BMRB Entry 27109
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27109
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Kaiser, Christoph; Peters, Carsten; Schmid, Philipp; Stavropoulou, Maria; Zou, Juan; Dahiya, Vinay; Mymrikov, Evgeny; Rockel, Beate; Asami, Sam; Haslbeck, Martin; Rappsilber, Juri; Reif, Bernd; Zacharias, Martin; Buchner, Johannes; Weinkauf, Sevil. "The structure and oxidation of the eye lens chaperone alphaA-crystallin" Nat. Struct. Mol. Biol. 26, 1141-1150 (2019).
PubMed: 31792453
Assembly members:
alphaA-crystallin_or_HspB1, polymer, 173 residues, Formula weight is not available
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: pET28b+
Entity Sequences (FASTA):
alphaA-crystallin_or_HspB1: MDVTIQHPWFKRTLGPFYPS
RLFDQFFGEGLFEYDLLPFL
SSTISPYYRQSLFRTVLDSG
ISEVRSDRDKFVIFLDVKHF
SPEDLTVKVQDDFVEIHGKH
NERQDDHGYISREFHRRYRL
PSNVDQSALSCSLSADGMLT
FCGPKIQTGLDATHAERAIP
VSREEKPTSAPSS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 81 |
| 15N chemical shifts | 22 |
| 1H chemical shifts | 111 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | alphaA-crystallin (or HSPB1) | 1 |
Entities:
Entity 1, alphaA-crystallin (or HSPB1) 173 residues - Formula weight is not available
| 1 | MET | ASP | VAL | THR | ILE | GLN | HIS | PRO | TRP | PHE | ||||
| 2 | LYS | ARG | THR | LEU | GLY | PRO | PHE | TYR | PRO | SER | ||||
| 3 | ARG | LEU | PHE | ASP | GLN | PHE | PHE | GLY | GLU | GLY | ||||
| 4 | LEU | PHE | GLU | TYR | ASP | LEU | LEU | PRO | PHE | LEU | ||||
| 5 | SER | SER | THR | ILE | SER | PRO | TYR | TYR | ARG | GLN | ||||
| 6 | SER | LEU | PHE | ARG | THR | VAL | LEU | ASP | SER | GLY | ||||
| 7 | ILE | SER | GLU | VAL | ARG | SER | ASP | ARG | ASP | LYS | ||||
| 8 | PHE | VAL | ILE | PHE | LEU | ASP | VAL | LYS | HIS | PHE | ||||
| 9 | SER | PRO | GLU | ASP | LEU | THR | VAL | LYS | VAL | GLN | ||||
| 10 | ASP | ASP | PHE | VAL | GLU | ILE | HIS | GLY | LYS | HIS | ||||
| 11 | ASN | GLU | ARG | GLN | ASP | ASP | HIS | GLY | TYR | ILE | ||||
| 12 | SER | ARG | GLU | PHE | HIS | ARG | ARG | TYR | ARG | LEU | ||||
| 13 | PRO | SER | ASN | VAL | ASP | GLN | SER | ALA | LEU | SER | ||||
| 14 | CYS | SER | LEU | SER | ALA | ASP | GLY | MET | LEU | THR | ||||
| 15 | PHE | CYS | GLY | PRO | LYS | ILE | GLN | THR | GLY | LEU | ||||
| 16 | ASP | ALA | THR | HIS | ALA | GLU | ARG | ALA | ILE | PRO | ||||
| 17 | VAL | SER | ARG | GLU | GLU | LYS | PRO | THR | SER | ALA | ||||
| 18 | PRO | SER | SER |
Samples:
sample_1: alphaA-crystallin (or HspB1), [U-100% 13C; U-100% 15N], 3 mM; HEPES 10 mM; EDTA 1 mM; DTT 2 mM
sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 300 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
NMR-STAR, CCPN - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks