BMRB Entry 51087

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51087

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Title:
Backbone chemical shift assignment and dynamics of N-terminal domain of ClpB from Francisella tularensis type VI secretion system
Deposition date:
2021-09-17
Original release date:
2021-09-23
Authors:
Mushtaq, Ameeq
Citation:

Citation: Mushtaq, Ameeq Ul; Aden, Jorgen; Alam, Athar; Sjostedt, Anders; Grobner, Gerhard. "Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system"  Biomol. NMR Assign. 16, 75-79 (2022).
PubMed: 34985724

Assembly members:

Assembly members:
entity_1, polymer, 156 residues, 17114.35 Da.

Natural source:

Natural source:   Common Name: Francisella tularensis   Taxonomy ID: 263   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Francisella tularensis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-His1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MNINKFTIKLQEALAEAQSY AFQQKATEFTSAHILKALLE QNDSVAISILSVCGVNIQNF IKAVNDMVDSVAVLSGEGNP QVTPSRDLIATLHKMQELAN KNGDEFISSEVFLLASLEDK SLTGLYNKFGITKEKLTKAV NDYRGGEKVSSQNQED

Data sets:
Data typeCount
13C chemical shifts406
15N chemical shifts135
1H chemical shifts135
T1 relaxation values131
T2 relaxation values131
heteronuclear NOE values132

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NTD ClpB1

Entities:

Entity 1, NTD ClpB 156 residues - 17114.35 Da.

NTD ClpB (1-156)

1   METASNILEASNLYSPHETHRILELYSLEU
2   GLNGLUALALEUALAGLUALAGLNSERTYR
3   ALAPHEGLNGLNLYSALATHRGLUPHETHR
4   SERALAHISILELEULYSALALEULEUGLU
5   GLNASNASPSERVALALAILESERILELEU
6   SERVALCYSGLYVALASNILEGLNASNPHE
7   ILELYSALAVALASNASPMETVALASPSER
8   VALALAVALLEUSERGLYGLUGLYASNPRO
9   GLNVALTHRPROSERARGASPLEUILEALA
10   THRLEUHISLYSMETGLNGLULEUALAASN
11   LYSASNGLYASPGLUPHEILESERSERGLU
12   VALPHELEULEUALASERLEUGLUASPLYS
13   SERLEUTHRGLYLEUTYRASNLYSPHEGLY
14   ILETHRLYSGLULYSLEUTHRLYSALAVAL
15   ASNASPTYRARGGLYGLYGLULYSVALSER
16   SERGLNASNGLNGLUASP

Samples:

sample_1: NTD ClpB (1-156), [U-99% 13C; U-99% 15N], 1.7 mM; NaPi 20 mM; NaCl 20 mM

sample_2: NTD ClpB (1-156), [U-99% 15N], 1.7 mM; NaPi 20 mM; NaCl 20 mM

sample_conditions_1: pH: 6.5; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
T1/R1 relaxationsample_1isotropicsample_conditions_1
T2/R2 relaxationsample_1isotropicsample_conditions_1
1H-15N heteronoesample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.6 - collection

NMRPipe v10.6 - processing

CcpNMR v2.4.2 - data analysis

NMRFAM-SPARKY v1.470 - data analysis

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

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