BMRB Entry 11563

Title:
Refined solution structure of the first RNA recognition motif domain in CPEB3
Deposition date:
2014-04-15
Original release date:
2016-07-13
Authors:
Tsuda, Kengo; Kuwasako, Kanako; Nagata, Takashi; Takahashi, Mari; Kigawa, Takanori; Kobayashi, Naohiro; Guntert, Peter; Shirouzu, Mikako; Yokoyama, Shigeyuki; Muto, Yutaka
Citation:

Citation: Tsuda, Kengo; Kuwasako, Kanako; Nagata, Takashi; Takahashi, Mari; Kigawa, Takanori; Kobayashi, Naohiro; Guntert, Peter; Shirouzu, Mikako; Yokoyama, Shigeyuki; Muto, Yutaka. "Novel RNA recognition motif domain in the cytoplasmic polyadenylation element binding protein 3"  Proteins 82, 2879-2886 (2014).
PubMed: 5066254

Assembly members:

Assembly members:
The_first_RNA_recognition_motif_domain, polymer, 114 residues, 12428.944 Da.

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: pCR2.1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts493
15N chemical shifts103
1H chemical shifts745

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1The_first_RNA_recognition_motif_domain1

Entities:

Entity 1, The_first_RNA_recognition_motif_domain 114 residues - 12428.944 Da.

1   GLYSERSERGLYSERSERGLYSERARGLYS
2   VALPHEVALGLYGLYLEUPROPROASPILE
3   ASPGLUASPGLUILETHRALASERPHEARG
4   ARGPHEGLYPROLEUVALVALASPTRPPRO
5   HISLYSALAGLUSERLYSSERTYRPHEPRO
6   PROLYSGLYTYRALAPHELEULEUPHEGLN
7   GLUGLUSERSERVALGLNALALEUILEASP
8   ALACYSLEUGLUGLUASPGLYLYSLEUTYR
9   LEUCYSVALSERSERPROTHRILELYSASP
10   LYSPROVALGLNILEARGPROTRPASNLEU
11   SERASPSERASPPHEVALMETASPSERGLY
12   PROSERSERGLY

Samples:

sample_1: The_first_RNA_recognition_motif_domain, [U-100% 13C; U-100% 15N], 1.06 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
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection

NMRPipe v20030801, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.0.4, Johnson, One Moon Scientific - data analysis

Kujira v0.9843, Kobayashi, N - data analysis

CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

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