BMRB Entry 30161

Name: Solution structure of response regulator protein from Burkholderia multivorans
Published: 2016-09-09

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PDB ID: 5t3y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30161
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of response regulator protein from Burkholderia multivorans

Deposition date:

2016-08-26

Original release date:

2016-09-09

Authors:

Yang, F.; Lim, Y.-B.; Barnwal, R.; Varani, G.

Citation:

Citation: Yang, F.; Lim, Y.-B.; Barnwal, R.; Varani, G.. "Solution structure of response regulator protein from Burkholderia multivorans" .

Assembly members:

Assembly members:
entity_1, polymer, 125 residues, 13024.712 Da.

Natural source:

Natural source: Common Name: Burkholderia multivorans Taxonomy ID: 87883 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia multivorans

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MIRTILAIDDSATMRALLHA TLAQAGYEVTVAADGEAGFD LAATTAYDLVLTDQNMPRKS GLELIAALRQLSAYADTPIL VLTTEGSDAFKAAARDAGAT GWIEKPIDPGVLVELVATLS EPAAN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	468
15N chemical shifts	111
1H chemical shifts	736

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 125 residues - 13024.712 Da.

1

MET

ILE

ARG

THR

ILE

LEU

ALA

ILE

ASP

2

SER

ALA

THR

MET

ARG

ALA

LEU

HIS

ALA

3

THR

LEU

ALA

GLN

ALA

GLY

TYR

GLU

VAL

THR

4

VAL

ALA

ASP

GLY

GLU

ALA

GLY

PHE

ASP

5

LEU

ALA

THR

ALA

TYR

ASP

LEU

VAL

6

LEU

THR

ASP

GLN

ASN

MET

PRO

ARG

LYS

SER

7

GLY

LEU

GLU

LEU

ILE

ALA

LEU

ARG

GLN

8

LEU

SER

ALA

TYR

ALA

ASP

THR

PRO

ILE

LEU

9

VAL

LEU

THR

GLU

GLY

SER

ASP

ALA

PHE

10

LYS

ALA

ARG

ASP

ALA

GLY

ALA

THR

11

GLY

TRP

ILE

GLU

LYS

PRO

ILE

ASP

PRO

GLY

12

VAL

LEU

VAL

GLU

LEU

VAL

ALA

THR

LEU

SER

13

GLU

PRO

ALA

ASN

Samples:

sample_1: HEPES 25 mM; response regulator protein, [U-13C; U-15N], 0.9 mM

sample_2: HEPES 25 mM; response regulator protein, [U-13C; U-15N], 0.9 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; 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	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	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 aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

CcpNMR, CCPN - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 500 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks