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 27435

Title: NMR assignments of Decorator, a phage-cementing 15 KDa monomer   PubMed: 30109462

Deposition date: 2018-03-28 Original release date: 2018-09-19

Authors: Newcomer, Rebecca; Belato, Helen; Teschke, Carolyn; Alexandrescu, Andrei

Citation: Newcomer, Rebecca; Belato, Helen; Teschke, Carolyn; Alexandrescu, Andrei. "NMR assignments for monomeric phage L decoration protein"  Biomol. NMR Assignments 12, 339-343 (2018).

Assembly members:
Decorator, polymer, 137 residues, Formula weight is not available

Natural source:   Common Name: Enterobacteria phage L   Taxonomy ID: 45441   Superkingdom: Viruses   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
Decorator: GSHMANPNFTPSWPLYKDAD GVYVSALPIKAIKYANDGSA NAEFDGPYADQYMSAQTVAV FKPEVGGYLFRSQYGELLYM SKTAFEANYTSASGSVANAE TADKLSTARTITLTGAVTGS ASFDGSANVTIETTSGS

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts141
1H chemical shifts739

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Decorator monomer1

Entities:

Entity 1, Decorator monomer 137 residues - Formula weight is not available

The residues 'gsh' are an artifact of thrombin cleavage. The actual sequence of Dec begins with 'M...', with M being residue 1.

1   GLYSERHISMETALAASNPROASNPHETHR
2   PROSERTRPPROLEUTYRLYSASPALAASP
3   GLYVALTYRVALSERALALEUPROILELYS
4   ALAILELYSTYRALAASNASPGLYSERALA
5   ASNALAGLUPHEASPGLYPROTYRALAASP
6   GLNTYRMETSERALAGLNTHRVALALAVAL
7   PHELYSPROGLUVALGLYGLYTYRLEUPHE
8   ARGSERGLNTYRGLYGLULEULEUTYRMET
9   SERLYSTHRALAPHEGLUALAASNTYRTHR
10   SERALASERGLYSERVALALAASNALAGLU
11   THRALAASPLYSLEUSERTHRALAARGTHR
12   ILETHRLEUTHRGLYALAVALTHRGLYSER
13   ALASERPHEASPGLYSERALAASNVALTHR
14   ILEGLUTHRTHRSERGLYSER

Samples:

sample_1: sodium acetate 20 mM; sodium chloride 50 mM; EDTA 1 mM; Decorator, [U-100% 13C; U-100% 15N; U-80% 2H], 0.08 mM

sample_2: sodium acetate 40 mM; sodium chloride 100 mM; EDTA 2 mM; Decorator, [U-10% 13C; U-100% 15N], 1 mM

sample_3: sodium acetate 20 mM; sodium chloride 50 mM; EDTA 1 mM; Decorator, [U-100% 15N], 0.15 mM

sample_4: Decorator, [U-100% 13C; U-100% 15N; U-50% 2H], 0.2 mM; sodium acetate 20 mM; sodium chloride 50 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 4; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_4isotropicsample_conditions_1

Software:

Felix, Accelrys Software Inc. - processing

CcpNMR_Analysis, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

GB AY795968.1

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