BMRB Entry 19069
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19069
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NMR-STAR v3 text file.
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Citation: Juranic, Nenad; Atanasova, Elena; Prendergast, Franklyn. "NMR signature of HBDI chromophore in folded EFGP" .
Assembly members:
EFGP, polymer, 241 residues, 319.313 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 1037 |
| 15N chemical shifts | 245 |
| 1H chemical shifts | 1663 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EFGP | 1 |
Entities:
Entity 1, EFGP 241 residues - 319.313 Da.
Non-standard residue name of the chromophore CRO(65-67) created from residues T65,Y66,G67
| 1 | GLY | HIS | MET | VAL | SER | LYS | GLY | GLU | GLU | LEU | ||||
| 2 | PHE | THR | GLY | VAL | VAL | PRO | ILE | LEU | VAL | GLU | ||||
| 3 | LEU | ASP | GLY | ASP | VAL | ASN | GLY | HIS | LYS | PHE | ||||
| 4 | SER | VAL | SER | GLY | GLU | GLY | GLU | GLY | ASP | ALA | ||||
| 5 | THR | TYR | GLY | LYS | LEU | THR | LEU | LYS | PHE | ILE | ||||
| 6 | CYS | THR | THR | GLY | LYS | LEU | PRO | VAL | PRO | TRP | ||||
| 7 | PRO | THR | LEU | VAL | THR | THR | LEU | CRO | CRO | CRO | ||||
| 8 | VAL | GLN | CYS | PHE | SER | ARG | TYR | PRO | ASP | HIS | ||||
| 9 | MET | LYS | GLN | HIS | ASP | PHE | PHE | LYS | SER | ALA | ||||
| 10 | MET | PRO | GLU | GLY | TYR | VAL | GLN | GLU | ARG | THR | ||||
| 11 | ILE | PHE | PHE | LYS | ASP | ASP | GLY | ASN | TYR | LYS | ||||
| 12 | THR | ARG | ALA | GLU | VAL | LYS | PHE | GLU | GLY | ASP | ||||
| 13 | THR | LEU | VAL | ASN | ARG | ILE | GLU | LEU | LYS | GLY | ||||
| 14 | ILE | ASP | PHE | LYS | GLU | ASP | GLY | ASN | ILE | LEU | ||||
| 15 | GLY | HIS | LYS | LEU | GLU | TYR | ASN | TYR | ASN | SER | ||||
| 16 | HIS | ASN | VAL | TYR | ILE | MET | ALA | ASP | LYS | GLN | ||||
| 17 | LYS | ASN | GLY | ILE | LYS | VAL | ASN | PHE | LYS | ILE | ||||
| 18 | ARG | HIS | ASN | ILE | GLU | ASP | GLY | SER | VAL | GLN | ||||
| 19 | LEU | ALA | ASP | HIS | TYR | GLN | GLN | ASN | THR | PRO | ||||
| 20 | ILE | GLY | ASP | GLY | PRO | VAL | LEU | LEU | PRO | ASP | ||||
| 21 | ASN | HIS | TYR | LEU | SER | THR | GLN | SER | ALA | LEU | ||||
| 22 | SER | LYS | ASP | PRO | ASN | GLU | LYS | ARG | ASP | HIS | ||||
| 23 | MET | VAL | LEU | LEU | GLU | PHE | VAL | THR | ALA | ALA | ||||
| 24 | GLY | ILE | THR | LEU | GLY | MET | ASP | GLU | LEU | TYR | ||||
| 25 | LYS |
Related Database Links:
| PDB | 1BFP 1C4F 1EMB 1EMC 1EME 1EMF 1EMG 1EMK 1EML 1EMM 1GFL 1HCJ 1OXD 1OXE 1OXF 1Q4A 1Q4B 1Q4C 1Q4D 1Q4E 1QYF 1QYQ 1RM9 1RMM 1RMO 1RMP 1S6Z 1W7S 1W7T 1W7U 1YFP 1Z1P 1Z1Q 2AWK 2AWL 2DUE 2DUF 2DUG 2DUH 2DUI 2EMD 2EMN 2EMO 2FZU 2G16 2G2S 2G3D 2G5Z 2G6E 2H6V 2H9W 2HCG 2HJO 2HQZ 2O24 2O29 2O2B 2OKW 2OKY 2QLE 2QRF 2QZ0 2WSN 2WUR 2Y0G 3AI4 3DPW 3DPX 3DPZ 3DQ1 3DQ2 3DQ3 3DQ4 3DQ5 3DQ6 3DQ7 3DQ8 3DQ9 3DQA 3DQC 3DQD 3DQE 3DQF 3DQH 3DQI 3DQJ 3DQK 3DQL 3DQM 3DQN 3DQO 3DQU 3OGO 3SRY 3SS0 3SSH 3SSK 3SSL 3SSP 3SST 3SSV 3SSY 3SVE 3V3D 3VHT 3W1C 4ANJ 4BDU 4EUL 4KA9 4KAG 4KEX 4N3D 4XL5 4XVP |
| DBJ | BAB11884 BAB32740 BAB61869 BAB61870 BAB61871 |
| EMBL | CAC40615 CAC40618 CAC40622 CAC40625 CAC40629 |
| GB | AAA27721 AAA69675 AAB01173 AAB02572 AAB02574 |
| REF | WP_012569506 WP_031943942 YP_002302326 YP_009062989 |
| SP | P42212 |
| AlphaFold | P42212 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks