BMRB Entry 10164
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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/BMR10164
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Title: Solution structure of the A1pp domain from human protein C6orf130
Deposition date: 2007-12-28 Original release date: 2009-02-23
Authors: Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation: Tomizawa, T.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the A1pp domain from human protein C6orf130" . ., .-..
Assembly members:
A1pp domain, polymer, 149 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
Entity Sequences (FASTA):
A1pp domain: GSSGSSGGSRITYVKGDLFA
CPKTDSLAHCISEDCRMGAG
IAVLFKKKFGGVQELLNQQK
KSGEVAVLKRDGRYIYYLIT
KKRASHKPTYENLQKSLEAM
KSHCLKNGVTDLSMPRIGCG
LDRLQWENVSAMIEEVFEAT
DIKITVYTL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 646 |
15N chemical shifts | 146 |
1H chemical shifts | 1029 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Uncharacterized protein C6orf130 | 1 |
Entities:
Entity 1, Uncharacterized protein C6orf130 149 residues - Formula weight is not available
1 | GLY | SER | SER | GLY | SER | SER | GLY | GLY | SER | ARG | ||||
2 | ILE | THR | TYR | VAL | LYS | GLY | ASP | LEU | PHE | ALA | ||||
3 | CYS | PRO | LYS | THR | ASP | SER | LEU | ALA | HIS | CYS | ||||
4 | ILE | SER | GLU | ASP | CYS | ARG | MET | GLY | ALA | GLY | ||||
5 | ILE | ALA | VAL | LEU | PHE | LYS | LYS | LYS | PHE | GLY | ||||
6 | GLY | VAL | GLN | GLU | LEU | LEU | ASN | GLN | GLN | LYS | ||||
7 | LYS | SER | GLY | GLU | VAL | ALA | VAL | LEU | LYS | ARG | ||||
8 | ASP | GLY | ARG | TYR | ILE | TYR | TYR | LEU | ILE | THR | ||||
9 | LYS | LYS | ARG | ALA | SER | HIS | LYS | PRO | THR | TYR | ||||
10 | GLU | ASN | LEU | GLN | LYS | SER | LEU | GLU | ALA | MET | ||||
11 | LYS | SER | HIS | CYS | LEU | LYS | ASN | GLY | VAL | THR | ||||
12 | ASP | LEU | SER | MET | PRO | ARG | ILE | GLY | CYS | GLY | ||||
13 | LEU | ASP | ARG | LEU | GLN | TRP | GLU | ASN | VAL | SER | ||||
14 | ALA | MET | ILE | GLU | GLU | VAL | PHE | GLU | ALA | THR | ||||
15 | ASP | ILE | LYS | ILE | THR | VAL | TYR | THR | LEU |
Samples:
sample_1: A1pp domain, [U-13C; U-15N], 1.22 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 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 13C-separated NOESY | sample_1 | not available | condition_1 |
3D 15N-separated NOESY | sample_1 | not available | condition_1 |
Software:
xwinnmr v3.5, Bruker - collection
NMRPipe v20060524, Delaglio, F - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.9823, Kobayashi, N. - data analysis
CYANA v2.0.17, Guentert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
BMRB | 15593 17421 |
PDB | |
DBJ | BAF83628 BAG36161 |
GB | AAH11709 AIC53444 AIC58012 EAX04011 EAX04012 |
REF | NP_001181654 NP_659500 XP_001117219 XP_001117235 XP_001174030 |
SP | Q9Y530 |
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