BMRB Entry 16150
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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/BMR16150
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Title: NMR assignment of jerdostatin mutant R24K from Trimeresurus jerdonii PubMed: 21656569
Deposition date: 2009-01-30 Original release date: 2012-08-07
Authors: Carbajo, Rodrigo; Sanz, Libia; Mosulen, Silvia; Calvete, Juan Jose; Pineda-Lucena, Antonio
Citation: Carbajo, Rodrigo; Sanz, Libia; Mosulen, Silvia; Perez, Alicia; Marcinkiewicz, Cezary; Pineda-Lucena, Antonio; Calvete, Juan. "NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin 11." Proteins 79, 2530-2542 (2011).
Assembly members:
jerdostatin_R24K, polymer, 46 residues, Formula weight is not available
Natural source: Common Name: snake Taxonomy ID: 135726 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Trimeresurus jerdonii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
jerdostatin_R24K: AMDCTTGPCCRQCKLKPAGT
TCWKTSVSSHYCTGRSCECP
SYPGNG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 119 |
| 15N chemical shifts | 46 |
| 1H chemical shifts | 272 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | jerdostatin R24K | 1 |
Entities:
Entity 1, jerdostatin R24K 46 residues - Formula weight is not available
Residues 1-3 (AMD) are a cloning artifact
| 1 | ALA | MET | ASP | CYS | THR | THR | GLY | PRO | CYS | CYS | ||||
| 2 | ARG | GLN | CYS | LYS | LEU | LYS | PRO | ALA | GLY | THR | ||||
| 3 | THR | CYS | TRP | LYS | THR | SER | VAL | SER | SER | HIS | ||||
| 4 | TYR | CYS | THR | GLY | ARG | SER | CYS | GLU | CYS | PRO | ||||
| 5 | SER | TYR | PRO | GLY | ASN | GLY |
Samples:
sample_1: jerdostatin R24K, [U-100% 15N], 0.5 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 0 M; pH: 4.5; pressure: 1.0 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
TOPSPIN, Bruker Biospin - collection, processing
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
Related Database Links:
| UNP | Q7ZZM2 |
| BMRB | 16136 16151 16152 |
| PDB | |
| EMBL | CAJ34936 CAK12627 CAL18287 |
| GB | AAP20878 |
| SP | Q3BK17 Q7ZZM2 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts