BMRB Entry 10124

Title:
Solution structure of the second PDZ domain of human membrane associated guanylate kinase inverted-2 (MAGI-2)
Deposition date:
2007-04-02
Original release date:
2008-09-02
Authors:
Nameki, N.; Koshiba, S.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Nameki, N.; Koshiba, S.; Kigawa, T.; Yokoyama, S.. "Solution structure of the second PDZ domain of human membrane associated guanylate kinase inverted-2 (MAGI-2)"  .

Assembly members:

Assembly members:
PDZ domain, polymer, 96 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: P021030-28

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts95
1H chemical shifts614

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MEMBRANE ASSOCIATED GUANYLATE KINASE INVERTED-2 (MAGI-2)1

Entities:

Entity 1, MEMBRANE ASSOCIATED GUANYLATE KINASE INVERTED-2 (MAGI-2) 96 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLNALAGLU
2   LEUMETTHRLEUTHRILEVALLYSGLYALA
3   GLNGLYPHEGLYPHETHRILEALAASPSER
4   PROTHRGLYGLNARGVALLYSGLNILELEU
5   ASPILEGLNGLYCYSPROGLYLEUCYSGLU
6   GLYASPLEUILEVALGLUILEASNGLNGLN
7   ASNVALGLNASNLEUSERHISTHRGLUVAL
8   VALASPILELEULYSASPCYSPROILEGLY
9   SERGLUTHRSERLEUILEILEHISARGGLY
10   SERGLYPROSERSERGLY

Samples:

sample_1: PDZ domain, [U-13C; U-15N], 1.3 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 100 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 v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.811, Kobayashi, N. - data analysis

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

OPALp, Billeter, M., Guntert, P., Koradi, R. - refinement

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB

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