BMRB Entry 10072
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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/BMR10072
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Title: Solution structure of RRM domain in HNRPC protein
Deposition date: 2006-12-25 Original release date: 2008-08-14
Authors: He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.
Citation: He, F.; Muto, Y.; Inoue, M.; Kigawa, T.; Shirouzu, M.; Terada, T.; Yokoyama, S.. "Solution structure of RRM domain in HNRPC protein" . ., .-..
Assembly members:
RRM domain, polymer, 98 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):
RRM domain: GSSGSSGKTDPRSMNSRVFI
GNLNTLVVKKSDVEAIFSKY
GKIVGCSVHKGFAFVQYVNE
RNARAAVAGEDGRMIAGQVL
DINLAAEPKVNRSGPSSG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 376 |
15N chemical shifts | 89 |
1H chemical shifts | 605 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Heterogeneous nuclear ribonucleoproteins C1/C2 | 1 |
Entities:
Entity 1, Heterogeneous nuclear ribonucleoproteins C1/C2 98 residues - Formula weight is not available
1 | GLY | SER | SER | GLY | SER | SER | GLY | LYS | THR | ASP | ||||
2 | PRO | ARG | SER | MET | ASN | SER | ARG | VAL | PHE | ILE | ||||
3 | GLY | ASN | LEU | ASN | THR | LEU | VAL | VAL | LYS | LYS | ||||
4 | SER | ASP | VAL | GLU | ALA | ILE | PHE | SER | LYS | TYR | ||||
5 | GLY | LYS | ILE | VAL | GLY | CYS | SER | VAL | HIS | LYS | ||||
6 | GLY | PHE | ALA | PHE | VAL | GLN | TYR | VAL | ASN | GLU | ||||
7 | ARG | ASN | ALA | ARG | ALA | ALA | VAL | ALA | GLY | GLU | ||||
8 | ASP | GLY | ARG | MET | ILE | ALA | GLY | GLN | VAL | LEU | ||||
9 | ASP | ILE | ASN | LEU | ALA | ALA | GLU | PRO | LYS | VAL | ||||
10 | ASN | ARG | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: RRM domain, [U-13C; U-15N], 0.8 mM; d-Tris-HCl(pH 7.0) 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: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 15N-separated NOESY | sample_1 | not available | condition_1 |
3D 13C-separated NOESY | sample_1 | not available | condition_1 |
Software:
xwinnmr v2.6, Bruker - collection
NMRPipe v20020425, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.863, Kobayashi, N. - data analysis
CYANA v2.0.29, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
PDB | |
GB | AAV66399 EDL42257 EDL42258 |
REF | XP_005372243 XP_009989486 XP_012325381 XP_013226683 |
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