BMRB Entry 15548
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15548
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Title: Backbone assignment of stefin B monomer PubMed: 18021806
Deposition date: 2007-11-08 Original release date: 2007-12-11
Authors: Morgan, Gareth; Hounslow, Andrea; Waltho, Jonathan
Citation: Morgan, Gareth; Giannini, Silva; Hounslow, Andrea; Craven, C; Zerovnik, Eva; Turk, Vito; Waltho, Jonathan; Staniforth, Rosemary. "Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein" J. Mol. Biol. 375, 487-498 (2007).
Assembly members:
stefin_B, polymer, 98 residues, 11124 Da.
Natural source: Common Name: not available Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
stefin_B: MMSGAPSATQPATAETQHIA
DQVRSQLEEKENKKFPVFKA
VSFKSQVVAGTNYFIKVHVG
DEDFVHLRVFQSLPHENKPL
TLSNYQTNKAKHDELTYF
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 283 |
15N chemical shifts | 91 |
1H chemical shifts | 91 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | stefin B | 1 |
Entities:
Entity 1, stefin B 98 residues - 11124 Da.
1 | MET | MET | SER | GLY | ALA | PRO | SER | ALA | THR | GLN | ||||
2 | PRO | ALA | THR | ALA | GLU | THR | GLN | HIS | ILE | ALA | ||||
3 | ASP | GLN | VAL | ARG | SER | GLN | LEU | GLU | GLU | LYS | ||||
4 | GLU | ASN | LYS | LYS | PHE | PRO | VAL | PHE | LYS | ALA | ||||
5 | VAL | SER | PHE | LYS | SER | GLN | VAL | VAL | ALA | GLY | ||||
6 | THR | ASN | TYR | PHE | ILE | LYS | VAL | HIS | VAL | GLY | ||||
7 | ASP | GLU | ASP | PHE | VAL | HIS | LEU | ARG | VAL | PHE | ||||
8 | GLN | SER | LEU | PRO | HIS | GLU | ASN | LYS | PRO | LEU | ||||
9 | THR | LEU | SER | ASN | TYR | GLN | THR | ASN | LYS | ALA | ||||
10 | LYS | HIS | ASP | GLU | LEU | THR | TYR | PHE |
Samples:
sample_1: stefin B, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 100 mM; H20 90%; D2O 10%
sample_conditions_1: ionic strength: 110 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
FELIX v2004, Accelrys Software Inc. - data analysis
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker DRX 600 MHz
- Bruker DRX 500 MHz
Related Database Links:
PDB | |
DBJ | BAA95541 BAC20304 BAC20305 BAC20306 BAC20307 |
EMBL | CAG46945 |
GB | AAA35727 AAA72786 AAA99014 AAF44059 AAH03370 |
REF | NP_000091 NP_001009095 XP_002830797 XP_011809620 |
SP | P04080 P60575 P60576 Q76LA0 Q8I030 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts