BMRB Entry 15826
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15826
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NMR-STAR v3 text file.
XML gzip file.
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Citation: Hsu, Shang-Te Danny; Behrens, Caroline; Cabrita, Lisa; Dobson, Christopher. "1H, 15N and 13C assignments of yellow fluorescent protein (YFP) Venus" Biomol. NMR Assignments 3, 67-72 (2009).
PubMed: 19636949
Assembly members:
YFP, polymer, 247 residues, Formula weight is not available
Natural source: Common Name: Aequorea victoria Taxonomy ID: 6100 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Aequorea victoria
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: N/A
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 806 |
| 13C chemical shifts | 663 |
| 15N chemical shifts | 199 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YFP Venus pH 7.4 | 1 |
Entities:
Entity 1, YFP Venus pH 7.4 247 residues - Formula weight is not available
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | ALA | SER | VAL | ||||
| 2 | SER | LYS | GLY | GLU | GLU | LEU | PHE | THR | GLY | VAL | ||||
| 3 | VAL | PRO | ILE | LEU | VAL | GLU | LEU | ASP | GLY | ASP | ||||
| 4 | VAL | ASN | GLY | HIS | LYS | PHE | SER | VAL | SER | GLY | ||||
| 5 | GLU | GLY | GLU | GLY | ASP | ALA | THR | TYR | GLY | LYS | ||||
| 6 | LEU | THR | LEU | LYS | LEU | ILE | CYS | THR | THR | GLY | ||||
| 7 | LYS | LEU | PRO | VAL | PRO | TRP | PRO | THR | LEU | VAL | ||||
| 8 | THR | THR | LEU | GLY | TYR | GLY | LEU | GLN | CYS | PHE | ||||
| 9 | ALA | ARG | TYR | PRO | ASP | HIS | MET | LYS | GLN | HIS | ||||
| 10 | ASP | PHE | PHE | LYS | SER | ALA | MET | PRO | GLU | GLY | ||||
| 11 | TYR | VAL | GLN | GLU | ARG | THR | ILE | PHE | PHE | LYS | ||||
| 12 | ASP | ASP | GLY | ASN | TYR | LYS | THR | ARG | ALA | GLU | ||||
| 13 | VAL | LYS | PHE | GLU | GLY | ASP | THR | LEU | VAL | ASN | ||||
| 14 | ARG | ILE | GLU | LEU | LYS | GLY | ILE | ASP | PHE | LYS | ||||
| 15 | GLU | ASP | GLY | ASN | ILE | LEU | GLY | HIS | LYS | LEU | ||||
| 16 | GLU | TYR | ASN | TYR | ASN | SER | HIS | ASN | VAL | TYR | ||||
| 17 | ILE | THR | ALA | ASP | LYS | GLN | LYS | ASN | GLY | ILE | ||||
| 18 | LYS | ALA | ASN | PHE | LYS | ILE | ARG | HIS | ASN | ILE | ||||
| 19 | GLU | ASP | GLY | GLY | VAL | GLN | LEU | ALA | ASP | HIS | ||||
| 20 | TYR | GLN | GLN | ASN | THR | PRO | ILE | GLY | ASP | GLY | ||||
| 21 | PRO | VAL | LEU | LEU | PRO | ASP | ASN | HIS | TYR | LEU | ||||
| 22 | SER | TYR | GLN | SER | ALA | LEU | SER | LYS | ASP | PRO | ||||
| 23 | ASN | GLU | LYS | ARG | ASP | HIS | MET | VAL | LEU | LEU | ||||
| 24 | GLU | PHE | VAL | THR | ALA | ALA | GLY | ILE | THR | LEU | ||||
| 25 | GLY | MET | ASP | GLU | LEU | TYR | LYS |
Samples:
13C_15N_YFP: YFP, [U-98% 13C; U-98% 15N], 0.4 mM; TRIS 20 mM
2H_13C_15N_YFP: YFP, [U-13C; U-15N; U-2H], 0.4 mM; TRIS 20 mM
(U-15N_13C-F_I_L_V)_YFP: YFP, [U-15N; 13C-I,L,V,F], 0.4 mM; TRIS 20 mM
(U-15N_13C-F_K)_YFP: YFP, [U-15N; 13C-F,\K], 0.4 mM; TRIS 20 mM
(U-15N_K_L)_YFP: YFP, [U-15N-\K\L], 0.4 mM; TRIS 20 mM
(U-15N_M_K_I_L)_YFP: YFP, [U-15N-\M\K\I\L], 0.4 mM; TRIS 20 mM
(U-15N_M_I)_YFP: YFP, [U-15N-\M\I], 0.4 mM; TRIS 20 mM
(U-15N_13C-L_V)_YFP: YFP, [U-15N, 13C-L,V], 0.4 mM; TRIS 20 mM
310: temperature: 310 K; pH: 7.4; pressure: 1 atm; ionic strength: 0.0 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 2H_13C_15N_YFP | isotropic | 310 |
| 3D HNCO | 2H_13C_15N_YFP | isotropic | 310 |
| 3D HNCACB | 2H_13C_15N_YFP | isotropic | 310 |
| 3D intra-HNCACB | 2H_13C_15N_YFP | isotropic | 310 |
| 3D HN(CA)CO | 2H_13C_15N_YFP | isotropic | 310 |
| 2D 1H-15N TROSY | 2H_13C_15N_YFP | isotropic | 310 |
| 3D HcCH-TOCSY | (U-15N_13C-F_I_L_V)_YFP | isotropic | 310 |
| 2D 1H-13C HSQC | (U-15N_13C-F_I_L_V)_YFP | isotropic | 310 |
| 3D hCCH-TOCSY | (U-15N_13C-F_I_L_V)_YFP | isotropic | 310 |
| 3D HBHA(CO)NH | 2H_13C_15N_YFP | isotropic | 310 |
| 3D HCCH-COSY | (U-15N_13C-F_I_L_V)_YFP | isotropic | 310 |
| 2D HNCO | (U-15N_13C-F_I_L_V)_YFP | isotropic | 310 |
| 2D HNCO | (U-15N_13C-F_K)_YFP | isotropic | 310 |
| 2D HNCO | (U-15N_13C-L_V)_YFP | isotropic | 310 |
| 2D 1H-15N HSQC | (U-15N_K_L)_YFP | isotropic | 310 |
| 2D 1H-15N HSQC | (U-15N_M_K_I_L)_YFP | isotropic | 310 |
| 2D 1H-15N HSQC | (U-15N_M_I)_YFP | isotropic | 310 |
| 3D 1H-15N NOESY | (U-15N_13C-F_I_L_V)_YFP | isotropic | 310 |
| 3D 1H-13C NOESY | (U-15N_13C-F_I_L_V)_YFP | isotropic | 310 |
Software:
SPARKY v3.1, Goddard - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAB11884 BAB61868 BAC16311 BAC16312 BAD84181 |
| EMBL | CAD53302 CAO79590 CAO81988 CAO91534 CAP04964 |
| GB | AAF65454 AAF65455 AAO48591 AAO48597 AAO48599 |
| REF | XP_013248715 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks