BMRB Entry 17279
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17279
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Peng, Yu; Zhang, Xu; Liu, Jiafu; Liu, Qiang; Guo, Chenyun; Zhang, Yonglian; Lin, Donghai. "Solution structure of the protein lipocalin 12 from rat epididymis." Proteins 79, 2316-2320 (2011).
PubMed: 21538546
Assembly members:
rat_epididymal_lipocalin_12, polymer, 184 residues, 20124.996 Da.
Natural source: Common Name: Norway rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b
Entity Sequences (FASTA):
rat_epididymal_lipocalin_12: MGQSPTMPQGFSQMTSFQSN
KFQGEWFVLGLADNTYKREH
RPLLHSFITLFKLRDNSEFQ
VTNSMTRGKHCSTWSYTLIP
TNKPGQFTRDNRGSGPGADK
ENIQVIETDYVKFALVLSLR
QASNQNITRVSLLGRDWKIT
HKTIDRFIALTKTQNLTKNN
LLFPDLTDWLLDPKVCLEHH
HHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 728 |
| 15N chemical shifts | 182 |
| 1H chemical shifts | 1098 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | rat epididymal lipocalin 12 | 1 |
Entities:
Entity 1, rat epididymal lipocalin 12 184 residues - 20124.996 Da.
| 1 | MET | GLY | GLN | SER | PRO | THR | MET | PRO | GLN | GLY | ||||
| 2 | PHE | SER | GLN | MET | THR | SER | PHE | GLN | SER | ASN | ||||
| 3 | LYS | PHE | GLN | GLY | GLU | TRP | PHE | VAL | LEU | GLY | ||||
| 4 | LEU | ALA | ASP | ASN | THR | TYR | LYS | ARG | GLU | HIS | ||||
| 5 | ARG | PRO | LEU | LEU | HIS | SER | PHE | ILE | THR | LEU | ||||
| 6 | PHE | LYS | LEU | ARG | ASP | ASN | SER | GLU | PHE | GLN | ||||
| 7 | VAL | THR | ASN | SER | MET | THR | ARG | GLY | LYS | HIS | ||||
| 8 | CYS | SER | THR | TRP | SER | TYR | THR | LEU | ILE | PRO | ||||
| 9 | THR | ASN | LYS | PRO | GLY | GLN | PHE | THR | ARG | ASP | ||||
| 10 | ASN | ARG | GLY | SER | GLY | PRO | GLY | ALA | ASP | LYS | ||||
| 11 | GLU | ASN | ILE | GLN | VAL | ILE | GLU | THR | ASP | TYR | ||||
| 12 | VAL | LYS | PHE | ALA | LEU | VAL | LEU | SER | LEU | ARG | ||||
| 13 | GLN | ALA | SER | ASN | GLN | ASN | ILE | THR | ARG | VAL | ||||
| 14 | SER | LEU | LEU | GLY | ARG | ASP | TRP | LYS | ILE | THR | ||||
| 15 | HIS | LYS | THR | ILE | ASP | ARG | PHE | ILE | ALA | LEU | ||||
| 16 | THR | LYS | THR | GLN | ASN | LEU | THR | LYS | ASN | ASN | ||||
| 17 | LEU | LEU | PHE | PRO | ASP | LEU | THR | ASP | TRP | LEU | ||||
| 18 | LEU | ASP | PRO | LYS | VAL | CYS | LEU | GLU | HIS | HIS | ||||
| 19 | HIS | HIS | HIS | HIS |
Samples:
sample: rLcn12, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%; NaAC 20 MM; EDTA 0.5 MM
sample_conditions_1: ionic strength: 20 mM; pH: 4.5; pressure: 1 Pa; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample | isotropic | sample_conditions_1 |
| 3D HNCACB | sample | isotropic | sample_conditions_1 |
| 3D HNCO | sample | isotropic | sample_conditions_1 |
| 4D 1H-15N NOESY | sample | isotropic | sample_conditions_1 |
| 4D 1H-13C NOESY | sample | isotropic | sample_conditions_1 |
| 3D MQ-CCH-TOCSY | sample | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample | isotropic | sample_conditions_1 |
| 3D HNCA | sample | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger A. T. et.al. - refinement
ARIA v2.2, Linge, O'Donoghue and Nilges - chemical shift assignment
NMR spectrometers:
- Bruker Advance III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks