BMRB Entry 18794
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18794
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Title: Structure of module 2 from the E1 domain of C. elegans APL-1 PubMed: 24276282
Deposition date: 2012-10-20 Original release date: 2013-10-21
Authors: Hinds, Mark; Leong, Su Ling
Citation: Leong, Su Ling; Young, Tessa; Barnham, Kevin; Wedd, Anthony; Hinds, Mark; Xiao, Zhiguang; Cappai, Roberto. "Quantification of copper binding to amyloid precursor protein domain 2 and its Caenorhabditis elegans ortholog. Implications for biological function." Metallomics 6, 105-116 (2014).
Assembly members:
entity, polymer, 65 residues, 7428.485 Da.
Natural source: Common Name: Caenorhabditis elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans
Experimental source: Production method: recombinant technology Host organism: Pichia pastoris
Entity Sequences (FASTA):
entity: EACQFSHVNSRDQCNDYQHW
KDEAGKQCKTKKSKGNKDMI
VRSFAVLEPCALDMFTGVEF
VCCPN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 252 |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 439 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | module 2 from the E1 domain of C. elegans APL-1 | 1 |
Entities:
Entity 1, module 2 from the E1 domain of C. elegans APL-1 65 residues - 7428.485 Da.
residues 133-197 of C. elegans APL-1
| 1 | GLU | ALA | CYS | GLN | PHE | SER | HIS | VAL | ASN | SER | ||||
| 2 | ARG | ASP | GLN | CYS | ASN | ASP | TYR | GLN | HIS | TRP | ||||
| 3 | LYS | ASP | GLU | ALA | GLY | LYS | GLN | CYS | LYS | THR | ||||
| 4 | LYS | LYS | SER | LYS | GLY | ASN | LYS | ASP | MET | ILE | ||||
| 5 | VAL | ARG | SER | PHE | ALA | VAL | LEU | GLU | PRO | CYS | ||||
| 6 | ALA | LEU | ASP | MET | PHE | THR | GLY | VAL | GLU | PHE | ||||
| 7 | VAL | CYS | CYS | PRO | ASN |
Samples:
sample_1: APL-1 0.5 mM; APL-1, [U-100% 15N], 0.5 mM; APL-1, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 10 mM; pH: 6.9; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker AG - collection
XEASY, Bartels et al. - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| UNP | Q10651 |
| PDB | |
| EMBL | CCD65568 CCD65569 |
| GB | AAC46470 |
| REF | NP_508870 NP_508871 |
| SP | Q10651 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts