BMRB Entry 16317
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16317
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: Solution structure of human interleukin-33 PubMed: 19888696
Deposition date: 2009-05-26 Original release date: 2009-07-23
Authors: Lingel, Andreas; Fairbrother, Wayne
Citation: Lingel, Andreas; Fairbrother, Wayne. "NMR assignments of the human cytokine interleukin-33" Biomol. NMR Assignments 3, 223-225 (2009).
Assembly members:
human interleukin-33, polymer, 161 residues, Formula weight is not available
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
Entity Sequences (FASTA):
human interleukin-33: GSSITGISPITEYLASLSTY
NDQSITFALEDESYEIYVED
LKKDEKKDKVLLSYYESQHP
SNESGDGVDGKMLMVTLSPT
KDFWLHANNKEHSVELHKCE
KPLPDQAFFVLHNMHSNCVS
FECKTDPGVFIGVKDNHLAL
IKVDSSENLCTENILFKLSE
T
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 548 |
| 15N chemical shifts | 151 |
| 1H chemical shifts | 1046 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | human interleukin-33 | 1 |
Entities:
Entity 1, human interleukin-33 161 residues - Formula weight is not available
| 1 | GLY | SER | SER | ILE | THR | GLY | ILE | SER | PRO | ILE | ||||
| 2 | THR | GLU | TYR | LEU | ALA | SER | LEU | SER | THR | TYR | ||||
| 3 | ASN | ASP | GLN | SER | ILE | THR | PHE | ALA | LEU | GLU | ||||
| 4 | ASP | GLU | SER | TYR | GLU | ILE | TYR | VAL | GLU | ASP | ||||
| 5 | LEU | LYS | LYS | ASP | GLU | LYS | LYS | ASP | LYS | VAL | ||||
| 6 | LEU | LEU | SER | TYR | TYR | GLU | SER | GLN | HIS | PRO | ||||
| 7 | SER | ASN | GLU | SER | GLY | ASP | GLY | VAL | ASP | GLY | ||||
| 8 | LYS | MET | LEU | MET | VAL | THR | LEU | SER | PRO | THR | ||||
| 9 | LYS | ASP | PHE | TRP | LEU | HIS | ALA | ASN | ASN | LYS | ||||
| 10 | GLU | HIS | SER | VAL | GLU | LEU | HIS | LYS | CYS | GLU | ||||
| 11 | LYS | PRO | LEU | PRO | ASP | GLN | ALA | PHE | PHE | VAL | ||||
| 12 | LEU | HIS | ASN | MET | HIS | SER | ASN | CYS | VAL | SER | ||||
| 13 | PHE | GLU | CYS | LYS | THR | ASP | PRO | GLY | VAL | PHE | ||||
| 14 | ILE | GLY | VAL | LYS | ASP | ASN | HIS | LEU | ALA | LEU | ||||
| 15 | ILE | LYS | VAL | ASP | SER | SER | GLU | ASN | LEU | CYS | ||||
| 16 | THR | GLU | ASN | ILE | LEU | PHE | LYS | LEU | SER | GLU | ||||
| 17 | THR |
Samples:
15N_sample: Interleukin-33, [U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; beta-mercaptoethanol 5 mM; H2O 95%; D2O 5%
unlabeled_sample: Interleukin-33 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; beta-mercaptoethanol, [U-100% 2H], 5 mM; D2O 100%
15N_13C_sample: Interleukin-33, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; beta-mercaptoethanol 5 mM; H2O 95%; D2O 5%
15N_13C_sample_D2O: Interleukin-33, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; beta-mercaptoethanol, [U-100% 2H], 5 mM; D2O 100%
Condition_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | 15N_sample | isotropic | Condition_1 |
| 3D 1H-13C NOESY | 15N_13C_sample_D2O | isotropic | Condition_1 |
| 3D HNHA | 15N_sample | isotropic | Condition_1 |
| 2D 1H-1H NOESY | unlabeled_sample | isotropic | Condition_1 |
| 3D HNCA | 15N_13C_sample | isotropic | Condition_1 |
| 3D HNCACB | 15N_13C_sample | isotropic | Condition_1 |
| 3D CBCA(CO)NH | 15N_13C_sample | isotropic | Condition_1 |
| 3D C(CO)NH | 15N_13C_sample | isotropic | Condition_1 |
| 3D H(CCO)NH | 15N_13C_sample | isotropic | Condition_1 |
| 3D HCCH-TOCSY | 15N_13C_sample_D2O | isotropic | Condition_1 |
| 2D 1H-15N HSQC | 15N_sample | isotropic | Condition_1 |
| 2D 1H-13C HSQC | 15N_13C_sample | isotropic | Condition_1 |
Software:
TOPSPIN, Bruker - collection
CCPN, CCPN - data analysis
TALOS, Cornilescu, Delaglio and Bax - data analysis
ARIA v2.2, Linge, O, . - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
Molmol, Koradi, Billeter and Wuthrich - Display
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 800 MHz
- Bruker DRX 900 MHz
Related Database Links:
| PDB | |
| DBJ | BAA75892 BAG36208 BAG58697 BAJ20898 |
| EMBL | CAG28547 |
| GB | AAH47085 AAX86998 ADR77828 AIC52722 EAW58748 |
| REF | NP_001186570 NP_001300973 NP_001300974 NP_001300975 NP_001300976 |
| SP | O95760 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts