BMRB Entry 19314
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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/BMR19314
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Title: Solution NMR Structure of Microtubule-associated serine/threonine-protein kinase 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR9151A
Deposition date: 2013-06-20 Original release date: 2013-07-08
Authors: Xu, Xianzhong; Eletsky, Alexander; Shastry, Ritu; Lee, Dan; Hamilton, Keith; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas
Citation: Xu, Xianzhong; Eletsky, Alexander; Shastry, Ritu; Lee, Dan; Hamilton, Keith; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Microtubule-associated serine/threonine-protein kinase 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR9151A" To be published ., .-..
Assembly members:
HR9151A, polymer, 112 residues, 13040.079 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):
HR9151A: MGHHHHHHSHMPKATAQMEE
KLRDFTRAYEPDSVLPLADG
VLSFIHHQIIELARDCLTKS
RDGLITTVYFYELQENLEKL
LQDAYERSESLEVAFVTQLV
KKLLIIISRPAR
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 453 |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 743 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR9151A | 1 |
Entities:
Entity 1, HR9151A 112 residues - 13040.079 Da.
First 11 residues are the purification His tag. Residues 12-112 represents that native protein from residue 187 to 287.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | PRO | LYS | ALA | THR | ALA | GLN | MET | GLU | GLU | ||||
| 3 | LYS | LEU | ARG | ASP | PHE | THR | ARG | ALA | TYR | GLU | ||||
| 4 | PRO | ASP | SER | VAL | LEU | PRO | LEU | ALA | ASP | GLY | ||||
| 5 | VAL | LEU | SER | PHE | ILE | HIS | HIS | GLN | ILE | ILE | ||||
| 6 | GLU | LEU | ALA | ARG | ASP | CYS | LEU | THR | LYS | SER | ||||
| 7 | ARG | ASP | GLY | LEU | ILE | THR | THR | VAL | TYR | PHE | ||||
| 8 | TYR | GLU | LEU | GLN | GLU | ASN | LEU | GLU | LYS | LEU | ||||
| 9 | LEU | GLN | ASP | ALA | TYR | GLU | ARG | SER | GLU | SER | ||||
| 10 | LEU | GLU | VAL | ALA | PHE | VAL | THR | GLN | LEU | VAL | ||||
| 11 | LYS | LYS | LEU | LEU | ILE | ILE | ILE | SER | ARG | PRO | ||||
| 12 | ALA | ARG |
Samples:
HR9151A.011: HR9151A.011, [U-100% 13C; U-100% 15N], 0.508 mM; DTT 5 mM; NaCl 100 mM; Tris-HCl pH 7.5 10 mM; NaN3 0.02%; DSS 50 uM
HR9151A.009: HR9151A.011, [%5-13C; U-100% 15N], 0.39 mM; DTT 5 mM; NaCl 100 mM; Tris-HCl pH 7.5 10 mM; NaN3 0.02%; DSS 50 uM
sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | HR9151A.011 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT HSQC aliphatic | HR9151A.011 | isotropic | sample_conditions_1 |
| 3D HNCO | HR9151A.011 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | HR9151A.011 | isotropic | sample_conditions_1 |
| 3D HNCACB | HR9151A.011 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT HSQC aromatic | HR9151A.011 | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | HR9151A.011 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | HR9151A.011 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | HR9151A.011 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | HR9151A.011 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC_wide | HR9151A.011 | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSYali | HR9151A.011 | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSYaro | HR9151A.011 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC methyl | HR9151A.009 | isotropic | sample_conditions_1 |
Software:
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution
AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement
AutoAssign v2.3.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment
XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment
VNMRJ v2.2D, Varian - collection
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PSVS v1.4, Bhattacharya, Montelione - structure validation
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
PROSA, Guntert - processing
CSI, (CSI)-Wishart and Sykes - data analysis
NMR spectrometers:
- Varian INOVA 750 MHz
Related Database Links:
| UNP | Q9Y2H9 |
| PDB | |
| REF | XP_004023623 XP_007622501 XP_008046233 XP_010853832 XP_011287990 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts