BMRB Entry 18547
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18547
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Title: Solution NMR Structure of CalU16 from Micromonospora echinospora, Northeast Structural Genomics Consortium (NESG) Target MiR12
Deposition date: 2012-06-22 Original release date: 2012-08-27
Authors: Ramelot, Theresa; Yang, Yunhuang; Lee, Hsiau-Wei; Pederson, Kari; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Wrobel, Russel; Bingman, Craig; Singh, Shanteri; Thorson, Jon; Prestegard, James; Montelione, Gaetano; Phillips Jr., George; Kennedy, Michael
Citation: Ramelot, Theresa; Yang, Yunhuang; Lee, Hsiau-Wei; Pederson, Kari; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Wrobel, Russel; Bingman, Craig; Singh, Shanteri; Thorson, Jon; Prestegard, James; Montelione, Gaetano; Phillips Jr., George; Kennedy, Michael. "Solution NMR Structure of CalU16 from Micromonospora echinospora, Northeast Structural Genomics Consortium (NESG) Target MiR12" To be published ., .-..
Assembly members:
MiR12, polymer, 192 residues, 21347.8 Da.
Natural source: Common Name: high GC Gram+ Taxonomy ID: 1877 Superkingdom: Bacteria Kingdom: not available Genus/species: Micromonospora echinospora
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MiR12: MGHHHHHHSHMASGQATERA
LGRRTIPAGEARSIIIRQRY
DAPVDEVWSACTDPNRINRW
FIEPKGDLREGGNFALQGNA
SGDILRCEPPRRLTISWVYE
GKPDSEVELRLSEEGDGTLL
ELEHATTSEQMLVEVGVGWE
MALDFLGMFIRGDLPGGPVP
EDAAEEFEPSPEMMRISQER
GEAWAALVHSGS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 783 |
| 15N chemical shifts | 201 |
| 1H chemical shifts | 1258 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MiR12 | 1 |
Entities:
Entity 1, MiR12 192 residues - 21347.8 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | ALA | SER | GLY | GLN | ALA | THR | GLU | ARG | ALA | ||||
| 3 | LEU | GLY | ARG | ARG | THR | ILE | PRO | ALA | GLY | GLU | ||||
| 4 | ALA | ARG | SER | ILE | ILE | ILE | ARG | GLN | ARG | TYR | ||||
| 5 | ASP | ALA | PRO | VAL | ASP | GLU | VAL | TRP | SER | ALA | ||||
| 6 | CYS | THR | ASP | PRO | ASN | ARG | ILE | ASN | ARG | TRP | ||||
| 7 | PHE | ILE | GLU | PRO | LYS | GLY | ASP | LEU | ARG | GLU | ||||
| 8 | GLY | GLY | ASN | PHE | ALA | LEU | GLN | GLY | ASN | ALA | ||||
| 9 | SER | GLY | ASP | ILE | LEU | ARG | CYS | GLU | PRO | PRO | ||||
| 10 | ARG | ARG | LEU | THR | ILE | SER | TRP | VAL | TYR | GLU | ||||
| 11 | GLY | LYS | PRO | ASP | SER | GLU | VAL | GLU | LEU | ARG | ||||
| 12 | LEU | SER | GLU | GLU | GLY | ASP | GLY | THR | LEU | LEU | ||||
| 13 | GLU | LEU | GLU | HIS | ALA | THR | THR | SER | GLU | GLN | ||||
| 14 | MET | LEU | VAL | GLU | VAL | GLY | VAL | GLY | TRP | GLU | ||||
| 15 | MET | ALA | LEU | ASP | PHE | LEU | GLY | MET | PHE | ILE | ||||
| 16 | ARG | GLY | ASP | LEU | PRO | GLY | GLY | PRO | VAL | PRO | ||||
| 17 | GLU | ASP | ALA | ALA | GLU | GLU | PHE | GLU | PRO | SER | ||||
| 18 | PRO | GLU | MET | MET | ARG | ILE | SER | GLN | GLU | ARG | ||||
| 19 | GLY | GLU | ALA | TRP | ALA | ALA | LEU | VAL | HIS | SER | ||||
| 20 | GLY | SER |
Samples:
mir12.006: mir12.006, [U-100% 13C; U-100% 15N], 0.9 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%
mir12.006_d2o: mir12.006, [U-100% 13C; U-100% 15N], 0.9 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 100%; DSS 50 uM
mir12.011: mir12.011, [U-100% 13C; U-100% 15N], 0.9 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%
mir12.008_NC5: mir12.008, [U-100% 15N], 5% 13C stereo, 0.9 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; 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 | mir12.006 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | mir12.006 | isotropic | sample_conditions_1 |
| 3D HNCO | mir12.006 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | mir12.006 | isotropic | sample_conditions_1 |
| 3D HNCACB | mir12.006 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | mir12.006 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | mir12.006 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | mir12.006 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | mir12.006_d2o | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | mir12.008_NC5 | isotropic | sample_conditions_1 |
| 4D CC-NOESY | mir12.006_d2o | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | mir12.006 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | mir12.006 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | mir12.006 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | mir12.006 | isotropic | sample_conditions_1 |
| NUS 3D 1H-13C NOESY aliphatic | mir12.011 | isotropic | sample_conditions_1 |
| NUS 3D 1H-15N NOESY | mir12.011 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | mir12.006 | 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 vASDP-1.0, Huang, Tejero, Powers and Montelione - data analysis,refinement
NMRPipe v2008 linux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN v2.1.4 and 3.1, Bruker Biospin - collection
VNMRJ v1.1 D, Varian - collection
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY v3.113, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, Bax) - geometry optimization
PSVS v1.5, Bhattacharya, Montelione - structure validation
FMCGUI, Alex Lemak, Cheryl Arrowsmith, University of Toronto - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
- Bruker AvanceIII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts