BMRB Entry 15722
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15722
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Title: 1H, 13C and 15N Resonance Assignments of Ca2+ bound collagen-binding domain derived from a clostridial collagenase PubMed: 19636886
Deposition date: 2008-04-08 Original release date: 2008-08-08
Authors: Philominathan, Sagaya T. Leena; Matsushita, Osamu; Jordan, J. Brad; Sakon, Joshua
Citation: Philominathan, Sagaya Theresa Leena; Matsushita, Osamu; Jordan, John Brad; Sakon, Joshua. "1H, 13C and 15N resonance assignments of Ca2+ bound collagen-binding domain derived from a clostridial collagenase" Biomol. NMR Assignments 2, 127-129 (2008).
Assembly members:
Collagen_binding_domain_derived_from_Clostridium_Histolyticum, polymer, 122 residues, 13786 Da.
CA, non-polymer, Formula weight is not available
Natural source: Common Name: Bacillus histolyticus Taxonomy ID: 1498 Superkingdom: Eubacteria Kingdom: not available Genus/species: Clostridium histolyticum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-4T-2
Entity Sequences (FASTA):
Collagen_binding_domain_derived_from_Clostridium_Histolyticum: GSPGIPGNEKLKEKENNDSS
DKATVIPNFNTTMQGSLLGD
DSRDYYSFEVKEEGEVNIEL
DKKDEFGVTWTLHPESNIND
RITYGQVDGNKVSNKVKLRP
GKYYLLVYKYSGSGNYELRV
NK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 420 |
| 15N chemical shifts | 105 |
| 1H chemical shifts | 593 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Collagen binding domain derived from Clostridium Histolyticum | 1 |
| 2 | Calcium ion, 2+ | 2 |
Entities:
Entity 1, Collagen binding domain derived from Clostridium Histolyticum 122 residues - 13786 Da.
Residues 887-892 are introduced as clonging artifact
| 1 | GLY | SER | PRO | GLY | ILE | PRO | GLY | ASN | GLU | LYS | ||||
| 2 | LEU | LYS | GLU | LYS | GLU | ASN | ASN | ASP | SER | SER | ||||
| 3 | ASP | LYS | ALA | THR | VAL | ILE | PRO | ASN | PHE | ASN | ||||
| 4 | THR | THR | MET | GLN | GLY | SER | LEU | LEU | GLY | ASP | ||||
| 5 | ASP | SER | ARG | ASP | TYR | TYR | SER | PHE | GLU | VAL | ||||
| 6 | LYS | GLU | GLU | GLY | GLU | VAL | ASN | ILE | GLU | LEU | ||||
| 7 | ASP | LYS | LYS | ASP | GLU | PHE | GLY | VAL | THR | TRP | ||||
| 8 | THR | LEU | HIS | PRO | GLU | SER | ASN | ILE | ASN | ASP | ||||
| 9 | ARG | ILE | THR | TYR | GLY | GLN | VAL | ASP | GLY | ASN | ||||
| 10 | LYS | VAL | SER | ASN | LYS | VAL | LYS | LEU | ARG | PRO | ||||
| 11 | GLY | LYS | TYR | TYR | LEU | LEU | VAL | TYR | LYS | TYR | ||||
| 12 | SER | GLY | SER | GLY | ASN | TYR | GLU | LEU | ARG | VAL | ||||
| 13 | ASN | LYS |
Entity 2, Calcium ion, 2+ - Formula weight is not available
| 1 | CA |
Samples:
sample_1: Collagen binding domain derived from Clostridium Histolyticum, [U-100% 13C; U-100% 15N], 0.75 mM; Calcium Chloride 20 mM; TRIS, [U-100% 2H], 50 mM; sodium chloride 100 mM; sodium azide 0.3 mM
sample_2: Collagen binding domain derived from Clostridium Histolyticum, [U-99% 15N], 0.75 mM; Calcium Chloride 20 mM; TRIS, [U-100% 2H], 50 mM; sodium chloride 100 mM; sodium azide 0.3 mM
sample_3: Collagen binding domain derived from Clostridium Histolyticum, [U-100% 13C], 0.75 mM; Calcium Chloride 20 mM; TRIS, [U-100% 2H], 50 mM; sodium chloride 100 mM; sodium azide 0.3 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - processing
SPARKY, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
| PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts