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 18369

Title: Backbone 1H and 15N Chemical Shift Assignments for Hen Egg White Lysozyme mutant W111G.   PubMed: 22468860

Authors: Sziegat, Friederike; Silvers, Robert; Haehnke, Martin; Jensen, Malene; Blackledge, Martin; Wirmer-Bartoschek, Julia; Schwalbe, Harald

Citation: Sziegat, Friederike; Silvers, Robert; Hahnke, Martin; Jensen, Malene Ringkjbing; Blackledge, Martin; Wirmer-Bartoschek, Julia; Schwalbe, Harald. "Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme."  Biochemistry 51, 3361-3372 (2012).

Assembly members:
W111G, polymer, 129 residues, Formula weight is not available

Natural source:   Common Name: Chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

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

Entity Sequences (FASTA):
W111G: KVFGRAELAAAMKRHGLDNY RGYSLGNWVAAAKFESNFNT QATNRNTDGSTDYGILQINS RWWANDGRTPGSRNLANIPA SALLSSDITASVNAAKKIVS DGNGMNAWVAGRNRAKGTDV QAWIRGARL

Data sets:
Data typeCount
15N chemical shifts122
1H chemical shifts122

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1W111G1

Entities:

Entity 1, W111G 129 residues - Formula weight is not available

1   LYSVALPHEGLYARGALAGLULEUALAALA
2   ALAMETLYSARGHISGLYLEUASPASNTYR
3   ARGGLYTYRSERLEUGLYASNTRPVALALA
4   ALAALALYSPHEGLUSERASNPHEASNTHR
5   GLNALATHRASNARGASNTHRASPGLYSER
6   THRASPTYRGLYILELEUGLNILEASNSER
7   ARGTRPTRPALAASNASPGLYARGTHRPRO
8   GLYSERARGASNLEUALAASNILEPROALA
9   SERALALEULEUSERSERASPILETHRALA
10   SERVALASNALAALALYSLYSILEVALSER
11   ASPGLYASNGLYMETASNALATRPVALALA
12   GLYARGASNARGALALYSGLYTHRASPVAL
13   GLNALATRPILEARGGLYALAARGLEU

Samples:

sample_1: W111G, [U-99% 15N], 300 uM; H2O 49.95 M; D2O, [U-2H], 5.55 M

sample_conditions_1: pH: 2.0; pressure: 1 atm; temperature: 293 K

Experiments:

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

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

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