BMRB Entry 16052

Name: Assignment of 1HN, 13C, and 15N chemical shift resonances for the STAS domain of Rv1739c, a putative sulfate transporter of Mycobacterium tuberculosis
Published: 2009-03-23

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16052

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Assignment of 1HN, 13C, and 15N chemical shift resonances for the STAS domain of Rv1739c, a putative sulfate transporter of Mycobacterium tuberculosis PubMed: 19636956

Deposition date: 2008-12-04 Original release date: 2009-03-23

Authors: Sharma, Alok; Ye, Liwen; Zolotarev, Alexander; Alper, Seth; Rigby, Alan

Citation: Sharma, Alok; Ye, Liwen; Zolotarev, Alexander; Alper, Seth; Rigby, Alan. "NMR assignment and secondary structure of the STAS domain of Rv1739c, a putative sulfate transporter of Mycobacterium tuberculosis" Biomol. NMR Assignments 3, 99-102 (2009).

Assembly members:
STAS_domain_of_Rv1739C, polymer, 130 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
STAS_domain_of_Rv1739C: MHDIDDYPQAKRVPGLVVYR YDAPLCFANAEDFRRRALTV VDQDPGQVEWFVLNAESNVE VDLTALDALDQLRTELLRRG IVFAMARVKQDLRESLRAAS LLDKIGEDHIFMTLPTAVQA FRRRHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	509
15N chemical shifts	122
1H chemical shifts	875

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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1	MET	HIS	ASP	ILE	ASP	ASP	TYR	PRO	GLN	ALA
2	LYS	ARG	VAL	PRO	GLY	LEU	VAL	VAL	TYR	ARG
3	TYR	ASP	ALA	PRO	LEU	CYS	PHE	ALA	ASN	ALA
4	GLU	ASP	PHE	ARG	ARG	ARG	ALA	LEU	THR	VAL
5	VAL	ASP	GLN	ASP	PRO	GLY	GLN	VAL	GLU	TRP
6	PHE	VAL	LEU	ASN	ALA	GLU	SER	ASN	VAL	GLU
7	VAL	ASP	LEU	THR	ALA	LEU	ASP	ALA	LEU	ASP
8	GLN	LEU	ARG	THR	GLU	LEU	LEU	ARG	ARG	GLY
9	ILE	VAL	PHE	ALA	MET	ALA	ARG	VAL	LYS	GLN
10	ASP	LEU	ARG	GLU	SER	LEU	ARG	ALA	ALA	SER
11	LEU	LEU	ASP	LYS	ILE	GLY	GLU	ASP	HIS	ILE
12	PHE	MET	THR	LEU	PRO	THR	ALA	VAL	GLN	ALA
13	PHE	ARG	ARG	ARG	HIS	HIS	HIS	HIS	HIS	HIS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HC(CO)NH, HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
15N-TOCSY-HSQC	sample_1	isotropic	sample_conditions_1
1H-13C NOESY	sample_1	isotropic	sample_conditions_1

PDB	2KLN
DBJ	BAH26041 BAL65707 BAQ05756 GAA45466
EMBL	CAL71765 CCC26828 CCC44085 CCC64338 CCE37238
GB	AAK46054 ABQ73499 ABR06098 ACT25325 AEB04397
REF	NP_216255 NP_855420 WP_003408524 WP_003898994 WP_003901239
SP	P9WGF6 P9WGF7

Biological Magnetic Resonance Data Bank

BMRB Entry 16052

Title: Assignment of 1HN, 13C, and 15N chemical shift resonances for the STAS domain of Rv1739c, a putative sulfate transporter of Mycobacterium tuberculosis PubMed: 19636956

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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