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 16248

Title: PknB-phosphorylated Rv1827   PubMed: 19318624

Deposition date: 2009-04-08 Original release date: 2009-05-20

Authors: Smerdon, Stephen; Nott, Timothy; Kelly, Geoff

Citation: Nott, Timothy; Kelly, Geoff; Stach, Lasse; Li, Jiejin; Westcott, Sarah; Patel, Dony; Hunt, Debbie; Howell, Stephen; Buxton, Roger; O'Hare, Helen; Smerdon, Stephen. "An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis"  Sci. Signal 2, .-. (2009).

Assembly members:
PknB-phosphorylated Rv1827, polymer, 167 residues, 17280.926 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6P1

Entity Sequences (FASTA):
PknB-phosphorylated Rv1827: GPLGSVTDMNPDIEKDQTSD EVTVETXSVFRADFLSELDA PAQAGTESAVSGVEGLPPGS ALLVVKRGPNAGSRFLLDQA ITSAGRHPDSDIFLDDVTVS RRHAEFRLENNEFNVVDVGS LNGTYVNREPVDSAVLANGD EVQIGKFRLVFLTGPKQGED DGSTGGP

Data sets:
Data typeCount
13C chemical shifts643
15N chemical shifts176
1H chemical shifts1029

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PknB-phosphorylated Rv18271

Entities:

Entity 1, PknB-phosphorylated Rv1827 167 residues - 17280.926 Da.

1   GLYPROLEUGLYSERVALTHRASPMETASN
2   PROASPILEGLULYSASPGLNTHRSERASP
3   GLUVALTHRVALGLUTHRTPOSERVALPHE
4   ARGALAASPPHELEUSERGLULEUASPALA
5   PROALAGLNALAGLYTHRGLUSERALAVAL
6   SERGLYVALGLUGLYLEUPROPROGLYSER
7   ALALEULEUVALVALLYSARGGLYPROASN
8   ALAGLYSERARGPHELEULEUASPGLNALA
9   ILETHRSERALAGLYARGHISPROASPSER
10   ASPILEPHELEUASPASPVALTHRVALSER
11   ARGARGHISALAGLUPHEARGLEUGLUASN
12   ASNGLUPHEASNVALVALASPVALGLYSER
13   LEUASNGLYTHRTYRVALASNARGGLUPRO
14   VALASPSERALAVALLEUALAASNGLYASP
15   GLUVALGLNILEGLYLYSPHEARGLEUVAL
16   PHELEUTHRGLYPROLYSGLNGLYGLUASP
17   ASPGLYSERTHRGLYGLYPRO

Samples:

sample_1: sodium acetate 20 mM; sodium chloride 50 mM; Rv1827 pThr 22, [U-99% 13C; U-99% 15N], 0.3 – 1.0 mM; H2O 90%; D2O 10%

sample_2: sodium acetate 20 mM; sodium chloride 50 mM; Rv1827 pThr 22, [U-99% 13C; U-99% 15N], 0.3 – 1.0 mM; D2O 100%

sample_conditions_1: pH: 5.8; pressure: 1 atm; temperature: 298 K

sample_conditions_2: pH: 5.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_2
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

ARIA_1.2, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

  • Varian INOVA 800 MHz

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