BMRB Entry 10039

Title:
Solution Structure of the Pleckstrin Homology Domain of Mouse Ethanol Decreased 4 Protein
Deposition date:
2006-11-09
Original release date:
2008-08-13
Authors:
Li, H.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Li, H.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the Pleckstrin Homology Domain of Mouse Ethanol Decreased 4 Protein"  .

Assembly members:

Assembly members:
Pleckstrin Homology domain, polymer, 109 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: cell free synthesis   Vector: P030212-46

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts489
15N chemical shifts112
1H chemical shifts744

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FYVE, RhoGEF and PH domain containing 6; ethanol decreased 41

Entities:

Entity 1, FYVE, RhoGEF and PH domain containing 6; ethanol decreased 4 109 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYSERTHRMET
2   SERGLYTYRLEUTYRARGSERLYSGLYSER
3   LYSLYSPROTRPLYSHISLEUTRPPHEVAL
4   ILELYSASNLYSVALLEUTYRTHRTYRALA
5   ALASERGLUASPVALALAALALEUGLUSER
6   GLNPROLEULEUGLYPHETHRVALTHRLEU
7   VALLYSASPGLUASNSERGLUSERLYSVAL
8   PHEGLNLEULEUHISLYSGLYMETVALPHE
9   TYRVALPHELYSALAASPASPALAHISSER
10   THRGLNARGTRPILEASPALAPHEGLNGLU
11   GLYTHRVALSERGLYPROSERSERGLY

Samples:

sample_1: Pleckstrin Homology domain, [U-13C, U-15N], 1.22 mM; Phosphate 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1not availablecondition_1
3D 15N-separated NOESYsample_1not availablecondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.897, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 600 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