BMRB Entry 18494

Name: Assignment of the -Helical Membrane Protein TM0026 from Thermotoga maritima.
Published: 2013-01-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18494

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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:

Assignment of the -Helical Membrane Protein TM0026 from Thermotoga maritima.

Deposition date:

2012-05-30

Original release date:

2013-01-03

Authors:

Kroncke, Brett; Columbus, Linda

Citation:

Citation: Kroncke, Brett; Columbus, Linda. "Backbone 1H, 13C and 15N resonance assignments of the -helical membrane protein TM0026 from Thermotoga maritima." Biomol. NMR Assignments 7, 203-206 (2013).
PubMed: 23011877

Assembly members:

Assembly members:
TM0026, polymer, 80 residues, 9576.3 Da.

Natural source:

Natural source: Common Name: thermotogales Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: Thermotoga Genus/species: Thermotoga Maritima

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET25b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TM0026: MGSDKIHHHHHHMFTKAVLS IFSWALVLELIVLFYYLWRG LRPVEFYLNLGLLGLTVPFL VFLVVREKKKRREEDDGKDR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	171
15N chemical shifts	59
1H chemical shifts	59

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TM0026 monomer	1

Entities:

Entity 1, TM0026 monomer 80 residues - 9576.3 Da.

Residues 1-12 represent a non-native affinity tag

1	MET	GLY	SER	ASP	LYS	ILE	HIS	HIS	HIS	HIS
2	HIS	HIS	MET	PHE	THR	LYS	ALA	VAL	LEU	SER
3	ILE	PHE	SER	TRP	ALA	LEU	VAL	LEU	GLU	LEU
4	ILE	VAL	LEU	PHE	TYR	TYR	LEU	TRP	ARG	GLY
5	LEU	ARG	PRO	VAL	GLU	PHE	TYR	LEU	ASN	LEU
6	GLY	LEU	LEU	GLY	LEU	THR	VAL	PRO	PHE	LEU
7	VAL	PHE	LEU	VAL	VAL	ARG	GLU	LYS	LYS	LYS
8	ARG	ARG	GLU	GLU	ASP	ASP	GLY	LYS	ASP	ARG

Samples:

sample_1: TM0026, [U-100% 13C]; [U-100% 15N]; [U-95% 2H], 500 ± 100 mM; H2O 90 ± 100 %; D2O 10 ± 100 %

sample_conditions_1: pH: 6.2; pressure: 1 atm; temperature: 273 K

Experiments:

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

Software:

TOPSPIN v3.0.3, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Keller and Wuthrich - chemical shift assignment, collection, processing

NMR spectrometers:

Bruker AMX 600 MHz
Bruker AMX 800 MHz

REF	NP_227842 NP_227842 WP_004082479 WP_011943474 WP_012896089
GB	AAD35120 ABQ46915 ACB09270 ADA66753 AGL48949

1	MET	GLY	SER	ASP	LYS	ILE	HIS	HIS	HIS	HIS
2	HIS	HIS	MET	PHE	THR	LYS	ALA	VAL	LEU	SER
3	ILE	PHE	SER	TRP	ALA	LEU	VAL	LEU	GLU	LEU
4	ILE	VAL	LEU	PHE	TYR	TYR	LEU	TRP	ARG	GLY
5	LEU	ARG	PRO	VAL	GLU	PHE	TYR	LEU	ASN	LEU
6	GLY	LEU	LEU	GLY	LEU	THR	VAL	PRO	PHE	LEU
7	VAL	PHE	LEU	VAL	VAL	ARG	GLU	LYS	LYS	LYS
8	ARG	ARG	GLU	GLU	ASP	ASP	GLY	LYS	ASP	ARG

1	MET	GLY	SER	ASP	LYS	ILE	HIS	HIS	HIS	HIS
2	HIS	HIS	MET	PHE	THR	LYS	ALA	VAL	LEU	SER
3	ILE	PHE	SER	TRP	ALA	LEU	VAL	LEU	GLU	LEU
4	ILE	VAL	LEU	PHE	TYR	TYR	LEU	TRP	ARG	GLY
5	LEU	ARG	PRO	VAL	GLU	PHE	TYR	LEU	ASN	LEU
6	GLY	LEU	LEU	GLY	LEU	THR	VAL	PRO	PHE	LEU
7	VAL	PHE	LEU	VAL	VAL	ARG	GLU	LYS	LYS	LYS
8	ARG	ARG	GLU	GLU	ASP	ASP	GLY	LYS	ASP	ARG