BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 34261

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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/BMR34261
MolProbity Validation Chart

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Title: The solution structure of the LptA-Thanatin complex   PubMed: 30443594

Deposition date: 2018-04-22 Original release date: 2018-11-19

Authors: Moehle, K.; Zerbe, O.

Citation: Vetterli, Stefan; Zerbe, Katja; Muller, Maik; Urfer, Matthias; Mondal, Milon; Wang, Shuang-Yan; Moehle, Kerstin; Zerbe, Oliver; Vitale, Alessandra; Pessi, Gabriella; Eberl, Leo; Wollscheid, Bernd; Robinson, John. "Thanatin Targets the Inter-Membrane Protein Bridge Required for Lipopolysaccharide Transport in Escherichia coli"  Sci. Adv. 4, eaau2634-eaau2634 (2018).

Assembly members:
entity_1, polymer, 117 residues, 12769.169 Da.
entity_2, polymer, 21 residues, 2441.984 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 83333   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: VTGDTDQPIHIESDQQSLDM QGNVVTFTGNVIVTQGTIKI NADKVVVTRPGGEQGKEVID GYGKPATFYQMQDNGKPVEG HASQMHYELAKDFVVLTGNA YLQQVDSNIKGDKITYL
entity_2: GSKKPVPIIYCNRRTGKCQR M

Data typeCount
13C chemical shifts502
15N chemical shifts123
1H chemical shifts826

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 117 residues - 12769.169 Da.

1   VALTHRGLYASPTHRASPGLNPROILEHIS
2   ILEGLUSERASPGLNGLNSERLEUASPMET
3   GLNGLYASNVALVALTHRPHETHRGLYASN
4   VALILEVALTHRGLNGLYTHRILELYSILE
5   ASNALAASPLYSVALVALVALTHRARGPRO
6   GLYGLYGLUGLNGLYLYSGLUVALILEASP
7   GLYTYRGLYLYSPROALATHRPHETYRGLN
8   METGLNASPASNGLYLYSPROVALGLUGLY
9   HISALASERGLNMETHISTYRGLULEUALA
10   LYSASPPHEVALVALLEUTHRGLYASNALA
11   TYRLEUGLNGLNVALASPSERASNILELYS
12   GLYASPLYSILETHRTYRLEU

Entity 2, entity_2 21 residues - 2441.984 Da.

1   GLYSERLYSLYSPROVALPROILEILETYR
2   CYSASNARGARGTHRGLYLYSCYSGLNARG
3   MET

Samples:

sample_1: entity_1 mM; entity_2 mM; sodium chloride 150 ± 2 mM; CHAPS 20 ± 1 mM; sodium phosphate 50 ± 2 mM

sample_2: entity_1 mM; entity_2 mM; sodium chloride 150 ± 2 mM; CHAPS 20 ± 1 mM; sodium phosphate 50 ± 2 mM

sample_3: entity_1 mM; entity_2 mM; sodium chloride 150 ± 2 mM; CHAPS 20 ± 1 mM; sodium phosphate 50 ± 2 mM

sample_4: entity_1 mM; entity_2 mM; sodium chloride 150 ± 2 mM; CHAPS 20 ± 1 mM; sodium phosphate 50 ± 2 mM

sample_conditions_1: ionic strength: 1.15 M; pH: 7.5; pressure: 1 bar; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_4isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
13C,15N filtered, 13C edited (aliph) NOESYsample_4isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
13C,15N filtered, 13C edited (aliph.) NOESYsample_2isotropicsample_conditions_1
3D 13C,15N-filtered, 15N edited NOESYsample_4isotropicsample_conditions_1
3D 13C,15N-filtered, 15N edited NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D HBHA(CO)NHsample_4isotropicsample_conditions_1
3D HNCACBsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_4isotropicsample_conditions_1
HBCBCGCDHEsample_2isotropicsample_conditions_1
HBCBCGCDCEHEsample_2isotropicsample_conditions_1
13C,15N filtered, 13C edited (aro.) NOESYsample_2isotropicsample_conditions_1
13C,15N filtered, 13C edited (arom.) NOESYsample_4isotropicsample_conditions_1

Software:

CARA v1.48, Keller and Wuthrich - chemical shift assignment

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - structure calculation

XPLOR-NIH, Schwieters, Bruenger - refinement

CcpNMR, CCPN - peak picking

NMR spectrometers:

  • Bruker Avance-Neo 600 MHz
  • Bruker Avance-Neo 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts