BMRB Entry 18310

Name: Chemical Shift 1H, 13C, 15N Assignments of N-terminal domain of Thermotoga Maritima flagellar motor protein FliG bound to unlabeled FliF C-terminal peptide
Published: 2012-06-13

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18310

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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:

Chemical Shift 1H, 13C, 15N Assignments of N-terminal domain of Thermotoga Maritima flagellar motor protein FliG bound to unlabeled FliF C-terminal peptide

Deposition date:

2012-03-01

Original release date:

2012-06-13

Authors:

Levenson, Robert

Citation:

Citation: Levenson, Robert; Zhou, Hongjun; Dahlquist, Frederick. "Structural insights into the interaction between the bacterial flagellar motor proteins FliF and FliG." Biochemistry 51, 5052-5060 (2012).
PubMed: 22670715

Assembly members:

Assembly members:
FliGn, polymer, 122 residues, Formula weight is not available
FliFc, polymer, 38 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermotoga maritima

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pJY5

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FliGn: MDHHHHHHHHASENLYFQGH MPEKKIDGRRKAAVLLVALG PEKAAQVMKHLDEETVEQLV VEIANIGRVTPEEKKQVLEE FLSLAKAKEMISEGGIEYAK KVLEKAFGPERARKIIERLT SS
FliFc: VSPEEKELLELLEELENIFS RSPSDIAEIVRLWFFERG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	311
15N chemical shifts	103
1H chemical shifts	103

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit	1
2	peptide	2

Entities:

Entity 1, subunit 122 residues - Formula weight is not available

1

MET

ASP

HIS

2

ALA

SER

GLU

ASN

LEU

TYR

PHE

GLN

GLY

HIS

3

MET

PRO

GLU

LYS

ILE

ASP

GLY

ARG

4

LYS

ALA

VAL

LEU

VAL

ALA

LEU

GLY

5

PRO

GLU

LYS

ALA

GLN

VAL

MET

LYS

HIS

6

LEU

ASP

GLU

THR

VAL

GLU

GLN

LEU

VAL

7

VAL

GLU

ILE

ALA

ASN

ILE

GLY

ARG

VAL

THR

8

PRO

GLU

LYS

GLN

VAL

LEU

GLU

9

PHE

LEU

SER

LEU

ALA

LYS

ALA

LYS

GLU

MET

10

ILE

SER

GLU

GLY

ILE

GLU

TYR

ALA

LYS

11

LYS

VAL

LEU

GLU

LYS

ALA

PHE

GLY

PRO

GLU

12

ARG

ALA

ARG

LYS

ILE

GLU

ARG

LEU

THR

13

SER

Entity 2, peptide 38 residues - Formula weight is not available

1

VAL

SER

PRO

GLU

LYS

GLU

LEU

GLU

2

LEU

GLU

LEU

GLU

ASN

ILE

PHE

SER

3

ARG

SER

PRO

SER

ASP

ILE

ALA

GLU

ILE

VAL

4

ARG

LEU

TRP

PHE

GLU

ARG

GLY

Samples:

sample_1: FliGn, [U-13C; U-15N; U-2H], 400 ± 100 uM; FliFc 500 ± 50 uM; Sodium Phosphate 50 mM; NaCl 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 125 mM; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

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

Software:

ANSIG, Kraulis - chemical shift assignment

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

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	18309
GB	AAD35312 ABQ46724 ACB09081 ADA66942 AGL49144 AAD35313 ABQ46723 ACB09080 ADA66943 AGL49145
REF	NP_228035 WP_004082903 WP_008193872 WP_011943308 WP_012310706 NP_228036 WP_004082905 WP_008193870 WP_011943307 WP_012310705
SP	Q9WY63
AlphaFold	Q9WY63