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 25263

Title: NMR assignments of the CUS-3 phage coat protein insertion domain.   PubMed: 25694158

Deposition date: 2014-10-02 Original release date: 2015-08-07

Authors: Tripler, Therese; Maciejewski, Mark; Teschke, Carolyn; Alexandrescu, Andrei

Citation: Tripler, Therese; Maciejewski, Mark; Teschke, Carolyn; Alexandrescu, Andrei. "NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein"  Biomol. NMR Assign. 9, 333-336 (2015).

Assembly members:
CUS-3id, polymer, 126 residues, Formula weight is not available

Natural source:   Common Name: Viruses   Taxonomy ID: 38018   Superkingdom: Viruses   Kingdom: not available   Genus/species: CUS-3 Bacteriophage

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

Entity Sequences (FASTA):
CUS-3id: MASGSTESLTVSGQPEHKVE AKDSNGMPVDNRQGTITVSA SGLQVGDAFTIAGVNSVHQI TKDTTGQPQVFRVLAVSGTT VTISPKILPVENTDVASRPY ANVDAKPAESAAITILNKLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts461
15N chemical shifts119
1H chemical shifts742

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1CUS-3id, chain 11
2CUS-3id, chain 21

Entities:

Entity 1, CUS-3id, chain 1 126 residues - Formula weight is not available

contains C-terminal 6x his-tag; additional residues: at N-terminus: MAS from vector design and C-terminus: LE

1   METALASERGLYSERTHRGLUSERLEUTHR
2   VALSERGLYGLNPROGLUHISLYSVALGLU
3   ALALYSASPSERASNGLYMETPROVALASP
4   ASNARGGLNGLYTHRILETHRVALSERALA
5   SERGLYLEUGLNVALGLYASPALAPHETHR
6   ILEALAGLYVALASNSERVALHISGLNILE
7   THRLYSASPTHRTHRGLYGLNPROGLNVAL
8   PHEARGVALLEUALAVALSERGLYTHRTHR
9   VALTHRILESERPROLYSILELEUPROVAL
10   GLUASNTHRASPVALALASERARGPROTYR
11   ALAASNVALASPALALYSPROALAGLUSER
12   ALAALAILETHRILELEUASNLYSLEUGLU
13   HISHISHISHISHISHIS

Samples:

sample_1: insertion domain, [U-100% 15N], 1.9 mM; insertion domain, [U-100% 13C; U-100% 15N], 1.9 mM; H2O 90%; D2O 10%

sample_2: insertion domain, [U-100% 13C; U-100% 15N], 1.9 mM; D2O 100%

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-C13 HSQCsample_2isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1
2D TOCSYsample_2isotropicsample_conditions_1
2D NOESYsample_2isotropicsample_conditions_1

Software:

Ccpnmr_analysis, CCPN - chemical shift assignment, peak picking

Felix, Accelrys Software Inc. - processing

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

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