BMRB Entry 16312
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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/BMR16312
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Title: Solution NMR structure of a domain from a putative phage integrase protein Nmul_A0064 from Nitrosospira multiformis, Northeast Structural Genomics Consortium Target NmR46C.
Deposition date: 2009-05-21 Original release date: 2009-06-11
Authors: Mills, Jeffrey; Eletsky, Alexander; Ghosh, Arindam; Wang, Dongyang; Lee, Hsiau-Wei; Ciccosanti, Colleen; Jiang, Mei; Nair, R.; Rost, Burkhard; Swapna, G. V. T.; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas
Citation: Mills, Jeffrey. "Solution NMR structure of a domain from a putative phage integrase protein Nmul_A0064 from Nitrosospira multiformis, Northeast Structural Genomics Consortium Target NmR46C." Not known ., .-..
Assembly members:
NmR46C, polymer, 116 residues, 13400.581 Da.
Natural source: Common Name: Nitrosospira multiformis Taxonomy ID: 1231 Superkingdom: Bacteria Kingdom: not available Genus/species: Nitrosospira multiformis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NmR46C: MAEKNAYTVAQLADEYFERM
IAGRWKHPNIVRSRIEKDIK
PAIGSLKVEDVKPRHIDDVL
KAVMKRGAPSIANDTLRWLK
RMFNYAIKRHIIEYNPAAAF
DPGDAGGKLEHHHHHH
- assigned_chemical_shifts
- RDCs
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 392 |
| 15N chemical shifts | 124 |
| 1H chemical shifts | 830 |
| residual dipolar couplings | 72 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NmR46C | 1 |
Entities:
Entity 1, NmR46C 116 residues - 13400.581 Da.
L46 is a sequence variation; Please add a "remark 999"
| 1 | MET | ALA | GLU | LYS | ASN | ALA | TYR | THR | VAL | ALA | ||||
| 2 | GLN | LEU | ALA | ASP | GLU | TYR | PHE | GLU | ARG | MET | ||||
| 3 | ILE | ALA | GLY | ARG | TRP | LYS | HIS | PRO | ASN | ILE | ||||
| 4 | VAL | ARG | SER | ARG | ILE | GLU | LYS | ASP | ILE | LYS | ||||
| 5 | PRO | ALA | ILE | GLY | SER | LEU | LYS | VAL | GLU | ASP | ||||
| 6 | VAL | LYS | PRO | ARG | HIS | ILE | ASP | ASP | VAL | LEU | ||||
| 7 | LYS | ALA | VAL | MET | LYS | ARG | GLY | ALA | PRO | SER | ||||
| 8 | ILE | ALA | ASN | ASP | THR | LEU | ARG | TRP | LEU | LYS | ||||
| 9 | ARG | MET | PHE | ASN | TYR | ALA | ILE | LYS | ARG | HIS | ||||
| 10 | ILE | ILE | GLU | TYR | ASN | PRO | ALA | ALA | ALA | PHE | ||||
| 11 | ASP | PRO | GLY | ASP | ALA | GLY | GLY | LYS | LEU | GLU | ||||
| 12 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC: NmR46C, [U-98% 13C; U-98% 15N], 1.2 mM; D2O 10%; H2O 90%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; protease inhibitors 1x v/v; sodium azide 0.02%
NC5: NmR46C, [U-5% 13C; U-98% 15N], 1.2 mM; D2O 10%; H2O 90%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; protease inhibitors 1x v/v; sodium azide 0.02%
NC5ani: NmR46C, [U-5% 13C; U-98% 15N], 1.2 mM; D2O 10%; H2O 90%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; protease inhibitors 1x v/v; sodium azide 0.02%
sample_conditions_1: ionic strength: 430 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC5 | isotropic | sample_conditions_1 |
| 3D sim 15N,13C NOESY | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| (4,3)D HNCABCA | NC | isotropic | sample_conditions_1 |
| GFT (4,3)D CABCA(CO)NH | NC | isotropic | sample_conditions_1 |
| GFT (4,3)D HABCAB(CO)NH | NC | isotropic | sample_conditions_1 |
| GFT (4,3)D arom. HCCH | NC | isotropic | sample_conditions_1 |
| GFT (4,3)D aliph. HCCH | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | NC5ani | anisotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | NC5ani | anisotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPSCAN, Glaser - processing
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, refinement, structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
Molmol, Koradi, Billeter and Wuthrich - data analysis, refinement, structure solution
AutoStruct, Huang, Tejero, Powers and Montelione - chemical shift assignment, refinement, structure solution
PSVS, Bhattacharya and Montelione - refinement
NMR spectrometers:
- Varian INOVA 750 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