BMRB Entry 25278

Name: Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS. Seattle Structural Genomics Center for Infectious Disease target BupsA.00863.i.
Published: 2014-11-11

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR25278

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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 chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS. Seattle Structural Genomics Center for Infectious Disease target BupsA.00863.i.

Deposition date:

2014-10-09

Original release date:

2014-11-11

Authors:

Buchko, Garry

Citation:

Citation: Buchko, Garry; Edwards, Thomas; Hewitt, Stephen; Phan, Isabelle; Van Voorhis, Wesley; Miller, Samuel; Myler, Peter. "Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS - An "invisible" dimer interface." .

Assembly members:

Assembly members:
RisS, polymer, 127 residues, Formula weight is not available

Natural source:

Natural source: Common Name: b-proteobacteria 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):
RisS: GPGSMSFRVIEREPRAQRVA LQLVAIVKLTRTALLYSDPD LRRALLQDLESNEGVRVYPR EKTDKFKLQPDESVNRLIEH DIRSRLGDDTVIAQSVNDIP GVWISFKIDDDDYWVALDRD QLDTVTG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	247
1H chemical shifts	75
15N chemical shifts	77

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 127 residues - Formula weight is not available

1

GLY

PRO

GLY

SER

MET

SER

PHE

ARG

VAL

ILE

2

GLU

ARG

GLU

PRO

ARG

ALA

GLN

ARG

VAL

ALA

3

LEU

GLN

LEU

VAL

ALA

ILE

VAL

LYS

LEU

THR

4

ARG

THR

ALA

LEU

TYR

SER

ASP

PRO

ASP

5

LEU

ARG

ALA

LEU

GLN

ASP

LEU

GLU

6

SER

ASN

GLU

GLY

VAL

ARG

VAL

TYR

PRO

ARG

7

GLU

LYS

THR

ASP

LYS

PHE

LYS

LEU

GLN

PRO

8

ASP

GLU

SER

VAL

ASN

ARG

LEU

ILE

GLU

HIS

9

ASP

ILE

ARG

SER

ARG

LEU

GLY

ASP

THR

10

VAL

ILE

ALA

GLN

SER

VAL

ASN

ASP

ILE

PRO

11

GLY

VAL

TRP

ILE

SER

PHE

LYS

ILE

ASP

12

ASP

TYR

TRP

VAL

ALA

LEU

ASP

ARG

ASP

13

GLN

LEU

ASP

THR

VAL

THR

GLY

Samples:

sample_1: RisS, [U-13C; U-15N; U-2H], 1 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; H2O 93 ± 0.1 %; D2O 7 ± 0.1 %

sample_conditions_1: temperature: 203 K; pH: 7; pressure: 1 atm; ionic strength: 0.12 M

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

Felix v2007, Accelrys Software Inc. - processing

SPARKY v3.115, Goddard - data analysis

NMR spectrometers:

Agilent INOVA 750 MHz
Agilent INOVA 600 MHz

PDB	3LR0 3LR3 3LR4 3LR5 3TE8
DBJ	BAG43831
EMBL	CAH36098 CAR52312 CDN60458 CDU28740 CFB52363
GB	AAU47661 ABA50560 ABB08844 ABC38194 ABF81004
REF	WP_004196632 WP_004531418 WP_006402221 WP_006408378 WP_006415644