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 15931

Title: Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form   PubMed: 19679089

Deposition date: 2008-08-27 Original release date: 2009-09-03

Authors: Stott, Katherine

Citation: Stott, Katherine; Yusof, Adlina; Perham, Richard; Jones, Dafydd. "A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure"  Structure 17, 1117-1127 (2009).

Assembly members:
E2plipD4, polymer, 85 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
E2plipD4: MVKEVNVPDIVEVTEVMVKV GDKVAAEQSLITVEGDKASM EVPAPFAGVVKELKVNVGDK VKTGSLIMIFEVEGAAPAAA PAKQE

Data sets:
Data typeCount
15N chemical shifts72
1H chemical shifts495

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E2plipD4, chain 11
2E2plipD4, chain 21

Entities:

Entity 1, E2plipD4, chain 1 85 residues - Formula weight is not available

1   METVALLYSGLUVALASNVALPROASPILE
2   VALGLUVALTHRGLUVALMETVALLYSVAL
3   GLYASPLYSVALALAALAGLUGLNSERLEU
4   ILETHRVALGLUGLYASPLYSALASERMET
5   GLUVALPROALAPROPHEALAGLYVALVAL
6   LYSGLULEULYSVALASNVALGLYASPLYS
7   VALLYSTHRGLYSERLEUILEMETILEPHE
8   GLUVALGLUGLYALAALAPROALAALAALA
9   PROALALYSGLNGLU

Samples:

sample_1: E2plipD4, [U-15N], 1 mM; sodium phosphate 20 mM; TSP 40 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O, . - structure solution

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

PDB
EMBL CSG13687 CSG39424
GB EFI22553 EGB41640 EGI23519 EGI24249 EGI43488
REF WP_000374927 WP_032230881 WP_050541395

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