BMRB Entry 10067
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10067
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Title: Solution Structure of The FHA Domain of Arabidopsis thaliana Hypothetical Protein
Deposition date: 2006-12-25 Original release date: 2008-08-14
Authors: Tomizawa, T.; Inoue, M.; Koshiba, S.; Hayashi, F.; Shirouzu, M.; Terada, T.; Yabuki, T.; Aoki, M.; Matsuda, T.; Seki, E.; Hirota, H.; Yoshida, M.; Tanaka, A.; Osanai, T.; Shinozaki, K.; Seki, M.; Kigawa, T.; Yokoyama, S.
Citation: Tomizawa, T.; Inoue, M.; Koshiba, S.; Hayashi, F.; Shirouzu, M.; Terada, T.; Yabuki, T.; Aoki, M.; Matsuda, T.; Seki, E.; Hirota, H.; Yoshida, M.; Tanaka, A.; Osanai, T.; Shinozaki, K.; Seki, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of The FHA Domain of Arabidopsis thaliana Hypothetical Protein" . ., .-..
Assembly members:
Forkhead Associated Domain, FHA domain, polymer, 118 residues, Formula weight is not available
Natural source: Common Name: thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: cell free synthesis
Entity Sequences (FASTA):
Forkhead Associated Domain, FHA domain: GSSGSSGMVTPSLRLVFVKG
PREGDALDYKPGSTIRVGRI
VRGNEIAIKDAGISTKHLRI
ESDSGNWVIQDLGSSNGTLL
NSNALDPETSVNLGDGDVIK
LGEYTSILVNFVSGPSSG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 473 |
15N chemical shifts | 113 |
1H chemical shifts | 761 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | expressed protein | 1 |
Entities:
Entity 1, expressed protein 118 residues - Formula weight is not available
1 | GLY | SER | SER | GLY | SER | SER | GLY | MET | VAL | THR | ||||
2 | PRO | SER | LEU | ARG | LEU | VAL | PHE | VAL | LYS | GLY | ||||
3 | PRO | ARG | GLU | GLY | ASP | ALA | LEU | ASP | TYR | LYS | ||||
4 | PRO | GLY | SER | THR | ILE | ARG | VAL | GLY | ARG | ILE | ||||
5 | VAL | ARG | GLY | ASN | GLU | ILE | ALA | ILE | LYS | ASP | ||||
6 | ALA | GLY | ILE | SER | THR | LYS | HIS | LEU | ARG | ILE | ||||
7 | GLU | SER | ASP | SER | GLY | ASN | TRP | VAL | ILE | GLN | ||||
8 | ASP | LEU | GLY | SER | SER | ASN | GLY | THR | LEU | LEU | ||||
9 | ASN | SER | ASN | ALA | LEU | ASP | PRO | GLU | THR | SER | ||||
10 | VAL | ASN | LEU | GLY | ASP | GLY | ASP | VAL | ILE | LYS | ||||
11 | LEU | GLY | GLU | TYR | THR | SER | ILE | LEU | VAL | ASN | ||||
12 | PHE | VAL | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: FHA domain, [U-13C; U-15N], 1.09 mM; Tris-HCl 20 mM; NaCl 100 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 13C-separated NOESY | not available | not available | not available |
3D 15N-separated NOESY | not available | not available | not available |
Software:
VNMR v6.1C, Varian - collection
NMRPipe v20020425, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.820, Kobayashi, N. - data analysis
CYANA v1.0.7, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Varian INOVA 800 MHz
Related Database Links:
PDB | |
EMBL | CAB10228 CAB78491 |
GB | AAM20599 AAM91265 AEE83450 |
REF | NP_193185 |
SP | O23305 |
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