BMRB Entry 15478

Title:
1H and 15N resonance assignment of M7, a computationally-designed artificial protein
Deposition date:
2007-09-19
Original release date:
2008-06-25
Authors:
Stordeur, Claudius; Dalluege, Roman; Birkenmeier, Olaf; Wienk, Hans; Rudolph, Rainer; Lange, Christian; Luecke, Christian
Citation:

Citation: Stordeur, Claudius; Dalluege, Roman; Birkenmeier, Olaf; Wienk, Hans; Rudolph, Rainer; Lange, Christian; Luecke, Christian. "The NMR solution structure of the artificial protein M7 matches the computationally designed model"  Proteins 72, 1104-1107 (2008).
PubMed: 18498106

Assembly members:

Assembly members:
M7, polymer, 96 residues, 10820.4 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not applicable

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28a

Data sets:
Data typeCount
15N chemical shifts111
1H chemical shifts728

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1M71

Entities:

Entity 1, M7 96 residues - 10820.4 Da.

The first four residues GSHM represent a cloning artifact; the protein sequence starts at Lys1.

1   GLYSERHISMETLYSVALASPILETHRILE
2   LYSILEGLNARGASPGLYGLNGLUILEGLU
3   ILEASPILEARGVALSERTHRGLYLYSGLU
4   LEUGLUARGALALEUGLNGLULEUGLULYS
5   ALALEUALAARGALAGLYALAARGASNVAL
6   GLNILETHRILESERALAGLUASNASPGLU
7   GLNALALYSGLULEULEUGLULEUILEALA
8   ARGLEULEUGLNLYSLEUGLYTYRLYSASP
9   ILEASNVALARGVALASNGLYTHRGLUVAL
10   LYSILEGLUVALARGVAL

Samples:

sample_1: M7 1.0 mM; sodium phosphate 25 mM; sodium azide 0.05%; H2O 95%; D2O 5%

sample_2: M7, [U-98% 15N], 1.3 mM; sodium phosphate 25 mM; sodium azide 0.05%; H2O 95%; D2O 5%

sample_3: M7 1.0 mM; sodium phosphate 25 mM; sodium azide 0.05%; D2O 100%

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HTQCsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection, processing

FELIX v2000, Accelrys Software Inc. - data analysis

DYANA v1.5, Guntert, Braun and Wuthrich - structure solution

DISCOVER v2000, Accelrys Software Inc. - refinement

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

PDB

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