BMRB Entry 11348

Title:
Solution structure of the NEUZ domain in KIAA1787 protein
Deposition date:
2010-09-07
Original release date:
2011-09-07
Authors:
He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.
Citation:

Citation: He, F.; Saito, K.; Kobayashi, N.; Harada, T.; Watanabe, S.; Kigawa, T.; Guntert, P.; Ohara, O.; Tanaka, A.; Unzai, S.; Muto, Y.; Yokoyama, S.. "Structural and functional characterization of the NHR1 domain of the Drosophila neuralized E3 ligase in the notch signaling pathway."  J. Mol. Biol. ., .-..

Assembly members:

Assembly members:
neuralized domain, polymer, 170 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P060508-08

Data sets:
Data typeCount
13C chemical shifts706
15N chemical shifts170
1H chemical shifts1129

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1neuralized domain1

Entities:

Entity 1, neuralized domain 170 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLULEUHIS
2   PROARGTHRGLYARGLEUVALSERLEUSER
3   ALACYSGLYARGTHRALAARGARGGLNGLN
4   PROGLYGLNGLUPHEASNHISGLYLEUVAL
5   LEUSERARGGLUPROLEUARGASPGLYARG
6   VALPHETHRVALARGILEASPARGLYSVAL
7   ASNSERTRPSERGLYSERILEGLUILEGLY
8   VALTHRALALEUASPPROSERVALLEUASP
9   PHEPROSERSERALATHRGLYLEULYSGLY
10   GLYSERTRPVALVALSERGLYCYSSERVAL
11   LEUARGASPGLYARGSERVALLEUGLUGLU
12   TYRGLYGLNASPLEUASPGLNLEUGLYGLU
13   GLYASPARGVALGLYVALGLUARGTHRVAL
14   ALAGLYGLULEUARGLEUTRPVALASNGLY
15   ARGASPCYSGLYVALALAALATHRGLYLEU
16   PROPROARGVALTRPALAVALVALASPLEU
17   TYRGLYLYSCYSTHRGLNILETHRVALLEU

Samples:

sample_1: neuralized domain, [U-13C; U-15N], 1.0 ± 0.1 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 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-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 v0.9819, Kobayashi N. - data analysis

CYANA v2.1, Guntert P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB

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