BMRB Entry 19396

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19396
MolProbity Validation Chart

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Title:
Lasiocepsin
Deposition date:
2013-07-30
Original release date:
2014-01-13
Authors:
Monincova, Lenka; Budesinsky, Milos; Cujova, Sabina; Cerovsky, Vaclav; Veverka, Vaclav
Citation:

Citation: Monincova, Lenka; Budinsky, Milos; Cujova, Sabina; Ceovsky, Vaclav; Veverka, Vaclav. "Structural basis for antimicrobial activity of lasiocepsin."  Chembiochem 15, 301-308 (2014).
PubMed: 24339323

Assembly members:

Assembly members:
lasiocepsin, polymer, 27 residues, 2906.848 Da.

Natural source:

Natural source:   Common Name: bees   Taxonomy ID: 88510   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Lasioglossum laticeps

Experimental source:

Experimental source:   Production method: chemical synthesis   Host organism: na   Vector: na

Entity Sequences (FASTA):

Entity Sequences (FASTA):
lasiocepsin: GLPRKILCAIAKKKGKCKGP LKLVCKC

Data sets:
Data typeCount
13C chemical shifts90
15N chemical shifts25
1H chemical shifts212

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Lasiocepsin1

Entities:

Entity 1, Lasiocepsin 27 residues - 2906.848 Da.

1   GLYLEUPROARGLYSILELEUCYSALAILE
2   ALALYSLYSLYSGLYLYSCYSLYSGLYPRO
3   LEULYSLEUVALCYSLYSCYS

Samples:

sample_1: H2O 90%; D2O 10%; lasiocepsin 4 mM

sample_conditions_1: ionic strength: 0 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

SPARKY, Goddard - data analysis

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB

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