BMRB Entry 16920

Title:
NMR structure of human Tra2beta1 RRM in complex with AAGAAC RNA   PubMed: 21399644
Deposition date:
2010-05-10
Original release date:
2011-03-24
Authors:
Clery, Antoine; Benderska, Natalya; Jayne, Sandrine; Dominguez, Cyril; Stamm, Stefan; Allain, Frederic
Citation:

Citation: Clery, Antoine; Jayne, Sandrine; Benderska, Natalya; Dominguez, Cyril; Stamm, Stefan; Allain, Frederic H-T. "Molecular basis of purine-rich RNA recognition by the human SR-like protein Tra2-1."  Nat. Struct. Mol. Biol. 18, 443-450 (2011).

Assembly members:

Assembly members:
RNA, polymer, 6 residues, 1922.268 Da.
Tra2beta1, polymer, 95 residues, 10944.354 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: chemical synthesis

Experimental source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts280
15N chemical shifts92
1H chemical shifts653

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RNA (5'-R(*AP*AP*GP*AP*AP*C)-3')1
2Tra2beta12

Entities:

Entity 1, RNA (5'-R(*AP*AP*GP*AP*AP*C)-3') 6 residues - 1922.268 Da.

1   AAGAAC

Entity 2, Tra2beta1 95 residues - 10944.354 Da.

1   ARGHISVALGLYASNARGALAASNPROASP
2   PROASNCYSCYSLEUGLYVALPHEGLYLEU
3   SERLEUTYRTHRTHRGLUARGASPLEUARG
4   GLUVALPHESERLYSTYRGLYPROILEALA
5   ASPVALSERILEVALTYRASPGLNGLNSER
6   ARGARGSERARGGLYPHEALAPHEVALTYR
7   PHEGLUASNVALASPASPALALYSGLUALA
8   LYSGLUARGALAASNGLYMETGLULEUASP
9   GLYARGARGILEARGVALASPPHESERILE
10   THRLYSARGPROHIS

Samples:

sample_1: Tra2beta1, [U-15N], 0.8 ± 0.05 mM; Tra2beta1, [U-13C; U-15N], 0.8 ± 0.05 mM; RNA 0.8 ± 0.05 mM; NaH2PO4 20 mM; L-Arg 50 mM; L-Glu 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 5.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

AMBER v8, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY v3.113, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 11400 11409 11410 11411 11412 11413
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

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