BMRB Entry 16774

Title:
Solution structure of the Mycobacterium tuberculosis protein Rv0543c, a member of the DUF3349 superfamily. Seattle Structural Genomics Center for Infectious Disease (SSGCID) target MytuD.17112.a
Deposition date:
2010-03-12
Original release date:
2010-03-22
Authors:
Buchko, Garry; Kim, Chang; Thomas, Terwilliger
Citation:

Citation: Buchko, Garry; Phan, Isabelle; Myler, Peter; Terwilliger, Thomas; Kim, Chang-Yub. "Inaugural structure from the DUF3349 superfamily of proteins, Mycobacterium tuberculosis Rv0543c."  Arch. Biochem. Biophys. 506, 150-156 (2011).
PubMed: 21144816

Assembly members:

Assembly members:
Rv0543c, polymer, 103 residues, Formula weight is not available

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   Vector: pET28b

Data sets:
Data typeCount
13C chemical shifts418
15N chemical shifts94
1H chemical shifts671

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv0543c1

Entities:

Entity 1, Rv0543c 103 residues - Formula weight is not available

Residues 1-3 are non-natural residues that remain after cleavage of an affinity tag.

1   GLYSERHISMETASNARGPHELEUTHRSER
2   ILEVALALATRPLEUARGALAGLYTYRPRO
3   GLUGLYILEPROPROTHRASPSERPHEALA
4   VALLEUALALEULEUCYSARGARGLEUSER
5   HISASPGLUVALLYSALAVALALAASNGLU
6   LEUMETARGLEUGLYASPPHEASPGLNILE
7   ASPILEGLYVALVALILETHRHISPHETHR
8   ASPGLULEUPROSERPROGLUASPVALGLU
9   ARGVALARGALAARGLEUALAALAGLNGLY
10   TRPPROLEUASPASPVALARGASPARGGLU
11   GLUHISALA

Samples:

sample_1: Rv0543c 1-2 ± 0.2 mM; sodium chloride 300 ± 10 mM; TRIS 20 ± 2 mM; DTT 1 ± 0.2 mM

sample_2: Rv0543c 1-2 ± 0.2 mM; sodium chloride 300 ± 10 mM; TRIS 20 ± 2 mM; DTT 1 ± 0.2 mM

sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

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

FELIX v2007, Accelrys Software Inc. - processing

SPARKY v3.115, Goddard - data analysis

PSVS v1.1, Bhattacharya and Montelione - data analysis

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz
  • Varian UnityPlus 500 MHz

Related Database Links:

PDB
DBJ BAH24852 BAL64411 BAQ04425 GAA44326
EMBL CAL70572 CCC25622 CCC42886 CCC63147 CCE36083
GB ABQ72273 ABR04897 ACT23581 AEB02684 AEJ45701
REF NP_215057 NP_854218 WP_003402896 WP_003909241 WP_024456652

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