BMRB Entry 19792
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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/BMR19792
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Title: NMR structure of the RRM domain of RBMX from homo sapiens
Deposition date: 2014-02-14 Original release date: 2014-03-10
Authors: Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Serrano, Pedro; Wuthrich, Kurt; Geralt, Michael; Dutta, Samit. "NMR structure of the first RRM domain of the protein RBM39 from homo sapiens" Not known ., .-..
Assembly members:
entity, polymer, 92 residues, 10093.535 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):
entity: GHMVEADRPGKLFIGGLNTE
TNEKALEAVFGKYGRIVEVL
LMKDRETNKSRGFAFVTFES
PADAKDAARDMNGKSLDGKA
IKVEQATKPSFE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 366 |
| 15N chemical shifts | 92 |
| 1H chemical shifts | 581 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RBMX | 1 |
Entities:
Entity 1, RBMX 92 residues - 10093.535 Da.
| 1 | GLY | HIS | MET | VAL | GLU | ALA | ASP | ARG | PRO | GLY | ||||
| 2 | LYS | LEU | PHE | ILE | GLY | GLY | LEU | ASN | THR | GLU | ||||
| 3 | THR | ASN | GLU | LYS | ALA | LEU | GLU | ALA | VAL | PHE | ||||
| 4 | GLY | LYS | TYR | GLY | ARG | ILE | VAL | GLU | VAL | LEU | ||||
| 5 | LEU | MET | LYS | ASP | ARG | GLU | THR | ASN | LYS | SER | ||||
| 6 | ARG | GLY | PHE | ALA | PHE | VAL | THR | PHE | GLU | SER | ||||
| 7 | PRO | ALA | ASP | ALA | LYS | ASP | ALA | ALA | ARG | ASP | ||||
| 8 | MET | ASN | GLY | LYS | SER | LEU | ASP | GLY | LYS | ALA | ||||
| 9 | ILE | LYS | VAL | GLU | GLN | ALA | THR | LYS | PRO | SER | ||||
| 10 | PHE | GLU |
Samples:
sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 100 mM; sodium acetate, [U-99% 2H], 10 mM; sodium azide 5 mM; DTT 2 mM
sample_conditions_1: ionic strength: 0.220 M; pH: 5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY HACACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert P., Luginbuhl, Guntert, Billeter and Wuthrich - refinement
TOPSPIN, Bruker Biospin - collection, processing
CAra, Keller and Wuthrich - chemical shift assignment, data analysis
UNIO, UNIO Herrmann and Wuthrich - chemical shift assignment, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 19382 |
| PDB | |
| DBJ | BAC31099 BAE00972 BAE22448 BAE37998 BAF62396 |
| EMBL | CAA80599 CAB51361 CAB51362 CAG31684 CAI46148 |
| GB | AAH03710 AAH06550 AAH07435 AAH11441 AAH12942 |
| PIR | S41766 |
| REF | NP_001020834 NP_001073196 NP_001100890 NP_001128678 NP_001156008 |
| SP | A5A6M3 D4AE41 P38159 P84586 Q4R7F0 |
| TPG | DAA13328 DAA13329 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts