BMRB Entry 50025

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB)
Published: 2020-03-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50025

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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 ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB)

Deposition date:

2019-09-25

Original release date:

2020-03-27

Authors:

Bartkevihi, Leonardo; Almeida, Fabio; Ano Bom, Cristiane

Citation:

Citation: Bartkevihi, Leonardo; Martins, Bruna; de Oliveira, Danielle Maria Perpetua; Pires, Jose Ricardo; Anobom, Cristiane Dinis; Almeida, Fabio. "Backbone assignment of ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB)" Biomol. NMR Assignments 14, 119-122 (2020).
PubMed: 32030620

Assembly members:

Assembly members:
entity_1, polymer, 170 residues, 18312.6696 Da.

Natural source:

Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pCRT7/NT-TOPO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAHHHHHHMSGMRVYLGADH AGYELKQRIIEHLKQTGHEP IDCGALRYDADDDYPAFCIA AATRTVADPGSLGIVLGGSG NGEQIAANKVPGARCALAWS VQTAALAREHNNAQLIGIGG RMHTVAEALAIVDAFVTTPW SKAQRHQRRIDILAEYERTH EAPPVPGAPA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	416
15N chemical shifts	146
1H chemical shifts	146

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Molecule 1, 1	1
2	Molecule 1, 2	1

Entities:

Entity 1, Molecule 1, 1 170 residues - 18312.6696 Da.

1	MET	ALA	HIS	HIS	HIS	HIS	HIS	HIS	MET	SER
2	GLY	MET	ARG	VAL	TYR	LEU	GLY	ALA	ASP	HIS
3	ALA	GLY	TYR	GLU	LEU	LYS	GLN	ARG	ILE	ILE
4	GLU	HIS	LEU	LYS	GLN	THR	GLY	HIS	GLU	PRO
5	ILE	ASP	CYS	GLY	ALA	LEU	ARG	TYR	ASP	ALA
6	ASP	ASP	ASP	TYR	PRO	ALA	PHE	CYS	ILE	ALA
7	ALA	ALA	THR	ARG	THR	VAL	ALA	ASP	PRO	GLY
8	SER	LEU	GLY	ILE	VAL	LEU	GLY	GLY	SER	GLY
9	ASN	GLY	GLU	GLN	ILE	ALA	ALA	ASN	LYS	VAL
10	PRO	GLY	ALA	ARG	CYS	ALA	LEU	ALA	TRP	SER
11	VAL	GLN	THR	ALA	ALA	LEU	ALA	ARG	GLU	HIS
12	ASN	ASN	ALA	GLN	LEU	ILE	GLY	ILE	GLY	GLY
13	ARG	MET	HIS	THR	VAL	ALA	GLU	ALA	LEU	ALA
14	ILE	VAL	ASP	ALA	PHE	VAL	THR	THR	PRO	TRP
15	SER	LYS	ALA	GLN	ARG	HIS	GLN	ARG	ARG	ILE
16	ASP	ILE	LEU	ALA	GLU	TYR	GLU	ARG	THR	HIS
17	GLU	ALA	PRO	PRO	VAL	PRO	GLY	ALA	PRO	ALA

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

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

BMRB Entry 50025

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	MET	ALA	HIS	HIS	HIS	HIS	HIS	HIS	MET	SER
2	GLY	MET	ARG	VAL	TYR	LEU	GLY	ALA	ASP	HIS
3	ALA	GLY	TYR	GLU	LEU	LYS	GLN	ARG	ILE	ILE
4	GLU	HIS	LEU	LYS	GLN	THR	GLY	HIS	GLU	PRO
5	ILE	ASP	CYS	GLY	ALA	LEU	ARG	TYR	ASP	ALA
6	ASP	ASP	ASP	TYR	PRO	ALA	PHE	CYS	ILE	ALA
7	ALA	ALA	THR	ARG	THR	VAL	ALA	ASP	PRO	GLY
8	SER	LEU	GLY	ILE	VAL	LEU	GLY	GLY	SER	GLY
9	ASN	GLY	GLU	GLN	ILE	ALA	ALA	ASN	LYS	VAL
10	PRO	GLY	ALA	ARG	CYS	ALA	LEU	ALA	TRP	SER
11	VAL	GLN	THR	ALA	ALA	LEU	ALA	ARG	GLU	HIS
12	ASN	ASN	ALA	GLN	LEU	ILE	GLY	ILE	GLY	GLY
13	ARG	MET	HIS	THR	VAL	ALA	GLU	ALA	LEU	ALA
14	ILE	VAL	ASP	ALA	PHE	VAL	THR	THR	PRO	TRP
15	SER	LYS	ALA	GLN	ARG	HIS	GLN	ARG	ARG	ILE
16	ASP	ILE	LEU	ALA	GLU	TYR	GLU	ARG	THR	HIS
17	GLU	ALA	PRO	PRO	VAL	PRO	GLY	ALA	PRO	ALA

