Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16599
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Titushin, Maxim; Feng, Yingang; Stepanyuk, Galina; Li, Yang; Markova, Svetlana; Golz, Stefan; Wang, Bi-Cheng; Lee, John; Wang, Jinfeng; Vysotski, Eugene; Liu, Zhi-Jie. "NMR-derived topology of a GFP-photoprotein energy transfer complex." J. Biol. Chem. 285, 40891-40900 (2010).
PubMed: 20926380
Assembly members:
clytin, polymer, 198 residues, Formula weight is not available
CZH, non-polymer, 455.462 Da.
Natural source: Common Name: C. gregaria Taxonomy ID: 27801 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Clytia gregaria
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b
Data type | Count |
13C chemical shifts | 542 |
15N chemical shifts | 194 |
1H chemical shifts | 557 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | component1 | 1 |
2 | component2 | 2 |
Entity 1, component1 198 residues - Formula weight is not available
1 | MET | THR | ASP | THR | ALA | SER | LYS | TYR | ALA | VAL | ||||
2 | LYS | LEU | LYS | THR | ASN | PHE | GLU | ASP | PRO | LYS | ||||
3 | TRP | VAL | ASN | ARG | HIS | LYS | PHE | MET | PHE | ASN | ||||
4 | PHE | LEU | ASP | ILE | ASN | GLY | ASN | GLY | LYS | ILE | ||||
5 | THR | LEU | ASP | GLU | ILE | VAL | SER | LYS | ALA | SER | ||||
6 | ASP | ASP | ILE | CYS | ALA | LYS | LEU | GLY | ALA | THR | ||||
7 | PRO | ALA | GLN | THR | GLN | ARG | HIS | GLN | GLU | ALA | ||||
8 | VAL | GLU | ALA | PHE | PHE | LYS | LYS | ILE | GLY | LEU | ||||
9 | ASP | TYR | GLY | LYS | GLU | VAL | GLU | PHE | PRO | ALA | ||||
10 | PHE | VAL | ASN | GLY | TRP | LYS | GLU | LEU | ALA | LYS | ||||
11 | HIS | ASP | LEU | LYS | LEU | TRP | SER | GLN | ASN | LYS | ||||
12 | LYS | SER | LEU | ILE | ARG | ASN | TRP | GLY | GLU | ALA | ||||
13 | VAL | PHE | ASP | ILE | PHE | ASP | LYS | ASP | GLY | SER | ||||
14 | GLY | SER | ILE | SER | LEU | ASP | GLU | TRP | LYS | THR | ||||
15 | TYR | GLY | GLY | ILE | SER | GLY | ILE | CYS | PRO | SER | ||||
16 | ASP | GLU | ASP | ALA | GLU | LYS | THR | PHE | LYS | HIS | ||||
17 | CYS | ASP | LEU | ASP | ASN | SER | GLY | LYS | LEU | ASP | ||||
18 | VAL | ASP | GLU | MET | THR | ARG | GLN | HIS | LEU | GLY | ||||
19 | PHE | TRP | TYR | THR | LEU | ASP | PRO | ASN | ALA | ASP | ||||
20 | GLY | LEU | TYR | GLY | ASN | PHE | VAL | PRO |
Entity 2, component2 - C26 H21 N3 O5 - 455.462 Da.
1 | CZH |
sample_1: clytin, [U-13C; U-15N], 1.0 mM; Tris-HCl 20 mM; sodium chloride 10 mM; EDTA 2 mM; DSS 0.02%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HBHANH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
xwinnmr, Bruker Biospin - collection
FELIX, Accelrys Software Inc. - chemical shift assignment, processing
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks