BMRB Entry 10214

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PDB ID:
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/BMR10214
MolProbity Validation Chart

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Title:
Solution structure 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 domain, polymer, 60 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: P061024-05

Entity Sequences (FASTA):

Entity Sequences (FASTA):
WW domain: GSSGSSGLDSELELPAGWEK IEDPVYGIYYVDHINRKTQY ENPVLEAKRKKQLESGPSSG

Data sets:
Data typeCount
13C chemical shifts253
15N chemical shifts57
1H chemical shifts369

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1WW domain1

Entities:

Entity 1, WW domain 60 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYLEUASPSER
2   GLULEUGLULEUPROALAGLYTRPGLULYS
3   ILEGLUASPPROVALTYRGLYILETYRTYR
4   VALASPHISILEASNARGLYSTHRGLNTYR
5   GLUASNPROVALLEUGLUALALYSARGLYS
6   LYSGLNLEUGLUSERGLYPROSERSERGLY

Samples:

sample_1: WW domain, [U-13C; U-15N], 1.0 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_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

Related Database Links:

PDB
DBJ BAA32002 BAD90296 BAE07184 BAE07185 BAE37498
EMBL CAH91366
GB AAB91995 AAC04844 AAH95943 AAI50821 AAI67863
REF NP_001025021 NP_001028229 NP_001076789 NP_001076790 NP_001125806
SP Q6RHR9 Q96QZ7
TPG DAA17112
AlphaFold Q6RHR9 Q96QZ7

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