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 11499

Title: Solution structure of RNF146 WWE domain   PubMed: 23010590

Deposition date: 2012-05-08 Original release date: 2018-12-18

Authors: He, Fahu; Muto, Yutaka; Inoue, Makoto; Kigawa, Takanori; Mikako, Mikako; Terada, Takaho; Yokoyama, Shigeyuki

Citation: He, Fahu; Tsuda, Kengo; Takahashi, Mari; Kuwasako, Kanako; Terada, Takano; Shirouzu, Mikako; Watanabe, Satoru; Kigawa, Takanori; Kobayashi, Naohiro; Guntert, Peter; Yokoyama, Shigeyuki; Muto, Yutaka. "Structural insight into the interaction of ADP-ribose with the PARP WWE domains."  FEBS Lett. 586, 3858-3864 (2012).

Assembly members:
RNF146, polymer, 110 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: recombinant technology   Host organism: E. coli - cell free

Entity Sequences (FASTA):
RNF146: PSSGSSGFLDKPTLLSPEEL KAASRGNGEYAWYYEGRNGW WQYDERTSRELEDAFSKGKK NTEMLIAGFLYVADLENMVQ YRRNEHGRRRKIKRDIIDIP KKGVSGPSSG

Data sets:
Data typeCount
13C chemical shifts467
15N chemical shifts112
1H chemical shifts730

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WWE1

Entities:

Entity 1, WWE 110 residues - Formula weight is not available

1   PROSERSERGLYSERSERGLYPHELEUASP
2   LYSPROTHRLEULEUSERPROGLUGLULEU
3   LYSALAALASERARGGLYASNGLYGLUTYR
4   ALATRPTYRTYRGLUGLYARGASNGLYTRP
5   TRPGLNTYRASPGLUARGTHRSERARGGLU
6   LEUGLUASPALAPHESERLYSGLYLYSLYS
7   ASNTHRGLUMETLEUILEALAGLYPHELEU
8   TYRVALALAASPLEUGLUASNMETVALGLN
9   TYRARGARGASNGLUHISGLYARGARGARG
10   LYSILELYSARGASPILEILEASPILEPRO
11   LYSLYSGLYVALSERGLYPROSERSERGLY

Samples:

sample_1: WWE, [U-99% 13C; U-99% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; 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:

xwinnmr, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - chemical shift assignment

Kujira, N. Kobayashi - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 800 MHz

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