BMRB Entry 28100

Name: Chemical shift assignment for human EDC3 residues 104-197
Published: 2020-11-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28100

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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:

Chemical shift assignment for human EDC3 residues 104-197

Deposition date:

2020-03-12

Original release date:

2020-11-12

Authors:

Peti, Wolfgang; Page, Rebecca; Li, Yang; Clarkson, Michael

Citation:

Citation: Bearss, Jeremiah; Padi, Sathish Kr; Singh, Neha; Cardo-Vila, Marina; Song, Jin; Mouneimne, Ghassan; Fernandes, Nikita; Li, Yang; Harter, Matthew; Gard, Jaime Mc; Cress, Anne; Peti, Wolfgang; Nelson, Andrew Dl; Buchan, J Ross; Kraft, Andrew; Okumura, Koichi. "EDC3 phosphorylation regulates growth and invasion through controlling P-body formation and dynamics" EMBO Rep. 22, e50835-e50835 (2021).
PubMed: 33586867

Assembly members:

Assembly members:
EDC3_residues_104-197, polymer, 97 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: RP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EDC3_residues_104-197: GHMVKKPASSSSAPQNIPKR TDVKSQDVAVSPQQQQCSKS YVDRHMESLSQSKSFRRRHN SWSSSSRHPNQATPKKSGLK NGQMKNKDDECFGDDIE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	237
15N chemical shifts	86
1H chemical shifts	86

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EDC3 residues 104-197	1

Entities:

Entity 1, EDC3 residues 104-197 97 residues - Formula weight is not available

GHM are cloning artifact; EDC3 sequence starts with VKKPA

1

GLY

HIS

MET

VAL

LYS

PRO

ALA

SER

2

SER

ALA

PRO

GLN

ASN

ILE

PRO

LYS

ARG

3

THR

ASP

VAL

LYS

SER

GLN

ASP

VAL

ALA

VAL

4

SER

PRO

GLN

CYS

SER

LYS

SER

5

TYR

VAL

ASP

ARG

HIS

MET

GLU

SER

LEU

SER

6

GLN

SER

LYS

SER

PHE

ARG

HIS

ASN

7

SER

TRP

SER

ARG

HIS

PRO

ASN

8

GLN

ALA

THR

PRO

LYS

SER

GLY

LEU

LYS

9

ASN

GLY

GLN

MET

LYS

ASN

LYS

ASP

GLU

10

CYS

PHE

GLY

ASP

ILE

GLU

Samples:

sample_1: EDC3 residues 104-197, [U-99% 13C; U-99% 15N], 0.7 mM; sodium phosphate 20 mM; sodium chloride 150 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	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 HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance NEO 600 MHz

UNP	Q96F86
AlphaFold	Q9H797