BMRB Entry 11214

Name: Solution structure of the SH3 domain of Fyn-related kinase
Published: 2011-07-21

Click here to enlarge.

PDB ID: 2d8j
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11214
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of the SH3 domain of Fyn-related kinase

Deposition date:

2010-07-22

Original release date:

2011-07-21

Authors:

Qin, X.; Kurosaki, C.; Yoshida, M.; Hayashi, F.; Yokoyama, S.

Citation:

Citation: Qin, X.; Kurosaki, C.; Yoshida, M.; Hayashi, F.; Yokoyama, S.. "Solution structure of the SH3 domain of Fyn-related kinase" .

Assembly members:

Assembly members:
SH3 domain, polymer, 77 residues, Formula weight is not available

Natural source:

Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: P050425-22

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH3 domain: GSSGSSGQYFVALFDYQART AEDLSFRAGDKLQVLDTSHE GWWLARHLEKKGTGLGQQLQ GYIPSNYVAEDSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	322
15N chemical shifts	79
1H chemical shifts	488

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SH3 domain of Fyn-related kinase	1

Entities:

Entity 1, SH3 domain of Fyn-related kinase 77 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

GLN

TYR

PHE

2

VAL

ALA

LEU

PHE

ASP

TYR

GLN

ALA

ARG

THR

3

ALA

GLU

ASP

LEU

SER

PHE

ARG

ALA

GLY

ASP

4

LYS

LEU

GLN

VAL

LEU

ASP

THR

SER

HIS

GLU

5

GLY

TRP

LEU

ALA

ARG

HIS

LEU

GLU

LYS

6

LYS

GLY

THR

GLY

LEU

GLY

GLN

LEU

GLN

7

GLY

TYR

ILE

PRO

SER

ASN

TYR

VAL

ALA

GLU

8

ASP

SER

GLY

PRO

SER

GLY

Samples:

sample_1: SH3 domain, [U-13C; U-15N], 1.17 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

Delta NMR v4.3, JEOL - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9296, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

JEOL ECA 800 MHz

PDB	2D8J
DBJ	BAC26155 BAC35063 BAC36718 BAE38741
EMBL	CAA88658
GB	AAA65197 AAH07137 EDL04891 EDL04892 EDL04893
REF	NP_001153016 NP_034367 XP_006512597 XP_006512598 XP_006512599
SP	Q922K9
AlphaFold	Q922K9