BMRB Entry 11529

Title:
Solution structure of a regulatory domain of meiosis inhibitor
Deposition date:
2013-07-04
Original release date:
2014-07-14
Authors:
Shoji, S; Muto, Y; Ikeda, M; He, F; Tsuda, K; Ohsawa, N; Akasaka, R; Terada, T; Wakiyama, M; Shirouzu, M; Yokoyama, S
Citation:

Citation: Shoji, S.; Muto, Y.; Ikeda, M.; He, F.; Tsuda, K.; Ohsawa, N.; Akasaka, R.; Terada, T.; Wakiyama, M.; Shirouzu, M.; Yokoyama, S.. "The zinc-binding region (ZBR) fragment of Emi2 can inhibit APC/C by targeting its association with the coactivator Cdc20 and UBE2C-mediated ubiquitylation"  FEBS OPEN BIO. 4, 689-703 (2014).
PubMed: 25161877

Assembly members:

Assembly members:
entity_1, polymer, 59 residues, 5830.834 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: PCR2.1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts225
15N chemical shifts50
1H chemical shifts341

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2ZINC ION_12
3ZINC ION_22

Entities:

Entity 1, entity_1 59 residues - 5830.834 Da.

The first 7 residues (GSSGSSG) are cloning artifacts.

1   GLYSERSERGLYSERSERGLYTHRASPGLU
2   ALALEULYSPROCYSPROARGCYSGLNSER
3   PROALALYSTYRGLNPROHISLYSLYSARG
4   GLYLEUCYSSERARGLEUALACYSGLYPHE
5   ASPPHECYSVALLEUCYSLEUCYSALATYR
6   HISGLYSERGLUASPCYSARGARGGLY

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.47 mM; H2O 90%; D2O 10%; dTris-HCl, [U-2H], 20 mM; NaCl 100 mM; d-DTT, [U-2H], 1 mM; ZnCl2 50 uM; NaN3 0.02%

sample_conditions_1: ionic strength: 120 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - data analysis

Kujira, Kobayashi, N - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAC26733
GB AAH26503 AAH82107 AAH98484 EDL08829 EDM16401
REF NP_001012117 NP_001074722 XP_006241597 XP_006520259 XP_006520260
SP Q66H04 Q8CDI2
AlphaFold Q8CDI2 Q66H04

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