BMRB Entry 17314
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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/BMR17314
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Title: Solution Structure of a Nonphosphorylated Peptide Recognizing Domain
Deposition date: 2010-11-22 Original release date: 2012-07-25
Authors: Dai, Kun; Liao, Shanhui; Zhang, Jiahai; Zhang, Xuecheng; Tu, Xiaoming
Citation: Dai, Kun; Liao, Shanhui; Zhang, Jiahai; Zhang, Xuecheng; Tu, Xiaoming. "Solution Structure of a Nonphosphorylated Peptide Recognizing Domain" .
Assembly members:
Protein_Domain, polymer, 123 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: not available Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22
Entity Sequences (FASTA):
Protein_Domain: MDTSKFWYKPHLSRDQAIAL
LKDKDPGAFLIRDSHSFQGA
YGLALKVATPPPSAQPWKGD
PVEQLVRHFLIETGPKGVKI
KGCPSEPYFGSLSALVSQHS
ISPISLPCCLRIPSKLEHHH
HHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 388 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 678 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Nonphosphorylated Peptide Recognizing Domain | 1 |
Entities:
Entity 1, Nonphosphorylated Peptide Recognizing Domain 123 residues - Formula weight is not available
| 1 | MET | ASP | THR | SER | LYS | PHE | TRP | TYR | LYS | PRO | ||||
| 2 | HIS | LEU | SER | ARG | ASP | GLN | ALA | ILE | ALA | LEU | ||||
| 3 | LEU | LYS | ASP | LYS | ASP | PRO | GLY | ALA | PHE | LEU | ||||
| 4 | ILE | ARG | ASP | SER | HIS | SER | PHE | GLN | GLY | ALA | ||||
| 5 | TYR | GLY | LEU | ALA | LEU | LYS | VAL | ALA | THR | PRO | ||||
| 6 | PRO | PRO | SER | ALA | GLN | PRO | TRP | LYS | GLY | ASP | ||||
| 7 | PRO | VAL | GLU | GLN | LEU | VAL | ARG | HIS | PHE | LEU | ||||
| 8 | ILE | GLU | THR | GLY | PRO | LYS | GLY | VAL | LYS | ILE | ||||
| 9 | LYS | GLY | CYS | PRO | SER | GLU | PRO | TYR | PHE | GLY | ||||
| 10 | SER | LEU | SER | ALA | LEU | VAL | SER | GLN | HIS | SER | ||||
| 11 | ILE | SER | PRO | ILE | SER | LEU | PRO | CYS | CYS | LEU | ||||
| 12 | ARG | ILE | PRO | SER | LYS | LEU | GLU | HIS | HIS | HIS | ||||
| 13 | HIS | HIS | HIS |
Samples:
sample: Protein Domain, [U-99% 13C; U-99% 15N], 0.6 mM; sodium chloride 150 mM; sodium phosphate 20 mM; EDTA 2 mM; Arginine 50 mM; glutamine 50 mM; H2O 90%; D2O 10%
sample_conditions: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample | isotropic | sample_conditions |
| 3D CBCA(CO)NH | sample | isotropic | sample_conditions |
| 3D HNCACB | sample | isotropic | sample_conditions |
| 3D C(CO)NH | sample | isotropic | sample_conditions |
| 3D HBHA(CO)NH | sample | isotropic | sample_conditions |
| 3D H(CCO)NH | sample | isotropic | sample_conditions |
| 3D HN(CO)CA | sample | isotropic | sample_conditions |
| 3D 1H-15N NOESY | sample | isotropic | sample_conditions |
| 3D 1H-13C NOESY | sample | isotropic | sample_conditions |
| 3D HCCH-COSY | sample | isotropic | sample_conditions |
Software:
CYANA, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Guntert, Mumenthaler and Wuthrich - data analysis, processing, structure solution
NMR spectrometers:
- Bruker DMX 500 MHz
Related Database Links:
| BMRB | 16472 |
| PDB | |
| DBJ | BAA83027 BAG09960 |
| EMBL | CAB70815 CAH56176 |
| GB | AAH25818 AAH42190 AAH54099 AAI10855 AAI29829 |
| REF | NP_056134 NP_705761 NP_736610 NP_938072 XP_001102202 |
| SP | Q63HR2 Q8CGB6 |
| AlphaFold | Q63HR2 Q8CGB6 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts