BMRB Entry 17030
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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/BMR17030
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Title: Solution NMR Structure of the Ras-binding domain of Serine/threonine-protein kinase B-raf from Homo sapiens, Northeast Structural Genomics Consortium Target HR4694F
Deposition date: 2010-06-30 Original release date: 2010-07-07
Authors: Aramini, James; Janjua, Haleema; Ciccosanti, Colleen; Shastry, Ritu; Huang, Yuanpeng; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano
Citation: Aramini, James; Janjua, Haleema; Ciccosanti, Colleen; Shastry, Ritu; Huang, Yuanpeng; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano. "Solution NMR Structure of the Ras-binding domain of Serine/threonine-protein kinase B-raf from Homo sapiens, Northeast Structural Genomics Consortium Target HR4694F" To be published ., .-..
Assembly members:
HR4694F, polymer, 95 residues, 9778.635 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):
HR4694F: MGHHHHHHSHMPKSPQKPIV
RVFLPNKQRTVVPARCGVTV
RDSLKKALMMRGLIPECCAV
YRIQDGEKKPIGWDTDISWL
TGEELHVEVLENVPL
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 394 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 640 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR4694F | 1 |
Entities:
Entity 1, HR4694F 95 residues - 9778.635 Da.
N-terminal MGHHHHHHSHM tag.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | PRO | LYS | SER | PRO | GLN | LYS | PRO | ILE | VAL | ||||
| 3 | ARG | VAL | PHE | LEU | PRO | ASN | LYS | GLN | ARG | THR | ||||
| 4 | VAL | VAL | PRO | ALA | ARG | CYS | GLY | VAL | THR | VAL | ||||
| 5 | ARG | ASP | SER | LEU | LYS | LYS | ALA | LEU | MET | MET | ||||
| 6 | ARG | GLY | LEU | ILE | PRO | GLU | CYS | CYS | ALA | VAL | ||||
| 7 | TYR | ARG | ILE | GLN | ASP | GLY | GLU | LYS | LYS | PRO | ||||
| 8 | ILE | GLY | TRP | ASP | THR | ASP | ILE | SER | TRP | LEU | ||||
| 9 | THR | GLY | GLU | GLU | LEU | HIS | VAL | GLU | VAL | LEU | ||||
| 10 | GLU | ASN | VAL | PRO | LEU |
Samples:
sample_1: HR4694F, [U-100% 13C; U-100% 15N], 0.84 mM; ammonium acetate 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; DSS 50 uM; H2O 90%; D2O 10%
sample_2: HR4694F, [U-5% 13C; U-100% 15N], 0.69 mM; ammonium acetate 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; DSS 50 uM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 4.5; 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 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 |
| 2D 1H-13C HSQC high resolution (L/V methyl stereoassignment) | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N hetNOE | sample_1 | isotropic | sample_conditions_1 |
| 1D 15N T1 and T2 | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,structure solution
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF analysis
PSVS v1.4, Bhattacharya and Montelione - structure quality analysis
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
MolProbity v3.17, Richardson - structure quality analysis
TOPSPIN v2.1, Bruker Biospin - collection, data analysis
PDBStat v5.1, Tejero & Montelione - PDB coordinate analysis
PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY v3.112, Goddard - data analysis, peak picking
TALOS+, Shen, Cornilescu, Delaglio and Bax - dihedral angle constraints
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAD19009 BAE02474 BAE24384 BAI47380 |
| EMBL | CAA46301 CAA47436 CAB81555 |
| GB | AAA35609 AAA49492 AAA49493 AAI01758 AAI12080 |
| PIR | I51153 |
| REF | NP_004324 NP_647455 NP_990633 XP_001070228 XP_001496314 |
| SP | P15056 P28028 P34908 Q04982 |
| TPG | DAA30146 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts