BMRB Entry 18126
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18126
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Title: Backbone Chemical Shifts of the designed protein Z-L2LBT PubMed: 22851279
Deposition date: 2011-12-08 Original release date: 2012-09-10
Authors: Barb, Adam; Ho, Tienhuei; Prestegard, James
Citation: Barb, Adam; Ho, Tienhuei Grace; Flanagan-Steet, Heather; Prestegard, James. "Lanthanide binding and IgG affinity construct: potential applications in solution NMR, MRI, and luminescence microscopy." Protein Sci. 21, 1456-1466 (2012).
Assembly members:
Z-L2LBT, polymer, 88 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Z-L2LBT: MGSSHHHHHHSSGVDNKFNK
EQQNAFYEILHLPNLNEEQR
NAFIQSLKDDSYIDTNNDGA
YEGDELSGSQSANLLAEAKK
LNDAQAPK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 223 |
| 15N chemical shifts | 73 |
| 1H chemical shifts | 73 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Z-L2LBT | 1 |
Entities:
Entity 1, Z-L2LBT 88 residues - Formula weight is not available
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | VAL | ASP | ASN | LYS | PHE | ASN | LYS | ||||
| 3 | GLU | GLN | GLN | ASN | ALA | PHE | TYR | GLU | ILE | LEU | ||||
| 4 | HIS | LEU | PRO | ASN | LEU | ASN | GLU | GLU | GLN | ARG | ||||
| 5 | ASN | ALA | PHE | ILE | GLN | SER | LEU | LYS | ASP | ASP | ||||
| 6 | SER | TYR | ILE | ASP | THR | ASN | ASN | ASP | GLY | ALA | ||||
| 7 | TYR | GLU | GLY | ASP | GLU | LEU | SER | GLY | SER | GLN | ||||
| 8 | SER | ALA | ASN | LEU | LEU | ALA | GLU | ALA | LYS | LYS | ||||
| 9 | LEU | ASN | ASP | ALA | GLN | ALA | PRO | LYS |
Samples:
sample_1: Z-L2LBT, [U-98% 13C; U-98% 15N], 100 – 800 uM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 8.0; pressure: 1 atm; temperature: 273 K
Experiments:
| 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Varian VXRS 900 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts