BMRB Entry 27359

Name: Backbone (HN, N, HA) Resonance Assignment and 15N T1, T2 Relaxation Parameters for Abl1 SH3
Published: 2019-01-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27359

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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 (HN, N, HA) Resonance Assignment and 15N T1, T2 Relaxation Parameters for Abl1 SH3

Deposition date:

2018-01-15

Original release date:

2019-01-18

Authors:

Toke, Orsolya; Mero, Balazs; Radnai, Laszlo; Buday, Laszlo

Citation:

Citation: Mero, Balazs; Radnai, Laszlo; Gogl, Gergo; Toke, Orsolya; Leveles, Ibolya; Koprivanacz, Kitti; Szeder, Balint; Dulk, Metta; Kudlik, Gyongyi; Vas, Virag; Cserkaszky, Anna; Sipeki, Szabolcs; Nyitray, Laszlo; Vertessy, Beata; Buday, Laszlo. "Structural insights into the tyrosine phosphorylation-mediated inhibition of SH3 domain-ligand interactions" J. Biol. Chem. 294, 4608-4620 (2019).
PubMed: 30659095

Assembly members:

Assembly members:
Abl1_SH3, polymer, 58 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: modified pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Abl1_SH3: MNLFVALYDFVASGDNTLSI TKGEKLRVLGYNHNGEWCEA QTKNGQGWVPSNYITPVN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
15N chemical shifts	50
1H chemical shifts	105
T1 relaxation values	50
T2 relaxation values	50

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Src homology domain 3	1

Entities:

Entity 1, Src homology domain 3 58 residues - Formula weight is not available

1

MET

ASN

LEU

PHE

VAL

ALA

LEU

TYR

ASP

PHE

2

VAL

ALA

SER

GLY

ASP

ASN

THR

LEU

SER

ILE

3

THR

LYS

GLY

GLU

LYS

LEU

ARG

VAL

LEU

GLY

4

TYR

ASN

HIS

ASN

GLY

GLU

TRP

CYS

GLU

ALA

5

GLN

THR

LYS

ASN

GLY

GLN

GLY

TRP

VAL

PRO

6

SER

ASN

TYR

ILE

THR

PRO

VAL

ASN

Samples:

sample_1: Abl1 SH3, [U-15N], 1 mM; NaN3 3 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 70 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC T1 relaxation	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC T2 relaxation	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - data collection

CcpNMR, CCPN - data analysis

Felix, Accelrys - chemical shift assignment

NMR spectrometers:

Varian Varian NMR System 600 MHz

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