BMRB Entry 34155
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34155
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Title: NMR solution structure of U11/U12 65K protein's C-terminal RRM domain (381-516) PubMed: 29255062
Deposition date: 2017-06-28 Original release date: 2018-01-23
Authors: Norppa, A.; Kauppala, T.; Heikkinen, H.; Verma, B.; Iwai, H.; Frilander, M.
Citation: Norppa, A.; Kauppala, T.; Heikkinen, H.; Verma, B.; Iwai, H.; Frilander, M.. "Mutations in the U11/U12-65K protein associated with isolated growth hormone deficiency lead to structural destabilization and impaired binding of U12 snRNA." RNA 24, 396-409 (2018).
Assembly members:
entity_1, polymer, 136 residues, 15796.292 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_1: SDEMPSECISRRELEKGRIS
REEMETLSVFRSYEPGEPNC
RIYVKNLAKHVQEKDLKYIF
GRYVDFSSETQRIMFDIRLM
KEGRMKGQAFIGLPNEKAAA
KALKEANGYVLFGKPMVVQF
ARSARPKQDPKEGKRK
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 607 |
| 15N chemical shifts | 139 |
| 1H chemical shifts | 968 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 136 residues - 15796.292 Da.
| 1 | SER | ASP | GLU | MET | PRO | SER | GLU | CYS | ILE | SER | ||||
| 2 | ARG | ARG | GLU | LEU | GLU | LYS | GLY | ARG | ILE | SER | ||||
| 3 | ARG | GLU | GLU | MET | GLU | THR | LEU | SER | VAL | PHE | ||||
| 4 | ARG | SER | TYR | GLU | PRO | GLY | GLU | PRO | ASN | CYS | ||||
| 5 | ARG | ILE | TYR | VAL | LYS | ASN | LEU | ALA | LYS | HIS | ||||
| 6 | VAL | GLN | GLU | LYS | ASP | LEU | LYS | TYR | ILE | PHE | ||||
| 7 | GLY | ARG | TYR | VAL | ASP | PHE | SER | SER | GLU | THR | ||||
| 8 | GLN | ARG | ILE | MET | PHE | ASP | ILE | ARG | LEU | MET | ||||
| 9 | LYS | GLU | GLY | ARG | MET | LYS | GLY | GLN | ALA | PHE | ||||
| 10 | ILE | GLY | LEU | PRO | ASN | GLU | LYS | ALA | ALA | ALA | ||||
| 11 | LYS | ALA | LEU | LYS | GLU | ALA | ASN | GLY | TYR | VAL | ||||
| 12 | LEU | PHE | GLY | LYS | PRO | MET | VAL | VAL | GLN | PHE | ||||
| 13 | ALA | ARG | SER | ALA | ARG | PRO | LYS | GLN | ASP | PRO | ||||
| 14 | LYS | GLU | GLY | LYS | ARG | LYS |
Samples:
sample_1: U11/U12 65K C-terminal RRM, [U-100% 13C; U-100% 15N], 0.2 mM
sample_conditions_1: ionic strength: 20.0 mM; pH: 6.0; pressure: 1 atm; temperature: 303.3 K
sample_conditions_2: ionic strength: 20.0 mM; pH: 6.0; pressure: 1 atm; temperature: 298.3 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 HNCA | sample_1 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_2 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_2 |
| HNCO | sample_1 | isotropic | sample_conditions_1 |
| HN(CA)CO | sample_1 | isotropic | sample_conditions_2 |
| CON | sample_1 | isotropic | sample_conditions_2 |
| CACO | sample_1 | isotropic | sample_conditions_2 |
| (H)CCCONH | sample_1 | isotropic | sample_conditions_1 |
| H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| HBHACONH | sample_1 | isotropic | sample_conditions_1 |
| HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| CBCGCDHD | sample_1 | isotropic | sample_conditions_1 |
| CBCGCDCEHE | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
AMBER v14.0, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
CcpNMR v2.4.1, CCPN - chemical shift assignment
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation
TALOS vN, Cornilescu, Delaglio and Bax - structure calculation
PSVS v1.5, Bhattacharya and Montelione - data analysis
TOPSPIN v3.2, Bruker Biospin - processing
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- Bruker AvanceIII 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts