BMRB Entry 6519
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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/BMR6519
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: Venkitaramani, Deepa; Fulton, D.; Andreotti, Amy; Johansen, Kristen; Johansen, Jorgen. "Solution structure and backbone dynamics of Calsensin, an invertebrate
neuronal calcium-binding protein." Protein Sci. 14, 1894-1901 (2005).
PubMed: 15937283
Assembly members:
Calsensin, polymer, 83 residues, Formula weight is not available
Natural source: Common Name: Leech Taxonomy ID: 38567 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Haemopis marmorata
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
Calsensin: MACKVKAELEAAFKKLDANG
DGYVTALELQTFMVTLDAYK
ALSKDKVKEASAKLIKMADK
NSDGKISKEEFLNANAELLC
QLK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 217 |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 467 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Calsensin | 1 |
Entities:
Entity 1, Calsensin 83 residues - Formula weight is not available
| 1 | MET | ALA | CYS | LYS | VAL | LYS | ALA | GLU | LEU | GLU | ||||
| 2 | ALA | ALA | PHE | LYS | LYS | LEU | ASP | ALA | ASN | GLY | ||||
| 3 | ASP | GLY | TYR | VAL | THR | ALA | LEU | GLU | LEU | GLN | ||||
| 4 | THR | PHE | MET | VAL | THR | LEU | ASP | ALA | TYR | LYS | ||||
| 5 | ALA | LEU | SER | LYS | ASP | LYS | VAL | LYS | GLU | ALA | ||||
| 6 | SER | ALA | LYS | LEU | ILE | LYS | MET | ALA | ASP | LYS | ||||
| 7 | ASN | SER | ASP | GLY | LYS | ILE | SER | LYS | GLU | GLU | ||||
| 8 | PHE | LEU | ASN | ALA | ASN | ALA | GLU | LEU | LEU | CYS | ||||
| 9 | GLN | LEU | LYS |
Samples:
sample_1: Calsensin, [U-95% 13C; U-98% 15N], 1.7 mM; Sodium chloride 75 mM; Sodium Phosphate 50 mM; Dithiothreotol 2 mM
conditions_1: ionic strength: 0.125 M; pH: 6.0; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | not available | not available | not available |
| 3D 1H-15N TOCSY | not available | not available | not available |
| 3D 1H-13C NOESY | not available | not available | not available |
| 3D 1H-13N HCCH | not available | not available | not available |
| 3D 1H-13C-15N HNCACB | not available | not available | not available |
| 3D 1H-13C-15N HN(CO)CACB | not available | not available | not available |
| 3D 15N-15N-1H NOESY | not available | not available | not available |
| 2D 1H-15NHSQC | not available | not available | not available |
| 2D 1H-1H NOESY | not available | not available | not available |
| 2D 1H-1H COSY | not available | not available | not available |
| 2D 1H-1H TOCSY | not available | not available | not available |
Software:
xwinnmr - Phasing, Spectrum acquisition
NMRView v5.0.4 - Assignments, restraint generation
NMR spectrometers:
- Bruker DRX 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks