BMRB Entry 18487
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18487
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Title: Solution NMR Structure of NifU-like protein from Saccharomyces cerevisiae, Northeast Structural Genomics Consortium (NESG) Target YR313A
Deposition date: 2012-05-29 Original release date: 2012-07-02
Authors: Liu, Gaohua; Xiao, Rong; Hamilton, Keith; Janjua, Haleema; Shastry, Ritu; Kohan, Eitan; Acton, Thomas; Everett, John; Lee, Hsiau-Wei; Huang, Yuangpeng; Montelione, Gaetano
Citation: Liu, Gaohua; Xiao, Rong; Hamilton, Keith; Janjua, Haleema; Shastry, Ritu; Kohan, Eitan; Acton, Thomas; Everett, John; Lee, Hsiau-Wei; Huang, Yuangpeng; Montelione, Gaetano. "Solution NMR Structure of NifU-like protein from Saccharomyces cerevisiae, Northeast Structural Genomics Consortium (NESG) Target YR313A" To be published ., .-..
Assembly members:
YR313A, polymer, 119 residues, 13639.707 Da.
Natural source: Common Name: Baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
YR313A: MGHHHHHHSHMNSQRLIHIK
TLTTPNENALKFLSTDGEML
QTRGSKSIVIKNTDENLINH
SKLAQQIFLQCPGVESLMIG
DDFLTINKDRMVHWNSIKPE
IIDLLTKQLAYGEDVISKE
- assigned_chemical_shifts
- RDCs
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 386 |
| 15N chemical shifts | 119 |
| 1H chemical shifts | 812 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YR313A | 1 |
Entities:
Entity 1, YR313A 119 residues - 13639.707 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | ASN | SER | GLN | ARG | LEU | ILE | HIS | ILE | LYS | ||||
| 3 | THR | LEU | THR | THR | PRO | ASN | GLU | ASN | ALA | LEU | ||||
| 4 | LYS | PHE | LEU | SER | THR | ASP | GLY | GLU | MET | LEU | ||||
| 5 | GLN | THR | ARG | GLY | SER | LYS | SER | ILE | VAL | ILE | ||||
| 6 | LYS | ASN | THR | ASP | GLU | ASN | LEU | ILE | ASN | HIS | ||||
| 7 | SER | LYS | LEU | ALA | GLN | GLN | ILE | PHE | LEU | GLN | ||||
| 8 | CYS | PRO | GLY | VAL | GLU | SER | LEU | MET | ILE | GLY | ||||
| 9 | ASP | ASP | PHE | LEU | THR | ILE | ASN | LYS | ASP | ARG | ||||
| 10 | MET | VAL | HIS | TRP | ASN | SER | ILE | LYS | PRO | GLU | ||||
| 11 | ILE | ILE | ASP | LEU | LEU | THR | LYS | GLN | LEU | ALA | ||||
| 12 | TYR | GLY | GLU | ASP | VAL | ILE | SER | LYS | GLU |
Samples:
sample_NC: YR313A.037, [U-100% 13C; U-100% 15N], 1.027 mM; NaCl 450 mM; Na2PO4 25 mM; DTT 10 mM; ZnSO4 20 uM; Proteinase inhibitors 1 X; NaN3 0.02%; D2O 10%; H2O 90%
sample_NC5: YR313A.040, [U-10% 13C; U-100% 15N], 0.52 mM; NaCl 450 mM; Na2PO4 25 mM; DTT 10 mM; ZnSO4 20 uM; Proteinase inhibitors 1 X; NaN3 0.02%; 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_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 |
| 2D 1H-15N HSQC | sample_NC5 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_NC | 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
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, 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 | GAA24684 |
| EMBL | CAA49299 CAA81875 CAY81046 |
| GB | AAS56230 AHY76203 AJP39997 AJS30195 AJS30496 |
| REF | NP_012884 |
| SP | P32860 |
| TPG | DAA09116 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts