BMRB Entry 18526
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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/BMR18526
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Title: Solution NMR Structure of PH Domain of Tyrosine-protein kinase Tec from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR3504C
Deposition date: 2012-06-15 Original release date: 2012-08-13
Authors: Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Hamilton, Keith; Shastry, Ritu; Kohan, Eitan; Acton, Thomas; Everett, John; Lee, Hsiau-Wei; Pederson, Kari; Huang, Yuangpeng; Montelione, Gaetano
Citation: Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Hamilton, Keith; Shastry, Ritu; Kohan, Eitan; Acton, Thomas; Everett, John; Lee, Hsiau-Wei; Pederson, Kari; Huang, Yuangpeng; Montelione, Gaetano. "Solution NMR Structure of PH Domain of Tyrosine-protein kinase Tec from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR3504C" To be published ., .-..
Assembly members:
HR3504C, polymer, 165 residues, 19577.119 Da.
ZINC ION, non-polymer, 65.409 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):
HR3504C: MGHHHHHHSHMNFNTILEEI
LIKRSQQKKKTSPLNYKERL
FVLTKSMLTYYEGRAEKKYR
KGFIDVSKIKCVEIVKNDDG
VIPCQNKYPFQVVHDANTLY
IFAPSPQSRDLWVKKLKEEI
KNNNNIMIKYHPKFWTDGSY
QCCRQTEKLAPGCEKYNLFE
SSIRX
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 13C chemical shifts | 700 |
| 15N chemical shifts | 152 |
| 1H chemical shifts | 1131 |
| residual dipolar couplings | 67 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR3504C | 1 |
| 2 | Zinc ion | 2 |
Entities:
Entity 1, HR3504C 165 residues - 19577.119 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | ASN | PHE | ASN | THR | ILE | LEU | GLU | GLU | ILE | ||||
| 3 | LEU | ILE | LYS | ARG | SER | GLN | GLN | LYS | LYS | LYS | ||||
| 4 | THR | SER | PRO | LEU | ASN | TYR | LYS | GLU | ARG | LEU | ||||
| 5 | PHE | VAL | LEU | THR | LYS | SER | MET | LEU | THR | TYR | ||||
| 6 | TYR | GLU | GLY | ARG | ALA | GLU | LYS | LYS | TYR | ARG | ||||
| 7 | LYS | GLY | PHE | ILE | ASP | VAL | SER | LYS | ILE | LYS | ||||
| 8 | CYS | VAL | GLU | ILE | VAL | LYS | ASN | ASP | ASP | GLY | ||||
| 9 | VAL | ILE | PRO | CYS | GLN | ASN | LYS | TYR | PRO | PHE | ||||
| 10 | GLN | VAL | VAL | HIS | ASP | ALA | ASN | THR | LEU | TYR | ||||
| 11 | ILE | PHE | ALA | PRO | SER | PRO | GLN | SER | ARG | ASP | ||||
| 12 | LEU | TRP | VAL | LYS | LYS | LEU | LYS | GLU | GLU | ILE | ||||
| 13 | LYS | ASN | ASN | ASN | ASN | ILE | MET | ILE | LYS | TYR | ||||
| 14 | HIS | PRO | LYS | PHE | TRP | THR | ASP | GLY | SER | TYR | ||||
| 15 | GLN | CYS | CYS | ARG | GLN | THR | GLU | LYS | LEU | ALA | ||||
| 16 | PRO | GLY | CYS | GLU | LYS | TYR | ASN | LEU | PHE | GLU | ||||
| 17 | SER | SER | ILE | ARG | ZN |
Entity 2, Zinc ion - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_NC: hr3504c.023, [U-100% 13C; U-100% 15N], 0.614 mM; DSS 50 uM; DTT 10 mM; ZnSO4 50 uM; NaN3 0.02%; NaCL 100 mM; MES pH 6.5 20 mM; Proteinase Inhibitors 1 X; D2O 10%; H2O 90%
sample_NC5: hr3504c.025, [U-5% 13C; U-100% 15N], 0.828 mM; DSS 50 uM; DTT 10 mM; ZnSO4 50 uM; NaN3 0.02%; NaCL 100 mM; MES pH 6.5 20 mM; Proteinase Inhibitors 1 X; D2O 10%; H2O 90%
sample_NC5_RDC: hr3504c.027, [U-5% 13C; U-100% 15N], 0.52 mM; DSS 50 uM; DTT 10 mM; ZnSO4 50 uM; NaN3 0.02%; NaCL 100 mM; MES pH 6.5 20 mM; Proteinase Inhibitors 1 X; D2O 10%; H2O 90%
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_NC | isotropic | sample_conditions_1 |
| 3D HNCO | sample_NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_NC | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_NC | isotropic | sample_conditions_1 |
| 3D 1H-13C arom NOESY | sample_NC | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_NC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_NC | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_NC5 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_NC5_RDC | isotropic | sample_conditions_1 |
Software:
CNS, 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 v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
REDCAT, Valafar, Prestegard - geometry optimization
PSVS, Bhattacharya, Montelione - structure validation
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA06171 |
| GB | AAI01712 AAI01714 AAI43488 AAQ02597 EAW93055 |
| REF | NP_003206 XP_001103213 XP_001493391 XP_002688295 XP_002806710 |
| SP | P42680 |
| TPG | DAA28680 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts