BMRB Entry 27526

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for alpha-N catenin actin-binding domain H1 mutant
Published: 2018-12-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27526

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for alpha-N catenin actin-binding domain H1 mutant

Deposition date:

2018-06-23

Original release date:

2018-12-12

Authors:

Nishikawa, Tadateru

Citation:

Citation: Ishiyama, Noboru; Sarpal, Ritu; Wood, Megan; Barrick, Samantha; Nishikawa, Tadateru; Hayashi, Hanako; Kobb, Anna; Flozak, Annette; Yemelyanov, Alex; Fernandez-Gonzalez, Rodrigo; Yonemura, Shigenobu; Leckband, Deborah; Gottardi, Cara; Tepass, Ulrich; Ikura, Mitsuhiko. "Force-dependent allostery of the alpha-catenin actin-binding domain controls adherens junction dynamics and functions" Nat. Commun. 9, 5121-5121 (2018).
PubMed: 30504777

Assembly members:

Assembly members:
Catenin_alpha-2, polymer, 209 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX4T1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Catenin_alpha-2: GSQTEDDQLIAGQSAGSGSA QLPQEEKAKIAEQVEIFHQE KSKLDAEVAKWDDSGNDIIV LAKQMCMIMMEMTDFTRGKG PLKNTSDVINAAKKIAEAGS RMDKLARAVADQCPDSACKQ DLLAYLQRIALYCHQLNICS KVKAEVQNLGGELIVSGLDS ATSLIQAAKNLMNAVVLTVK ASYVASTKYQKVYGTAAVNS PVVSWKMKA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	566
15N chemical shifts	184
1H chemical shifts	184

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Catenin alpha-2	1

Entities:

Entity 1, Catenin alpha-2 209 residues - Formula weight is not available

1

GLY

SER

GLN

THR

GLU

ASP

GLN

LEU

ILE

2

ALA

GLY

GLN

SER

ALA

GLY

SER

GLY

SER

ALA

3

GLN

LEU

PRO

GLN

GLU

LYS

ALA

LYS

ILE

4

ALA

GLU

GLN

VAL

GLU

ILE

PHE

HIS

GLN

GLU

5

LYS

SER

LYS

LEU

ASP

ALA

GLU

VAL

ALA

LYS

6

TRP

ASP

SER

GLY

ASN

ASP

ILE

VAL

7

LEU

ALA

LYS

GLN

MET

CYS

MET

ILE

MET

8

GLU

MET

THR

ASP

PHE

THR

ARG

GLY

LYS

GLY

9

PRO

LEU

LYS

ASN

THR

SER

ASP

VAL

ILE

ASN

10

ALA

LYS

ILE

ALA

GLU

ALA

GLY

SER

11

ARG

MET

ASP

LYS

LEU

ALA

ARG

ALA

VAL

ALA

12

ASP

GLN

CYS

PRO

ASP

SER

ALA

CYS

LYS

GLN

13

ASP

LEU

ALA

TYR

LEU

GLN

ARG

ILE

ALA

14

LEU

TYR

CYS

HIS

GLN

LEU

ASN

ILE

CYS

SER

15

LYS

VAL

LYS

ALA

GLU

VAL

GLN

ASN

LEU

GLY

16

GLY

GLU

LEU

ILE

VAL

SER

GLY

LEU

ASP

SER

17

ALA

THR

SER

LEU

ILE

GLN

ALA

LYS

ASN

18

LEU

MET

ASN

ALA

VAL

LEU

THR

VAL

LYS

19

ALA

SER

TYR

VAL

ALA

SER

THR

LYS

TYR

GLN

20

LYS

VAL

TYR

GLY

THR

ALA

VAL

ASN

SER

21

PRO

VAL

SER

TRP

LYS

MET

LYS

ALA

Samples:

sample_1: Catenin alpha-2, [U-100% 13C; U-100% 15N], 0.4 mM; potassium phosphate 20 mM; sodium chloride 150 mM; TCEP 1 mM; sodium azide 1 mM

sample_conditions_1: ionic strength: 0.17 M; pH: 6.5; pressure: 1 atm; temperature: 288 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz