BMRB Entry 19087

Title:
The NMR chemical shift assignments for backbone 1H, 13C, and 15N of VirR (Rv0431)
Deposition date:
2013-03-13
Original release date:
2014-02-24
Authors:
Huang, Chengdong; Wang, Tao; Li, Huilin
Citation:

Citation: Rath, Poonam; Huang, Chengdong; Wang, Tao; Wang, Tianzhi; Li, Huilin; Prados-Rosales, Rafael; Elemento, Olivier; Casadevall, Arturo; Nathan, Carl. "Genetic regulation of vesiculogenesis and immunomodulation in Mycobacterium tuberculosis"  Proc. Natl. Acad. Sci. U. S. A. 110, E4790-E4797 (2013).
PubMed: 24248369

Assembly members:

Assembly members:
entity, polymer, 366 residues, 37006.906 Da.

Natural source:

Natural source:   Common Name: Bacillus 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: unknown

Data sets:
Data typeCount
13C chemical shifts351
15N chemical shifts88
1H chemical shifts471

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal RV04311

Entities:

Entity 1, C-terminal RV0431 366 residues - 37006.906 Da.

1   GLYSERSERPROASNSERGLUASPASPSER
2   SERALAILESERTHRMETTHRTHRTHRTHR
3   ALAALAPROTHRSERTHRSERVALLYSPRO
4   ALAALAPROARGALAGLUVALARGVALTYR
5   ASNILESERGLYTHRGLUGLYALAALAALA
6   ARGTHRALAASPARGLEULYSALAALAGLY
7   PHETHRVALTHRASPVALGLYASNLEUSER
8   LEUPROASPVALALAALATHRTHRVALTYR
9   TYRTHRGLUVALGLUGLYGLUARGALATHR
10   ALAASPALAVALGLYARGTHRLEUGLYALA
11   ALAVALGLULEUARGLEUPROGLULEUSER
12   ASPGLNPROPROGLYVALILEVALVALVAL
13   THRGLYGLYSERSERPROASNSERGLUASP
14   ASPSERSERALAILESERTHRMETTHRTHR
15   THRTHRALAALAPROTHRSERTHRSERVAL
16   LYSPROALAALAPROARGALAGLUVALARG
17   VALTYRASNILESERGLYTHRGLUGLYALA
18   ALAALAARGTHRALAASPARGLEULYSALA
19   ALAGLYPHETHRVALTHRASPVALGLYASN
20   LEUSERLEUPROASPVALALAALATHRTHR
21   VALTYRTYRTHRGLUVALGLUGLYGLUARG
22   ALATHRALAASPALAVALGLYARGTHRLEU
23   GLYALAALAVALGLULEUARGLEUPROGLU
24   LEUSERASPGLNPROPROGLYVALILEVAL
25   VALVALTHRGLYGLYSERSERPROASNSER
26   GLUASPASPSERSERALAILESERTHRMET
27   THRTHRTHRTHRALAALAPROTHRSERTHR
28   SERVALLYSPROALAALAPROARGALAGLU
29   VALARGVALTYRASNILESERGLYTHRGLU
30   GLYALAALAALAARGTHRALAASPARGLEU
31   LYSALAALAGLYPHETHRVALTHRASPVAL
32   GLYASNLEUSERLEUPROASPVALALAALA
33   THRTHRVALTYRTYRTHRGLUVALGLUGLY
34   GLUARGALATHRALAASPALAVALGLYARG
35   THRLEUGLYALAALAVALGLULEUARGLEU
36   PROGLULEUSERASPGLNPROPROGLYVAL
37   ILEVALVALVALTHRGLY

Samples:

sample_1: C-terminal RV0431, [U-100% 13C; U-100% 15N], ; potassium phosphate 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.5 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

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