BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25437

Title: Endo T5-ZN+2   PubMed: 27376687

Authors: Prokhorov, Dmitry; Mikoulinskaia, Galina; Molochkov, Nikolai; Kutyshenko, Victor

Citation: Kutyshenko, Victor; Mikoulinskaia, Galina; Molochkov, Nikolai; Prokhorov, Dmitry; Taran, Sergei; Uversky, Vladimir. "Structure and dynamics of the retro-form of the bacteriophage T5 endolysin"  Biochim. Biophys. Acta 1864, 1281-1291 (2016).

Assembly members:
l-alanoyl-d-glutamate_peptidase, polymer, 137 residues, 15286.351 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:   Common Name: Bacteriophage T5   Taxonomy ID: 10726   Superkingdom: Viruses   Kingdom: not available   Genus/species: T5likevirus Enterobacteria phage T5

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

Entity Sequences (FASTA):
l-alanoyl-d-glutamate_peptidase: MSFKFGKNSEKQLATVKPEL QKVARRALELSPYDFTIVQG IRTVAQSAQNIANGTSFLKD PSKSKHITGDAIDFAPYING KIDWNDLEAFWAVKKAFEQA GKELGIKLRFGADWNASGDY HDEIKRGTYDGGHVELV

Data sets:
Data typeCount
13C chemical shifts475
15N chemical shifts135
1H chemical shifts932

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1l-alanoyl-d-glutamate_peptidase1
2ZINC ION2

Entities:

Entity 1, l-alanoyl-d-glutamate_peptidase 137 residues - 15286.351 Da.

1   METSERPHELYSPHEGLYLYSASNSERGLU
2   LYSGLNLEUALATHRVALLYSPROGLULEU
3   GLNLYSVALALAARGARGALALEUGLULEU
4   SERPROTYRASPPHETHRILEVALGLNGLY
5   ILEARGTHRVALALAGLNSERALAGLNASN
6   ILEALAASNGLYTHRSERPHELEULYSASP
7   PROSERLYSSERLYSHISILETHRGLYASP
8   ALAILEASPPHEALAPROTYRILEASNGLY
9   LYSILEASPTRPASNASPLEUGLUALAPHE
10   TRPALAVALLYSLYSALAPHEGLUGLNALA
11   GLYLYSGLULEUGLYILELYSLEUARGPHE
12   GLYALAASPTRPASNALASERGLYASPTYR
13   HISASPGLUILELYSARGGLYTHRTYRASP
14   GLYGLYHISVALGLULEUVAL

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: l-alanoyl-d-glutamate peptidase, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 4.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance III 600 MHz

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