BMRB Entry 15334

Name: Solution Structure of the Beryllofluoride-Activated NtrC4 Receiver Domain Dimer
Published: 2012-08-03

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PDB ID: 2jrl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15334
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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:

Solution Structure of the Beryllofluoride-Activated NtrC4 Receiver Domain Dimer

Deposition date:

2007-06-27

Original release date:

2012-08-03

Authors:

Lee, Chul-Jin; Hong, Eunmi; Doucleff, Michaeleen; Pelton, Jeffrey; Wemmer, David

Citation:

Citation: Hastings, Curtis; Lee, Seok-Yong; Cho, Ho; Yan, Dalai; Kustu, Sydney; Wemmer, David. "High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain." Biochemistry 42, 9081-9090 (2003).
PubMed: 12885241

Assembly members:

Assembly members:
NtrC4 Receiver domain dimer, polymer, 121 residues, 13671.741 Da.

Natural source:

Natural source: Common Name: AQUIFEX AEOLICUS VF5 Taxonomy ID: 63363 Superkingdom: Bacteria Kingdom: not available Genus/species: Aquifex aeolicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: ESCHERICHIA COLI Vector: PET21A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NtrC4 Receiver domain dimer: MKRVLVVDDEESITSSLSAI LEEEGYHPDTAKTLREAEKK IKELFFPVIVLDVWMPDGDG VNFIDFIKENSPDSVVIVIT GHGSVDTAVKAIKKGAYEFL EKPFSVERFLLTIKHAFEEY S

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	384
15N chemical shifts	115
1H chemical shifts	821

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NtrC4 Receiver domain 1	1
2	NtrC4 Receiver domain 2	1

Entities:

Entity 1, NtrC4 Receiver domain 1 121 residues - 13671.741 Da.

1

MET

LYS

ARG

VAL

LEU

VAL

ASP

GLU

2

GLU

SER

ILE

THR

SER

LEU

SER

ALA

ILE

3

LEU

GLU

GLY

TYR

HIS

PRO

ASP

THR

4

ALA

LYS

THR

LEU

ARG

GLU

ALA

GLU

LYS

5

ILE

LYS

GLU

LEU

PHE

PRO

VAL

ILE

VAL

6

LEU

ASP

VAL

TRP

MET

PRO

ASP

GLY

ASP

GLY

7

VAL

ASN

PHE

ILE

ASP

PHE

ILE

LYS

GLU

ASN

8

SER

PRO

ASP

SER

VAL

ILE

VAL

ILE

THR

9

GLY

HIS

GLY

SER

VAL

ASP

THR

ALA

VAL

LYS

10

ALA

ILE

LYS

GLY

ALA

TYR

GLU

PHE

LEU

11

GLU

LYS

PRO

PHE

SER

VAL

GLU

ARG

PHE

LEU

12

LEU

THR

ILE

LYS

HIS

ALA

PHE

GLU

TYR

13

SER

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	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 HNCA	sample_1	isotropic	sample_conditions_1
15N-IPAP-HSQC	sample_1	isotropic	sample_conditions_1
[F1] 13C-edited [F3] 13C-filtered HSQC-NOESY	sample_2	isotropic	sample_conditions_1
HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

PDB	1ZIT 2JRL 3DZD
GB	AAC06509
REF	NP_213111 WP_010880049

BMRB Entry 15334

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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