BMRB Entry 25104
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25104
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Jankowski, Wojciech; Saleh, Tamjeed; Rossi, Paolo; Kalodimos, Charalampos. "STRUCTURAL BASIS FOR THE REGULATION OF CRKII BY CYCLOPHILIN A" .
Assembly members:
entity_1, polymer, 165 residues, 18036.637 Da.
entity_2, polymer, 9 residues, 955.032 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 Vector: PET28A
Entity Sequences (FASTA):
entity_1: MVNPTVFFDIAVDGEPLGRV
SFELFADKVPKTAENFRALS
TGEKGFGYKGSCFHRIIPGF
MCQGGDFTRHNGTGGKSIYG
EKFEDENFILKHTGPGILSM
ANAGPNTNGSQFFICTAKTE
WLDGKHVVFGKVKEGMNIVE
AMERFGSRNGKTSKKITIAD
CGQLE
entity_2: PEPGPYAQP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 670 |
| 15N chemical shifts | 167 |
| 1H chemical shifts | 1028 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 165 residues - 18036.637 Da.
| 1 | MET | VAL | ASN | PRO | THR | VAL | PHE | PHE | ASP | ILE | ||||
| 2 | ALA | VAL | ASP | GLY | GLU | PRO | LEU | GLY | ARG | VAL | ||||
| 3 | SER | PHE | GLU | LEU | PHE | ALA | ASP | LYS | VAL | PRO | ||||
| 4 | LYS | THR | ALA | GLU | ASN | PHE | ARG | ALA | LEU | SER | ||||
| 5 | THR | GLY | GLU | LYS | GLY | PHE | GLY | TYR | LYS | GLY | ||||
| 6 | SER | CYS | PHE | HIS | ARG | ILE | ILE | PRO | GLY | PHE | ||||
| 7 | MET | CYS | GLN | GLY | GLY | ASP | PHE | THR | ARG | HIS | ||||
| 8 | ASN | GLY | THR | GLY | GLY | LYS | SER | ILE | TYR | GLY | ||||
| 9 | GLU | LYS | PHE | GLU | ASP | GLU | ASN | PHE | ILE | LEU | ||||
| 10 | LYS | HIS | THR | GLY | PRO | GLY | ILE | LEU | SER | MET | ||||
| 11 | ALA | ASN | ALA | GLY | PRO | ASN | THR | ASN | GLY | SER | ||||
| 12 | GLN | PHE | PHE | ILE | CYS | THR | ALA | LYS | THR | GLU | ||||
| 13 | TRP | LEU | ASP | GLY | LYS | HIS | VAL | VAL | PHE | GLY | ||||
| 14 | LYS | VAL | LYS | GLU | GLY | MET | ASN | ILE | VAL | GLU | ||||
| 15 | ALA | MET | GLU | ARG | PHE | GLY | SER | ARG | ASN | GLY | ||||
| 16 | LYS | THR | SER | LYS | LYS | ILE | THR | ILE | ALA | ASP | ||||
| 17 | CYS | GLY | GLN | LEU | GLU |
Entity 2, entity_2 9 residues - 955.032 Da.
| 1 | PRO | GLU | PRO | GLY | PRO | TYR | ALA | GLN | PRO |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.8 mM; H20 90%; D20 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 305 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks