BMRB Entry 17508
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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/BMR17508
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Title: Solution NMR Structure of RRM domain of RNA-binding protein FUS from homo sapiens, Northeast Structural Genomics onsortium Target HR6430A
Deposition date: 2011-03-04 Original release date: 2011-05-02
Authors: Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Lee, Hsiau-Wei; Acton, Thomas; Everett, John; Huang, Yuanpeng; Montelione, Gaetano
Citation: Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Lee, Hsiau-Wei; Ciccosanti, Colleen; Acton, Thomas; Everett, John; Huang, Yuanpeng; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target HR6430A" To be published ., .-..
Assembly members:
HR6430A, polymer, 99 residues, 10970.295 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):
HR6430A: MGHHHHHHSHSDNNTIFVQG
LGENVTIESVADYFKQIGII
KTNKKTGQPMINLYTDRETG
KLKGEATVSFDDPPSAKAAI
DWFDGKEFSGNPIKVSFAT
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 13C chemical shifts | 391 |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 620 |
| residual dipolar couplings | 69 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR6430A | 1 |
Entities:
Entity 1, HR6430A 99 residues - 10970.295 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | SER | ASP | ASN | ASN | THR | ILE | PHE | VAL | GLN | GLY | ||||
| 3 | LEU | GLY | GLU | ASN | VAL | THR | ILE | GLU | SER | VAL | ||||
| 4 | ALA | ASP | TYR | PHE | LYS | GLN | ILE | GLY | ILE | ILE | ||||
| 5 | LYS | THR | ASN | LYS | LYS | THR | GLY | GLN | PRO | MET | ||||
| 6 | ILE | ASN | LEU | TYR | THR | ASP | ARG | GLU | THR | GLY | ||||
| 7 | LYS | LEU | LYS | GLY | GLU | ALA | THR | VAL | SER | PHE | ||||
| 8 | ASP | ASP | PRO | PRO | SER | ALA | LYS | ALA | ALA | ILE | ||||
| 9 | ASP | TRP | PHE | ASP | GLY | LYS | GLU | PHE | SER | GLY | ||||
| 10 | ASN | PRO | ILE | LYS | VAL | SER | PHE | ALA | THR |
Samples:
sample_NC: HR6430A, [U-100% 13C; U-100% 15N], 0.83 mM; NaN3 0.02%; DTT 10 mM; CaCl2 5 mM; NaCl 100 mM; Proteinase Inhibitor 1; MES 20 mM; DSS 50 uM; H2O 95%; D2O 5%
sample_NC5: HR6430A, [U-5% 13C; U-100% 15N], 0.794 mM; NaN3 0.02%; DTT 10 mM; CaCl2 5 mM; NaCl 100 mM; Proteinase Inhibitor 1; MES 20 mM; DSS 50 uM; H2O 95%; D2O 5%
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_NC5 | 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-15N HSQC | sample_NC5 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution
AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts