BMRB Entry 19023

Name: Solution structure and sigma factor interactions of Mycobacterium tuberculosis RNA polymerase binding protein A
Published: 2013-04-11

Click here to enlarge.

PDB ID: 2m4v
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19023
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: Solution structure and sigma factor interactions of Mycobacterium tuberculosis RNA polymerase binding protein A PubMed: 23548911

Deposition date: 2013-02-11 Original release date: 2013-04-11

Authors: Bortoluzzi, Alessio; Muskett, Frederick; Waters, Lorna; Adiss, Philip; Rieck, Barbara; Munder, Thomas; Schleier, Susanne; Forti, Francesca; Ghisotti, Daniela; Carr, Mark; O'Hare, Helen

Citation: Bortoluzzi, Alessio; Muskett, Frederick; Waters, Lorna; Adiss, Philip; Rieck, Barbara; Munder, Thomas; Schleier, Susanne; Forti, Francesca; Ghisotti, Daniela; Carr, Mark; O'Hare, Helen. "Structural characterization of Mycobacterium tuberculosis RNA polymerase binding protein A (RbpA) and its interactions with sigma factors" J. Biol. Chem. 288, 14438-14450 (2013).

Assembly members:
entity, polymer, 80 residues, 9026.145 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):
entity: SMADRVLRGSRLGAVSYETD RNHDLAPRQIARYRTDNGEE FEVPFADDAEIPGTWLCRNG MEGTLIEGDLPEPKKVKPPR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	252
15N chemical shifts	76
1H chemical shifts	485

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

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

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_3	isotropic	sample_conditions_1

BMRB	19149
PDB	2M4V 2M6P 4X8K
DBJ	BAH26349 BAL66056 BAN31760 BAQ06108 GAA45755
EMBL	CAB11301 CAC30389 CAL72057 CAR71533 CCC27135
GB	AAK46389 AAS04115 ABK68564 ABQ73825 ABR06418
REF	NP_216566 NP_302017 NP_855726 WP_003410601 WP_003872122
SP	P9WHJ4 P9WHJ5

Biological Magnetic Resonance Data Bank

BMRB Entry 19023

Title: Solution structure and sigma factor interactions of Mycobacterium tuberculosis RNA polymerase binding protein A PubMed: 23548911

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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