BMRB Entry 18922

Name: 1H, 13C and 15N assignments of the dimeric receiver domain of PmrAn response regulator from Klebsiella pneumonia
Published: 2014-04-22

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR18922

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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:

1H, 13C and 15N assignments of the dimeric receiver domain of PmrAn response regulator from Klebsiella pneumonia

Deposition date:

2012-12-29

Original release date:

2014-04-22

Authors:

Luo, Shih-chi

Citation:

Citation: Luo, Shih-Chi; Lou, Yuan-Chao; Rajasekaran, Mahalingam; Chang, Yi-Wei; Hsiao, Chwan-Deng; Chen, Chinpan. "Structural basis of a physical blockage mechanism for the interaction of response regulator PmrA with connector protein PmrD from Klebsiella pneumoniae." J. Biol. Chem. 288, 25551-25561 (2013).
PubMed: 23861396

Assembly members:

Assembly members:
PmrAn, polymer, 123 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Klebsiella pneumoniae Taxonomy ID: 573 Superkingdom: Bacteria Kingdom: not available Genus/species: Klebsiella pneumoniae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PmrAn: MKILVIEDDALLLQGLILAM QSEGYVCDGVSTAHEAALSL ASNHYSLIVLDLGLPDEDGL HFLSRMRREKMTQPVLILTA RDTLEDRISGLDTGADDYLV KPFALEELNARIRALLRRHN NQG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	352
15N chemical shifts	117
1H chemical shifts	428

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PmrAn, subunit 1	1
2	PmrAn, subunit 2	1

Entities:

Entity 1, PmrAn, subunit 1 123 residues - Formula weight is not available

1

MET

LYS

ILE

LEU

VAL

ILE

GLU

ASP

ALA

2

LEU

GLN

GLY

LEU

ILE

LEU

ALA

MET

3

GLN

SER

GLU

GLY

TYR

VAL

CYS

ASP

GLY

VAL

4

SER

THR

ALA

HIS

GLU

ALA

LEU

SER

LEU

5

ALA

SER

ASN

HIS

TYR

SER

LEU

ILE

VAL

LEU

6

ASP

LEU

GLY

LEU

PRO

ASP

GLU

ASP

GLY

LEU

7

HIS

PHE

LEU

SER

ARG

MET

ARG

GLU

LYS

8

MET

THR

GLN

PRO

VAL

LEU

ILE

LEU

THR

ALA

9

ARG

ASP

THR

LEU

GLU

ASP

ARG

ILE

SER

GLY

10

LEU

ASP

THR

GLY

ALA

ASP

TYR

LEU

VAL

11

LYS

PRO

PHE

ALA

LEU

GLU

LEU

ASN

ALA

12

ARG

ILE

ARG

ALA

LEU

ARG

HIS

ASN

13

ASN

GLN

GLY

Samples:

sample_1: PmrAn, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 – 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 8; pressure: 1 atm; temperature: 310 K

Experiments:

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

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance 850 MHz
Bruker Avance 800 MHz

BMRB	26532 26535
PDB	3W9S 4S04 4S05
DBJ	BAH62495 BAS36450
EMBL	CCI78009 CCM81779 CCM90377 CCM95353 CCN28862
GB	ABR76243 ACI11257 ADC59454 AEJ97287 AEW60332
REF	WP_002895659 WP_004142095 WP_004886130 WP_008805743 WP_016947497