BMRB Entry 18569

Name: 13C, 15N and 1H backbone and sidechain assignments of the ENA-VASP homology 1 (EVH1) domain of the human vasodilator-stimulated phosphoprotein (VASP)
Published: 2012-07-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18569

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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:

13C, 15N and 1H backbone and sidechain assignments of the ENA-VASP homology 1 (EVH1) domain of the human vasodilator-stimulated phosphoprotein (VASP)

Deposition date:

2012-07-05

Original release date:

2012-07-18

Authors:

Ball, Linda; Peter, Schmieder; Jarchau, Thomas; Walter, Ulrich; Oschkinat, Hartmut

Citation:

Citation: Ball, Linda; Kuehne, Ronald; Hoffmann, Berit; Haefner, Angelika; Schmieder, Peter; Volkmer, Rudolf; Hof, Martin; Wahl, Martin; Schneider-Mergener, Jens; Walter, Ulrich; Oschkinat, Hartmut; Jarchau, Thomas. "Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity" EMBO J. 19, 4903-4914 (2000).
PubMed: 10990454

Assembly members:

Assembly members:
EVH1, polymer, 115 residues, 12732.3 Da.

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: pGEX-4T-1 (Pharmacia)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EVH1: MSETVICSSRATVMLYDDGN KRWLPAGTGPQAFSRVQIYH NPTANSFRVVGRKMQPDQQV VINCAIVRGVKYNQATPNFH QWRDARQVWGLNFGSKEDAA QFAAGMASALEALEG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- combined_NOESY_peak_list

Data type	Count
13C chemical shifts	371
15N chemical shifts	137
1H chemical shifts	789

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EVH1	1

Entities:

Entity 1, EVH1 115 residues - 12732.3 Da.

1

MET

SER

GLU

THR

VAL

ILE

CYS

SER

ARG

2

ALA

THR

VAL

MET

LEU

TYR

ASP

GLY

ASN

3

LYS

ARG

TRP

LEU

PRO

ALA

GLY

THR

GLY

PRO

4

GLN

ALA

PHE

SER

ARG

VAL

GLN

ILE

TYR

HIS

5

ASN

PRO

THR

ALA

ASN

SER

PHE

ARG

VAL

6

GLY

ARG

LYS

MET

GLN

PRO

ASP

GLN

VAL

7

VAL

ILE

ASN

CYS

ALA

ILE

VAL

ARG

GLY

VAL

8

LYS

TYR

ASN

GLN

ALA

THR

PRO

ASN

PHE

HIS

9

GLN

TRP

ARG

ASP

ALA

ARG

GLN

VAL

TRP

GLY

10

LEU

ASN

PHE

GLY

SER

LYS

GLU

ASP

ALA

11

GLN

PHE

ALA

GLY

MET

ALA

SER

ALA

LEU

12

GLU

ALA

LEU

GLU

GLY

Samples:

sample_1: EVH1, [U-100% 15N], 2 mM; D2O 10%; potassium phosphate, pH 6.0 20 mM; potassium chloride 50 mM; sodium azide 0.2 mM

sample_2: EVH1, [U-100% 13C; U-100% 15N], 1.3 mM; D2O 10%; potassium phosphate, pH 6.0 20 mM; potassium chloride 50 mM; sodium azide 0.2 mM

sample_3: EVH1, [U-100% 13C; U-100% 15N], 1.3 mM; D2O 100%; potassium phosphate, pH 6.0 20 mM; potassium chloride 50 mM; sodium azide 0.2 mM

sample_4: EVH1, [U-100% 15N], 2 mM; D2O 100%; potassium phosphate, pH 6.0 20 mM; potassium chloride 50 mM; sodium azide 0.2 mM

sample_conditions_1: ionic strength: 0.07 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

sample_conditions_2: ionic strength: 0.07 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

sample_conditions_3: ionic strength: 0.07 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

sample_conditions_4: ionic strength: 0.07 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D CBCANH	sample_2	isotropic	sample_conditions_2
3D C(CO)NH	sample_2	isotropic	sample_conditions_2
3D H(CCO)NH	sample_2	isotropic	sample_conditions_2
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_3
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_3
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
2D 1H-15N HSQC exchange series	sample_4	isotropic	sample_conditions_4
2D 15N T1 and T2 relaxation series	sample_1	isotropic	sample_conditions_1
2D 15N-1H heteronuclear NOE on and off	sample_1	isotropic	sample_conditions_1

Software:

AZARA v2.1, Boucher - peak picking, processing

xwinnmr v1.3, Bruker Biospin - collection, processing

ANSIG v3.3, Kraulis - data analysis, peak picking

CNS v0.9a, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMR spectrometers:

Bruker DRX 600 MHz
Bruker DMX 750 MHz

PDB	1EGX
UNP	P50552
SP	P50552
NCBI	GI:1718079
AlphaFold	Q93035