BMRB Entry 6948

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6948

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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 1H, 13C, and 15N Chemical Shift assignments for monomeric E. coli Ferric Uptake Regulator (Fur).

Deposition date:

2006-01-24

Original release date:

2006-05-09

Authors:

Pecqueur, Ludovic; D'Autreaux, Benoit; Brutscher, Bernhard; Michaud-Soret, Isabelle; Bersch, Beate

Citation:

Citation: Pecqueur, Ludovic; D'Autreaux, Benoit; Dupuy, Jerome; Nicolet, Yvain; Jacquamet, Lilian; Brutscher, Bernhard; Michaud-Soret, Isabelle; Bersch, Beate. "Structural changes of E. coli Ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography" J. Biol. Chem. 281, 21286-21295 (2006).
PubMed: 16690618

Assembly members:

Assembly members:
Fur, polymer, 147 residues, 17000 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Vector: pET30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Fur: TDNNTALKKAGLKVTLPRLK ILEVLQEPDNHHVSAEDLYK RLIDMGEEIGLATVYRVLNQ FDDAGIVTRHNFEGGKSVFE LTQQHHHDHLICLDCGKVIE FSDDSIEARQREIAAKHGIR LTNHSLYLYGHCAEGDCRED EHAHEGK

Data sets:

assigned_chemical_shifts
- monomer

Data type	Count
13C chemical shifts	317
15N chemical shifts	116
1H chemical shifts	116

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Fur monomer	1

Entities:

Entity 1, Fur monomer 147 residues - 17000 Da.

the sequence numbering corresponds to the biological unit after NMet cleavage

1

THR

ASP

ASN

THR

ALA

LEU

LYS

ALA

2

GLY

LEU

LYS

VAL

THR

LEU

PRO

ARG

LEU

LYS

3

ILE

LEU

GLU

VAL

LEU

GLN

GLU

PRO

ASP

ASN

4

HIS

VAL

SER

ALA

GLU

ASP

LEU

TYR

LYS

5

ARG

LEU

ILE

ASP

MET

GLY

GLU

ILE

GLY

6

LEU

ALA

THR

VAL

TYR

ARG

VAL

LEU

ASN

GLN

7

PHE

ASP

ALA

GLY

ILE

VAL

THR

ARG

HIS

8

ASN

PHE

GLU

GLY

LYS

SER

VAL

PHE

GLU

9

LEU

THR

GLN

HIS

ASP

HIS

LEU

10

ILE

CYS

LEU

ASP

CYS

GLY

LYS

VAL

ILE

GLU

11

PHE

SER

ASP

SER

ILE

GLU

ALA

ARG

GLN

12

ARG

GLU

ILE

ALA

LYS

HIS

GLY

ILE

ARG

13

LEU

THR

ASN

HIS

SER

LEU

TYR

LEU

TYR

GLY

14

HIS

CYS

ALA

GLU

GLY

ASP

CYS

ARG

GLU

ASP

15

GLU

HIS

ALA

HIS

GLU

GLY

LYS

Samples:

sample_1: FurM, [U-97% 15N; U-13C], 2 ± 0.1 mM; MOPS 100 mM; KCl 500 mM; EDTA 20 mM; D20 7%

conditions_2: pH: 7.5; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H15N_HSQC	sample_1	not available	conditions_2
1H15N13C_MQ_COHNCA	sample_1	not available	conditions_2
1H15N13C_MQ_HNCOCA	sample_1	not available	conditions_2
1H15N13C_HNCACO	sample_1	not available	conditions_2
1H15N13C_HN(CA)CB	sample_1	not available	conditions_2
1H15N13C_HN(COCA)CB	sample_1	not available	conditions_2
HNCO	sample_1	not available	conditions_2

Software:

FELIX v2000, Accelrys -

NMR spectrometers:

Varian Inova 600 MHz
Varian Inova 800 MHz

BMRB	6947
PDB	2FU4
DBJ	BAA35331 BAB34137 BAG76269 BAI24074 BAI29542
EMBL	CAA26429 CAD05156 CAP75172 CAQ31148 CAQ89925
GB	AAB51077 AAC73777 AAG55006 AAL19637 AAN42248
PIR	AB0586
REF	NP_286398 NP_308741 NP_415209 NP_455254 NP_459678
SP	P0A9A9 P0A9B0 P0A9B1 P45599 Q83S79
AlphaFold	P0A9A9 P0A9B0 P0A9B1 P45599 Q83S79