BMRB Entry 34341

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34341
MolProbity Validation Chart

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Title:
Structural investigation of the TasA anchoring protein TapA from Bacillus subtilis
Deposition date:
2018-12-20
Original release date:
2020-01-24
Authors:
Higman, V.; Schmieder, P.; Diehl, A.; Oschkinat, H.
Citation:

Citation: Roske, Yvette; Lindemann, Florian; Diehl, Anne; Cremer, Nils; Higman, Victoria; Schlegel, Brigitte; Leidert, Martina; Driller, Kristina; Turgay, Kursad; Schmieder, Peter; Heinemann, Udo; Oschkinat, Hartmut. "TapA acts as specific chaperone in TasA filament formation by strand complementation"  Proc. Natl. Acad. Sci. U.S.A. 120, e2217070120-e2217070120 (2023).
PubMed: 37068239

Assembly members:

Assembly members:
entity_1, polymer, 147 residues, 17010.301 Da.

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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AFHDIETFDVSLQTCKDFQH TDKNCHYDKRWDQSDLHISD QTDTKGTVCSPFALFAVLEN TGEKLKKSKWKWELHKLENA RKPLKDGNVIEKGFVSNQIG DSLYKIETKKKMKPGIYAFK VYKPAGYPANGSTFEWSEPM RLAKCDE

Data sets:
Data typeCount
13C chemical shifts522
15N chemical shifts114
1H chemical shifts804

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 147 residues - 17010.301 Da.

1   ALAPHEHISASPILEGLUTHRPHEASPVAL
2   SERLEUGLNTHRCYSLYSASPPHEGLNHIS
3   THRASPLYSASNCYSHISTYRASPLYSARG
4   TRPASPGLNSERASPLEUHISILESERASP
5   GLNTHRASPTHRLYSGLYTHRVALCYSSER
6   PROPHEALALEUPHEALAVALLEUGLUASN
7   THRGLYGLULYSLEULYSLYSSERLYSTRP
8   LYSTRPGLULEUHISLYSLEUGLUASNALA
9   ARGLYSPROLEULYSASPGLYASNVALILE
10   GLULYSGLYPHEVALSERASNGLNILEGLY
11   ASPSERLEUTYRLYSILEGLUTHRLYSLYS
12   LYSMETLYSPROGLYILETYRALAPHELYS
13   VALTYRLYSPROALAGLYTYRPROALAASN
14   GLYSERTHRPHEGLUTRPSERGLUPROMET
15   ARGLEUALALYSCYSASPGLU

Samples:

sample_1: TasA anchoring/assembly protein, [U-99% 15N], 1 mM; sodium chloride 50 mM; potassium phosphate 20 mM

sample_2: TasA anchoring/assembly protein, [U-99% 13C; U-99% 15N], 0.54 mM; sodium chloride 50 mM; potassium phosphate 20 mM

sample_conditions_1: ionic strength: 76 mM; pH: 7; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection, processing

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMR spectrometers:

  • Bruker AVANCE 750 MHz
  • Bruker AVANCE III 600 MHz

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