BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15438

Title: Solution structure of IPI*   PubMed: 18037438

Deposition date: 2007-08-17 Original release date: 2008-06-26

Authors: Rifat, Dalin; Wright, Nathan; Varney, Kristen; Weber, David; Black, Lindsay

Citation: Rifat, Dalin; Wright, Nathan; Varney, Kristen; Weber, David; Black, Lindsay. "Restriction endonuclease inhibitor IPI* of bacteriophage T4: a novel structure for a dedicated target"  J. Mol. Biol. 375, 720-734 (2008).

Assembly members:
IP1*, polymer, 76 residues, 8060.466 Da.

Natural source:   Common Name: T4 phage   Taxonomy ID: 10665   Superkingdom: Viruses   Kingdom: not available   Genus/species: T4-like viruses Enterobacteria phage T4 sensu lato

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

Entity Sequences (FASTA):
IP1*: ATLTSEVIKANKGREGKPMI SLVDGEEIKGTVYLGDGWSA KKDGATIVISPAEETALFKA KHISAAHLKIIAKNLL

Data sets:
Data typeCount
13C chemical shifts221
15N chemical shifts72
1H chemical shifts452

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1IP1*1

Entities:

Entity 1, IP1* 76 residues - 8060.466 Da.

1   ALATHRLEUTHRSERGLUVALILELYSALA
2   ASNLYSGLYARGGLUGLYLYSPROMETILE
3   SERLEUVALASPGLYGLUGLUILELYSGLY
4   THRVALTYRLEUGLYASPGLYTRPSERALA
5   LYSLYSASPGLYALATHRILEVALILESER
6   PROALAGLUGLUTHRALALEUPHELYSALA
7   LYSHISILESERALAALAHISLEULYSILE
8   ILEALALYSASNLEULEU

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 500 mM; sodium acetate 20 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 4.8; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D 15N-13C NOESYsample_1isotropicsample_conditions_1
4D 13C-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker Avance 800 MHz

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