BMRB Entry 15932
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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/BMR15932
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Title: Solution Structure of the Catalytic Domain of Procaspase-8 PubMed: 19278658
Deposition date: 2008-08-28 Original release date: 2009-03-11
Authors: Keller, Nadine; Zerbe, Oliver; Mares, Jiri; Gruetter, Markus
Citation: Keller, Nadine; Mares, Jiri; Zerbe, Oliver; Gruetter, Markus. "Structural and Biochemical Studies on Procaspase-8: New Insights on Initiator Caspase Activation" Structure 17, 438-448 (2009).
Assembly members:
procaspase8, polymer, 266 residues, 24713.402 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
Entity Sequences (FASTA):
procaspase8: MRGSESQTLDKVYQMKSKPR
GYCLIINNHNFAKAREKVPK
LHSIRDRNGTHLDAGALTTT
FEELHFEIKPHDDCTVEQIY
EILKIYQLMDHSNMDCFICC
ILSHGDKGIIYGTDGQEAPI
YELTSQFTGLKCPSLAGKPK
VFFIQAAQGDNYQKGIPVET
DSEEQPYLEMDLSSPQTRYI
PDEADFLLGMATVNNCVSYR
NPAEGTWYIQSLCQSLRERC
PRGDDILTILTEVNYEVSNK
DDKKNMGKQMPQPTFTLRKK
LVFPSD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 922 |
| 15N chemical shifts | 209 |
| 1H chemical shifts | 1346 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | procaspase8 | 1 |
Entities:
Entity 1, procaspase8 266 residues - 24713.402 Da.
| 1 | MET | ARG | GLY | SER | GLU | SER | GLN | THR | LEU | ASP | ||||
| 2 | LYS | VAL | TYR | GLN | MET | LYS | SER | LYS | PRO | ARG | ||||
| 3 | GLY | TYR | CYS | LEU | ILE | ILE | ASN | ASN | HIS | ASN | ||||
| 4 | PHE | ALA | LYS | ALA | ARG | GLU | LYS | VAL | PRO | LYS | ||||
| 5 | LEU | HIS | SER | ILE | ARG | ASP | ARG | ASN | GLY | THR | ||||
| 6 | HIS | LEU | ASP | ALA | GLY | ALA | LEU | THR | THR | THR | ||||
| 7 | PHE | GLU | GLU | LEU | HIS | PHE | GLU | ILE | LYS | PRO | ||||
| 8 | HIS | ASP | ASP | CYS | THR | VAL | GLU | GLN | ILE | TYR | ||||
| 9 | GLU | ILE | LEU | LYS | ILE | TYR | GLN | LEU | MET | ASP | ||||
| 10 | HIS | SER | ASN | MET | ASP | CYS | PHE | ILE | CYS | CYS | ||||
| 11 | ILE | LEU | SER | HIS | GLY | ASP | LYS | GLY | ILE | ILE | ||||
| 12 | TYR | GLY | THR | ASP | GLY | GLN | GLU | ALA | PRO | ILE | ||||
| 13 | TYR | GLU | LEU | THR | SER | GLN | PHE | THR | GLY | LEU | ||||
| 14 | LYS | CYS | PRO | SER | LEU | ALA | GLY | LYS | PRO | LYS | ||||
| 15 | VAL | PHE | PHE | ILE | GLN | ALA | ALA | GLN | GLY | ASP | ||||
| 16 | ASN | TYR | GLN | LYS | GLY | ILE | PRO | VAL | GLU | THR | ||||
| 17 | ASP | SER | GLU | GLU | GLN | PRO | TYR | LEU | GLU | MET | ||||
| 18 | ASP | LEU | SER | SER | PRO | GLN | THR | ARG | TYR | ILE | ||||
| 19 | PRO | ASP | GLU | ALA | ASP | PHE | LEU | LEU | GLY | MET | ||||
| 20 | ALA | THR | VAL | ASN | ASN | CYS | VAL | SER | TYR | ARG | ||||
| 21 | ASN | PRO | ALA | GLU | GLY | THR | TRP | TYR | ILE | GLN | ||||
| 22 | SER | LEU | CYS | GLN | SER | LEU | ARG | GLU | ARG | CYS | ||||
| 23 | PRO | ARG | GLY | ASP | ASP | ILE | LEU | THR | ILE | LEU | ||||
| 24 | THR | GLU | VAL | ASN | TYR | GLU | VAL | SER | ASN | LYS | ||||
| 25 | ASP | ASP | LYS | LYS | ASN | MET | GLY | LYS | GLN | MET | ||||
| 26 | PRO | GLN | PRO | THR | PHE | THR | LEU | ARG | LYS | LYS | ||||
| 27 | LEU | VAL | PHE | PRO | SER | ASP |
Samples:
sample_1: procaspase8, [U-99% 13C; U-99% 15N], 0.8 mM; DTT 10 mM; sodium chloride 100 mM; TRIS, [U-2H], 20 mM; H2O 90%; D2O 10%
sample_2: procaspase8, [U-100% 13C; U-100% 15N; 80% 2H], 0.8 mM; DTT 10 mM; sodium chloride 100 mM; TRIS, [U-2H], 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 8.0; pressure: 1 atm; temperature: 305 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CG | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCG | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| HN(CACO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
AMBER v6.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - geometry optimization
CYANA v2.2, Guntert, Mumenthaler and Wuthrich - structure solution
XEASY v1.55, Bartels et al. - chemical shift assignment
CARA, Keller, W thrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB32555 BAG70096 BAG70228 |
| EMBL | CAA66853 CAA66854 CAA66855 |
| GB | AAB70913 AAC50602 AAC50645 AAD24962 AAL87628 |
| REF | NP_001073593 NP_001073594 NP_001125222 NP_001219 NP_203519 |
| SP | Q14790 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts