BMRB Entry 17640

Name: EL222(14-222)
Published: 2012-06-04

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17640

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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:

EL222(14-222)

Deposition date:

2011-05-12

Original release date:

2012-06-04

Authors:

Nash, Abigail; McNulty, Reginald; Shillito, Mary; Swartz, Trevor; Bogomolni, Roberto; Luecke, Hartmut; Gardner, Kevin

Citation:

Citation: Nash, Abigail; McNulty, Reginald; Shillito, Mary Elizabeth; Swartz, Trevor; Bogomolni, Roberto; Luecke, Hartmut; Gardner, Kevin. "Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein." Proc. Natl. Acad. Sci. U.S.A. 108, 9449-9454 (2011).
PubMed: 21606338

Assembly members:

Assembly members:
EL222(14-222), polymer, 212 residues, Formula weight is not available
FMN, non-polymer, 456.344 Da.

Natural source:

Natural source: Common Name: Erythrobacter litoralis Taxonomy ID: 314225 Superkingdom: Bacteria Kingdom: not available Genus/species: Erythrobacter litoralis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: His6-GB1 parallel

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EL222(14-222): GEFGADDTRVEVQPPAQWVL DLIEASPIASVVSDPRLADN PLIAINQAFTDLTGYSEEEC VGRNCRFLAGSGTEPWLTDK IRQGVREHKPVLVEILNYKK DGTPFRNAVLVAPIYDDDDE LLYFLGSQVEVDDDQPNMGM ARRERAAEMLKTLSPRQLEV TTLVASGLRNKEVAARLGLS EKTVKMHRGLVMEKLNLKTS ADLVRIAVEAGI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	437
15N chemical shifts	167
1H chemical shifts	655

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EL222(14-222) protein	1
2	FMN	2

Entities:

Entity 1, EL222(14-222) protein 212 residues - Formula weight is not available

EL222 = Erythrobactor litoralis HTCC2594 protein, 222aa total. GB incorrectly annotated to function and start Met aa. first three residues (GEF) are vector-derived; remainder of sequence are residues 14-222 of protein

1

GLY

GLU

PHE

GLY

ALA

ASP

THR

ARG

VAL

2

GLU

VAL

GLN

PRO

ALA

GLN

TRP

VAL

LEU

3

ASP

LEU

ILE

GLU

ALA

SER

PRO

ILE

ALA

SER

4

VAL

SER

ASP

PRO

ARG

LEU

ALA

ASP

ASN

5

PRO

LEU

ILE

ALA

ILE

ASN

GLN

ALA

PHE

THR

6

ASP

LEU

THR

GLY

TYR

SER

GLU

CYS

7

VAL

GLY

ARG

ASN

CYS

ARG

PHE

LEU

ALA

GLY

8

SER

GLY

THR

GLU

PRO

TRP

LEU

THR

ASP

LYS

9

ILE

ARG

GLN

GLY

VAL

ARG

GLU

HIS

LYS

PRO

10

VAL

LEU

VAL

GLU

ILE

LEU

ASN

TYR

LYS

11

ASP

GLY

THR

PRO

PHE

ARG

ASN

ALA

VAL

LEU

12

VAL

ALA

PRO

ILE

TYR

ASP

GLU

13

LEU

TYR

PHE

LEU

GLY

SER

GLN

VAL

GLU

14

VAL

ASP

GLN

PRO

ASN

MET

GLY

MET

15

ALA

ARG

GLU

ARG

ALA

GLU

MET

LEU

16

LYS

THR

LEU

SER

PRO

ARG

GLN

LEU

GLU

VAL

17

THR

LEU

VAL

ALA

SER

GLY

LEU

ARG

ASN

18

LYS

GLU

VAL

ALA

ARG

LEU

GLY

LEU

SER

19

GLU

LYS

THR

VAL

LYS

MET

HIS

ARG

GLY

LEU

20

VAL

MET

GLU

LYS

LEU

ASN

LEU

LYS

THR

SER

21

ALA

ASP

LEU

VAL

ARG

ILE

ALA

VAL

GLU

ALA

22

GLY

ILE

Entity 2, FMN - C17 H21 N4 O9 P - 456.344 Da.

1

FMN

Samples:

sample_1: EL222(14-222), [U-100% 13C; U-100% 15N], 0.1-1 mM; H20 90%; D20 10%

sample_2: EL222(14-222), [U-100% 13C; U-100% 15N], 0.1-1 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 600 MHz

PDB	3P7N
GB	ABC63043
REF	WP_041685679