BMRB Entry 15543

Title:
Solution conformation of RNA-bound NELF-E RRM
Deposition date:
2007-11-02
Original release date:
2008-11-03
Authors:
Jampani, N. Rao; Schweimer, Kristian; Wenzel, Sabine; Woehrl, Birgitta; Roesch, Paul
Citation:

Citation: Jampani, N. Rao; Schweimer, Kristian; Wenzel, Sabine; Woehrl, Birgitta; Roesch, Paul. "RRMNELF-E RRM Undergoes Major Structural Changes in Flexible Protein Regions on Target RNA Binding"  Biochemistry 47, 3756-3761 (2008).
PubMed: 18303858

Assembly members:

Assembly members:
rna_bound_nelfe-rrm, polymer, 121 residues, 9494.886 Da.
TAR(49-57), polymer, 9 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: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Data sets:
Data typeCount
13C chemical shifts224
15N chemical shifts91
1H chemical shifts510

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1nelfe-rrm1
2TAR(49-57)2

Entities:

Entity 1, nelfe-rrm 121 residues - 9494.886 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLYPROPHEARGARGSERASPSERPHE
4   PROGLUARGARGALAPROARGLYSGLYASN
5   THRLEUTYRVALTYRGLYGLUASPMETTHR
6   PROTHRLEULEUARGGLYALAPHESERPRO
7   PHEGLYASNILEILEASPLEUSERMETASP
8   PROPROARGASNCYSALAPHEVALTHRTYR
9   GLULYSMETGLUSERALAASPGLNALAVAL
10   ALAGLULEUASNGLYTHRGLNVALGLUSER
11   VALGLNLEULYSVALASNILEALAARGLYS
12   GLNPROMETLEUASPALAALATHRGLYLYS
13   SER

Entity 2, TAR(49-57) 9 residues - Formula weight is not available

1   UAGGGAACC

Samples:

sample_1: rna bound nelfe-rrm, [U-98% 13C; U-98% 15N], 0.4 mM; TAR(49-57) 0.8 mM

sample_conditions_1: pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB28206 BAE20893 BAE27605 BAG62393 BAG63891
EMBL CAA34231 CAE83971 CAN87695 CAN87696
GB AAA36308 AAA39680 AAB67979 AAC37523 AAC84161
REF NP_001039328 NP_001039329 NP_001069672 NP_001095295 NP_001159373
SP P18615 P19426 Q0V898
TPG DAA16391
AlphaFold Q0V898 P18615 P19426

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