BMRB Entry 10245

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PDB ID: 1x6g
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR10245
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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:

Solution structures of the SH3 domain of human megakaryocyte-associated tyrosine-protein kinase.

Deposition date:

2008-10-24

Original release date:

2009-11-03

Authors:

Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structures of the SH3 domain of human megakaryocyte-associated tyrosine-protein kinase." .

Assembly members:

Assembly members:
SH3 domain, polymer, 81 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: cell free synthesis Vector: P041101-07

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH3 domain: GSSGSSGRMPTRRWAPGTQC ITKCEHTRPKPGELAFRKGD VVTILEACENKSWYRVKHHT SGQEGLLAAGALRERSGPSS G

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	313
15N chemical shifts	69
1H chemical shifts	488

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SH3 domain	1

Entities:

Entity 1, SH3 domain 81 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ARG

MET

PRO

2

THR

ARG

TRP

ALA

PRO

GLY

THR

GLN

CYS

3

ILE

THR

LYS

CYS

GLU

HIS

THR

ARG

PRO

LYS

4

PRO

GLY

GLU

LEU

ALA

PHE

ARG

LYS

GLY

ASP

5

VAL

THR

ILE

LEU

GLU

ALA

CYS

GLU

ASN

6

LYS

SER

TRP

TYR

ARG

VAL

LYS

HIS

THR

7

SER

GLY

GLN

GLU

GLY

LEU

ALA

GLY

8

ALA

LEU

ARG

GLU

ARG

SER

GLY

PRO

SER

9

GLY

Samples:

sample_1: SH3 domain, [U-13C; U-15N], 1 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: 296 K

Experiments:

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

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9295, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1X6G
GB	AAA16703