BMRB Entry 16315
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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/BMR16315
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Title: NMR structure of fragment 87-196 from the putative phage integrase IntS of E. coli: Northeast Structural Genomics Consortium target ER652A
Deposition date: 2009-05-25 Original release date: 2012-08-03
Authors: Cort, John; Ramelot, Theresa; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Swapna, G.V.T.; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation: Cort, John; Montelione, Gaetano; Kennedy, Michael. "NMR structure of fragment 87-196 from the putative phage integrase IntS of E. coli" Not known ., .-..
Assembly members:
fragment 87-196, polymer, 236 residues, Formula weight is not available
Natural source: Common Name: E. Coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
fragment 87-196: SSNNNSFSAIYKEWYEHKKQ
VWSVGYATELAKMFDDDILP
IIGGLEIQDIEPMQLLEVIR
RFEDRGAMERANKARRRCGE
VFRYAIVTGRAKYNPAPDLA
DAMKGYRKKNLEHHHHHHSS
NNNSFSAIYKEWYEHKKQVW
SVGYATELAKMFDDDILPII
GGLEIQDIEPMQLLEVIRRF
EDRGAMERANKARRRCGEVF
RYAIVTGRAKYNPAPDLADA
MKGYRKKNLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 492 |
| 15N chemical shifts | 124 |
| 1H chemical shifts | 721 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | fragment 87-196 | 1 |
Entities:
Entity 1, fragment 87-196 236 residues - Formula weight is not available
| 1 | SER | SER | ASN | ASN | ASN | SER | PHE | SER | ALA | ILE | ||||
| 2 | TYR | LYS | GLU | TRP | TYR | GLU | HIS | LYS | LYS | GLN | ||||
| 3 | VAL | TRP | SER | VAL | GLY | TYR | ALA | THR | GLU | LEU | ||||
| 4 | ALA | LYS | MET | PHE | ASP | ASP | ASP | ILE | LEU | PRO | ||||
| 5 | ILE | ILE | GLY | GLY | LEU | GLU | ILE | GLN | ASP | ILE | ||||
| 6 | GLU | PRO | MET | GLN | LEU | LEU | GLU | VAL | ILE | ARG | ||||
| 7 | ARG | PHE | GLU | ASP | ARG | GLY | ALA | MET | GLU | ARG | ||||
| 8 | ALA | ASN | LYS | ALA | ARG | ARG | ARG | CYS | GLY | GLU | ||||
| 9 | VAL | PHE | ARG | TYR | ALA | ILE | VAL | THR | GLY | ARG | ||||
| 10 | ALA | LYS | TYR | ASN | PRO | ALA | PRO | ASP | LEU | ALA | ||||
| 11 | ASP | ALA | MET | LYS | GLY | TYR | ARG | LYS | LYS | ASN | ||||
| 12 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | ||||
| 13 | ASN | ASN | ASN | SER | PHE | SER | ALA | ILE | TYR | LYS | ||||
| 14 | GLU | TRP | TYR | GLU | HIS | LYS | LYS | GLN | VAL | TRP | ||||
| 15 | SER | VAL | GLY | TYR | ALA | THR | GLU | LEU | ALA | LYS | ||||
| 16 | MET | PHE | ASP | ASP | ASP | ILE | LEU | PRO | ILE | ILE | ||||
| 17 | GLY | GLY | LEU | GLU | ILE | GLN | ASP | ILE | GLU | PRO | ||||
| 18 | MET | GLN | LEU | LEU | GLU | VAL | ILE | ARG | ARG | PHE | ||||
| 19 | GLU | ASP | ARG | GLY | ALA | MET | GLU | ARG | ALA | ASN | ||||
| 20 | LYS | ALA | ARG | ARG | ARG | CYS | GLY | GLU | VAL | PHE | ||||
| 21 | ARG | TYR | ALA | ILE | VAL | THR | GLY | ARG | ALA | LYS | ||||
| 22 | TYR | ASN | PRO | ALA | PRO | ASP | LEU | ALA | ASP | ALA | ||||
| 23 | MET | LYS | GLY | TYR | ARG | LYS | LYS | ASN | LEU | GLU | ||||
| 24 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: H2O 95%; D2O, [U-2H], 5%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 w/v; protein, [biosynthetically directed 5%C; U-99% 15N], 0.95 mM
sample_2: D2O, [U-2H], 100%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 w/v; protein, [U-99% 13C; U-99% 15N], 1.2 mM
sample_3: D2O, [U-2H], 100%; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02 w/v; protein, [5% 13C; natural abundance, 1.2 mM
sample_conditions_1: ionic strength: 215 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 4D 1H-13C-13C-1H HMQC-NOESY-HMQC | sample_2 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment, data analysis
AutoStruct, Huang, Tejero, Powers and Montelione - structure solution
FELIX, Accelrys Software Inc. - processing
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts