BMRB Entry 18190
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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/BMR18190
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Title: NMR structure of the protein BC008182, a DNAJ-like domain from Homo sapiens
Deposition date: 2012-01-09 Original release date: 2012-02-13
Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; JCSG, JCSG
Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; JCSG, JCSG. "NMR structure of the protein BC008182, DNAJ homolog from Homo sapiens" Not known ., .-..
Assembly members:
entity, polymer, 71 residues, 8224.376 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):
entity: GMVKETTYYDVLGVKPNATQ
EELKKAYRKLALKYHPDKNP
NEGEKFKQISQAYEVLSDAK
KRELYDKGGEQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 249 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 498 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BC008182 | 1 |
Entities:
Entity 1, BC008182 71 residues - 8224.376 Da.
| 1 | GLY | MET | VAL | LYS | GLU | THR | THR | TYR | TYR | ASP | ||||
| 2 | VAL | LEU | GLY | VAL | LYS | PRO | ASN | ALA | THR | GLN | ||||
| 3 | GLU | GLU | LEU | LYS | LYS | ALA | TYR | ARG | LYS | LEU | ||||
| 4 | ALA | LEU | LYS | TYR | HIS | PRO | ASP | LYS | ASN | PRO | ||||
| 5 | ASN | GLU | GLY | GLU | LYS | PHE | LYS | GLN | ILE | SER | ||||
| 6 | GLN | ALA | TYR | GLU | VAL | LEU | SER | ASP | ALA | LYS | ||||
| 7 | LYS | ARG | GLU | LEU | TYR | ASP | LYS | GLY | GLY | GLU | ||||
| 8 | GLN |
Samples:
sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium azide 5 mM; sodium chloride 50 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.080 M; 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 |
| 4D HACANH APSY | sample_1 | isotropic | sample_conditions_1 |
| 5D HACACONH APSY | sample_1 | isotropic | sample_conditions_1 |
| 5D CBCACONH APSY | 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 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, G ntert P. - structure solution
TOPSPIN v2.1, Bruker - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 19163 |
| PDB | |
| DBJ | BAA02656 BAC38744 BAC82111 BAD82815 BAE26788 |
| EMBL | CAI29674 |
| GB | AAA98855 AAC37517 AAC78597 AAH08182 AAH57876 |
| PIR | S34632 |
| REF | NP_001015637 NP_001127102 NP_001158143 NP_001158144 NP_001231092 |
| SP | P31689 P63036 P63037 Q5E954 Q5NVI9 |
| TPG | DAA12974 DAA26671 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts