BMRB Entry 12010

Name: Backbone 1H, 13C, 15N chemical shift assignments for FliGc protein
Published: 2018-12-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR12010

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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 for FliGc protein

Deposition date:

2017-04-19

Original release date:

2018-12-11

Authors:

Miyanoiri, Yohei; Hijikata, Atsushi; Nishino, Yuuki; Gohara, Mizuki; Onoue, Yasuhiro; Kojima, Seiji; Kojima, Chojiro; Shirai, Tsuyoshi; Kainosho, Masatsune; Homma, Michio

Citation:

Citation: Miyanoiri, Yohei; Hijikata, Atsushi; Nishino, Yuuki; Gohara, Mizuki; Onoue, Yasuhiro; Kojima, Seiji; Kojima, Chojiro; Shirai, Tsuyoshi; Kainosho, Masatsune; Homma, Michio. "Structural and Functional Analysis of the C-Terminal Region of FliG, an Essential Motor Component of Vibrio Na+ -Driven Flagella." Structure 25, 1540-1548 (2017).
PubMed: 28919442

Assembly members:

Assembly members:
flagellar_protein_FliGc, polymer, 116 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Vibrio alginolyticus Taxonomy ID: 663 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio alginolyticus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
flagellar_protein_FliGc: MNHKVHHHHHHIEGRHMMFV FENLVEVDDQGIQKLLRDVP QDVLQKALKGADDSLREKVF KNMSKRAAEMMRDDIEAMPP VRVADVEAAQKEILAIARRM ADAGELMLSGGADEFL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	288
15N chemical shifts	96
1H chemical shifts	96

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	flagellar protein FliGc	1

Entities:

Entity 1, flagellar protein FliGc 116 residues - Formula weight is not available

1

MET

ASN

HIS

LYS

VAL

HIS

2

HIS

ILE

GLU

GLY

ARG

HIS

MET

PHE

VAL

3

PHE

GLU

ASN

LEU

VAL

GLU

VAL

ASP

GLN

4

GLY

ILE

GLN

LYS

LEU

ARG

ASP

VAL

PRO

5

GLN

ASP

VAL

LEU

GLN

LYS

ALA

LEU

LYS

GLY

6

ALA

ASP

SER

LEU

ARG

GLU

LYS

VAL

PHE

7

LYS

ASN

MET

SER

LYS

ARG

ALA

GLU

MET

8

MET

ARG

ASP

ILE

GLU

ALA

MET

PRO

9

VAL

ARG

VAL

ALA

ASP

VAL

GLU

ALA

GLN

10

LYS

GLU

ILE

LEU

ALA

ILE

ALA

ARG

MET

11

ALA

ASP

ALA

GLY

GLU

LEU

MET

LEU

SER

GLY

12

GLY

ALA

ASP

GLU

PHE

LEU

Samples:

sample_1: FliGc, [U-15N], 0.9 mM; Tris-HCl 50 mM; sodium chloride 150 mM; DSS 0.01 % w/v; H2O 95%; D2O, [U-2H], 5%

sample_2: FliGc, [U-13C; U-15N], 0.9 mM; Tris-HCl 50 mM; sodium chloride 150 mM; DSS 0.01 % w/v; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - data analysis, processing

SPARKY, Goddard - chemical shift assignment, peak picking

TALOS vtalos-n, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker Avance 600 MHz

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