BMRB Entry 5047
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5047
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Title: NMR structure of the LCCL Domain and its Implications for DFNA9 Deafness Disorder PubMed: 11574466
Deposition date: 2001-06-06 Original release date: 2001-11-14
Authors: Liepinsh, Edvards; Trexler, Maria; Kaikkonen, Andrei; Weigelt, Johan; Banyai, Laszlo; Patthy, Laszlo; Otting, Gottfried
Citation: Liepinsh, Edvards; Trexler, Maria; Kaikkonen, Andrei; Weigelt, Johan; Banyai, Laszlo; Patthy, Laszlo; Otting, Gottfried. "NMR structure of the LCCL Domain and its Implications for DFNA9 Deafness Disorder" EMBO J. 20, 5347-5353 (2001).
Assembly members:
Human coch-5h2 protein, polymer, 100 residues, 10467 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Human coch-5h2 protein: TAPIAITCFTRGLDIRKEKA
DVLCPGGCPLEEFSVYGNIV
YASVSSICGAAVHRGVISNS
GGPVRVYSLPGRENYSSVDA
NGIQSQMLSRWSASFTVTLE
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 108 |
1H chemical shifts | 685 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | LCCL domain 1 | 1 |
Entities:
Entity 1, LCCL domain 1 100 residues - 10467 Da.
1 | THR | ALA | PRO | ILE | ALA | ILE | THR | CYS | PHE | THR | |
2 | ARG | GLY | LEU | ASP | ILE | ARG | LYS | GLU | LYS | ALA | |
3 | ASP | VAL | LEU | CYS | PRO | GLY | GLY | CYS | PRO | LEU | |
4 | GLU | GLU | PHE | SER | VAL | TYR | GLY | ASN | ILE | VAL | |
5 | TYR | ALA | SER | VAL | SER | SER | ILE | CYS | GLY | ALA | |
6 | ALA | VAL | HIS | ARG | GLY | VAL | ILE | SER | ASN | SER | |
7 | GLY | GLY | PRO | VAL | ARG | VAL | TYR | SER | LEU | PRO | |
8 | GLY | ARG | GLU | ASN | TYR | SER | SER | VAL | ASP | ALA | |
9 | ASN | GLY | ILE | GLN | SER | GLN | MET | LEU | SER | ARG | |
10 | TRP | SER | ALA | SER | PHE | THR | VAL | THR | LEU | GLU |
Samples:
sample_1: Human coch-5h2 protein 1.0 mM; NaCl 0.1 M
sample_2: Human coch-5h2 protein, [U-95% 15N], 3.0 mg/mL; NaCl 0.1 M
sample_3: Human coch-5h2 protein, [U-95% 15N], 3.3 mg/mL; NaCl 0.1 M
Ex-cond_1: ionic strength: 0.1 M; pH: 4.9; temperature: 301 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H DQF-COSY | not available | not available | not available |
2D 1H-1H HOHAHA | not available | not available | not available |
2D 1H-1H NOESY | not available | not available | not available |
2D 1H-1H ROESY | not available | not available | not available |
2D 1H-15N HSQC | not available | not available | not available |
3D 1H-1H-15N TOCSY | not available | not available | not available |
3D 1H-1H-15N NOESY | not available | not available | not available |
Software:
XWINNMR - spectral processing
PROSA - spectral processing
NMR spectrometers:
- Bruker DMX 500 MHz
- Bruker DMX 600 MHz
- Varian UnityPlus 800 MHz
Related Database Links:
PDB | |
DBJ | BAF85413 |
GenBank | AAC39545 AAH07230 AAQ89259 AAW82432 EAW65963 |
REF | NP_004077 XP_001114738 XP_001114756 XP_001114785 XP_001114797 |
SWISS-PROT | O43405 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts