BMRB Entry 16144

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16144

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Deposition date:

2009-01-28

Original release date:

2009-01-30

Authors:

Buchko, Garry; Hewitt, Stephen; Napuli, Alberto; Van Voorhis, Wesley; Myler, Peter

Citation:

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).
PubMed: 19888681

Assembly members:

Assembly members:
organic_hydroperoxide_resistance_protein_(Ohr), polymer, 160 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Burkholderia pseudomallei Taxonomy ID: 28450 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia pseudomallei

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: AVA0421

Entity Sequences (FASTA):

Entity Sequences (FASTA):
organic_hydroperoxide_resistance_protein_(Ohr): MAHHHHHHMGTLEAQTQGPG SMNILYKTAATSTGGRDGRA TSHDQKLDVKLSAPRELGGA GAEGTNPEQLFAAGYSACFL SAMKFVAGQNKQTLPADTTV TAEVGIGPNEEGGFALDVEL RVALPGLDAAAAKTLVDRAH HVCPYSNATRNNVAVRLVVA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	517
15N chemical shifts	139
1H chemical shifts	782

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

EMBL	CAH39258 CDU31823 CFB51471 CFD89896 CFD92517
GB	AAU46184 ABA51242 ABM49396 ABM99747 ABN87360
REF	WP_004190960 WP_004529046 WP_004540142 WP_011832128 WP_038742729

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

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