BMRB Entry 16563
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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/BMR16563
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Title: Solution NMR structure of Lin0431 protein from Listeria innocua. Northeast Structural Genomics Consortium Target LkR112
Deposition date: 2009-10-18 Original release date: 2009-11-23
Authors: Tang, Yuefeng; Montelione, Gaetano; Ciccosanti, Colleen; Lee, Dan; Janjua, Haleema; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rose, Burkhard; Xiao, Rong
Citation: Tang, Yuefeng; Montelione, Gaetano; Ciccosanti, Colleen; Lee, Dan; Janjua, Haleema; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rose, Burkhard; Xiao, Rong. "Solution NMR structure of Lin0431 protein from Listeria innocua. Northeast Structural Genomics Consortium Target LkR112" Not known ., .-..
Assembly members:
LkR112, polymer, 114 residues, 12784.5 Da.
Natural source: Common Name: Listeria innocua Taxonomy ID: 1642 Superkingdom: Eubacteria Kingdom: not available Genus/species: Listeria innocua
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
LkR112: MKNTGDEVVAIISQNGKVIR
EIPLTGHKGNEQFTIKGKGA
QYNLMEVDGERIRIKEDNSP
DQVGVKMGWKSKAGDTIVCL
PHKVFVEIKSTQKDSKDPDT
DLIVPNLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 474 |
| 15N chemical shifts | 117 |
| 1H chemical shifts | 781 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LkR112 | 1 |
Entities:
Entity 1, LkR112 114 residues - 12784.5 Da.
| 1 | MET | LYS | ASN | THR | GLY | ASP | GLU | VAL | VAL | ALA | ||||
| 2 | ILE | ILE | SER | GLN | ASN | GLY | LYS | VAL | ILE | ARG | ||||
| 3 | GLU | ILE | PRO | LEU | THR | GLY | HIS | LYS | GLY | ASN | ||||
| 4 | GLU | GLN | PHE | THR | ILE | LYS | GLY | LYS | GLY | ALA | ||||
| 5 | GLN | TYR | ASN | LEU | MET | GLU | VAL | ASP | GLY | GLU | ||||
| 6 | ARG | ILE | ARG | ILE | LYS | GLU | ASP | ASN | SER | PRO | ||||
| 7 | ASP | GLN | VAL | GLY | VAL | LYS | MET | GLY | TRP | LYS | ||||
| 8 | SER | LYS | ALA | GLY | ASP | THR | ILE | VAL | CYS | LEU | ||||
| 9 | PRO | HIS | LYS | VAL | PHE | VAL | GLU | ILE | LYS | SER | ||||
| 10 | THR | GLN | LYS | ASP | SER | LYS | ASP | PRO | ASP | THR | ||||
| 11 | ASP | LEU | ILE | VAL | PRO | ASN | LEU | GLU | HIS | HIS | ||||
| 12 | HIS | HIS | HIS | HIS |
Samples:
sample_1: LkR112, [U-100% 13C; U-100% 15N], 0.851 mM; MES 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; DSS 50 uM; H2O 95%; D2O 5%
sample_2: LkR112, [U-5% 13C; U-100% 15N], 0.887 mM; MES 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; DSS 50 uM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D High Resolution 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D aromatic 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C aliphatic NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C aromatic NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D simutaeous NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
SPARKY v3.110, Goddard - data analysis
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS, Bhattacharya and Montelione - structure validation
PDBStat v5.1, Tejero and Montelione - PDB analysis
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| EMBL | CAC95664 |
| GB | EFR91908 EFR94989 EHN61892 KJR52371 KJR53096 |
| REF | WP_003760402 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts