BMRB Entry 16316
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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/BMR16316
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Title: NMR structure of IntB phage-integrase-like protein fragment 90-199 from Erwinia carotova subsp. atroseptica: Northeast Structural Genomics Consortium target EwR217E
Deposition date: 2009-05-26 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.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation: Cort, John; Montelione, Gaetano; Kennedy, Michael. "NMR structure of IntB phage-integrase-like protein fragment 90-199 from Erwinia carotova subsp. atroseptica" Not known ., .-..
Assembly members:
fragment 90-199, polymer, 118 residues, Formula weight is not available
Natural source: Common Name: Bacterium carotovorum Taxonomy ID: 554 Superkingdom: Bacteria Kingdom: not available Genus/species: Erwinia carotovora
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
fragment 90-199: KSVQEKRNNTRAFKTVAKSW
FATKTTWSEDYQRSVWTRLE
TYLFPDIGNKDIAELDTGDL
LVPIKKIEKLGYLEIAMRVK
QYATAIMRYAVQQKMIRFNP
AYDLEGAVQKLEHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 505 |
15N chemical shifts | 122 |
1H chemical shifts | 778 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | fragment 90-199 | 1 |
Entities:
Entity 1, fragment 90-199 118 residues - Formula weight is not available
1 | LYS | SER | VAL | GLN | GLU | LYS | ARG | ASN | ASN | THR | ||||
2 | ARG | ALA | PHE | LYS | THR | VAL | ALA | LYS | SER | TRP | ||||
3 | PHE | ALA | THR | LYS | THR | THR | TRP | SER | GLU | ASP | ||||
4 | TYR | GLN | ARG | SER | VAL | TRP | THR | ARG | LEU | GLU | ||||
5 | THR | TYR | LEU | PHE | PRO | ASP | ILE | GLY | ASN | LYS | ||||
6 | ASP | ILE | ALA | GLU | LEU | ASP | THR | GLY | ASP | LEU | ||||
7 | LEU | VAL | PRO | ILE | LYS | LYS | ILE | GLU | LYS | LEU | ||||
8 | GLY | TYR | LEU | GLU | ILE | ALA | MET | ARG | VAL | LYS | ||||
9 | GLN | TYR | ALA | THR | ALA | ILE | MET | ARG | TYR | ALA | ||||
10 | VAL | GLN | GLN | LYS | MET | ILE | ARG | PHE | ASN | PRO | ||||
11 | ALA | TYR | ASP | LEU | GLU | GLY | ALA | VAL | GLN | LYS | ||||
12 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; sodium azide 0.02 w/v; H2O 95%; D2O, [U-99% 2H], 5%
sample_2: entity, [5% biosynthetically directed 13C; U-99% 15N], 0.7 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; sodium azide 0.02 w/v; H2O 95%; D2O, [U-99% 2H], 5%
sample_3: entity, [U-99% 13C; U-99% 15N], 0.7 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; sodium azide 0.02 w/v; D2O, [U-99% 2H], 100%
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 HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | 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 C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | 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_2 | isotropic | sample_conditions_1 |
4D 1H-13C-13C-1H HMQC-NOESY-HMQC | sample_3 | isotropic | sample_conditions_1 |
Software:
AutoStruct, Huang, Tejero, Powers and Montelione - structure solution
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
SPARKY, Goddard - chemical shift assignment, data analysis
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
FELIX, Accelrys Software Inc. - processing
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