BMRB Entry 30772
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30772
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: Xie, T.; Saleh, T.; Rossi, P.; Kalodimos, C.. "Conformational states dynamically populated by a kinase determine its function" Science 370, eabc2754-eabc2754 (2020).
PubMed: 33004676
Assembly members:
entity_1, polymer, 287 residues, 33296.992 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(DE3)
Entity Sequences (FASTA):
entity_1: SPNYDKWEMERTDITMKHKL
GEGQYGEVYEGVWKKYSLTV
AVKTLKEDTMEVEEFLKEAA
VLKEIKHPNLVQLLGVCTRE
PPFYIITEFMTYGNLLDYLR
ECNRQEVNAVVLLYMATQIS
SAMEYLEKKNFIHRDLAARN
CLVGENHLVKVADFGLSRLM
YGDTYTAHAGAKFPIKWTAP
ESLAYNKFSIKSDVWAFGVL
LWEIATYGMSPYPGIDLSQV
YELLEKDYRMERPEGCPEKV
YELMRACWQWNPSDRPSFAE
IHQAFETMFQESSISDEVEK
ELGKQGV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 139 |
| 1H chemical shifts | 414 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 287 residues - 33296.992 Da.
| 1 | SER | PRO | ASN | TYR | ASP | LYS | TRP | GLU | MET | GLU | ||||
| 2 | ARG | THR | ASP | ILE | THR | MET | LYS | HIS | LYS | LEU | ||||
| 3 | GLY | GLU | GLY | GLN | TYR | GLY | GLU | VAL | TYR | GLU | ||||
| 4 | GLY | VAL | TRP | LYS | LYS | TYR | SER | LEU | THR | VAL | ||||
| 5 | ALA | VAL | LYS | THR | LEU | LYS | GLU | ASP | THR | MET | ||||
| 6 | GLU | VAL | GLU | GLU | PHE | LEU | LYS | GLU | ALA | ALA | ||||
| 7 | VAL | LEU | LYS | GLU | ILE | LYS | HIS | PRO | ASN | LEU | ||||
| 8 | VAL | GLN | LEU | LEU | GLY | VAL | CYS | THR | ARG | GLU | ||||
| 9 | PRO | PRO | PHE | TYR | ILE | ILE | THR | GLU | PHE | MET | ||||
| 10 | THR | TYR | GLY | ASN | LEU | LEU | ASP | TYR | LEU | ARG | ||||
| 11 | GLU | CYS | ASN | ARG | GLN | GLU | VAL | ASN | ALA | VAL | ||||
| 12 | VAL | LEU | LEU | TYR | MET | ALA | THR | GLN | ILE | SER | ||||
| 13 | SER | ALA | MET | GLU | TYR | LEU | GLU | LYS | LYS | ASN | ||||
| 14 | PHE | ILE | HIS | ARG | ASP | LEU | ALA | ALA | ARG | ASN | ||||
| 15 | CYS | LEU | VAL | GLY | GLU | ASN | HIS | LEU | VAL | LYS | ||||
| 16 | VAL | ALA | ASP | PHE | GLY | LEU | SER | ARG | LEU | MET | ||||
| 17 | TYR | GLY | ASP | THR | TYR | THR | ALA | HIS | ALA | GLY | ||||
| 18 | ALA | LYS | PHE | PRO | ILE | LYS | TRP | THR | ALA | PRO | ||||
| 19 | GLU | SER | LEU | ALA | TYR | ASN | LYS | PHE | SER | ILE | ||||
| 20 | LYS | SER | ASP | VAL | TRP | ALA | PHE | GLY | VAL | LEU | ||||
| 21 | LEU | TRP | GLU | ILE | ALA | THR | TYR | GLY | MET | SER | ||||
| 22 | PRO | TYR | PRO | GLY | ILE | ASP | LEU | SER | GLN | VAL | ||||
| 23 | TYR | GLU | LEU | LEU | GLU | LYS | ASP | TYR | ARG | MET | ||||
| 24 | GLU | ARG | PRO | GLU | GLY | CYS | PRO | GLU | LYS | VAL | ||||
| 25 | TYR | GLU | LEU | MET | ARG | ALA | CYS | TRP | GLN | TRP | ||||
| 26 | ASN | PRO | SER | ASP | ARG | PRO | SER | PHE | ALA | GLU | ||||
| 27 | ILE | HIS | GLN | ALA | PHE | GLU | THR | MET | PHE | GLN | ||||
| 28 | GLU | SER | SER | ILE | SER | ASP | GLU | VAL | GLU | LYS | ||||
| 29 | GLU | LEU | GLY | LYS | GLN | GLY | VAL |
Samples:
sample_1: Abl 1b G269E/M309L/T408Y variant, [U-100% 13C; U-100% 15N; U-100% 2H], 250 uM; sodium phosphate 25 mM; sodium chloride 75 mM; beta-mercaptoethanol 2.5 mM
sample_2: Abl 1b G269E/M309L/T408Y variant, N-ILVMAT-FY, 250 uM; sodium phosphate 25 mM; sodium chloride 75 mM; beta-mercaptoethanol 2.5 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.7; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HMQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_2 | isotropic | sample_conditions_1 |
| 3D CaCmHm_sofastNOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D CCH NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
I-PINE, Lee, Bahrami, Dashti, Eghbalnia, Tonelli, Westler and Markley - chemical shift assignment
Sparky, Goddard - peak picking
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
PSVS, Bhattacharya and Montelione - refinement
TopSpin, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker AVANCE 1100 MHz
- Bruker AVANCE 850 MHz