BMRB Entry 16144
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16144
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Title: Backbone and side chain 1H, 13C, and 15N NMR assignments for the organic hydroperoxide resistance protein (Ohr) from Burkholderia pseudomallei, Seattle Structural Genomics Center for Infectious Disease (SSGCID) target BupsA.00074 PubMed: 19888681
Deposition date: 2009-01-28 Original release date: 2009-01-30
Authors: Buchko, Garry; Hewitt, Stephen; Napuli, Alberto; Van Voorhis, Wesley; Myler, Peter
Citation: Buchko, Garry; Hewitt, Stephen; Napuli, Alberto; Van Voorhis, Wesley; Myler, Peter. "Backbone and side chain (1)H, (13)C, and (15)N NMR assignments for the organic hydroperoxide resistance protein (Ohr) from Burkholderia pseudomallei." Biomol. NMR Assignments 3, 163-166 (2009).
Assembly members:
organic_hydroperoxide_resistance_protein_(Ohr), polymer, 160 residues, Formula weight is not available
Natural source: Common Name: Burkholderia pseudomallei Taxonomy ID: 28450 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia pseudomallei
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
organic_hydroperoxide_resistance_protein_(Ohr): MAHHHHHHMGTLEAQTQGPG
SMNILYKTAATSTGGRDGRA
TSHDQKLDVKLSAPRELGGA
GAEGTNPEQLFAAGYSACFL
SAMKFVAGQNKQTLPADTTV
TAEVGIGPNEEGGFALDVEL
RVALPGLDAAAAKTLVDRAH
HVCPYSNATRNNVAVRLVVA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 517 |
15N chemical shifts | 139 |
1H chemical shifts | 782 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Bp-Ohr, chain 1 | 1 |
2 | Bp-Ohr, chain 2 | 1 |
Entities:
Entity 1, Bp-Ohr, chain 1 160 residues - Formula weight is not available
The first N-terminal 21 residues (MAHHHHHHMGTLEAQTQGPGS-) are a non-native tag. The first residue in the native sequence is M22.
1 | MET | ALA | HIS | HIS | HIS | HIS | HIS | HIS | MET | GLY | |
2 | THR | LEU | GLU | ALA | GLN | THR | GLN | GLY | PRO | GLY | |
3 | SER | MET | ASN | ILE | LEU | TYR | LYS | THR | ALA | ALA | |
4 | THR | SER | THR | GLY | GLY | ARG | ASP | GLY | ARG | ALA | |
5 | THR | SER | HIS | ASP | GLN | LYS | LEU | ASP | VAL | LYS | |
6 | LEU | SER | ALA | PRO | ARG | GLU | LEU | GLY | GLY | ALA | |
7 | GLY | ALA | GLU | GLY | THR | ASN | PRO | GLU | GLN | LEU | |
8 | PHE | ALA | ALA | GLY | TYR | SER | ALA | CYS | PHE | LEU | |
9 | SER | ALA | MET | LYS | PHE | VAL | ALA | GLY | GLN | ASN | |
10 | LYS | GLN | THR | LEU | PRO | ALA | ASP | THR | THR | VAL | |
11 | THR | ALA | GLU | VAL | GLY | ILE | GLY | PRO | ASN | GLU | |
12 | GLU | GLY | GLY | PHE | ALA | LEU | ASP | VAL | GLU | LEU | |
13 | ARG | VAL | ALA | LEU | PRO | GLY | LEU | ASP | ALA | ALA | |
14 | ALA | ALA | LYS | THR | LEU | VAL | ASP | ARG | ALA | HIS | |
15 | HIS | VAL | CYS | PRO | TYR | SER | ASN | ALA | THR | ARG | |
16 | ASN | ASN | VAL | ALA | VAL | ARG | LEU | VAL | VAL | ALA |
Samples:
sample_1: organic hydroperoxide resistance protein (Ohr), [U-99% 13C; U-99% 15N], 1.20 ± 0.2 mM; sodium chloride 100 ± 3 mM; DTT 1 ± 0.2 mM; TRIS 20 ± 1 mM
sample_2: organic hydroperoxide resistance protein (Ohr), [U-99% 13C; U-100% 15N; U-50% 2H], 1.20 ± 0.2 mM; sodium chloride 100 ± 3 mM; DTT 1 ± 0.2 mM; TRIS 20 ± 1 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7.1; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HN(COCA)CB | sample_2 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
Software:
FELIX v2007, Accelrys Software Inc. - processing
SPARKY v3.115, Goddard - data analysis
VNMR, Varian - collection
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
- Varian INOVA 800 MHz
Related Database Links:
EMBL | CAH39258 CDU31823 CFB51471 CFD89896 CFD92517 |
GB | AAU46184 ABA51242 ABM49396 ABM99747 ABN87360 |
REF | WP_004190960 WP_004529046 WP_004540142 WP_011832128 WP_038742729 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts