BMRB Entry 15596
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15596
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR Solution structure of Human MIP-3alpha/CCL20 PubMed: 18086840
Deposition date: 2007-12-14 Original release date: 2008-01-22
Authors: Chan, David; Hunter, Howard; Tack, Brian; Vogel, Hans
Citation: Chan, David; Hunter, Howard; Tack, Brian; Vogel, Hans. "Human macrophage inflammatory protein 3alpha: protein and peptide nuclear magnetic resonance solution structures, dimerization, dynamics, and anti-infective properties" Antimicrob. Agents Chemother. 52, 883-894 (2008).
Assembly members:
Chemokine, polymer, 70 residues, 8045.645 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: Chemical synthesis
Entity Sequences (FASTA):
Chemokine: ASNFDCCLGYTDRILHPKFI
VGFTRQLANEGCDINAIIFH
TKKKLSVCANPKQTWVKYIV
RLLSKKVKNM
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 535 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Protein | 1 |
Entities:
Entity 1, Protein 70 residues - 8045.645 Da.
| 1 | ALA | SER | ASN | PHE | ASP | CYS | CYS | LEU | GLY | TYR | |
| 2 | THR | ASP | ARG | ILE | LEU | HIS | PRO | LYS | PHE | ILE | |
| 3 | VAL | GLY | PHE | THR | ARG | GLN | LEU | ALA | ASN | GLU | |
| 4 | GLY | CYS | ASP | ILE | ASN | ALA | ILE | ILE | PHE | HIS | |
| 5 | THR | LYS | LYS | LYS | LEU | SER | VAL | CYS | ALA | ASN | |
| 6 | PRO | LYS | GLN | THR | TRP | VAL | LYS | TYR | ILE | VAL | |
| 7 | ARG | LEU | LEU | SER | LYS | LYS | VAL | LYS | ASN | MET |
Samples:
sample_1: Protein 0.9 mM; H2O 90%; D2O 10%
sample_2: Protein 0.9 mM; D2O 100%
sample_conditions_1: pH: 4.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Linge, O'Donoghue and Nilges - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMRView v5.0.4, Johnson, One Moon Scientific - data analysis
xwinnmr v3.0, 3.5, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 500 MHz