BMRB Entry 15941
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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/BMR15941
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Title: Solution structure of a zinc-binding methionine sulfoxide reductase PubMed: 21219456
Deposition date: 2008-09-05 Original release date: 2009-10-13
Authors: Carella, Michela; Ohlenschlager, Oliver; Gorlach, Matthias
Citation: Carella, Michela; Becher, Juliane; Ohlenschlager, Oliver; Ramachandran, Ramadurai; Guhrs, Karl-Heinz; Wellenreuther, Gerd; Meyer-Klaucke, Wolfram; Heinemann, Stefan; Gorlach, Matthias. "Structure-function relationship in an archaebacterial methionine sulphoxide reductase B." Mol. Microbiol. 79, 342-358 (2011).
Assembly members:
msrb, polymer, 154 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Methanothermobacter thermautotrophicus Taxonomy ID: 145262 Superkingdom: Archaea Kingdom: not available Genus/species: Methanothermobacter thermautotrophicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
msrb: GSHMKDRIPIFSVAKNRVEM
VERIELSDDEWREILDPEAF
RVARKAGTEPPFTGKYHDLH
DDGIYRCICCGTDLFDSETK
FDSGTGWPSFYDVVSEHNIK
LREDRSLGMVRCEVLCARCD
AHLGHVFDDGPRPTGKRYCM
NSAALKFIPRDQIG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 556 |
| 15N chemical shifts | 134 |
| 1H chemical shifts | 904 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit 1 | 1 |
| 2 | subunit 2 | 2 |
Entities:
Entity 1, subunit 1 154 residues - Formula weight is not available
amino acids 1-3 represent non-native residues derived from the vector sequence
| 1 | GLY | SER | HIS | MET | LYS | ASP | ARG | ILE | PRO | ILE | ||||
| 2 | PHE | SER | VAL | ALA | LYS | ASN | ARG | VAL | GLU | MET | ||||
| 3 | VAL | GLU | ARG | ILE | GLU | LEU | SER | ASP | ASP | GLU | ||||
| 4 | TRP | ARG | GLU | ILE | LEU | ASP | PRO | GLU | ALA | PHE | ||||
| 5 | ARG | VAL | ALA | ARG | LYS | ALA | GLY | THR | GLU | PRO | ||||
| 6 | PRO | PHE | THR | GLY | LYS | TYR | HIS | ASP | LEU | HIS | ||||
| 7 | ASP | ASP | GLY | ILE | TYR | ARG | CYS | ILE | CYS | CYS | ||||
| 8 | GLY | THR | ASP | LEU | PHE | ASP | SER | GLU | THR | LYS | ||||
| 9 | PHE | ASP | SER | GLY | THR | GLY | TRP | PRO | SER | PHE | ||||
| 10 | TYR | ASP | VAL | VAL | SER | GLU | HIS | ASN | ILE | LYS | ||||
| 11 | LEU | ARG | GLU | ASP | ARG | SER | LEU | GLY | MET | VAL | ||||
| 12 | ARG | CYS | GLU | VAL | LEU | CYS | ALA | ARG | CYS | ASP | ||||
| 13 | ALA | HIS | LEU | GLY | HIS | VAL | PHE | ASP | ASP | GLY | ||||
| 14 | PRO | ARG | PRO | THR | GLY | LYS | ARG | TYR | CYS | MET | ||||
| 15 | ASN | SER | ALA | ALA | LEU | LYS | PHE | ILE | PRO | ARG | ||||
| 16 | ASP | GLN | ILE | GLY |
Entity 2, subunit 2 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: msrb, [U-15N], 1.2 mM; Na-phosphate 20 mM; NaCl 20 mM; beta-mercaptoethanol 5 mM
sample_2: msrb, [U-13C; U-15N], 1.2 mM; Na-phosphate 20 mM; NaCl 20 mM; beta-mercaptoethanol 5 mM
sample_conditions_1: ionic strength: 40 mM; pH: 7.2; pressure: 1 atm; temperature: 318 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | 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 | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
VNMR v6.1 rev. C, Varian - collection, processing
XEASY v1.3.9, Bartels et al. - data analysis, peak picking
DYANA v1.5, Guntert, Braun and Wuthrich - structure solution
OPAL v2.6, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts