BMRB Entry 16996
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                PDB ID: 
                
                
                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16996
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Rad51D from 1 to 83 PubMed: 21111057
Deposition date: 2010-06-11 Original release date: 2011-06-01
Authors: Choi, Byong-Seok; Kim, Young Mee
Citation: Kim, Young Mee; Choi, Byong-Seok. "Structural and functional characterization of the N-terminal domain of human Rad51D." Int. J. Biochem. Cell Biol. 43, 416-422 (2011).
Assembly members:
human_Rad51D_N, polymer, 83 residues,   9070.740 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):
human_Rad51D_N: MGVLRVGLCPGLTEEMIQLL
RSHRIKTVVDLVSADLEEVA
QKCGLSYKALVALRRVLLAQ
FSAFPVNGADLYEELKTSTA
ILS
- assigned_chemical_shifts
 
| Data type | Count | 
| 13C chemical shifts | 333 | 
| 15N chemical shifts | 80 | 
| 1H chemical shifts | 587 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | human Rad51D N | 1 | 
Entities:
Entity 1, human Rad51D N 83 residues - 9070.740 Da.
| 1 | MET | GLY | VAL | LEU | ARG | VAL | GLY | LEU | CYS | PRO | ||||
| 2 | GLY | LEU | THR | GLU | GLU | MET | ILE | GLN | LEU | LEU | ||||
| 3 | ARG | SER | HIS | ARG | ILE | LYS | THR | VAL | VAL | ASP | ||||
| 4 | LEU | VAL | SER | ALA | ASP | LEU | GLU | GLU | VAL | ALA | ||||
| 5 | GLN | LYS | CYS | GLY | LEU | SER | TYR | LYS | ALA | LEU | ||||
| 6 | VAL | ALA | LEU | ARG | ARG | VAL | LEU | LEU | ALA | GLN | ||||
| 7 | PHE | SER | ALA | PHE | PRO | VAL | ASN | GLY | ALA | ASP | ||||
| 8 | LEU | TYR | GLU | GLU | LEU | LYS | THR | SER | THR | ALA | ||||
| 9 | ILE | LEU | SER | 
Samples:
sample_1: human Rad51D_N, [U-100% 15N], 1 mM; DTT 1 mM; sodium azide 0.02%; Tris-HCl 25 mM; NaCl 100 mM; D2O 100%
sample_2: human Rad51D_N, [U-99% 13C; U-99% 15N], 1 mM; TRIS 25 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 0.02%; D2O 100%
sample_3: human Rad51D_N, [U-99% 15N], 1 mM; TRIS 25 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 0.02%; D2O 90%; H2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 287 K
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 | 
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 | 
| 3D 1H-15N TOCSY | sample_3 | isotropic | sample_conditions_1 | 
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 | 
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 | 
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 | 
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 | 
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 | 
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 | 
Software:
CYANA v2.1, P.GUNTERT ET AL. - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
 - Bruker Avance 800 MHz
 
Related Database Links:
| PDB | |
| DBJ | BAA25914 BAA31747 BAA31748 BAA33779 BAA33780 | 
| EMBL | CAA75681 | 
| GB | AAC39719 AAH14422 AAT38112 ABM83244 ABM86446 | 
| REF | NP_002869 XP_001174459 XP_003818041 XP_004041973 XP_008969520 | 
| SP | O75771 | 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts