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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
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
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" .
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 Vector: SpeedET
Entity Sequences (FASTA):
RRM2: GAPRGRYGPPSRRSENRVVV
SGLPPSGSWQDLKDHMREAG
DVCYADVYRDGTGVVEFVRK
EDMTYAVRKLDNTKFRSHEG
ETAYIRVKVD
Data type | Count |
13C chemical shifts | 281 |
15N chemical shifts | 87 |
1H chemical shifts | 593 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RRM2 of Homo sapiens splicing factor, arginine/serine-rich 1 | 1 |
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 |
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
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 |
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
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 |
AlphaFold | Q07955 Q0VCY7 Q3YLA6 Q5R7H2 Q6DII2 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks