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 10253

Title: Solution structure of the PH domain of protein kinase C, D2 type from human

Deposition date: 2008-11-20 Original release date: 2009-11-20

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

Citation: Li, H.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PH domain of protein kinase C, D2 type from human"  .

Assembly members:
PH domain, polymer, 125 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   Vector: P041129-04

Entity Sequences (FASTA):
PH domain: GSSGSSGTLREGWVVHYSNK DTLRKRHYWRLDCKCITLFQ NNTTNRYYKEIPLSEILTVE SAQNFSLVPPGTNPHCFEIV TANATYFVGEMPGGTPGGPS GQGAEAARGWETAIRQALMS GPSSG

Data sets:
Data typeCount
13C chemical shifts498
15N chemical shifts120
1H chemical shifts802

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PH domain1

Entities:

Entity 1, PH domain 125 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRLEUARG
2   GLUGLYTRPVALVALHISTYRSERASNLYS
3   ASPTHRLEUARGLYSARGHISTYRTRPARG
4   LEUASPCYSLYSCYSILETHRLEUPHEGLN
5   ASNASNTHRTHRASNARGTYRTYRLYSGLU
6   ILEPROLEUSERGLUILELEUTHRVALGLU
7   SERALAGLNASNPHESERLEUVALPROPRO
8   GLYTHRASNPROHISCYSPHEGLUILEVAL
9   THRALAASNALATHRTYRPHEVALGLYGLU
10   METPROGLYGLYTHRPROGLYGLYPROSER
11   GLYGLNGLYALAGLUALAALAARGGLYTRP
12   GLUTHRALAILEARGGLNALALEUMETSER
13   GLYPROSERSERGLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.38 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 v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F - processing

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

Kujira v0.913, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAC11127 BAC11508 BAG53158 BAG62084 BAG64637
EMBL CAB43292
GB AAI56074 AAI56947 AAK01149 EAW57441 EHH59714
REF NP_001073349 NP_001073350 NP_001073351 NP_057541 XP_003915810
SP Q9BZL6
AlphaFold Q9BZL6

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