BMRB Entry 17747
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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/BMR17747
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Title: Solution NMR Structure of Fumarate reductase flavoprotein subunit from Lactobacillus plantarum, Northeast Structural Genomics Consortium Target LpR145J
Deposition date: 2011-06-29 Original release date: 2011-08-03
Authors: Liu, Gaohua; Tang, Yuefeng; Xiao, Rong; Janjua, Haleema; Ciccosanti, colleen; Wang, Huang; Acton, Thomas; Everett, John; Montelione, Gaetano
Citation: Liu, Gaohua; Tang, Yuefeng; Xiao, Rong; Janjua, Haleema; Ciccosanti, colleen; Wang, Huang; Acton, Thomas; Everett, John; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target LpR145J" To be published ., .-..
Assembly members:
LpR145J, polymer, 160 residues, 18527.973 Da.
Natural source: Common Name: Lactobacillus plantarum Taxonomy ID: 1590 Superkingdom: Bacteria Kingdom: not available Genus/species: Lactobacillus plantarum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
LpR145J: MVEPGVAKLTTYASKQATDM
GAIYVNSKGDRIVNESNVYT
TFRNAILKQADKVAYLVMDE
RTWKKVYDLLILHDFTPEEI
KSFFENKGKRPVFVKGSLES
AAEQAGIVVDELVQTVKNYQ
GYVQDGHDHDFGRDPKYLHQ
FEGETFYIIEQRLEHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 676 |
15N chemical shifts | 143 |
1H chemical shifts | 1080 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | LpR145J | 1 |
Entities:
Entity 1, LpR145J 160 residues - 18527.973 Da.
1 | MET | VAL | GLU | PRO | GLY | VAL | ALA | LYS | LEU | THR | |
2 | THR | TYR | ALA | SER | LYS | GLN | ALA | THR | ASP | MET | |
3 | GLY | ALA | ILE | TYR | VAL | ASN | SER | LYS | GLY | ASP | |
4 | ARG | ILE | VAL | ASN | GLU | SER | ASN | VAL | TYR | THR | |
5 | THR | PHE | ARG | ASN | ALA | ILE | LEU | LYS | GLN | ALA | |
6 | ASP | LYS | VAL | ALA | TYR | LEU | VAL | MET | ASP | GLU | |
7 | ARG | THR | TRP | LYS | LYS | VAL | TYR | ASP | LEU | LEU | |
8 | ILE | LEU | HIS | ASP | PHE | THR | PRO | GLU | GLU | ILE | |
9 | LYS | SER | PHE | PHE | GLU | ASN | LYS | GLY | LYS | ARG | |
10 | PRO | VAL | PHE | VAL | LYS | GLY | SER | LEU | GLU | SER | |
11 | ALA | ALA | GLU | GLN | ALA | GLY | ILE | VAL | VAL | ASP | |
12 | GLU | LEU | VAL | GLN | THR | VAL | LYS | ASN | TYR | GLN | |
13 | GLY | TYR | VAL | GLN | ASP | GLY | HIS | ASP | HIS | ASP | |
14 | PHE | GLY | ARG | ASP | PRO | LYS | TYR | LEU | HIS | GLN | |
15 | PHE | GLU | GLY | GLU | THR | PHE | TYR | ILE | ILE | GLU | |
16 | GLN | ARG | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_NC: LpR145J, [U-100% 13C; U-100% 15N], 1.41 mM; H2O 90%; D2O 10%
sample_NC5: LpR145J, [U-100% 13C; U-100% 15N], 0.90 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_NC | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_NC | 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 |
3D HCCH-TOCSY | sample_NC | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_NC5 | 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
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
PDB | |
EMBL | CCC80459 CDN28269 |
GB | ACT63669 ADO00073 AGE37659 AGL65584 AGO09388 |
REF | WP_003643070 WP_003643562 WP_003645691 WP_015641109 WP_021730084 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts