BMRB Entry 27893

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27893
MolProbity Validation Chart

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Title:
Constutively active Mutant D99N LicT-CAT-PRD1
Deposition date:
2019-05-07
Original release date:
2019-05-09
Authors:
Yang, Yinshan; Declerck, Nathalie
Citation:

Citation: Yang, Yinshan; Declerck, Nathalie; Demene, Helene. "NMR chemical shift assignment of a constitutively active fragment of the antitermination protein LicT"  Biomol. NMR Assignments 14, 19-23 (2020).
PubMed: 31612430

Assembly members:

Assembly members:
LicT, polymer, 175 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET15 derivative

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LicT: MKIAKVINNNVISVVNEQGK ELVVMGRGLAFQKKSGDDVD EARIEKVFTLDNKDVSEKFK TLLYDIPIECMEVSEEIISY AKLQLGKKLNDSIYVSLTNH INFAIQRNQKGLDIKNALLW ETKRLYKDEFAIGKEALVMV KNKTGVSLPEDEAGFIALHI VNAELNELQHHHHHH

Data sets:
Data typeCount
13C chemical shifts485
15N chemical shifts163
1H chemical shifts995

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1D99-LicT-CAT-PRD1, chain 11
2D99-LicT-CAT-PRD1, chain 21

Entities:

Entity 1, D99-LicT-CAT-PRD1, chain 1 175 residues - Formula weight is not available

1   METLYSILEALALYSVALILEASNASNASN
2   VALILESERVALVALASNGLUGLNGLYLYS
3   GLULEUVALVALMETGLYARGGLYLEUALA
4   PHEGLNLYSLYSSERGLYASPASPVALASP
5   GLUALAARGILEGLULYSVALPHETHRLEU
6   ASPASNLYSASPVALSERGLULYSPHELYS
7   THRLEULEUTYRASPILEPROILEGLUCYS
8   METGLUVALSERGLUGLUILEILESERTYR
9   ALALYSLEUGLNLEUGLYLYSLYSLEUASN
10   ASPSERILETYRVALSERLEUTHRASNHIS
11   ILEASNPHEALAILEGLNARGASNGLNLYS
12   GLYLEUASPILELYSASNALALEULEUTRP
13   GLUTHRLYSARGLEUTYRLYSASPGLUPHE
14   ALAILEGLYLYSGLUALALEUVALMETVAL
15   LYSASNLYSTHRGLYVALSERLEUPROGLU
16   ASPGLUALAGLYPHEILEALALEUHISILE
17   VALASNALAGLULEUASNGLULEUGLNHIS
18   HISHISHISHISHIS

Samples:

sample_1_norm: LicT, [U-99% 13C; U-99% 15N], 800 ± 25 uM; TRIS 10 ± 3 mM; sodium chloride 200 ± 10 mM; DTT 1 ± 0.1 mM; EDTA 0.2 ± 0.05 mM; benzamidine 0.2 ± 0.05 mM

sample_1_D20: LicT, [U-99% 13C; U-99% 15N], 350 ± 25 uM; TRIS 10 ± 3 mM; sodium chloride 200 ± 10 mM; DTT 1 ± 0.1 mM; EDTA 0.2 ± 0.05 mM; benzamidine 0.2 ± 0.05 mM

samplepH64: LicT, [U-99% 13C; U-99% 15N], 600 ± 25 uM; Phosphate 20 ± 3 mM; sodium chloride 200 ± 10 mM; DTT 1 ± 0.1 mM; EDTA 0.2 ± 0.05 mM; benzamidine 0.2 ± 0.05 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 8; pressure: 1 atm; temperature: 308 K

sample_condition_pH64: ionic strength: 0.2 M; pH: 8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1_normisotropicsample_conditions_1
3D CBCA(CO)NHsample_1_normisotropicsample_conditions_1
3D HNCOsample_1_normisotropicsample_conditions_1
3D HNCAsample_1_normisotropicsample_conditions_1
3D HN(CO)CAsample_1_normisotropicsample_conditions_1
3D 1H-15N NOESYsample_1_normisotropicsample_conditions_1
3D 1H-15N TOCSYsample_1_normisotropicsample_conditions_1
2D 1H-13C HSQCsample_1_D20isotropicsample_conditions_1
3D HCCH-TOCSYsample_1_D20isotropicsample_conditions_1
3D 1H-15N NOESYsamplepH64isotropicsample_condition_pH64
3D 1H-15N TOCSYsamplepH64isotropicsample_condition_pH64

Software:

GIFA, Marc Andre Delsuc - processing

Xplor, Brunger - structure calculation

NMR spectrometers:

  • Bruker Avance 800 MHz

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