BMRB Entry 26640
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26640
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Citation: Mainz, Andi; Peschek, Jirka; Stavropoulou, Maria; Back, Katrin; Asami, Sam; Bardiaux, Benjamin; Prade, Elke; Peters, Carsten; Weinkauf, Sevil; Buchner, Johannes; Reif, Bernd. "The chaperone AlphaB-crystallin uses different interfaces to capture an amorphous and an amyloid client" Nat. Struct. Mol. Biol. 22, 898-905 (2015).
PubMed: 26458046
Assembly members:
aB, polymer, 175 residues, 20159 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 Vector: pET30
| Data type | Count |
| 13C chemical shifts | 240 |
| 15N chemical shifts | 100 |
| 1H chemical shifts | 101 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | alpha B crystallin, 1 | 1 |
| 2 | alpha B crystallin, 2 | 1 |
| 3 | alpha B crystallin, 3 | 1 |
| 4 | alpha B crystallin, 4 | 1 |
| 5 | alpha B crystallin, 5 | 1 |
| 6 | alpha B crystallin, 6 | 1 |
| 7 | alpha B crystallin, 7 | 1 |
| 8 | alpha B crystallin, 8 | 1 |
| 9 | alpha B crystallin, 9 | 1 |
| 10 | alpha B crystallin, 10 | 1 |
| 11 | alpha B crystallin, 11 | 1 |
| 12 | alpha B crystallin, 12 | 1 |
| 13 | alpha B crystallin, 13 | 1 |
| 14 | alpha B crystallin, 14 | 1 |
| 15 | alpha B crystallin, 15 | 1 |
| 16 | alpha B crystallin, 16 | 1 |
| 17 | alpha B crystallin, 17 | 1 |
| 18 | alpha B crystallin, 18 | 1 |
| 19 | alpha B crystallin, 19 | 1 |
| 20 | alpha B crystallin, 20 | 1 |
| 21 | alpha B crystallin, 21 | 1 |
| 22 | alpha B crystallin, 22 | 1 |
| 23 | alpha B crystallin, 23 | 1 |
| 24 | alpha B crystallin, 24 | 1 |
| 25 | alpha B crystallin, 25 | 1 |
| 26 | alpha B crystallin, 26 | 1 |
| 27 | alpha B crystallin, 27 | 1 |
| 28 | alpha B crystallin, 28 | 1 |
Entities:
Entity 1, alpha B crystallin, 1 175 residues - 20159 Da.
| 1 | MET | ASP | ILE | ALA | ILE | HIS | HIS | PRO | TRP | ILE | ||||
| 2 | ARG | ARG | PRO | PHE | PHE | PRO | PHE | HIS | SER | PRO | ||||
| 3 | SER | ARG | LEU | PHE | ASP | GLN | PHE | PHE | GLY | GLU | ||||
| 4 | HIS | LEU | LEU | GLU | SER | ASP | LEU | PHE | PRO | THR | ||||
| 5 | SER | THR | SER | LEU | SER | PRO | PHE | TYR | LEU | ARG | ||||
| 6 | PRO | PRO | SER | PHE | LEU | ARG | ALA | PRO | SER | TRP | ||||
| 7 | PHE | ASP | THR | GLY | LEU | SER | GLU | MET | ARG | LEU | ||||
| 8 | GLU | LYS | ASP | ARG | PHE | SER | VAL | ASN | LEU | ASP | ||||
| 9 | VAL | LYS | HIS | PHE | SER | PRO | GLU | GLU | LEU | LYS | ||||
| 10 | VAL | LYS | VAL | LEU | GLY | ASP | VAL | ILE | GLU | VAL | ||||
| 11 | HIS | GLY | LYS | HIS | GLU | GLU | ARG | GLN | ASP | GLU | ||||
| 12 | HIS | GLY | PHE | ILE | SER | ARG | GLU | PHE | HIS | ARG | ||||
| 13 | LYS | TYR | ARG | ILE | PRO | ALA | ASP | VAL | ASP | PRO | ||||
| 14 | LEU | THR | ILE | THR | SER | SER | LEU | SER | SER | ASP | ||||
| 15 | GLY | VAL | LEU | THR | VAL | ASN | GLY | PRO | ARG | LYS | ||||
| 16 | GLN | VAL | SER | GLY | PRO | GLU | ARG | THR | ILE | PRO | ||||
| 17 | ILE | THR | ARG | GLU | GLU | LYS | PRO | ALA | VAL | THR | ||||
| 18 | ALA | ALA | PRO | LYS | LYS |
Related Database Links:
| PDB | 2KLR 2N0K 2WJ7 2YGD 3L1G |
| BMRB | 16391 25527 |
| DBJ | BAD51947 BAE27257 BAE40798 BAE87237 BAG36739 |
| EMBL | CAA42910 CAA42911 CAA64669 CAC33095 CAF02108 |
| GB | AAA03655 AAA37472 AAA40977 AAA52104 AAA67045 |
| PIR | I53319 |
| PRF | 2015215A |
| REF | NP_001012475 NP_001075876 NP_001125917 NP_001247830 NP_001271991 |
| SP | P02510 P02511 P23927 P23928 P41316 |
| TPG | DAA22360 |
| AlphaFold | P02510 P02511 P23927 P23928 P41316 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks