BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27394

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for FHA-1 domain of Rv1747 from Mycobacterium tuberculosis   PubMed: 29861345

Deposition date: 2018-01-30 Original release date: 2018-06-21

Authors: Heinkel, Florian; Shen, Leo; Richard-Greenblatt, Melissa; Av-Gay, Yossef; Gsponer, Joerg; McIntosh, Lawrence

Citation: Heinkel, Florian; Shen, Leo; Richard-Greenblatt, Melissa; Okon, Mark; Bui, Jennifer; Gee, Christine; Gay, Laurie; Alber, Tom; Av-Gay, Yossef; Gsponer, Joerg; McIntosh, Lawrence. "Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacteriumtuberculosis ABC Transporter Rv1747"  Structure 26, 972-986 (2018).

Assembly members:
Rv1747_FHA-1, polymer, 156 residues, Formula weight is not available

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28MHL

Entity Sequences (FASTA):
Rv1747_FHA-1: GHMSQPAAPPVLTVRYEGSE RTFAAGHDVVVGRDLRADVR VAHPLISRAHLLLRFDQGRW VAIDNGSLNGLYLNNRRVPV VDIYDAQRVHIGNPDGPALD FEVGRHRGSAGRPPQTTSIR LPNLSAGAWPTDGPPQTGTL GSGQLQQLPPATTRIP

Data sets:
Data typeCount
13C chemical shifts407
15N chemical shifts136
1H chemical shifts143

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv1747 FHA-11

Entities:

Entity 1, Rv1747 FHA-1 156 residues - Formula weight is not available

1   GLYHISMETSERGLNPROALAALAPROPRO
2   VALLEUTHRVALARGTYRGLUGLYSERGLU
3   ARGTHRPHEALAALAGLYHISASPVALVAL
4   VALGLYARGASPLEUARGALAASPVALARG
5   VALALAHISPROLEUILESERARGALAHIS
6   LEULEULEUARGPHEASPGLNGLYARGTRP
7   VALALAILEASPASNGLYSERLEUASNGLY
8   LEUTYRLEUASNASNARGARGVALPROVAL
9   VALASPILETYRASPALAGLNARGVALHIS
10   ILEGLYASNPROASPGLYPROALALEUASP
11   PHEGLUVALGLYARGHISARGGLYSERALA
12   GLYARGPROPROGLNTHRTHRSERILEARG
13   LEUPROASNLEUSERALAGLYALATRPPRO
14   THRASPGLYPROPROGLNTHRGLYTHRLEU
15   GLYSERGLYGLNLEUGLNGLNLEUPROPRO
16   ALATHRTHRARGILEPRO

Samples:

sample_1: Rv1747 FHA-1, [U-100% 13C; U-100% 15N], 300 uM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links:

UNP O65934

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