BMRB Entry 18255

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PDB ID: 2lpd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18255
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of a MbtH-like protein from Burkholderia pseudomallei, the etiological agent responsible for melioidosis. Seattle Structural Genomics Center for Infectious Disease (SSGCID) target BupsA.13472.b.

Deposition date: 2012-02-10 Original release date: 2012-03-19

Authors: Buchko, Garry

Citation: Buchko, Garry; Hewitt, Stephan; Napuli, Alberto; Van Voorhis, Wesley; Myler, Peter. "Solution structure of a MbtH-like protein from Burkholderia pseudomallei, the etiological agent responsible for melioidosis" Not known ., .-..

Assembly members:
entity, polymer, 95 residues, 10805.033 Da.

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):
entity: MAHHHHHHMGTLEAQTQGPG SMDDELYFVVRNNEGQYSVW MDGRSLPAGWETVGEPATKQ QCLQRIEQLWTDMVPASVRE HLNQHSGPGIDYAVR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	339
15N chemical shifts	84
1H chemical shifts	517

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MbtH-like protein	1

Entities:

Entity 1, MbtH-like protein 95 residues - 10805.033 Da.

The first 21 residues, MAHHHHHHMGTLEAQTQGPGS-,are non-native residue used to facilitate protein purification.

1

MET

ALA

HIS

MET

GLY

2

THR

LEU

GLU

ALA

GLN

THR

GLN

GLY

PRO

GLY

3

SER

MET

ASP

GLU

LEU

TYR

PHE

VAL

4

ARG

ASN

GLU

GLY

GLN

TYR

SER

VAL

TRP

5

MET

ASP

GLY

ARG

SER

LEU

PRO

ALA

GLY

TRP

6

GLU

THR

VAL

GLY

GLU

PRO

ALA

THR

LYS

GLN

7

GLN

CYS

LEU

GLN

ARG

ILE

GLU

GLN

LEU

TRP

8

THR

ASP

MET

VAL

PRO

ALA

SER

VAL

ARG

GLU

9

HIS

LEU

ASN

GLN

HIS

SER

GLY

PRO

GLY

ILE

10

ASP

TYR

ALA

VAL

ARG

Samples:

sample_1: MbtH, [U-99% 13C; U-99% 15N], 1.0 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.1 mM; H2O 93%; D2O 7%

sample_2: MbtH, [U-99% 15N], 1.0 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	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 HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
deuterium exchange	sample_2	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

FELIX v2007, Accelrys Software Inc. - processing

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.115, Goddard - data analysis, peak picking

PSVS, Bhattacharya and Montelione - data analysis

NMR spectrometers:

Varian VNMRS 800 MHz
Varian VNMRS 750 MHz
Varian INOVA 600 MHz

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