BMRB Entry 19681
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19681
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR structure of E. coli LpoB PubMed: 24691651
Deposition date: 2013-12-13 Original release date: 2014-04-11
Authors: Egan, Alexander; Jean, Nicolas; Koumoutsi, Alexandra; Bougault, Catherine; Biboy, Jacob; Sassine, Jad; Solovyova, Alexandra; Breukink, Eefjan; Typas, Athanasios; Vollmer, Waldemar; Simorre, Jean-Pierre
Citation: Jean, Nicolas; Bougault, Catherine; Egan, Alexander; Vollmer, Waldemar; Simorre, Jean-Pierre. "Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli." Biomol. NMR Assignments ., .-. (2014).
Assembly members:
LpoB, polymer, 197 residues, 20770.459 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
LpoB: GSHMVGQREPAPVEEVKPAP
EQPAEPQQPVPTVPSVPTIP
QQPGPIEHEDQTAPPAPHIR
HYDWNGAMQPMVSKMLGADG
VTAGSVLLVDSVNNRTNGSL
NAAEATETLRNALANNGKFT
LVSAQQLSMAKQQLGLSPQD
SLGTRSKAIGIARNVGAHYV
LYSSASGNVNAPTLQMQLML
VQTGEIIWSGKGAVSQQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 756 |
| 15N chemical shifts | 197 |
| 1H chemical shifts | 1165 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | E. coli LpoB | 1 |
Entities:
Entity 1, E. coli LpoB 197 residues - 20770.459 Da.
Residues 1 to 4 are reminiscent of the hexahistidine-tag left after thrombine cleavage
| 1 | GLY | SER | HIS | MET | VAL | GLY | GLN | ARG | GLU | PRO | ||||
| 2 | ALA | PRO | VAL | GLU | GLU | VAL | LYS | PRO | ALA | PRO | ||||
| 3 | GLU | GLN | PRO | ALA | GLU | PRO | GLN | GLN | PRO | VAL | ||||
| 4 | PRO | THR | VAL | PRO | SER | VAL | PRO | THR | ILE | PRO | ||||
| 5 | GLN | GLN | PRO | GLY | PRO | ILE | GLU | HIS | GLU | ASP | ||||
| 6 | GLN | THR | ALA | PRO | PRO | ALA | PRO | HIS | ILE | ARG | ||||
| 7 | HIS | TYR | ASP | TRP | ASN | GLY | ALA | MET | GLN | PRO | ||||
| 8 | MET | VAL | SER | LYS | MET | LEU | GLY | ALA | ASP | GLY | ||||
| 9 | VAL | THR | ALA | GLY | SER | VAL | LEU | LEU | VAL | ASP | ||||
| 10 | SER | VAL | ASN | ASN | ARG | THR | ASN | GLY | SER | LEU | ||||
| 11 | ASN | ALA | ALA | GLU | ALA | THR | GLU | THR | LEU | ARG | ||||
| 12 | ASN | ALA | LEU | ALA | ASN | ASN | GLY | LYS | PHE | THR | ||||
| 13 | LEU | VAL | SER | ALA | GLN | GLN | LEU | SER | MET | ALA | ||||
| 14 | LYS | GLN | GLN | LEU | GLY | LEU | SER | PRO | GLN | ASP | ||||
| 15 | SER | LEU | GLY | THR | ARG | SER | LYS | ALA | ILE | GLY | ||||
| 16 | ILE | ALA | ARG | ASN | VAL | GLY | ALA | HIS | TYR | VAL | ||||
| 17 | LEU | TYR | SER | SER | ALA | SER | GLY | ASN | VAL | ASN | ||||
| 18 | ALA | PRO | THR | LEU | GLN | MET | GLN | LEU | MET | LEU | ||||
| 19 | VAL | GLN | THR | GLY | GLU | ILE | ILE | TRP | SER | GLY | ||||
| 20 | LYS | GLY | ALA | VAL | SER | GLN | GLN |
Samples:
LpoB(sol): LpoB, [U-100% 13C; U-100% 15N], 0.8 mM; CH3COOH/CH3COONa buffer 100.0 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 0.100 M; pH: 5.000; pressure: 1.000 atm; temperature: 308.000 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D HNCO | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D BEST-HNCACB | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D BEST-HN(CO)CACB | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D HN(COCA)N(H) | LpoB(sol) | isotropic | sample_conditions_1 |
| 2D Pro-HN(COCAN) | LpoB(sol) | isotropic | sample_conditions_1 |
| 2D Pro-iHN(CAN) | LpoB(sol) | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | LpoB(sol) | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | LpoB(sol) | isotropic | sample_conditions_1 |
| 2D methyl 1H-13C-CT-HSQC | LpoB(sol) | isotropic | sample_conditions_1 |
| 2D 1H-15N HMQC optimized for His sidechains | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D H(C)CH-TOCSY | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D C(CO)NH | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | LpoB(sol) | isotropic | sample_conditions_1 |
| 3D methyl 1H-13C NOESY | LpoB(sol) | isotropic | sample_conditions_1 |
| Heteronuclear 1H-15N NOE | LpoB(sol) | isotropic | sample_conditions_1 |
Software:
Aria v2.3.1, Linge, O, http://aria.pasteur.fr/ - structure calculation
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - Refinement
CcpNmr_Analysis v2.2, CCPN - data analysis
Talos+, Yang Shen, Frank Delaglio, Gabriel Cornilescu, and Ad Bax - data analysis
Unio10' v2.0.2, Torsten Herrmann - peakpicking
nmrDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
nmrPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian vnmrs 800 MHz
- Varian vnmrs 600 MHz
- Bruker US2 950 MHz
Related Database Links:
| UNP | P0AB38 |
| PDB | |
| DBJ | BAA35912 BAB34906 BAG76694 BAI24739 BAI29989 |
| EMBL | CAP75597 CAQ31626 CAQ98004 CAR02445 CAR07449 |
| GB | AAC74189 AAG55851 AAN79848 AAP16615 AAZ87850 |
| REF | NP_309510 NP_415623 WP_000164436 WP_000164438 WP_000164439 |
| SP | P0AB38 P0AB39 Q3Z312 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts