BMRB Entry 26945

Name: Human SMAD4 MH1 domain
Published: 2017-11-06

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26945

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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 SMAD4 MH1 domain

Deposition date:

2016-11-17

Original release date:

2017-11-06

Authors:

Macias, Maria J.; Batet, Marta

Citation:

Citation: Martin-Malpartida, Pau; Batet, Marta; Kaczmarska, Zuzanna; Freier, Regina; Gomes, Tiago; Aragon, Eric; Zou, Yilong; Wang, Qiong; Xi, Qiaoran; Ruiz, Lidia; Vea, Angela; Marquez, Jose; Massague, Joan; Macias, Maria. "Structural basis for genome wide recognition of 5-bp GC motifs by SMAD transcription factors" Nat. Commun. 8, 2070-2070 (2017).
PubMed: 29234012

Assembly members:

Assembly members:
SMAD4, polymer, 135 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):
SMAD4: GAMGPTSNDACLSIVHSLMC HRQGGESETFAKRAIESLVK KLKEKKDELDSLITAITTNG AHPSKCVTIQRTLDGRLQVA GRKGFPHVIYARLWRWPDLH KNELKHVKYCQYAFDLKCDS VCVNPYHYERVVSPG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	233
15N chemical shifts	109
1H chemical shifts	110

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SMAD4	1

Entities:

Entity 1, SMAD4 135 residues - Formula weight is not available

Residues 6-9 are artifacts from the cloning site

1

GLY

ALA

MET

GLY

PRO

THR

SER

ASN

ASP

ALA

2

CYS

LEU

SER

ILE

VAL

HIS

SER

LEU

MET

CYS

3

HIS

ARG

GLN

GLY

GLU

SER

GLU

THR

PHE

4

ALA

LYS

ARG

ALA

ILE

GLU

SER

LEU

VAL

LYS

5

LYS

LEU

LYS

GLU

LYS

ASP

GLU

LEU

ASP

6

SER

LEU

ILE

THR

ALA

ILE

THR

ASN

GLY

7

ALA

HIS

PRO

SER

LYS

CYS

VAL

THR

ILE

GLN

8

ARG

THR

LEU

ASP

GLY

ARG

LEU

GLN

VAL

ALA

9

GLY

ARG

LYS

GLY

PHE

PRO

HIS

VAL

ILE

TYR

10

ALA

ARG

LEU

TRP

ARG

TRP

PRO

ASP

LEU

HIS

11

LYS

ASN

GLU

LEU

LYS

HIS

VAL

LYS

TYR

CYS

12

GLN

TYR

ALA

PHE

ASP

LEU

LYS

CYS

ASP

SER

13

VAL

CYS

VAL

ASN

PRO

TYR

HIS

TYR

GLU

ARG

14

VAL

SER

PRO

GLY

Samples:

sample_1: SMAD4, [U-100% 13C; U-100% 15N; U-80% 2H], 300 ± 10 uM; D2O, [U-2H], 10 ± 1 % v/v; sodium phosphate 100 mM; sodium chloride 80 mM; DTT 2 mM

sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 298 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 HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz