BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16368

Title: Solution NMR structure of the homodimeric winged helix-turn-helix DNA-binding domain (fragment 1-100) Mb0332 from Mycobacterium bovis, a possible ArsR-family transcriptional regulator. Northeast Structural Genomics Consortium Target MbR242E.

Authors: Ramelot, Theresa; Ramelot, John; Wang, D.; Ciccosanti, Colleen; Jiang, Mei; Nair, R.; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Cort, John; Wang, D.; Ciccosanti, Colleen; Jiang, Mei; Nair, R.; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the homodimeric winged helix-turn-helix DNA-binding domain (fragment 1-100) Mb0332 from Mycobacterium bovis, a possible ArsR-family transcriptional regulator. Northeast Structural Genomics Consortium Target MbR242E."  Not known ., .-..

Assembly members:
Mb0332, polymer, 109 residues, 11700 Da.

Natural source:   Common Name: Mycobacterium bovis   Taxonomy ID: 1765   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium bovis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Mb0332: XMAGQSDRKAALLDQVARVG KALANGRRLQILDLLAQGER AVEAIATATGMNLTTASANL QALKSGGLVEARREGTRQYY RIAGEDVARLFALVQVVADE HLEHHHHHH

Data typeCount
13C chemical shifts431
15N chemical shifts116
1H chemical shifts720

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Mb0332, chain A1
2Mb0332, chain B1

Entities:

Entity 1, Mb0332, chain A 109 residues - 11700 Da.

8 non-native residues at C-terminus (LEHHHHHH)

1   ACEMETALAGLYGLNSERASPARGLYSALA
2   ALALEULEUASPGLNVALALAARGVALGLY
3   LYSALALEUALAASNGLYARGARGLEUGLN
4   ILELEUASPLEULEUALAGLNGLYGLUARG
5   ALAVALGLUALAILEALATHRALATHRGLY
6   METASNLEUTHRTHRALASERALAASNLEU
7   GLNALALEULYSSERGLYGLYLEUVALGLU
8   ALAARGARGGLUGLYTHRARGGLNTYRTYR
9   ARGILEALAGLYGLUASPVALALAARGLEU
10   PHEALALEUVALGLNVALVALALAASPGLU
11   HISLEUGLUHISHISHISHISHISHIS

Samples:

NC_sample: MES 20 ± 2.5 mM; sodium chloride 200 ± 10 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 1.1 ± 0.05 mM; DSS 50 ± 2.5 uM; H2O 95%; D2O 5%

NC5_sample: MES 20 ± 2.5 mM; sodium chloride 200 ± 2.5 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-5% 13C; U-100% 15N], 0.8 ± 0.1 mM; DSS 50 ± 2.5 uM; H2O 95%; D2O 5%

NC50_sample: MES 20 ± 2.5 mM; sodium chloride 200 ± 2.5 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.5 ± 0.05 mM; DSS 50 ± 2.5 uM; protein .5 ± 0.05 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 200 mM; pH: 6.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aromNC5_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aromNC_sampleisotropicsample_conditions_1
3D CN filt 1H-13C NOESYNC50_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC50_sampleisotropicsample_conditions_1
3D HNCOCANC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphNC5_sampleisotropicsample_conditions_1
2D 1H-15N HSQCNC5_sampleisotropicsample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.3, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.1, (PDBStat) R. Tejero, G.T. Montelione - data analysis

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz
  • Varian INOVA 750 MHz

Related Database Links:

UNP Q7U294