BMRB Entry 18327

Name: Solution structure of the atypical SH3 domain of DOCK180
Published: 2013-01-03

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18327

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 atypical SH3 domain of DOCK180

Deposition date:

2012-03-14

Original release date:

2013-01-03

Authors:

Liu, Xiangrong

Citation:

Citation: Liu, Xiangrong; Li, Fengjuan; Pan, Zhu; Wang, Wenning; Wen, Wenyu. "Solution structure of the SH3 domain of DOCK180." Proteins 81, 906-910 (2013).
PubMed: 23239367

Assembly members:

Assembly members:
SH3, polymer, 74 residues, 8659.928 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH3: MTRWVPTKREEKYGVAFYNY DARGADELSLQIGDTVHILE TYEGWYRGYTLRKKSKKGIF PASYIHLKEAIVEG

Data sets:

assigned_chemical_shifts
- assigned_chem_shif

Data type	Count
13C chemical shifts	177
15N chemical shifts	57
1H chemical shifts	383

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	atypical SH3 domain of DOCK180	1

Entities:

Entity 1, atypical SH3 domain of DOCK180 74 residues - 8659.928 Da.

1

MET

THR

ARG

TRP

VAL

PRO

THR

LYS

ARG

GLU

2

GLU

LYS

TYR

GLY

VAL

ALA

PHE

TYR

ASN

TYR

3

ASP

ALA

ARG

GLY

ALA

ASP

GLU

LEU

SER

LEU

4

GLN

ILE

GLY

ASP

THR

VAL

HIS

ILE

LEU

GLU

5

THR

TYR

GLU

GLY

TRP

TYR

ARG

GLY

TYR

THR

6

LEU

ARG

LYS

SER

LYS

GLY

ILE

PHE

7

PRO

ALA

SER

TYR

ILE

HIS

LEU

LYS

GLU

ALA

8

ILE

VAL

GLU

GLY

Samples:

SH3-1: SH3, [U-100% 15N], 0.4 mM; PBS 50 mM; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

SH3-2: SH3, [U-100% 13C; U-100% 15N], 0.4 mM; PBS 50 mM; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

SH3-3: SH3, [U-100% 13C; U-100% 15N], 0.4 mM; PBS 50 mM; DTT, [U-100% 2H], 1 mM; EDTA 1 mM; D2O 100%

SH3-4: SH3 0.4 mM; PBS 50 mM; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_condition: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	SH3-1	isotropic	sample_condition
3D 1H-15N NOESY	SH3-1	isotropic	sample_condition
2D 1H-15N HSQC	SH3-2	isotropic	sample_condition
3D CBCA(CO)NH	SH3-2	isotropic	sample_condition
3D HNCACB	SH3-2	isotropic	sample_condition
3D HNCO	SH3-2	isotropic	sample_condition
2D 1H-13C HSQC	SH3-3	isotropic	sample_condition
3D 1H-13C NOESY	SH3-3	isotropic	sample_condition
2D 1H-1H NOESY	SH3-4	anisotropic	sample_condition
2D 1H-1H TOCSY	SH3-4	anisotropic	sample_condition

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

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

SPARKY, Goddard - peak picking

PIPP, Garrett - chemical shift assignment

NMR spectrometers:

Varian VNMRS 600 MHz

BMRB	18832
PDB	2M0Y
DBJ	BAA09454 BAC38645 BAE24599
GB	AAI46858 EDL17793 EDL17794 EDL17796 EDL17797
REF	NP_001028592 NP_001137330 NP_001277152 NP_001371 XP_001089124
SP	Q14185 Q8BUR4
TPG	DAA14676
AlphaFold	Q14185 Q8BUR4