BMRB Entry 19203
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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/BMR19203
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Title: NMR structure of RNA recognition motif 2 (RRM2) of Homo sapiens splicing factor, arginine/serine-rich 1
Deposition date: 2013-04-29 Original release date: 2013-05-13
Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of RNA recognition motif 2 (RRM2) of Homo sapiens splicing factor, arginine/serine-rich 1" Not known ., .-..
Assembly members:
RRM2, polymer, 90 residues, 10207.483 Da.
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):
RRM2: GAPRGRYGPPSRRSENRVVV
SGLPPSGSWQDLKDHMREAG
DVCYADVYRDGTGVVEFVRK
EDMTYAVRKLDNTKFRSHEG
ETAYIRVKVD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 281 |
| 15N chemical shifts | 87 |
| 1H chemical shifts | 593 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RRM2 of Homo sapiens splicing factor, arginine/serine-rich 1 | 1 |
Entities:
Entity 1, RRM2 of Homo sapiens splicing factor, arginine/serine-rich 1 90 residues - 10207.483 Da.
| 1 | GLY | ALA | PRO | ARG | GLY | ARG | TYR | GLY | PRO | PRO | |
| 2 | SER | ARG | ARG | SER | GLU | ASN | ARG | VAL | VAL | VAL | |
| 3 | SER | GLY | LEU | PRO | PRO | SER | GLY | SER | TRP | GLN | |
| 4 | ASP | LEU | LYS | ASP | HIS | MET | ARG | GLU | ALA | GLY | |
| 5 | ASP | VAL | CYS | TYR | ALA | ASP | VAL | TYR | ARG | ASP | |
| 6 | GLY | THR | GLY | VAL | VAL | GLU | PHE | VAL | ARG | LYS | |
| 7 | GLU | ASP | MET | THR | TYR | ALA | VAL | ARG | LYS | LEU | |
| 8 | ASP | ASN | THR | LYS | PHE | ARG | SER | HIS | GLU | GLY | |
| 9 | GLU | THR | ALA | TYR | ILE | ARG | VAL | LYS | VAL | ASP |
Samples:
sample_1: RRM2, [U-99% 13C; U-99% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 4D-HACANH-APSY | sample_1 | isotropic | sample_conditions_1 |
| 5D-CBCACONH-APSY | sample_1 | isotropic | sample_conditions_1 |
| 5D-HACACONH-APSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic with non-uniform sampling | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic with non-uniform sampling | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY with non-uniform sampling | sample_1 | isotropic | sample_conditions_1 |
Software:
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
j-UNIO, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
TOPSPIN v3.1, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 19248 |
| PDB | |
| DBJ | BAB93456 BAC37367 BAE29641 BAE88160 BAF82622 |
| EMBL | CAH92288 |
| GB | AAA03476 AAA35564 AAA35565 AAH10264 AAH42354 |
| REF | NP_001006919 NP_001033096 NP_001069862 NP_001071635 NP_001103022 |
| SP | Q07955 Q0VCY7 Q3YLA6 Q5R7H2 Q6DII2 |
| TPG | DAA19172 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts