BMRB Entry 15543
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15543
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Title: Solution conformation of RNA-bound NELF-E RRM PubMed: 18303858
Deposition date: 2007-11-02 Original release date: 2008-11-03
Authors: Jampani, N. Rao; Schweimer, Kristian; Wenzel, Sabine; Woehrl, Birgitta; Roesch, Paul
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).
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: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
rna_bound_nelfe-rrm: MGSSHHHHHHSSGLVPRGSH
MGPFRRSDSFPERRAPRKGN
TLYVYGEDMTPTLLRGAFSP
FGNIIDLSMDPPRNCAFVTY
EKMESADQAVAELNGTQVES
VQLKVNIARKQPMLDAATGK
S
TAR(49-57): UAGGGAACC
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 224 |
15N chemical shifts | 91 |
1H chemical shifts | 510 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | nelfe-rrm | 1 |
2 | TAR(49-57) | 2 |
Entities:
Entity 1, nelfe-rrm 121 residues - 9494.886 Da.
1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
3 | MET | GLY | PRO | PHE | ARG | ARG | SER | ASP | SER | PHE | ||||
4 | PRO | GLU | ARG | ARG | ALA | PRO | ARG | LYS | GLY | ASN | ||||
5 | THR | LEU | TYR | VAL | TYR | GLY | GLU | ASP | MET | THR | ||||
6 | PRO | THR | LEU | LEU | ARG | GLY | ALA | PHE | SER | PRO | ||||
7 | PHE | GLY | ASN | ILE | ILE | ASP | LEU | SER | MET | ASP | ||||
8 | PRO | PRO | ARG | ASN | CYS | ALA | PHE | VAL | THR | TYR | ||||
9 | GLU | LYS | MET | GLU | SER | ALA | ASP | GLN | ALA | VAL | ||||
10 | ALA | GLU | LEU | ASN | GLY | THR | GLN | VAL | GLU | SER | ||||
11 | VAL | GLN | LEU | LYS | VAL | ASN | ILE | ALA | ARG | LYS | ||||
12 | GLN | PRO | MET | LEU | ASP | ALA | ALA | THR | GLY | LYS | ||||
13 | SER |
Entity 2, TAR(49-57) 9 residues - Formula weight is not available
1 | U | A | G | G | G | A | A | C | C |
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_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 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts