BMRB Entry 18153

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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/BMR18153
MolProbity Validation Chart

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Title:
The solution structure of thermomacin
Deposition date:
2011-12-20
Original release date:
2012-02-28
Authors:
Jung, sascha; Soennichsen, Frank; Hung, Chien-Wen; Thoely, Andreas; Boidin-Wichlacz, Celine; Gelhaus, Christoph; Podschun, Rainer; Tasiemski, Aurelie; Leippe, Matthias; Groetzinger, Joachim
Citation:

Citation: Jung, sascha; Soennichsen, Frank; Hung, Chien-Wen; Thoely, Andreas; Boidin-Wichlacz, Celine; Gelhaus, Christoph; Podschun, Rainer; Tasiemski, Aurelie; Leippe, Matthias; Groetzinger, Joachim. "The Macin Family of Antimicrobial Proteins Combines Antimicrobial and Nerve-Repair Activities"  J. Biol. Chem. ., .-..

Assembly members:

Assembly members:
entity, polymer, 75 residues, 8465.560 Da.

Natural source:

Natural source:   Common Name: medicinal leech   Taxonomy ID: 6421   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Hirudo medicinalis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GCFEDWSRCSPSTASATGVL WRSCDSYCKVCFKADRGECY DSPSLNCPHRLPNNKQCRCI NARTAKDNRNPTCWA

Data sets:
Data typeCount
13C chemical shifts125
15N chemical shifts67
1H chemical shifts306

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1thermomacin1

Entities:

Entity 1, thermomacin 75 residues - 8465.560 Da.

1   GLYCYSPHEGLUASPTRPSERARGCYSSER
2   PROSERTHRALASERALATHRGLYVALLEU
3   TRPARGSERCYSASPSERTYRCYSLYSVAL
4   CYSPHELYSALAASPARGGLYGLUCYSTYR
5   ASPSERPROSERLEUASNCYSPROHISARG
6   LEUPROASNASNLYSGLNCYSARGCYSILE
7   ASNALAARGTHRALALYSASPASNARGASN
8   PROTHRCYSTRPALA

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; H2O 93%; D2O 7%; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 7.4; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Brunger, Adams, Clore, Gros, Nilges and Read, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Guntert, Mumenthaler and Wuthrich, Johnson, One Moon Scientific - chemical shift assignment, processing, refinement, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB ABV56207 ABV56569
SP A8I0L8
AlphaFold A8I0L8

Download HSQC peak lists in one of the following formats:
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