BMRB Entry 30332
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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/BMR30332
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Title: Abl1b Regulatory Module 'Activating' conformation PubMed: 28945248
Deposition date: 2017-08-11 Original release date: 2017-09-25
Authors: Kalodimos, C.; Rossi, P.; Saleh, T.
Citation: Kalodimos, C.; Rossi, P.; Saleh, T.. "Atomic view of the energy landscape in the allosteric regulation of Abl kinase" Nat. Struct. Mol. Biol. 24, 893-901 (2017).
Assembly members:
Tyrosine-protein kinase ABL1, polymer, 255 residues, 28350.389 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 BL21
Entity Sequences (FASTA):
Tyrosine-protein kinase ABL1: MGQQPGKVLGDQRRPSLPAL
HFIKGAGKRESSRHGGPHCN
VFVEHEALQRPVASDFEPQG
LSEAARWNSKENLLAGPSEN
DPNLFVALYDFVASGDNTLS
ITKGEKLRVLGYNHNGEWAE
AQTKNGQGWVPSNYITPVNS
LEKHSWYHGPVSRNAAEYLL
SSGINGSFLVRESESSPGQR
SISLRYEGRVYHYRINTASD
GKLYVSSESRFNTLAELVHH
HSTVADGLITTLHYPAPKRN
KPTVYGVSPNYDKWE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 834 |
| 15N chemical shifts | 180 |
| 1H chemical shifts | 1257 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 255 residues - 28350.389 Da.
| 1 | MET | GLY | GLN | GLN | PRO | GLY | LYS | VAL | LEU | GLY | ||||
| 2 | ASP | GLN | ARG | ARG | PRO | SER | LEU | PRO | ALA | LEU | ||||
| 3 | HIS | PHE | ILE | LYS | GLY | ALA | GLY | LYS | ARG | GLU | ||||
| 4 | SER | SER | ARG | HIS | GLY | GLY | PRO | HIS | CYS | ASN | ||||
| 5 | VAL | PHE | VAL | GLU | HIS | GLU | ALA | LEU | GLN | ARG | ||||
| 6 | PRO | VAL | ALA | SER | ASP | PHE | GLU | PRO | GLN | GLY | ||||
| 7 | LEU | SER | GLU | ALA | ALA | ARG | TRP | ASN | SER | LYS | ||||
| 8 | GLU | ASN | LEU | LEU | ALA | GLY | PRO | SER | GLU | ASN | ||||
| 9 | ASP | PRO | ASN | LEU | PHE | VAL | ALA | LEU | TYR | ASP | ||||
| 10 | PHE | VAL | ALA | SER | GLY | ASP | ASN | THR | LEU | SER | ||||
| 11 | ILE | THR | LYS | GLY | GLU | LYS | LEU | ARG | VAL | LEU | ||||
| 12 | GLY | TYR | ASN | HIS | ASN | GLY | GLU | TRP | ALA | GLU | ||||
| 13 | ALA | GLN | THR | LYS | ASN | GLY | GLN | GLY | TRP | VAL | ||||
| 14 | PRO | SER | ASN | TYR | ILE | THR | PRO | VAL | ASN | SER | ||||
| 15 | LEU | GLU | LYS | HIS | SER | TRP | TYR | HIS | GLY | PRO | ||||
| 16 | VAL | SER | ARG | ASN | ALA | ALA | GLU | TYR | LEU | LEU | ||||
| 17 | SER | SER | GLY | ILE | ASN | GLY | SER | PHE | LEU | VAL | ||||
| 18 | ARG | GLU | SER | GLU | SER | SER | PRO | GLY | GLN | ARG | ||||
| 19 | SER | ILE | SER | LEU | ARG | TYR | GLU | GLY | ARG | VAL | ||||
| 20 | TYR | HIS | TYR | ARG | ILE | ASN | THR | ALA | SER | ASP | ||||
| 21 | GLY | LYS | LEU | TYR | VAL | SER | SER | GLU | SER | ARG | ||||
| 22 | PHE | ASN | THR | LEU | ALA | GLU | LEU | VAL | HIS | HIS | ||||
| 23 | HIS | SER | THR | VAL | ALA | ASP | GLY | LEU | ILE | THR | ||||
| 24 | THR | LEU | HIS | TYR | PRO | ALA | PRO | LYS | ARG | ASN | ||||
| 25 | LYS | PRO | THR | VAL | TYR | GLY | VAL | SER | PRO | ASN | ||||
| 26 | TYR | ASP | LYS | TRP | GLU |
Samples:
sample_1: Abl1b, [U-99% 13C; U-99% 15N], 0.3 mM; beta-mercaptoethanol 5 mM; potassium chloride 100 mM; potassium phosphate 20 mM; sodium azide 0.05%
sample_conditions_1: ionic strength: 120 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY, Goddard - peak picking
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker AvanceIII 850 MHz
- Bruker AvanceIII 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts