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 7316

Title: Backbone 1HN, 15N, and 13C Chemical Shift Assignments for wt Im7* (* denotes his-tag) and its variants, Im7*L53AI54A and Im7*YY   PubMed: 17188712

Deposition date: 2006-10-17 Original release date: 2007-05-04

Authors: Whittaker, Sara; Spence, Graham; Grossmann, Guenter; Radford, Sheena; Moore, Geoffrey

Citation: Whittaker, Sara; Spence, Graham; Grossmann, Guenter; Radford, Sheena; Moore, Geoffrey. "NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7."  J. Mol. Biol. 366, 1001-1015 (2007).

Assembly members:
Im7*, polymer, 94 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Im7*: MEHHHHHHELKNSISDYTEA EFVQLLKEIEKENVAATDDV LDVLLEHFVKITEHPDGTDL IYYPSDNRDDSPEGIVKEIK EWRAANGKPGFKQG

Data sets:
Data typeCount
13C chemical shifts247
15N chemical shifts80
1H chemical shifts80

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Monomer1

Entities:

Entity 1, Monomer 94 residues - Formula weight is not available

The sequence of Im7* contains an N-terminal His-tag (denoted by *). Residue numbering starts at residue 2 of wt Im7 (no his-tag).

1   METGLUHISHISHISHISHISHISGLULEU
2   LYSASNSERILESERASPTYRTHRGLUALA
3   GLUPHEVALGLNLEULEULYSGLUILEGLU
4   LYSGLUASNVALALAALATHRASPASPVAL
5   LEUASPVALLEULEUGLUHISPHEVALLYS
6   ILETHRGLUHISPROASPGLYTHRASPLEU
7   ILETYRTYRPROSERASPASNARGASPASP
8   SERPROGLUGLYILEVALLYSGLUILELYS
9   GLUTRPARGALAALAASNGLYLYSPROGLY
10   PHELYSGLNGLY

Samples:

sample_1: Im7*, [U-13C; U-15N], 1 ± 0.2 mM; potassium phosphate buffer 50 mM; sodium sulphate 400 mM; H2O 90%; D2O 10%

sample_2: Im7*, [U-99% 15N], 1 ± 0.2 mM; potassium phosphate buffer 50 mM; sodium sulphate 400 mM; H2O 90%; D2O 10%

conditions_1: pH: 7; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H15N HSQCAll_samplesnot availableconditions_1
HNCOSamples_1_and_3_and_5not availableconditions_1
HNCASamples_3_and_5not availableconditions_1
HNCOCASamples_3_and_5_againnot availableconditions_1
CBCACONHSamples_3_and_5_again2not availableconditions_1
HNCACBsample_1not availableconditions_1
1H-1H-15N NOESY-HSQCsample_2not availableconditions_1

Software:

VNMR v6.1C, Varian - Data acquisition

NMRView v5.1.1, Varian - Data analysis

NMR spectrometers:

  • Varian Inova 500 MHz
  • Varian Inova 600 MHz
  • Varian Inova 750 MHz

Related Database Links:

BMRB 7188 7317
PDB
EMBL CAA45165 CDK50318
GB AAA23071 AIC79148 ELE46623 EOW15734 EQR11492
REF WP_001560791 WP_032277812 YP_009060494
SP Q03708
AlphaFold Q03708

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