BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 25869

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25869
MolProbity Validation Chart

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Title: Solution structure of LptE from Pseudomonas Aerigunosa   PubMed: 27166502

Deposition date: 2015-10-28 Original release date: 2016-05-23

Authors: Moehle, Kerstin; Kocherla, Harsha; Jurt, Simon; Robinson, John; Zerbe, Oliver; Zerbe, Katja; Bacsa, Bernadette

Citation: Moehle, Kerstin; Kocherla, Harsha; Bacsa, Bernadette; Zerbe, Katja; Robinson, John; Zerbe, Oliver. "Solution structure and dynamics of LptE from Pseudomonas aeruginosa"  Biochemistry 55, 2936-2943 (2016).

Assembly members:
entity, polymer, 166 residues, 18411.617 Da.

Natural source:   Common Name: g-proteobacteria   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pCDFduet-1

Entity Sequences (FASTA):
entity: GTSGFQLRGLGDAQFALKEI DVSARNAYGPTVRELKETLE NSGVKVTSNAPYHLVLVRED NQQRTVSYTGSARGAEFELT NTINYEIVGANDLVLMSNQV QVQKVYVHDENNLIGSDQEA AQLRSEMRRDLIQQLSMRLQ ALTPAQLDEAQRQAEAKAKA EAEALR

Data sets:
Data typeCount
13C chemical shifts587
15N chemical shifts162
1H chemical shifts1017

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 166 residues - 18411.617 Da.

1   GLYTHRSERGLYPHEGLNLEUARGGLYLEU
2   GLYASPALAGLNPHEALALEULYSGLUILE
3   ASPVALSERALAARGASNALATYRGLYPRO
4   THRVALARGGLULEULYSGLUTHRLEUGLU
5   ASNSERGLYVALLYSVALTHRSERASNALA
6   PROTYRHISLEUVALLEUVALARGGLUASP
7   ASNGLNGLNARGTHRVALSERTYRTHRGLY
8   SERALAARGGLYALAGLUPHEGLULEUTHR
9   ASNTHRILEASNTYRGLUILEVALGLYALA
10   ASNASPLEUVALLEUMETSERASNGLNVAL
11   GLNVALGLNLYSVALTYRVALHISASPGLU
12   ASNASNLEUILEGLYSERASPGLNGLUALA
13   ALAGLNLEUARGSERGLUMETARGARGASP
14   LEUILEGLNGLNLEUSERMETARGLEUGLN
15   ALALEUTHRPROALAGLNLEUASPGLUALA
16   GLNARGGLNALAGLUALALYSALALYSALA
17   GLUALAGLUALALEUARG

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 25 mM; CHAPS 20 mM; LptE, 15N-labeled, 0.45 mM; H2O 90%; D2O 10%

sample_2: sodium phosphate 50 mM; sodium chloride 25 mM; CHAPS 20 mM; LptE, 15N,13C-labeled, 0.35 mM; H2O 90%; D2O 10%

sample_3: sodium phosphate 50 mM; sodium chloride 25 mM; LptE, 2H,15N,13C-labeled, 0.35 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 55 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HN(CO)CACBsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

CYANA v3.9, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH v2-1.39, Schwieters, Kuszewski, Tjandra and Clore - refinement

CARA v1.9, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

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