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 16174

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16174

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Title: 15N, 13C and 1H resonance assignments for the Rv0287-Rv0288 complex   PubMed: 19888683

Deposition date: 2009-02-13 Original release date: 2009-07-22

Authors: Ilghari, Dariush; Waters, Lorna; Veverka, Vaclave; Muskett, Frederick; Carr, Mark

Citation: Ilghari, Dariush; Waters, Lorna; Veverka, Vaclav; Muskett, Frederick; Carr, Mark. "(15)N, (13)C and (1)H resonance assignments and secondary structure determination of the Mycobacterium tuberculosis Rv0287-Rv0288 protein complex."  Biomol. NMR Assignments 3, 171-174 (2009).

Assembly members:
Rv0287, polymer, 97 residues, 9777.91 Da.
Rv0288, polymer, 97 residues, 10477.6 Da.

Natural source:   Common Name: 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):
Rv0287: MSLLDAHIPQLVASQSAFAA KAGLMRHTIGQAEQAAMSAQ AFHQGESSAAFQAAHARFVA AAAKVNTLLDVAQANLGEAA GTYVAADAAAASTYTGF
Rv0288: SMSQIMYNYPAMLGHAGDMA GYAGTLQSLGAEIAVEQAAL QSAWQGDTGITYQAWQAQWN QAMEDLVRAYHAMSSTHEAN TMAMMARDTAEAAKWGG

Data sets:
Data typeCount
13C chemical shifts487
15N chemical shifts197
1H chemical shifts1146

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv02871
2Rv02882

Entities:

Entity 1, Rv0287 97 residues - 9777.91 Da.

1   METSERLEULEUASPALAHISILEPROGLN
2   LEUVALALASERGLNSERALAPHEALAALA
3   LYSALAGLYLEUMETARGHISTHRILEGLY
4   GLNALAGLUGLNALAALAMETSERALAGLN
5   ALAPHEHISGLNGLYGLUSERSERALAALA
6   PHEGLNALAALAHISALAARGPHEVALALA
7   ALAALAALALYSVALASNTHRLEULEUASP
8   VALALAGLNALAASNLEUGLYGLUALAALA
9   GLYTHRTYRVALALAALAASPALAALAALA
10   ALASERTHRTYRTHRGLYPHE

Entity 2, Rv0288 97 residues - 10477.6 Da.

1   SERMETSERGLNILEMETTYRASNTYRPRO
2   ALAMETLEUGLYHISALAGLYASPMETALA
3   GLYTYRALAGLYTHRLEUGLNSERLEUGLY
4   ALAGLUILEALAVALGLUGLNALAALALEU
5   GLNSERALATRPGLNGLYASPTHRGLYILE
6   THRTYRGLNALATRPGLNALAGLNTRPASN
7   GLNALAMETGLUASPLEUVALARGALATYR
8   HISALAMETSERSERTHRHISGLUALAASN
9   THRMETALAMETMETALAARGASPTHRALA
10   GLUALAALALYSTRPGLYGLY

Samples:

sample_1: Rv0287, [U-98% 15N], .7 mM; Rv0288 .7 mM; sodium phosphate 25 mM; sodium chloride 100 mM; PMSF 100 uM; sodium azide .02%; H2O 90%; D2O 10%

sample_2: Rv0288, [U-98% 15N], .7 mM; Rv0287 .7 mM; sodium phosphate 25 mM; sodium chloride 100 mM; PMSF 100 uM; sodium azide .02%; H2O 90%; D2O 10%

sample_3: Rv0287, [U-99% 13C], 1 mM; Rv0288 1 mM; sodium phosphate 25 mM; sodium chloride 100 mM; PMSF 100 uM; sodium azide .02%; D2O 100%

sample_4: Rv0288, [U-99% 13C], 1 mM; Rv0287 1 mM; sodium phosphate 25 mM; sodium chloride 100 mM; PMSF 100 uM; sodium azide .02%; D2O 100%

sample_5: Rv0287, [U-99% 13C; U-98% 15N], 1 mM; Rv0288 1 mM; sodium phosphate 25 mM; sodium chloride 100 mM; PMSF 100 uM; sodium azide .02%; D2O 10%; H2O 90%

sample_6: Rv0288, [U-99% 13C; U-98% 15N], 1 mM; Rv0287 1 mM; sodium phosphate 25 mM; sodium chloride 100 mM; PMSF 100 uM; sodium azide .02%; D2O 10%; H2O 90%

sample_7: Rv0288 .7 mM; Rv0287 .7 mM; sodium phosphate 25 mM; sodium chloride 100 mM; PMSF 100 uM; sodium azide .02%; D2O 100%

sample_conditions: ionic strength: .125 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions
2D 1H-13C HSQCsample_3isotropicsample_conditions
2D 1H-1H TOCSYsample_7isotropicsample_conditions
2D 1H-1H NOESYsample_7isotropicsample_conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions
3D 1H-15N TOCSYsample_1isotropicsample_conditions
3D HCCH-TOCSYsample_3isotropicsample_conditions
3D 1H-13C NOESYsample_3isotropicsample_conditions
3D HNCAsample_5isotropicsample_conditions
3D HNCACBsample_5isotropicsample_conditions
3D CBCA (CO) NHsample_5isotropicsample_conditions
TROSY HNCOCAsample_5isotropicsample_conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions
2D 1H-13C HSQCsample_4isotropicsample_conditions
3D 1H-15N NOESYsample_2isotropicsample_conditions
3D 1H-15N TOCSYsample_2isotropicsample_conditions
3D HCCH-COSYsample_4isotropicsample_conditions
3D 1H-13C NOESYsample_4isotropicsample_conditions
3D HNCAsample_6isotropicsample_conditions
3D HNCACBsample_6isotropicsample_conditions
3D CBCA(CO)NHsample_6isotropicsample_conditions
TROSY HNCOCAsample_6isotropicsample_conditions

Software:

TOPSPIN vBruker Topspin 2.0, Bruker Biospin - collection, processing

SPARKY v3.110, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAH24594 BAL64138 BAQ04147 GAA44081 BAH24595 BAL64139 BAQ04148 GAA44082
EMBL CAL70312 CCC25361 CCC42636 CCC62888 CCE35829 CAA05168 CAD93160 CAL70313 CCC25362 CCC42637
GB AAK44524 ABQ72014 ABR04637 ACT23320 AEB02425 AAK44525 ABQ72015 ABR04638 ACT23321 AEB02426
REF NP_214801 NP_853959 WP_003401503 WP_023643653 WP_031652217 NP_214802 NP_334711 NP_853960 WP_003401514 WP_003902934
SP P0A569 P9WNK2 P9WNK3

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts