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 10312

Title: Solution structure of the PH domain of Protein kinase C, nu type from human

Deposition date: 2009-03-11 Original release date: 2010-03-11

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 Protein kinase C, nu type from human"  .

Assembly members:
PH domain, polymer, 129 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: P050711-24

Entity Sequences (FASTA):
PH domain: GSSGSSGMVKEGWMVHYTSR DNLRKRHYWRLDSKCLTLFQ NESGSKYYKEIPLSEILRIS SPRDFTNISQGSNPHCFEII TDTMVYFVGENNGDSSHNPV LAATGVGLDVAQSWEKAIRQ ALMSGPSSG

Data sets:
Data typeCount
13C chemical shifts545
15N chemical shifts131
1H chemical shifts844

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PH domain1

Entities:

Entity 1, PH domain 129 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETVALLYS
2   GLUGLYTRPMETVALHISTYRTHRSERARG
3   ASPASNLEUARGLYSARGHISTYRTRPARG
4   LEUASPSERLYSCYSLEUTHRLEUPHEGLN
5   ASNGLUSERGLYSERLYSTYRTYRLYSGLU
6   ILEPROLEUSERGLUILELEUARGILESER
7   SERPROARGASPPHETHRASNILESERGLN
8   GLYSERASNPROHISCYSPHEGLUILEILE
9   THRASPTHRMETVALTYRPHEVALGLYGLU
10   ASNASNGLYASPSERSERHISASNPROVAL
11   LEUALAALATHRGLYVALGLYLEUASPVAL
12   ALAGLNSERTRPGLULYSALAILEARGGLN
13   ALALEUMETSERGLYPROSERSERGLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 0.42 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

Related Database Links:

PDB
DBJ BAA36514 BAG51354
GB AAH30706 AAY14817 ADZ15743 AIC62718 EAX00398
REF NP_001244477 NP_005804 XP_002757895 XP_002812168 XP_003125283
SP O94806
AlphaFold O94806

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