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 10113

Title: Solution Structure of the Pleckstrin Homology Domain of Mouse APS

Deposition date: 2007-02-15 Original release date: 2008-08-15

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

Citation: Li, H.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the Pleckstrin Homology Domain of Mouse APS"  .

Assembly members:
Pleckstrin Homology Domain, polymer, 136 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: P030212-26

Entity Sequences (FASTA):
Pleckstrin Homology Domain: GSSGSSGNLAAKVELVDIQR EGALRFMVADDAASGPGGTA QWQKCRLLLRRAVAGERFRL EFFVPPKASRPKVSIPLSAI IEVRTTMPLEMPEKDNTFVL KVENGAEYILETIDSLQKHS WVADIQGCVDSGPSSG

Data sets:
Data typeCount
13C chemical shifts556
15N chemical shifts125
1H chemical shifts909

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH2 and PH domain-containing adapter protein APS1

Entities:

Entity 1, SH2 and PH domain-containing adapter protein APS 136 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYASNLEUALA
2   ALALYSVALGLULEUVALASPILEGLNARG
3   GLUGLYALALEUARGPHEMETVALALAASP
4   ASPALAALASERGLYPROGLYGLYTHRALA
5   GLNTRPGLNLYSCYSARGLEULEULEUARG
6   ARGALAVALALAGLYGLUARGPHEARGLEU
7   GLUPHEPHEVALPROPROLYSALASERARG
8   PROLYSVALSERILEPROLEUSERALAILE
9   ILEGLUVALARGTHRTHRMETPROLEUGLU
10   METPROGLULYSASPASNTHRPHEVALLEU
11   LYSVALGLUASNGLYALAGLUTYRILELEU
12   GLUTHRILEASPSERLEUGLNLYSHISSER
13   TRPVALALAASPILEGLNGLYCYSVALASP
14   SERGLYPROSERSERGLY

Samples:

sample_1: Pleckstrin Homology domain, [U-13C; U-15N], 1.23 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: 7.5; 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 v0.854, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAE24331 BAE24336
GB AAC64408 AAF37891 AAH57334 EDL19313 EDL19314
REF NP_001289867 NP_001289868 NP_061295 NP_446121 XP_005080443
SP Q9JID9 Q9Z200
AlphaFold Q9JID9 Q9Z200

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