BMRB Entry 31140
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31140
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: Donaldson, L.. "NMR structure of the second RNA binding domain from Tetrahymena thermophila Mlp1" .
Assembly members:
entity_1, polymer, 138 residues, 15708.631 Da.
Natural source: Common Name: Tetrahymena thermophila Taxonomy ID: 312017 Superkingdom: Eukaryota Kingdom: not available Genus/species: Tetrahymena thermophila
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GSHMASMDPAEAAEKEAREA
EKKELINFYETFQPIIFSTA
CEQEGVANWRNITEALLKQH
NVHAPYCRFGKLEGNFALNK
DKTSQEVIDQLVQDGLQFGE
SKVTIKVSEGEALSKFWELH
GRHYNGVMELKKKEVNQT
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 518 |
| 15N chemical shifts | 137 |
| 1H chemical shifts | 784 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 138 residues - 15708.631 Da.
| 1 | GLY | SER | HIS | MET | ALA | SER | MET | ASP | PRO | ALA | ||||
| 2 | GLU | ALA | ALA | GLU | LYS | GLU | ALA | ARG | GLU | ALA | ||||
| 3 | GLU | LYS | LYS | GLU | LEU | ILE | ASN | PHE | TYR | GLU | ||||
| 4 | THR | PHE | GLN | PRO | ILE | ILE | PHE | SER | THR | ALA | ||||
| 5 | CYS | GLU | GLN | GLU | GLY | VAL | ALA | ASN | TRP | ARG | ||||
| 6 | ASN | ILE | THR | GLU | ALA | LEU | LEU | LYS | GLN | HIS | ||||
| 7 | ASN | VAL | HIS | ALA | PRO | TYR | CYS | ARG | PHE | GLY | ||||
| 8 | LYS | LEU | GLU | GLY | ASN | PHE | ALA | LEU | ASN | LYS | ||||
| 9 | ASP | LYS | THR | SER | GLN | GLU | VAL | ILE | ASP | GLN | ||||
| 10 | LEU | VAL | GLN | ASP | GLY | LEU | GLN | PHE | GLY | GLU | ||||
| 11 | SER | LYS | VAL | THR | ILE | LYS | VAL | SER | GLU | GLY | ||||
| 12 | GLU | ALA | LEU | SER | LYS | PHE | TRP | GLU | LEU | HIS | ||||
| 13 | GLY | ARG | HIS | TYR | ASN | GLY | VAL | MET | GLU | LEU | ||||
| 14 | LYS | LYS | LYS | GLU | VAL | ASN | GLN | THR |
Samples:
sample_1: sodium phosphate 20 mM; sodium chloride 135 mM; protein, [U-99% 13C; U-99% 15N], 0.8 mM
sample_conditions_1: ionic strength: 155 mM; pH: 7.4; 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 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 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 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CcpNmr Analysis v2.5.2, CCPN - data analysis
CYANA v3, Guntert, Mumenthaler and Wuthrich - structure calculation
Rosetta, Baker laboratory / RosettaCommons.org - refinement
TopSpin v3.5p17, Bruker Biospin - collection
NMRtist, Klukowski, P., Riek, R. & Guntert, P. - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks