BMRB Entry 18602

Name: Solution structure of the soluble domain of MmpS4 from Mycobacterium tuberculosis
Published: 2013-03-11

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PDB ID: 2lw3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18602
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the soluble domain of MmpS4 from Mycobacterium tuberculosis PubMed: 23431276

Deposition date: 2012-07-19 Original release date: 2013-03-11

Authors: Xi, Zhaoyong; Sun, Peibei; Wang, Wei; Lai, Chaohua; Wu, Fangming; Tian, Changlin

Citation: Wells, Ryan; Jones, Christopher; Xi, Zhaoyong; Speer, Alexander; Danilchanka, Olga; Doornbos, Kathryn; Sun, Peibei; Wu, Fangming; Tian, Changlin; Niederweis, Michael. "Discovery of a Siderophore Export System Essential for Virulence of Mycobacterium tuberculosis" Plos Pathog. 9, e1003120-e1003120 (2013).

Assembly members:
soluble domain of MmpS4, polymer, 90 residues, 9725.934 Da.

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):
soluble domain of MmpS4: MHLTYEIFGPPGTVADISYF DVNSEPQRVDGAVLPWSLHI TTNDAAVMGNIVAQGNSDSI GCRITVDGKVRAERVSNEVN AYTYCLVKSA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	296
15N chemical shifts	74
1H chemical shifts	453

Additional metadata:

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_3
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1

BMRB	18109
PDB	2LW3
DBJ	BAH24756 BAL64310 BAQ04318
EMBL	CAL70475 CCC25525 CCC42789 CCC63051 CCE35989
GB	AAK44690 ABQ72177 ABR04800 ACT23482 AEB02585
REF	NP_214965 NP_854122 WP_003402272 WP_015456133 WP_016719779
SP	P0A5K3 P9WJS8 P9WJS9

Biological Magnetic Resonance Data Bank

BMRB Entry 18602

Title: Solution structure of the soluble domain of MmpS4 from Mycobacterium tuberculosis PubMed: 23431276

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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