BMRB Entry 30163
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30163
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Title: NMR Structure of Apo-form Human Tear Lipocalin
Deposition date: 2016-08-28 Original release date: 2017-08-22
Authors: Vogel, H.; Liu, Z.
Citation: Vogel, H.; Liu, Z.. "NMR Structure of Apo-form Human Tear Lipocalin" . ., .-..
Assembly members:
entity_1, polymer, 158 residues, 17453.652 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 'BL21-Gold(DE3)pLysS AG'
Entity Sequences (FASTA):
entity_1: HHLLASDEEIQDVSGTWYLK
AMTVDREFPEMNLESVTPMT
LTTLEGGNLEAKVTMLISGR
CQEVKAVLEKTDEPGKYTAD
GGKHVAYIIRSHVKDHYIFY
SEGELHGKPVRGVKLVGRDP
KNNLEALEDFEKAAGARGLS
TESILIPRQSETCSPGSD
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 132 |
| 1H chemical shifts | 132 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 158 residues - 17453.652 Da.
| 1 | HIS | HIS | LEU | LEU | ALA | SER | ASP | GLU | GLU | ILE | ||||
| 2 | GLN | ASP | VAL | SER | GLY | THR | TRP | TYR | LEU | LYS | ||||
| 3 | ALA | MET | THR | VAL | ASP | ARG | GLU | PHE | PRO | GLU | ||||
| 4 | MET | ASN | LEU | GLU | SER | VAL | THR | PRO | MET | THR | ||||
| 5 | LEU | THR | THR | LEU | GLU | GLY | GLY | ASN | LEU | GLU | ||||
| 6 | ALA | LYS | VAL | THR | MET | LEU | ILE | SER | GLY | ARG | ||||
| 7 | CYS | GLN | GLU | VAL | LYS | ALA | VAL | LEU | GLU | LYS | ||||
| 8 | THR | ASP | GLU | PRO | GLY | LYS | TYR | THR | ALA | ASP | ||||
| 9 | GLY | GLY | LYS | HIS | VAL | ALA | TYR | ILE | ILE | ARG | ||||
| 10 | SER | HIS | VAL | LYS | ASP | HIS | TYR | ILE | PHE | TYR | ||||
| 11 | SER | GLU | GLY | GLU | LEU | HIS | GLY | LYS | PRO | VAL | ||||
| 12 | ARG | GLY | VAL | LYS | LEU | VAL | GLY | ARG | ASP | PRO | ||||
| 13 | LYS | ASN | ASN | LEU | GLU | ALA | LEU | GLU | ASP | PHE | ||||
| 14 | GLU | LYS | ALA | ALA | GLY | ALA | ARG | GLY | LEU | SER | ||||
| 15 | THR | GLU | SER | ILE | LEU | ILE | PRO | ARG | GLN | SER | ||||
| 16 | GLU | THR | CYS | SER | PRO | GLY | SER | ASP |
Samples:
sample_1: D2O 10 ± 1 %; H2O 90 ± 1 %; Lipocalin, [U-99% 13C; U-99% 15N], 1.0 ± 0.1 mM; sodium azide 0.04 ± 0.001 %; sodium phosphate 50 ± 1 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts