BMRB Entry 19048
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19048
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Karsisiotis, Andreas Ioannis; Damblon, Christian; Roberts, Gordon. "Complete 1H, 15N and 13C resonance assignments of Bacillus cereus metallo-beta-lactamase and its complex with the inhibitor R-thiomandelic acid" Biomol. NMR Assign. ., .-. (2013).
PubMed: 23838816
Assembly members:
BcII, polymer, 227 residues, 24995.738 Da.
3-(2-aminoquinolin-3-yl)-N-cyclohexyl-N-methylpropanamide, non-polymer, 311.421 Da.
ZINC ION, non-polymer, 65.409 Da.
Natural source: Common Name: Firmicutes Taxonomy ID: 1396 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus cereus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET9a/BCII
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 730 |
| 15N chemical shifts | 231 |
| 1H chemical shifts | 3080 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BcII | 1 |
| 2 | RTM | 2 |
| 3 | ZINC ION_1 | 3 |
| 4 | ZINC ION_2 | 3 |
Entities:
Entity 1, BcII 227 residues - 24995.738 Da.
| 1 | SER | GLN | LYS | VAL | GLU | LYS | THR | VAL | ILE | LYS | ||||
| 2 | ASN | GLU | THR | GLY | THR | ILE | SER | ILE | SER | GLN | ||||
| 3 | LEU | ASN | LYS | ASN | VAL | TRP | VAL | HIS | THR | GLU | ||||
| 4 | LEU | GLY | SER | PHE | ASN | GLY | GLU | ALA | VAL | PRO | ||||
| 5 | SER | ASN | GLY | LEU | VAL | LEU | ASN | THR | SER | LYS | ||||
| 6 | GLY | LEU | VAL | LEU | VAL | ASP | SER | SER | TRP | ASP | ||||
| 7 | ASP | LYS | LEU | THR | LYS | GLU | LEU | ILE | GLU | MET | ||||
| 8 | VAL | GLU | LYS | LYS | PHE | GLN | LYS | ARG | VAL | THR | ||||
| 9 | ASP | VAL | ILE | ILE | THR | HIS | ALA | HIS | ALA | ASP | ||||
| 10 | ARG | ILE | GLY | GLY | ILE | LYS | THR | LEU | LYS | GLU | ||||
| 11 | ARG | GLY | ILE | LYS | ALA | HIS | SER | THR | ALA | LEU | ||||
| 12 | THR | ALA | GLU | LEU | ALA | LYS | LYS | ASN | GLY | TYR | ||||
| 13 | GLU | GLU | PRO | LEU | GLY | ASP | LEU | GLN | THR | VAL | ||||
| 14 | THR | ASN | LEU | LYS | PHE | GLY | ASN | MET | LYS | VAL | ||||
| 15 | GLU | THR | PHE | TYR | PRO | GLY | LYS | GLY | HIS | THR | ||||
| 16 | GLU | ASP | ASN | ILE | VAL | VAL | TRP | LEU | PRO | GLN | ||||
| 17 | TYR | ASN | ILE | LEU | VAL | GLY | GLY | CYS | LEU | VAL | ||||
| 18 | LYS | SER | THR | SER | ALA | LYS | ASP | LEU | GLY | ASN | ||||
| 19 | VAL | ALA | ASP | ALA | TYR | VAL | ASN | GLU | TRP | SER | ||||
| 20 | THR | SER | ILE | GLU | ASN | VAL | LEU | LYS | ARG | TYR | ||||
| 21 | ARG | ASN | ILE | ASN | ALA | VAL | VAL | PRO | GLY | HIS | ||||
| 22 | GLY | GLU | VAL | GLY | ASP | LYS | GLY | LEU | LEU | LEU | ||||
| 23 | HIS | THR | LEU | ASP | LEU | LEU | LYS |
Entity 2, RTM - C19 H25 N3 O - 311.421 Da.
| 1 | RTM |
Entity 3, ZINC ION_1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: BcII, [U-99% 15N], 1 mM; R-Thiomandelic Acid 1 mM; MES 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%
sample_2: BcII, [U-99% 13C; U-99% 15N], 1 mM; R-Thiomandelic Acid 1 mM; MES 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 120 mM; pH: 6.4; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
CANDID, Guntert, Mumenthaler and Wuthrich - automated NOE assignment, structure solution
SPARKY, Goddard - data analysis, peak picking
Molmol, Koradi, Billeter and Wuthrich - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
xwinnmr, Bruker Biospin - collection
ProcheckNMR, Laskowski and MacArthur - validation
WhatIF, Vriend - validation
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
- Bruker Avance 600 MHz