BMRB Entry 11091
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Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11091
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Title: Solution structure of the C-terminal PapD-like domain from human HYDIN protein
Deposition date: 2010-01-18 Original release date: 2011-01-19
Authors: Li, H.; Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation: Li, H.; Sato, M.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the C-terminal PapD-like domain from human HYDIN protein" . ., .-..
Assembly members:
PapD domain, polymer, 112 residues, Formula weight is not available
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: Cell free synthesis Host organism: E. coli - cell free
Entity Sequences (FASTA):
PapD domain: GSSGSSGPKIHFNFELLDIG
KVFTGSAHCYEAILYNKGSI
DALFNMTPPTSALGACFVFS
PKEGIIEPSGVQAIQISFSS
IILGNFEEEFLVNVNGSPEP
VKLTIRGCVIGP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 484 |
| 15N chemical shifts | 107 |
| 1H chemical shifts | 756 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PapD domain | 1 |
Entities:
Entity 1, PapD domain 112 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | PRO | LYS | ILE | ||||
| 2 | HIS | PHE | ASN | PHE | GLU | LEU | LEU | ASP | ILE | GLY | ||||
| 3 | LYS | VAL | PHE | THR | GLY | SER | ALA | HIS | CYS | TYR | ||||
| 4 | GLU | ALA | ILE | LEU | TYR | ASN | LYS | GLY | SER | ILE | ||||
| 5 | ASP | ALA | LEU | PHE | ASN | MET | THR | PRO | PRO | THR | ||||
| 6 | SER | ALA | LEU | GLY | ALA | CYS | PHE | VAL | PHE | SER | ||||
| 7 | PRO | LYS | GLU | GLY | ILE | ILE | GLU | PRO | SER | GLY | ||||
| 8 | VAL | GLN | ALA | ILE | GLN | ILE | SER | PHE | SER | SER | ||||
| 9 | ILE | ILE | LEU | GLY | ASN | PHE | GLU | GLU | GLU | PHE | ||||
| 10 | LEU | VAL | ASN | VAL | ASN | GLY | SER | PRO | GLU | PRO | ||||
| 11 | VAL | LYS | LEU | THR | ILE | ARG | GLY | CYS | VAL | ILE | ||||
| 12 | GLY | PRO |
Samples:
sample_1: PapD domain, [U-13C; U-15N], 1.13 mM; TRIS, [U-2H], 20 mM; sodium chloride 100 mM; DTT, [U-2H], 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
| 3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
xwinnmr v3.5, Bruker - collection
NMRPipe v20030801, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.932, Kobayashi, N. - data analysis
CYANA v2.0.17, Guntert, P. - structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAB14314 BAG61096 BAG61346 |
| EMBL | CAD38687 CAD39007 |
| GB | AAH28351 AIC60203 EAW68881 |
| REF | NP_001185471 NP_001185472 NP_001257903 NP_060028 XP_004057985 |
| SP | Q4G0P3 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
or all simulated shifts