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 10278

Title: Solution structure of the PH domain of Pleckstrin homology domain-containing protein family B member 1 from mouse

Deposition date: 2008-12-15 Original release date: 2009-12-14

Authors: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PH domain of Pleckstrin homology domain-containing protein family B member 1 from mouse"  .

Assembly members:
PH domain, polymer, 130 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis   Vector: P050302-02

Entity Sequences (FASTA):
PH domain: GSSGSSGLVRGGWLWRQSSI LRRWKRNWFALWLDGTLGYY HDETAQDEEDRVVIHFNVRD IKVGQECQDVQPPEGRSRDG LLTVNLREGSRLHLCAETRD DAIAWKTALMEANSTPAPAG ATVPSGPSSG

Data sets:
Data typeCount
13C chemical shifts518
15N chemical shifts129
1H chemical shifts815

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PH domain1

Entities:

Entity 1, PH domain 130 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYLEUVALARG
2   GLYGLYTRPLEUTRPARGGLNSERSERILE
3   LEUARGARGTRPLYSARGASNTRPPHEALA
4   LEUTRPLEUASPGLYTHRLEUGLYTYRTYR
5   HISASPGLUTHRALAGLNASPGLUGLUASP
6   ARGVALVALILEHISPHEASNVALARGASP
7   ILELYSVALGLYGLNGLUCYSGLNASPVAL
8   GLNPROPROGLUGLYARGSERARGASPGLY
9   LEULEUTHRVALASNLEUARGGLUGLYSER
10   ARGLEUHISLEUCYSALAGLUTHRARGASP
11   ASPALAILEALATRPLYSTHRALALEUMET
12   GLUALAASNSERTHRPROALAPROALAGLY
13   ALATHRVALPROSERGLYPROSERSERGLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.12 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: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-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 v0.932, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

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