BMRB Entry 25689

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25689
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
1H, 15N and 13C resonance assignments of the C-terminal domain of the TolAIII domain of Vibrio cholerae.
Deposition date:
2015-07-02
Original release date:
2016-11-01
Authors:
Nouailler, Matthieu; Navarro, Romain; Bornet, Olivier; Houot, Laetitia; LLoubes, Roland; Guerlesquin, Francoise
Citation:

Citation: Navarro, Romain; Bornet, Olivier; Houot, Laetitia; LLoubes, Roland; Guerlesquin, Francoise; Nouailler, Matthieu. "(1)H, (15)N and (13)C resonance assignments of the C-terminal domain of Vibrio cholerae TolA protein"  Biomol. NMR Assign. 10, 311-313 (2016).
PubMed: 27436120

Assembly members:

Assembly members:
TolAIII, polymer, 128 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: g-proteobacteria   Taxonomy ID: 666   Superkingdom: bacteria   Kingdom: not available   Genus/species: vibrio cholerae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TolAIII: AEFAALNDIFGSLSEESQQN NAARQQFVTSEVGRYGAIYT QLIRQNLLVEDSFRGKQCRV NLKLIPTGTGALLGSLTVLD GDSRLCAATKRAVAQVNSFP LPKDQPDVVEKLKNINLTVA PEHHHHHH

Data sets:
Data typeCount
13C chemical shifts477
15N chemical shifts123
1H chemical shifts810

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TolAIII1

Entities:

Entity 1, TolAIII 128 residues - Formula weight is not available

1   ALAGLUPHEALAALALEUASNASPILEPHE
2   GLYSERLEUSERGLUGLUSERGLNGLNASN
3   ASNALAALAARGGLNGLNPHEVALTHRSER
4   GLUVALGLYARGTYRGLYALAILETYRTHR
5   GLNLEUILEARGGLNASNLEULEUVALGLU
6   ASPSERPHEARGGLYLYSGLNCYSARGVAL
7   ASNLEULYSLEUILEPROTHRGLYTHRGLY
8   ALALEULEUGLYSERLEUTHRVALLEUASP
9   GLYASPSERARGLEUCYSALAALATHRLYS
10   ARGALAVALALAGLNVALASNSERPHEPRO
11   LEUPROLYSASPGLNPROASPVALVALGLU
12   LYSLEULYSASNILEASNLEUTHRVALALA
13   PROGLUHISHISHISHISHISHIS

Samples:

sample_1_1H: TolAIII 1 ± 0.2 mM; H2O 90%; D2O 10%; NaCl 50 mM; NaPo4 50 mM

sample_13C15N: TolAIII, [U-100% 13C; U-100% 15N], 0.6 ± 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.9; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_13C15Nisotropicsample_conditions_1
2D 1H-1H NOESYsample_1_1Hisotropicsample_conditions_1
3D HNCOsample_13C15Nisotropicsample_conditions_1
3D HNCAsample_13C15Nisotropicsample_conditions_1
3D HNCACBsample_13C15Nisotropicsample_conditions_1
3D HN(CO)CAsample_13C15Nisotropicsample_conditions_1
3D HCCH-TOCSYsample_13C15Nisotropicsample_conditions_1
3D HNHAsample_13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_13C15Nisotropicsample_conditions_1
3D 1H-13C NOESYsample_13C15Nisotropicsample_conditions_1
3D 1H-15N NOESYsample_13C15Nisotropicsample_conditions_1
2D 1H-13C HSQCsample_13C15Nisotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_13C15Nisotropicsample_conditions_1
2D 1H-1H TOCSYsample_1_1Hisotropicsample_conditions_1
3D CBCA(CO)NHsample_13C15Nisotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AMX 950 MHz
  • Bruker AMX 600 MHz

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