BMRB Entry 19963
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/BMR19963
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: Structure of Bitistatin_B PubMed: 25363287
Deposition date: 2014-05-11 Original release date: 2014-11-10
Authors: Carbajo, Rodrigo; Calvete, Juan Jose; Sanz, Libia; Perez, Alicia
Citation: Carbajo, Rodrigo; Calvete, Juan Jose; Sanz, Libia; Perez, Alicia. "NMR structure of bitistatin, a missing piece in the evolutionary pathway of snake venom disintegrins" FEBS J. ., .-. (2014).
Assembly members:
Bitistatin_B, polymer, 83 residues, 9014.037 Da.
Natural source: Common Name: puff adder Taxonomy ID: 8692 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bitis arietans
Experimental source: Production method: purified from the natural source
Entity Sequences (FASTA):
Bitistatin_B: SPPVCGNKILEQGEDCDCGS
PANCQDRCCNAATCKLTPGS
QCNYGECCDQCRFKKAGTVC
RIARGDWNDDYCTGKSSDCP
WNH
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 507 |
| 13C chemical shifts | 172 |
| 15N chemical shifts | 86 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 83 residues - 9014.037 Da.
Seven S-S covalent bonds between cysteine residues: 5-34, 16-29, 18-24, 28-51, 42-48, 47-72, 60-79
| 1 | SER | PRO | PRO | VAL | CYS | GLY | ASN | LYS | ILE | LEU | ||||
| 2 | GLU | GLN | GLY | GLU | ASP | CYS | ASP | CYS | GLY | SER | ||||
| 3 | PRO | ALA | ASN | CYS | GLN | ASP | ARG | CYS | CYS | ASN | ||||
| 4 | ALA | ALA | THR | CYS | LYS | LEU | THR | PRO | GLY | SER | ||||
| 5 | GLN | CYS | ASN | TYR | GLY | GLU | CYS | CYS | ASP | GLN | ||||
| 6 | CYS | ARG | PHE | LYS | LYS | ALA | GLY | THR | VAL | CYS | ||||
| 7 | ARG | ILE | ALA | ARG | GLY | ASP | TRP | ASN | ASP | ASP | ||||
| 8 | TYR | CYS | THR | GLY | LYS | SER | SER | ASP | CYS | PRO | ||||
| 9 | TRP | ASN | HIS |
Samples:
sample_1: Bitistatin B, [U-99% 2H], 1 mM; H2O 90%; D2O 10%; sodium phosphate 50 mM
sample_2: Bitistatin_B, [U-100% 15N], 1 mM; H2O 90%; D2O, [U-99% 2H], 10%; sodium phosphate 50 mM
sample_conditions_1: temperature: 300 K; pH: 5; pressure: 1 atm; ionic strength: 50 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
TALOS, Cornilescu, Delaglio and Bax - data analysis
CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution, refinement
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts