BMRB Entry 27193

Name: Backbone 1H, 15N chemical shift for Y39E EVH1
Published: 2017-08-23

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27193

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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, 15N chemical shift for Y39E EVH1

Deposition date:

2017-07-22

Original release date:

2017-08-23

Authors:

Acevedo, Lucila; Greenwood, Alexander; Nicholson, Linda

Citation:

Citation: Acevedo, Lucila Andrea; Greenwood, Alexander; Nicholson, Linda. "A Noncanonical Binding Site in the EVH1 Domain of Vasodilator-Stimulated Phosphoprotein Regulates Its Interactions with the Proline Rich Region of Zyxin" Biochemistry 56, 4626-4636 (2017).
PubMed: 28783324

Assembly members:

Assembly members:
Y39E_EVH1, polymer, 121 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: pMW172

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Y39E_EVH1: GPGGRMSSETVICSSRATVM LYDDGNKRWLPAGTGPQAFS RVQIEHNPTANSFRVVGRKM QPDQQVVINCAIVRGVKYNQ ATPNFHQWRDARQVWGLNFG SKEDAAQFAAGMASALEALE G

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	123
1H chemical shifts	134

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Y39E EVH1	1

Entities:

Entity 1, Y39E EVH1 121 residues - Formula weight is not available

GPGGRMS is an artifact of cloning and 3cpro recognition, Y39E EVH1 is a mutation of Y39, and this contains the sequence from 2-115.

1

GLY

PRO

GLY

ARG

MET

SER

GLU

THR

2

VAL

ILE

CYS

SER

ARG

ALA

THR

VAL

MET

3

LEU

TYR

ASP

GLY

ASN

LYS

ARG

TRP

LEU

4

PRO

ALA

GLY

THR

GLY

PRO

GLN

ALA

PHE

SER

5

ARG

VAL

GLN

ILE

GLU

HIS

ASN

PRO

THR

ALA

6

ASN

SER

PHE

ARG

VAL

GLY

ARG

LYS

MET

7

GLN

PRO

ASP

GLN

VAL

ILE

ASN

CYS

8

ALA

ILE

VAL

ARG

GLY

VAL

LYS

TYR

ASN

GLN

9

ALA

THR

PRO

ASN

PHE

HIS

GLN

TRP

ARG

ASP

10

ALA

ARG

GLN

VAL

TRP

GLY

LEU

ASN

PHE

GLY

11

SER

LYS

GLU

ASP

ALA

GLN

PHE

ALA

12

GLY

MET

ALA

SER

ALA

LEU

GLU

ALA

LEU

GLU

13

GLY

Samples:

sample_1: Y39E EVH1, [U-99% 15N], 0.23 mM; potassium chloride 50 mM; potassium phosphate 20 mM; TCEP 1 mM; sodium azide 5 mM

sample_conditions_1: ionic strength: 94.76 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection

SPARKY, Goddard - data analysis

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

NMR spectrometers:

Varian INOVA 600 MHz

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