BMRB Entry 11412

Title:
Assigned chemical shifts of RNA binding domain in human Tra2 beta protein in complex with RNA (UCAAU)
Deposition date:
2010-09-09
Original release date:
2011-09-08
Authors:
Tsuda, K.; Kuwasako, K.; Takahashi, M.; Someya, T.; Inoue, M.; Kigawa, T.; Terada, T.; Shirouzu, M.; Sugano, S.; Muto, Y.; Yokoyama, S.
Citation:

Citation: Tsuda, K.; Kuwasako, K.; Someya, T.; Takahashi, M.; He, F.; Inoue, M.; Harada, T.; Watanabe, S.; Terada, T.; Kobayashi, N.; Shirouzu, M.; Kigawa, T.; Tanaka, A.; Sugano, S.; Guntert, P.; Yokoyama, S.; Muto, Y.. "Solution structure of RNA binding domain in human Tra2 beta protein in complex with RNA (GAAGAA)"  .

Assembly members:

Assembly members:
RNA recognition motif, polymer, 99 residues, Formula weight is not available
RNA, polymer, 6 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: P040517-05

Entity Sequences (FASTA):

Data sets:
Data typeCount
15N chemical shifts78
1H chemical shifts78

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RNA recognition motif1
2RNA2

Entities:

Entity 1, RNA recognition motif 99 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYASNARGALA
2   ASNPROASPPROASNCYSCYSLEUGLYVAL
3   PHEGLYLEUSERLEUTYRTHRTHRGLUARG
4   ASPLEUARGGLUVALPHESERLYSTYRGLY
5   PROILEALAASPVALSERILEVALTYRASP
6   GLNGLNSERARGARGSERARGGLYPHEALA
7   PHEVALTYRPHEGLUASNVALASPASPALA
8   LYSGLUALALYSGLUARGALAASNGLYMET
9   GLULEUASPGLYARGARGILEARGVALASP
10   PHESERILETHRLYSARGPROHISTHR

Entity 2, RNA 6 residues - Formula weight is not available

1   UCAAU

Samples:

sample_1: Human transformer 2 beta-1, [U-13C; U-15N], 0.2 mM; RNA 0.2 mM; salt 100 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropiccondition_1
2D 1H-1H NOESYsample_1isotropiccondition_1

Software:

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, Kollm - refinement

xwinnmr v3.6, Bruker, Biospin - collection

NMRPipe v20060801, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer, and, Bax - processing

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

Kujira v0.9843, N. Kobayashi - data analysis

CYANA v2.1, Guntert, Mumenthaler, and, Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 11400 11409 11410 11411 16920
PDB
DBJ BAA08556 BAC05256 BAC33819 BAD92445 BAE88784
EMBL CAA56518 CAH18071 CAH90742
GB AAB08701 AAC28242 AAD19277 AAD19278 AAG35783
REF NP_001006878 NP_001029948 NP_001070689 NP_001125414 NP_001230808
SP P62995 P62996 P62997 Q3ZBT6
TPG DAA33375
AlphaFold P62996 Q3ZBT6 P62997 P62995

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