BMRB Entry 18659

Name: NMR solution structure of peptide epsilon(103-120) from Mycobacterium tuberculosis F-ATPsynthase
Published: 2013-08-12

Click here to enlarge.

PDB ID: 2lx5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18659
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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:

NMR solution structure of peptide epsilon(103-120) from Mycobacterium tuberculosis F-ATPsynthase

Deposition date:

2012-08-14

Original release date:

2013-08-12

Authors:

Basak, Sandip; Rishikesan, Sankaranarayanan; Gruber, Gerhard

Citation:

Citation: Biukovic, Goran; Basak, Sandip; Manimekalai, Malathy Sony Subramanian; Rishikesan, Sankaranarayanan; Roessle, Manfred; Dick, Thomas; Rao, Srinivasa; Hunke, Cornelia; Gruber, Gerhard. "Variations of subunit {epsilon} of the Mycobacterium tuberculosis F1FO ATP synthase and a novel model for mechanism of action of the TB drug TMC207." Antimicrob. Agents Chemother. ., 168-176 (2012).
PubMed: 23089752

Assembly members:

Assembly members:
epsilon_103-120, polymer, 18 residues, 1924.300 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: chemical synthesis Host organism: Mycobacterium tuberculosis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
epsilon_103-120: DPRIAARGRARLRAVGAI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	114

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	peptide epsilon(103-120)	1

Entities:

Entity 1, peptide epsilon(103-120) 18 residues - 1924.300 Da.

1

ASP

PRO

ARG

ILE

ALA

ARG

GLY

ARG

ALA

2

ARG

LEU

ARG

ALA

VAL

GLY

ALA

ILE

Samples:

sample_1: epsilon103-120 2 mM; TFE, [U-99% 2H], 50%; sodium phosphate 25 mM; sodium chloride 300 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, chemical shift calculation, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2LX5
DBJ	BAH25634 BAL65266 BAQ05285 GAA45059
EMBL	CAC31527 CAL71358 CAR71241 CCC26405 CCC43660
GB	AAA63105 AAK45613 ABQ73060 ABR05681 ACT25749
PIR	T09973
REF	NP_215827 NP_301840 NP_854997 WP_003406708 WP_007773895
SP	A1KI99 A5U210 B8ZR43 C1AMV5 P45822
AlphaFold	A1KI99 A5U210 B8ZR43 C1AMV5 P45822