BMRB Entry 27852

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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/BMR27852
MolProbity Validation Chart

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Title:
NMR resonance assignments for the GSPII-B domain of the traffic ATPase PilF from Thermus thermophilus in the apo and c-di-GMP-bound states
Deposition date:
2019-03-26
Original release date:
2019-11-22
Authors:
Neissner, Konstantin; Keller, Heiko; Hacker, Carolin; Durchardt-Ferner, Elke; Woehnert, Jens
Citation:

Citation: Neissner, Konstantin; Keller, Heiko; Duchardt-Ferner, Elke; Hacker, Carolin; Kruse, Kerstin; Averhoff, Beate; Wohnert, Jens. "NMR resonance assignments for the GSPII-B domain of the traffic ATPase PilF from Thermus thermophilus in the apo and the c-di-GMP-bound state"  Biomol. NMR Assign. 13, 383-390 (2019).
PubMed: 31432400

Assembly members:

Assembly members:
PilF159-302, polymer, 146 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 274   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-11a_PilF159-302

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PilF159-302: GSSGEGQKDLKLGELLLQKG WISREALEEALVEQEKTGDL LGRILVRKGLPEEALYRALA EQKGLEFLESTEGIVPDPSA ALLLLRSDALRYGAVPIGFQ NGEVEVVLSDPRHKEAVAQL LNRPARFYLALPQAWEELFR RAYPQK

Data sets:
Data typeCount
13C chemical shifts647
15N chemical shifts147
1H chemical shifts1029

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PilF159-3021

Entities:

Entity 1, PilF159-302 146 residues - Formula weight is not available

The first two residues (G,S) remain from TEV-cleavage of a N-terminal His6-Tag.

1   GLYSERSERGLYGLUGLYGLNLYSASPLEU
2   LYSLEUGLYGLULEULEULEUGLNLYSGLY
3   TRPILESERARGGLUALALEUGLUGLUALA
4   LEUVALGLUGLNGLULYSTHRGLYASPLEU
5   LEUGLYARGILELEUVALARGLYSGLYLEU
6   PROGLUGLUALALEUTYRARGALALEUALA
7   GLUGLNLYSGLYLEUGLUPHELEUGLUSER
8   THRGLUGLYILEVALPROASPPROSERALA
9   ALALEULEULEULEUARGSERASPALALEU
10   ARGTYRGLYALAVALPROILEGLYPHEGLN
11   ASNGLYGLUVALGLUVALVALLEUSERASP
12   PROARGHISLYSGLUALAVALALAGLNLEU
13   LEUASNARGPROALAARGPHETYRLEUALA
14   LEUPROGLNALATRPGLUGLULEUPHEARG
15   ARGALATYRPROGLNLYS

Samples:

sample_1: PilF159-302, [U-13C; U-15N], 523 uM; D2O 10%; DSS 200 uM; Bis-TRIS 50 mM; beta-mercaptoethanol 1%; sodium chloride 200 mM

sample_conditions_1: pH: 5.8; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

CARA vv1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 599 MHz
  • 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