BMRB Entry 26908

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26908

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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, 15N chemical shift assignments of portions of Thermotoga maritima flagellar motor proteins FliG (N-terminal domain; FliGN) and FliF (C-terminal domain; FliFC) in complex

Deposition date:

2016-09-23

Original release date:

2017-02-15

Authors:

Levenson, Robert; Dahlquist, Frederick

Citation:

Citation: Lynch, Michael; Levenson, Robert; Kim, Eun; Sircar, Ria; Blair, David; Dahlquist, Frederick; Crane, Brian. "Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor" Structure 25, 317-328 (2017).
PubMed: 28089452

Assembly members:

Assembly members:
FliGn, polymer, 104 residues, Formula weight is not available
FliFc, polymer, 58 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: GHMPEKKIDGRRKAAVLLVA LGPEKAAQVMKHLDEETVEQ LVVEIANIGRVTPEEKKQVL EEFLSLAKAKEMISEGGIEY AKKVLEKAFGPERARKIIER LTSS
FliFc: MVSPEEKELLELLEELENIF SRSPSDIAEIVRLWFFERGL EDHHHHHHHHASENLYFQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	267
15N chemical shifts	131
1H chemical shifts	131

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FliGn	1
2	FliFc	2

Entities:

Entity 1, FliGn 104 residues - Formula weight is not available

1

GLY

HIS

MET

PRO

GLU

LYS

ILE

ASP

GLY

2

ARG

LYS

ALA

VAL

LEU

VAL

ALA

3

LEU

GLY

PRO

GLU

LYS

ALA

GLN

VAL

MET

4

LYS

HIS

LEU

ASP

GLU

THR

VAL

GLU

GLN

5

LEU

VAL

GLU

ILE

ALA

ASN

ILE

GLY

ARG

6

VAL

THR

PRO

GLU

LYS

GLN

VAL

LEU

7

GLU

PHE

LEU

SER

LEU

ALA

LYS

ALA

LYS

8

GLU

MET

ILE

SER

GLU

GLY

ILE

GLU

TYR

9

ALA

LYS

VAL

LEU

GLU

LYS

ALA

PHE

GLY

10

PRO

GLU

ARG

ALA

ARG

LYS

ILE

GLU

ARG

11

LEU

THR

SER

Entity 2, FliFc 58 residues - Formula weight is not available

1

MET

VAL

SER

PRO

GLU

LYS

GLU

LEU

2

GLU

LEU

GLU

LEU

GLU

ASN

ILE

PHE

3

SER

ARG

SER

PRO

SER

ASP

ILE

ALA

GLU

ILE

4

VAL

ARG

LEU

TRP

PHE

GLU

ARG

GLY

LEU

5

GLU

ASP

HIS

6

ALA

SER

GLU

ASN

LEU

TYR

PHE

GLN

Samples:

sample_1: FliGn, [U-13C; U-15N; U-2H], 400 ± 100 uM; FliFc, [U-13C; U-15N; U-2H], 400 ± 100 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:

Bruker Avance 800 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