Name: Ressonance assignments for the human Smad5 MH1 domain
Published: 2018-11-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27548

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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:

Ressonance assignments for the human Smad5 MH1 domain

Deposition date:

2018-07-17

Original release date:

2018-11-15

Authors:

Macias, Maria; Martin-Malpartida, Pau; Ruiz, Lidia; Aragon, Eric; Gomes, Tiago

Citation:

Citation: Guca, Ewelina; Sunol, David; Ruiz, Lidia; Konkol, Agnieszka; Cordero, Jorge; Torner, Carles; Aragon, Eric; Martin-Malpartida, Pau; Riera, Antoni; Macias, Maria. "TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-beta signaling." Nucleic Acids Res. 46, 9220-9235 (2018).
PubMed: 30060237

Assembly members:

Assembly members:
SMAD5-MH1, polymer, 137 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):
SMAD5-MH1: GPSFTSPAVKRLLGWKQGDE EEKWAEKAVDALVKKLKKKK GAMEELEKALSSPGQPSKCV TIPRSLDGRLQVSHRKGLPH VIYCRVWRWPDLQSHHELKP LDICEFPFGSKQKEVCINPY HYKRVESPVLPPVLVPR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	196
15N chemical shifts	84
1H chemical shifts	84

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SMAD5-MH1	1

Entities:

Entity 1, SMAD5-MH1 137 residues - Formula weight is not available

1

GLY

PRO

SER

PHE

THR

SER

PRO

ALA

VAL

LYS

2

ARG

LEU

GLY

TRP

LYS

GLN

GLY

ASP

GLU

3

GLU

LYS

TRP

ALA

GLU

LYS

ALA

VAL

ASP

4

ALA

LEU

VAL

LYS

LEU

LYS

5

GLY

ALA

MET

GLU

LEU

GLU

LYS

ALA

LEU

6

SER

PRO

GLY

GLN

PRO

SER

LYS

CYS

VAL

7

THR

ILE

PRO

ARG

SER

LEU

ASP

GLY

ARG

LEU

8

GLN

VAL

SER

HIS

ARG

LYS

GLY

LEU

PRO

HIS

9

VAL

ILE

TYR

CYS

ARG

VAL

TRP

ARG

TRP

PRO

10

ASP

LEU

GLN

SER

HIS

GLU

LEU

LYS

PRO

11

LEU

ASP

ILE

CYS

GLU

PHE

PRO

PHE

GLY

SER

12

LYS

GLN

LYS

GLU

VAL

CYS

ILE

ASN

PRO

TYR

13

HIS

TYR

LYS

ARG

VAL

GLU

SER

PRO

VAL

LEU

14

PRO

VAL

LEU

VAL

PRO

ARG

Samples:

sample_1: SMAD5-MH1, [U-100% 13C; U-100% 15N], 0.4 mM; TRIS, [U-2H], 20 mM; sodium chloride 100 mM

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

MDDNMR, Orekhov, V. - processing

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

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

Bruker Avance III 600 MHz

UNP	Q99717
AlphaFold	Q9UQA1