BMRB Entry 30677

Name: Solution structure of an organic hydroperoxide resistance protein from Burkholderia pseudomallei. Seattle Structural Genomics Center for Infectious Disease target BupsA.00074.a.
Published: 2019-10-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30677

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of an organic hydroperoxide resistance protein from Burkholderia pseudomallei. Seattle Structural Genomics Center for Infectious Disease target BupsA.00074.a. PubMed: 19888681

Deposition date: 2019-09-29 Original release date: 2019-10-14

Authors: Buchko, G.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), SSGCID

Citation: Buchko, G.; Hewitt, S.; Napuli, A.; Van Voorhis, W.; Myler, P.. "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 Assign. 3, 163-166 (2009).

Assembly members:
entity_1, polymer, 139 residues, 14413.182 Da.

Natural source: Common Name: Burkholderia pseudomallei Taxonomy ID: 320372 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia pseudomallei

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

Entity Sequences (FASTA):
entity_1: MNILYKTAATSTGGRDGRAT SHDQKLDVKLSAPRELGGAG AEGTNPEQLFAAGYSACFLS AMKFVAGQNKQTLPADTTVT AEVGIGPNEEGGFALDVELR VALPGLDAAAAKTLVDRAHH VCPYSNATRNNVAVRLVVA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	482
15N chemical shifts	134
1H chemical shifts	780

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1

Entities:

Entity 1, entity_1, 1 139 residues - 14413.182 Da.

1

MET

ASN

ILE

LEU

TYR

LYS

THR

ALA

THR

2

SER

THR

GLY

ARG

ASP

GLY

ARG

ALA

THR

3

SER

HIS

ASP

GLN

LYS

LEU

ASP

VAL

LYS

LEU

4

SER

ALA

PRO

ARG

GLU

LEU

GLY

ALA

GLY

5

ALA

GLU

GLY

THR

ASN

PRO

GLU

GLN

LEU

PHE

6

ALA

GLY

TYR

SER

ALA

CYS

PHE

LEU

SER

7

ALA

MET

LYS

PHE

VAL

ALA

GLY

GLN

ASN

LYS

8

GLN

THR

LEU

PRO

ALA

ASP

THR

VAL

THR

9

ALA

GLU

VAL

GLY

ILE

GLY

PRO

ASN

GLU

10

GLY

PHE

ALA

LEU

ASP

VAL

GLU

LEU

ARG

11

VAL

ALA

LEU

PRO

GLY

LEU

ASP

ALA

12

ALA

LYS

THR

LEU

VAL

ASP

ARG

ALA

HIS

13

VAL

CYS

PRO

TYR

SER

ASN

ALA

THR

ARG

ASN

14

ASN

VAL

ALA

VAL

ARG

LEU

VAL

ALA

Samples:

sample_1: TRIS 20 mM; sodium chloride 100 mM; DTT 1 mM; B74, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM

sample_2: TRIS 20 mM; sodium chloride 100 mM; DTT 1 mM; B74, 99% 13C; U-99% 15N; 50%-2H]], 1 ± 0.2 mM

sample_3: TRIS 20 mM; sodium chloride 100 mM; DTT 1 mM; B74, 99% 13C; U-99% 15N], 1 ± 0.2 mM

sample_4: TRIS 20 mM; sodium chloride 100 mM; DTT 1 mM; B74, [U-10% 13C; U-99% 15N], 1 ± 0.2 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
3D C(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 HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_4	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1

Software:

Felix v2007, Accelrys Software Inc. - processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement

Sparky v3.115, Goddard - chemical shift assignment, data analysis, peak picking

TALOS v+, Cornilescu, Delaglio and Bax - data analysis

PSVS v1.5, Bhattacharya and Montelione - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AVANCE II 750 MHz
Varian VXRS 750 MHz
Varian VXRS 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts