BMRB Entry 19443

Name: 1H, 13C and 15N Backbone Assignment of the EC-1 Domain of Human E-Cadherin
Published: 2013-09-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19443

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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:

1H, 13C and 15N Backbone Assignment of the EC-1 Domain of Human E-Cadherin

Deposition date:

2013-08-20

Original release date:

2013-09-19

Authors:

Prasasty, Vivitri; Krause, Mary; Siahaan, Teruna; Laurence, Jennifer; Tambunan, Usman; Anbanandam, Asokan

Citation:

Citation: Prasasty, Vivitri; Krause, Mary; Tambunan, Usman; Anbanandam, Asokan; Laurence, Jennifer; Siahaan, Teruna. "(1)H, (13)C and (15)N backbone assignment of the EC-1 domain of human E-cadherin." Biomol. NMR Assignments 9, 31-35 (2015).
PubMed: 24510398

Assembly members:

Assembly members:
EC1, polymer, 138 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: pASK-IBA6

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EC1: DWVIPPISCPENEKGPFPKN LVQIKSNKDKEGKVFYSITG QGADTPPVGVFIIERETGWL KVTEPLDRERIATYTLFSHA VSSNGNAVEDPMEILITVTD QNDNKPEFTQEVFKGSVMEG ALPGTSVMEVTATDADDD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	310
15N chemical shifts	117
1H chemical shifts	117

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EC1	1

Entities:

Entity 1, EC1 138 residues - Formula weight is not available

1

ASP

TRP

VAL

ILE

PRO

ILE

SER

CYS

PRO

2

GLU

ASN

GLU

LYS

GLY

PRO

PHE

PRO

LYS

ASN

3

LEU

VAL

GLN

ILE

LYS

SER

ASN

LYS

ASP

LYS

4

GLU

GLY

LYS

VAL

PHE

TYR

SER

ILE

THR

GLY

5

GLN

GLY

ALA

ASP

THR

PRO

VAL

GLY

VAL

6

PHE

ILE

GLU

ARG

GLU

THR

GLY

TRP

LEU

7

LYS

VAL

THR

GLU

PRO

LEU

ASP

ARG

GLU

ARG

8

ILE

ALA

THR

TYR

THR

LEU

PHE

SER

HIS

ALA

9

VAL

SER

ASN

GLY

ASN

ALA

VAL

GLU

ASP

10

PRO

MET

GLU

ILE

LEU

ILE

THR

VAL

THR

ASP

11

GLN

ASN

ASP

ASN

LYS

PRO

GLU

PHE

THR

GLN

12

GLU

VAL

PHE

LYS

GLY

SER

VAL

MET

GLU

GLY

13

ALA

LEU

PRO

GLY

THR

SER

VAL

MET

GLU

VAL

14

THR

ALA

THR

ASP

ALA

ASP

Samples:

sample_1: potassium phosphate, KCl, CaCl2, DTT, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.8; 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(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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