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 15645

Title: NMR STRUCTURE OF A MUTANT COLICIN E7 IMMUNITY PROTEIN IM7 WITH AN EXTENDED HELIX III   PubMed: 19651139

Authors: Figueiredo, Angelo; Whittaker, Sara; Spronk, Chris; Knowling, Stuart; Radford, Sheena; Moore, Geoffrey

Citation: Knowling, Stuart; Figueiredo, Angelo Miguel; Whittaker, Sara B-M; Moore, Geoffrey; Radford, Sheena. "Amino acid insertion reveals a necessary three-helical intermediate in the folding pathway of the colicin E7 immunity protein Im7."  J. Mol. Biol. 392, 1074-1086 (2009).

Assembly members:
Im7_mutant, polymer, 101 residues, 10009.231 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
Im7_mutant: MEHHHHHHELKNSISDYTEA EFVQLLKEIEKENVAATDDV LDVLLEHFVKITEHPDGTAL IYEAAARAAANPGGDGGGPE GIVKEIKEWRAANGKPGFKQ G

Data sets:
Data typeCount
13C chemical shifts403
15N chemical shifts95
1H chemical shifts641

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Im7_mutant1

Entities:

Entity 1, Im7_mutant 101 residues - 10009.231 Da.

1   METGLUHISHISHISHISHISHISGLULEU
2   LYSASNSERILESERASPTYRTHRGLUALA
3   GLUPHEVALGLNLEULEULYSGLUILEGLU
4   LYSGLUASNVALALAALATHRASPASPVAL
5   LEUASPVALLEULEUGLUHISPHEVALLYS
6   ILETHRGLUHISPROASPGLYTHRALALEU
7   ILETYRGLUALAALAALAARGALAALAALA
8   ASNPROGLYGLYASPGLYGLYGLYPROGLU
9   GLYILEVALLYSGLUILELYSGLUTRPARG
10   ALAALAASNGLYLYSPROGLYPHELYSGLN
11   GLY

Samples:

sample_1: potassium phosphate, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; Phosphate buffer 50 mM

sample_2: potassium phosphate, [U-99% 15N], 1 ± 0.2 mM; Phosphate buffer 50 mM

sample_3: potassium phosphate, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; Phosphate buffer 50 mM

sample_conditions_1: ionic strength: 50 mM; pH*: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRView v5.1.1, Johnson, One Moon Scientific - chemical shift assignment

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

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

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

ProcheckNMR, Laskowski and MacArthur - refinement

WhatIF, Vriend - refinement

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

ATHNOS-CANDID v1.1, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 900 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

BMRB 15666
PDB
GB EYB47026