1	MET	ALA	HIS	HIS	HIS	HIS	HIS	HIS	MET	SER
2	GLY	MET	ARG	VAL	TYR	LEU	GLY	ALA	ASP	HIS
3	ALA	GLY	TYR	GLU	LEU	LYS	GLN	ARG	ILE	ILE
4	GLU	HIS	LEU	LYS	GLN	THR	GLY	HIS	GLU	PRO
5	ILE	ASP	CYS	GLY	ALA	LEU	ARG	TYR	ASP	ALA
6	ASP	ASP	ASP	TYR	PRO	ALA	PHE	CYS	ILE	ALA
7	ALA	ALA	THR	ARG	THR	VAL	ALA	ASP	PRO	GLY
8	SER	LEU	GLY	ILE	VAL	LEU	GLY	GLY	SER	GLY
9	ASN	GLY	GLU	GLN	ILE	ALA	ALA	ASN	LYS	VAL
10	PRO	GLY	ALA	ARG	CYS	ALA	LEU	ALA	TRP	SER
11	VAL	GLN	THR	ALA	ALA	LEU	ALA	ARG	GLU	HIS
12	ASN	ASN	ALA	GLN	LEU	ILE	GLY	ILE	GLY	GLY
13	ARG	MET	HIS	THR	VAL	ALA	GLU	ALA	LEU	ALA
14	ILE	VAL	ASP	ALA	PHE	VAL	THR	THR	PRO	TRP
15	SER	LYS	ALA	GLN	ARG	HIS	GLN	ARG	ARG	ILE
16	ASP	ILE	LEU	ALA	GLU	TYR	GLU	ARG	THR	HIS
17	GLU	ALA	PRO	PRO	VAL	PRO	GLY	ALA	PRO	ALA

1	MET	ALA	HIS	HIS	HIS	HIS	HIS	HIS	MET	SER
2	GLY	MET	ARG	VAL	TYR	LEU	GLY	ALA	ASP	HIS
3	ALA	GLY	TYR	GLU	LEU	LYS	GLN	ARG	ILE	ILE
4	GLU	HIS	LEU	LYS	GLN	THR	GLY	HIS	GLU	PRO
5	ILE	ASP	CYS	GLY	ALA	LEU	ARG	TYR	ASP	ALA
6	ASP	ASP	ASP	TYR	PRO	ALA	PHE	CYS	ILE	ALA
7	ALA	ALA	THR	ARG	THR	VAL	ALA	ASP	PRO	GLY
8	SER	LEU	GLY	ILE	VAL	LEU	GLY	GLY	SER	GLY
9	ASN	GLY	GLU	GLN	ILE	ALA	ALA	ASN	LYS	VAL
10	PRO	GLY	ALA	ARG	CYS	ALA	LEU	ALA	TRP	SER
11	VAL	GLN	THR	ALA	ALA	LEU	ALA	ARG	GLU	HIS
12	ASN	ASN	ALA	GLN	LEU	ILE	GLY	ILE	GLY	GLY
13	ARG	MET	HIS	THR	VAL	ALA	GLU	ALA	LEU	ALA
14	ILE	VAL	ASP	ALA	PHE	VAL	THR	THR	PRO	TRP
15	SER	LYS	ALA	GLN	ARG	HIS	GLN	ARG	ARG	ILE
16	ASP	ILE	LEU	ALA	GLU	TYR	GLU	ARG	THR	HIS
17	GLU	ALA	PRO	PRO	VAL	PRO	GLY	ALA	PRO	ALA