BMRB Entry 26954

Name: Fyn SH3 V39V/N53P/V55L delta56
Published: 2017-02-06

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26954

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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:

Fyn SH3 V39V/N53P/V55L delta56

Deposition date:

2016-11-23

Original release date:

2017-02-06

Authors:

Libich, David; Tugarinov, Vitali; Ghirlando, Rodolfo; Clore, G. Marius

Citation:

Citation: Libich, David; Tugarinov, Vitali; Ghirlando, Rodolfo; Clore, G. Marius. "Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR" Biochemistry 56, 903-906 (2017).
PubMed: 28156097

Assembly members:

Assembly members:
VPLd56, polymer, 61 residues, Formula weight is not available

Natural source:

Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VPLd56: GAMVQISTLFEALYDYEART EDDLSFHKGEKFQILNSSEG DWWEVRSLTTGETGYIPSPY L

Data sets:

RDCs
- RDC_list_1
assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	171
15N chemical shifts	57
1H chemical shifts	57
residual dipolar couplings	43

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VPLd56	1

Entities:

Entity 1, VPLd56 61 residues - Formula weight is not available

1

GLY

ALA

MET

VAL

GLN

ILE

SER

THR

LEU

PHE

2

GLU

ALA

LEU

TYR

ASP

TYR

GLU

ALA

ARG

THR

3

GLU

ASP

LEU

SER

PHE

HIS

LYS

GLY

GLU

4

LYS

PHE

GLN

ILE

LEU

ASN

SER

GLU

GLY

5

ASP

TRP

GLU

VAL

ARG

SER

LEU

THR

6

GLY

GLU

THR

GLY

TYR

ILE

PRO

SER

PRO

TYR

7

LEU

Samples:

sample_1: VPLd56, [U-13C; U-15N], 0.1 mM; sodium phosphate 50 mM; EDTA 0.2 mM; sodium azide 0.05 % w/v

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, CCPN, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, processing

NMR spectrometers:

Bruker Avance 600 MHz

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