BMRB Entry 27408

Name: Axin RGS domain
Published: 2018-03-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27408

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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:

Axin RGS domain

Deposition date:

2018-02-21

Original release date:

2018-03-02

Authors:

Lee, Weontae; Yun, Jihye

Citation:

Citation: Cha, Pu-Hyeon; Cho, Yong-Hee; Lee, Sang-Kyu; Lee, JaeHeon; Jeong, Woo-Jeong; Moon, Byoung-San; Yun, Jihye; Yang, Jee Sun; Choi, Sooho; Soon, Juyong; Kim, Hyun-Yi; Kim, Mi-Yeon; Kaduwal, Saluja; Lee, Weontae; Min, Do Sik; Kim, Hoguen; Han, Gyoonhee; Choi, Kang-Yell. "Small-molecule binding of the axin RGS domain promotes beta-catenin and Ras degradation." Nat. Chem. Biol. 12, 593-600 (2016).
PubMed: 27294323

Assembly members:

Assembly members:
Axin_RGS_domain, polymer, 147 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):
Axin_RGS_domain: GSASPTPPYLKWAESLHSLL DDQDGISLFRTFLKQEGCAD LLDFWFACTGFRKLEPCDSN EEKRLKLARAIYRKYILDNN GIVSRQTKPATKSFIKGCIM KQLIDPAMFDQAQTEIQATM EENTYPSFLKSDIYLEYTRT GSESPKV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	216
15N chemical shifts	108
1H chemical shifts	108

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Axin RGS domain	1

Entities:

Entity 1, Axin RGS domain 147 residues - Formula weight is not available

1

GLY

SER

ALA

SER

PRO

THR

PRO

TYR

LEU

2

LYS

TRP

ALA

GLU

SER

LEU

HIS

SER

LEU

3

ASP

GLN

ASP

GLY

ILE

SER

LEU

PHE

ARG

4

THR

PHE

LEU

LYS

GLN

GLU

GLY

CYS

ALA

ASP

5

LEU

ASP

PHE

TRP

PHE

ALA

CYS

THR

GLY

6

PHE

ARG

LYS

LEU

GLU

PRO

CYS

ASP

SER

ASN

7

GLU

LYS

ARG

LEU

LYS

LEU

ALA

ARG

ALA

8

ILE

TYR

ARG

LYS

TYR

ILE

LEU

ASP

ASN

9

GLY

ILE

VAL

SER

ARG

GLN

THR

LYS

PRO

ALA

10

THR

LYS

SER

PHE

ILE

LYS

GLY

CYS

ILE

MET

11

LYS

GLN

LEU

ILE

ASP

PRO

ALA

MET

PHE

ASP

12

GLN

ALA

GLN

THR

GLU

ILE

GLN

ALA

THR

MET

13

GLU

ASN

THR

TYR

PRO

SER

PHE

LEU

LYS

14

SER

ASP

ILE

TYR

LEU

GLU

TYR

THR

ARG

THR

15

GLY

SER

GLU

SER

PRO

LYS

VAL

Samples:

sample_1: Axin RGS domain, [U-99% 13C; U-99% 15N], 0.5 mM; Axin RGS domain, [U-99% 15N], 0.5 mM

Axin_RGS_domain_conditions: ionic strength: 0.3 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DRX 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks