BMRB Entry 17131
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17131
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Title: NMR resonance assignment of the N-terminal domain of Latrodectus hesperus (black widow) major ampullate spider silk fibroin 1
Deposition date: 2010-08-16 Original release date: 2010-11-10
Authors: Kessler, Horst; Hagn, Franz
Citation: Hagn, Franz; Thamm, Christopher; Scheibel, Thomas; Kessler, Horst. "pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk--implications for fiber formation." Angew. Chem. Int. Ed. Engl. 50, 310-313 (2011).
Assembly members:
N1, polymer, 132 residues, Formula weight is not available
Natural source: Common Name: black widow spider Taxonomy ID: 256737 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Latrodectus hesperus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
N1: MGQANTPWSSKANADAFINS
FISAASNTGSFSQDQMEDMS
LIGNTLMAAMDNMGGRITPS
KLQALDMAFASSVAEIAASE
GGDLGVTTNAIADALTSAFY
QTTGVVNSRFISEIRSLIGM
FAQASANDVYAS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 458 |
15N chemical shifts | 131 |
1H chemical shifts | 496 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | N1 | 1 |
Entities:
Entity 1, N1 132 residues - Formula weight is not available
1 | MET | GLY | GLN | ALA | ASN | THR | PRO | TRP | SER | SER | ||||
2 | LYS | ALA | ASN | ALA | ASP | ALA | PHE | ILE | ASN | SER | ||||
3 | PHE | ILE | SER | ALA | ALA | SER | ASN | THR | GLY | SER | ||||
4 | PHE | SER | GLN | ASP | GLN | MET | GLU | ASP | MET | SER | ||||
5 | LEU | ILE | GLY | ASN | THR | LEU | MET | ALA | ALA | MET | ||||
6 | ASP | ASN | MET | GLY | GLY | ARG | ILE | THR | PRO | SER | ||||
7 | LYS | LEU | GLN | ALA | LEU | ASP | MET | ALA | PHE | ALA | ||||
8 | SER | SER | VAL | ALA | GLU | ILE | ALA | ALA | SER | GLU | ||||
9 | GLY | GLY | ASP | LEU | GLY | VAL | THR | THR | ASN | ALA | ||||
10 | ILE | ALA | ASP | ALA | LEU | THR | SER | ALA | PHE | TYR | ||||
11 | GLN | THR | THR | GLY | VAL | VAL | ASN | SER | ARG | PHE | ||||
12 | ILE | SER | GLU | ILE | ARG | SER | LEU | ILE | GLY | MET | ||||
13 | PHE | ALA | GLN | ALA | SER | ALA | ASN | ASP | VAL | TYR | ||||
14 | ALA | SER |
Samples:
sample_1: sodium phosphate 10 mM; sodium chloride 300 mM; H2O 95%; D2O 5%; N1, [U-99% 13C; U-99% 15N], 0.85 mM
sample_conditions_1: ionic strength: 0.32 M; pH: 7.2; pressure: 1 atm; temperature: 298 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 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3, Bruker Biospin - collection, processing
SPARKY v3.115, Goddard - chemical shift assignment, data analysis
PASTA v1.1, Kessler and Gemmercker - chemical shift assignment
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