BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 10215

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)   PubMed: 18562638

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: 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).

Assembly members:
WW domain1, polymer, 49 residues, Formula weight is not available

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: cell free synthesis

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

Data sets:
Data typeCount
13C chemical shifts198
15N chemical shifts44
1H chemical shifts294

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1WW domain11

Entities:

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

1   GLYSERSERGLYSERSERGLYLEUASPSER
2   GLULEUGLULEUPROALAGLYTRPGLULYS
3   ILEGLUASPPROVALTYRGLYILETYRTYR
4   VALASPHISILEASNARGLYSTHRGLNTYR
5   GLUASNPROSERGLYPROSERSERGLY

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:

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 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