BMRB Entry 25140

Name: Backbone chemical shift assingment of apo EL_LovR
Published: 2016-06-30

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25140

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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 assingment of apo EL_LovR

Deposition date:

2014-08-11

Original release date:

2016-06-30

Authors:

Ocasio, Victor; Correa, Fernando; Gardner, Kevin

Citation:

Citation: Ocasio, Victor; Correa, Fernando; Gardner, Kevin. "Ligand-induced folding of a two-component signaling receiver domain" Biochemistry 54, 1353-1363 (2015).
PubMed: 25629646

Assembly members:

Assembly members:
EL_LovR, polymer, 125 residues, Formula weight is not available

Natural source:

Natural source: Common Name: a-proteobacteria Taxonomy ID: 39960 Superkingdom: Bacteria Kingdom: not available Genus/species: Erythrobacter litoralis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHis-parallel

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EL_LovR: GAMGMPKVLVLEDEPLIAMN LQYAFEDEGAEVVVAATCEQ ALKSLADNPIDVAVLDVNLG PKSHCGPVADALKQRAIPFI LHTGDLDRHGELLRKIDAPV MAKPADTSDVAKRALEMCGG DKEPA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	186
15N chemical shifts	68
1H chemical shifts	372

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EL_LovR	1

Entities:

Entity 1, EL_LovR 125 residues - Formula weight is not available

1

GLY

ALA

MET

GLY

MET

PRO

LYS

VAL

LEU

VAL

2

LEU

GLU

ASP

GLU

PRO

LEU

ILE

ALA

MET

ASN

3

LEU

GLN

TYR

ALA

PHE

GLU

ASP

GLU

GLY

ALA

4

GLU

VAL

ALA

THR

CYS

GLU

GLN

5

ALA

LEU

LYS

SER

LEU

ALA

ASP

ASN

PRO

ILE

6

ASP

VAL

ALA

VAL

LEU

ASP

VAL

ASN

LEU

GLY

7

PRO

LYS

SER

HIS

CYS

GLY

PRO

VAL

ALA

ASP

8

ALA

LEU

LYS

GLN

ARG

ALA

ILE

PRO

PHE

ILE

9

LEU

HIS

THR

GLY

ASP

LEU

ASP

ARG

HIS

GLY

10

GLU

LEU

ARG

LYS

ILE

ASP

ALA

PRO

VAL

11

MET

ALA

LYS

PRO

ALA

ASP

THR

SER

ASP

VAL

12

ALA

LYS

ARG

ALA

LEU

GLU

MET

CYS

GLY

13

ASP

LYS

GLU

PRO

ALA

Samples:

sample_1: EL_LovR, [U-100% 13C; U-100% 15N], 700 uM; DTT 1 mM; TRIS 10 mM; sodium chloride 25 mM; sodium azide 3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.025 M; pH: 7.5; 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_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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	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

Software:

VNMRJ, Varian - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 600 MHz

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