BMRB Entry 30374
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30374
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: Rajagopal, P.; Klevit, R.. "HSPB5 alpha-crystallin domain mutant R120G-ACD" .
Assembly members:
entity_1, polymer, 89 residues, 10099.370 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: GLSEMRLEKDRFSVNLDVKH
FSPEELKVKVLGDVIEVHGK
HEERQDEHGFISREFHGKYR
IPADVDPLTITSSLSSDGVL
TVNGPRKQV
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 375 |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 492 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1, 1 | 1 |
| 2 | entity_1, 2 | 1 |
Entities:
Entity 1, entity_1, 1 89 residues - 10099.370 Da.
| 1 | GLY | LEU | SER | GLU | MET | ARG | LEU | GLU | LYS | ASP | ||||
| 2 | ARG | PHE | SER | VAL | ASN | LEU | ASP | VAL | LYS | HIS | ||||
| 3 | PHE | SER | PRO | GLU | GLU | LEU | LYS | VAL | LYS | VAL | ||||
| 4 | LEU | GLY | ASP | VAL | ILE | GLU | VAL | HIS | GLY | LYS | ||||
| 5 | HIS | GLU | GLU | ARG | GLN | ASP | GLU | HIS | GLY | PHE | ||||
| 6 | ILE | SER | ARG | GLU | PHE | HIS | GLY | LYS | TYR | ARG | ||||
| 7 | ILE | PRO | ALA | ASP | VAL | ASP | PRO | LEU | THR | ILE | ||||
| 8 | THR | SER | SER | LEU | SER | SER | ASP | GLY | VAL | LEU | ||||
| 9 | THR | VAL | ASN | GLY | PRO | ARG | LYS | GLN | VAL |
Samples:
sample_1: HSPB5 mutant R120G-ACD, [U-13C; U-15N], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 100 uM; PMSF 1 mM
sample_2: HSPB5 mutant R120G-ACD, [U-13C; U-15N; 50%-2H], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 100 uM; PMSF 1 mM
sample_3: HSPB5 mutant R120G-ACD, [U-13C; U-15N; U-2H], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; EDTA 100 uM; PMSF 1 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CSRosetta, David Baker - structure calculation
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker AvanceII 600 MHz
- Varian UNITYPLUS 800 MHz
- Bruker AvanceIII 500 MHz
- Varian UNITYPLUS 900 MHz
- Varian UNITYPLUS 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks