BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 10058

Title: Solution Structure of the PICOT homology 2 domain of the mouse PKC-interacting cousin of thioredoxin protein

Deposition date: 2006-11-29 Original release date: 2008-08-13

Authors: Miyamoto, K.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Miyamoto, K.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the PICOT homology 2 domain of the mouse PKC-interacting cousin of thioredoxin protein"  . ., .-..

Assembly members:
PICOT homology 2 domain, polymer, 109 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

Entity Sequences (FASTA):
PICOT homology 2 domain: GSSGSSGLKVLTNKASVMLF MKGNKQEAKCGFSKQILEIL NSTGVEYETFDILEDEEVRQ GLKTFSNWPTYPQLYVRGDL VGGLDIVKELKDNGELLPIL KGESGPSSG

Data sets:
Data typeCount
13C chemical shifts452
15N chemical shifts101
1H chemical shifts724

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Thioredoxin-like protein 21

Entities:

Entity 1, Thioredoxin-like protein 2 109 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYLEULYSVAL
2   LEUTHRASNLYSALASERVALMETLEUPHE
3   METLYSGLYASNLYSGLNGLUALALYSCYS
4   GLYPHESERLYSGLNILELEUGLUILELEU
5   ASNSERTHRGLYVALGLUTYRGLUTHRPHE
6   ASPILELEUGLUASPGLUGLUVALARGGLN
7   GLYLEULYSTHRPHESERASNTRPPROTHR
8   TYRPROGLNLEUTYRVALARGGLYASPLEU
9   VALGLYGLYLEUASPILEVALLYSGLULEU
10   LYSASPASNGLYGLULEULEUPROILELEU
11   LYSGLYGLUSERGLYPROSERSERGLY

Samples:

sample_1: PICOT homology 2 domain, [U-13C; U-15N], 0.65 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: 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 v3.5, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.8996, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 600 MHz

Related Database Links:

PDB

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