BMRB Entry 10215

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PDB ID: 2zaj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR10215
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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 structure of the short-isoform of the second WW domain from the human membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 (MAGI-1)

Deposition date:

2008-04-22

Original release date:

2009-04-04

Authors:

Ohnishi, S.; Tochio, N.; Tomizawa, T.; Akasaka, R.; Harada, T.; Seki, E.; Sato, M.; Watanabe, S.; Fujikura, Y.; Koshiba, S.; Terada, T.; Shirouzu, M.; Tanaka, A.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Ohnishi, S.; Tochio, N.; Tomizawa, T.; Akasaka, R.; Harada, T.; Seki, E.; Sato, M.; Watanabe, S.; Fujikura, Y.; Koshiba, S.; Terada, T.; Shirouzu, M.; Tanaka, A.; Kigawa, T.; Yokoyama, S.. "Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily." Protein Sci. 17, 1531-1541 (2008).
PubMed: 18562638

Assembly members:

Assembly members:
WW domain1, polymer, 49 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: P070305-17

Entity Sequences (FASTA):

Entity Sequences (FASTA):
WW domain1: GSSGSSGLDSELELPAGWEK IEDPVYGIYYVDHINRKTQY ENPSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	198
15N chemical shifts	44
1H chemical shifts	294

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	WW domain1	1

Entities:

Entity 1, WW domain1 49 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

LEU

ASP

SER

2

GLU

LEU

GLU

LEU

PRO

ALA

GLY

TRP

GLU

LYS

3

ILE

GLU

ASP

PRO

VAL

TYR

GLY

ILE

TYR

4

VAL

ASP

HIS

ILE

ASN

ARG

LYS

THR

GLN

TYR

5

GLU

ASN

PRO

SER

GLY

PRO

SER

GLY

Samples:

sample_1: WW domain1, [U-13C; U-15N], 0.7 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 13C-separated NOESY	sample_1	isotropic	condition_1
3D 15N-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.9820, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2ZAJ
DBJ	BAA32002 BAD90296 BAE37498 BAF82492 BAI46753
EMBL	CAH91366
GB	AAC04844 AAH95943 AAI50821 AAI67863 AAK94064
REF	NP_001025021 NP_001025216 NP_001028229 NP_001076789 NP_001076790
SP	Q4L1J4 Q6RHR9 Q96QZ7
TPG	DAA17112
AlphaFold	Q4L1J4 Q6RHR9 Q96QZ7