BMRB Entry 26010

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26010
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
NMR structure of the Mycobacterium tuberculosis LppM (Rv2171) protein folded domain.
Deposition date:
2016-03-22
Original release date:
2016-09-08
Authors:
Barthe, Philippe; Cohen-Gonsaud, Martin
Citation:

Citation: Barthe, Philippe; Veyron-Churlet, Romain; de Vish, Angelique; Gilleron, Martine; Saliou, Jean-Michel; Nigou, Jerome; Brodin, Priscille; Cohen-Gonsaud, Martin. "Mycobacterium tuberculosis LppM Displays an Original Structure and Domain Composition Linked to a Dual Localization"  Structure 24, 1788-1794 (2016).
PubMed: 27568926

Assembly members:

Assembly members:
entity, polymer, 171 residues, 18229.328 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GRENLYFQGHMLRVRASITI SPDDLVSGEIIAAAKPKNSK DTGPALDGDVPFSQKVAVSN YDSDGYVGSQAVFSDLTFAE LPQLANMNSDAAGVNLSLRR NGNIVILEGRADLTSVSDPD ADVELTVAFPAAVTSTNGDR IEPEVVQWKLKPGVVSTMSA QARYTDPNTRS

Data sets:
Data typeCount
13C chemical shifts461
15N chemical shifts169
1H chemical shifts1052

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 171 residues - 18229.328 Da.

1   GLYARGGLUASNLEUTYRPHEGLNGLYHIS
2   METLEUARGVALARGALASERILETHRILE
3   SERPROASPASPLEUVALSERGLYGLUILE
4   ILEALAALAALALYSPROLYSASNSERLYS
5   ASPTHRGLYPROALALEUASPGLYASPVAL
6   PROPHESERGLNLYSVALALAVALSERASN
7   TYRASPSERASPGLYTYRVALGLYSERGLN
8   ALAVALPHESERASPLEUTHRPHEALAGLU
9   LEUPROGLNLEUALAASNMETASNSERASP
10   ALAALAGLYVALASNLEUSERLEUARGARG
11   ASNGLYASNILEVALILELEUGLUGLYARG
12   ALAASPLEUTHRSERVALSERASPPROASP
13   ALAASPVALGLULEUTHRVALALAPHEPRO
14   ALAALAVALTHRSERTHRASNGLYASPARG
15   ILEGLUPROGLUVALVALGLNTRPLYSLEU
16   LYSPROGLYVALVALSERTHRMETSERALA
17   GLNALAARGTYRTHRASPPROASNTHRARG
18   SER

Samples:

sample_1: entity, [U-100% 15N], 0.9 ± 0.0045 mM; sodium phosphate 25 ± 0.125 mM; sodium chloride 150 ± 0.75 mM

sample_2: entity, [U-100% 13C; U-100% 15N], 0.9 ± 0.0045 mM; sodium phosphate 25 ± 0.125 mM; sodium chloride 150 ± 0.75 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection

GIFA v4.44, Delsuc - processing

CINDY v1.9, Padilla - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

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