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 16964

Title: Solid-state NMR assignment of the globular domain of HET-s(1-227) prion protein in microcrystalline form.   PubMed: 20572250

Authors: Schuetz, Anne; Wasmer, Christian; Habenstein, Birgit; Verel, Rene; Greenwald, Jason; Riek, Roland; Bockmann, Anja; Meier, Beat

Citation: Schuetz, Anne; Wasmer, Christian; Habenstein, Birgit; Verel, Rene; Greenwald, Jason; Riek, Roland; Bockmann, Anja; Meier, Beat. "Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227)."  Chembiochem 11, 1543-1551 (2010).

Assembly members:
HET-s, polymer, 229 residues, 25470 Da.

Natural source:   Common Name: ascomycetes   Taxonomy ID: 5145   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Podospora anserina

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

Entity Sequences (FASTA):
HET-s: GSMSEPFGIVAGALNVAGLF NNCVDCFEYVQLGRPFGRDY ERCQLRLDIAKARLSRWGEA VKINDDPRFHSSAPTDKSVQ LAKSIVEEILLLFESAQKTS KRYELVADQQDLVVFEDKDM KPIGRALHRRLNDLVSRRQK QTSLAKKTAWALYDGKSLEK IVDQVARFVDELEKAFPIEA VCHKLAEIEIEEVEDEASLT ILKDAAGGIDAAMSDAAAQK IDAIVGRNS

Data sets:
Data typeCount
13C chemical shifts817
15N chemical shifts205

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HET-s(1-227)1

Entities:

Entity 1, HET-s(1-227) 229 residues - 25470 Da.

The first two residues represent non-native remainders of a cleaved HIS-tag. This is the globular domain of a prion protein.

1   GLYSERMETSERGLUPROPHEGLYILEVAL
2   ALAGLYALALEUASNVALALAGLYLEUPHE
3   ASNASNCYSVALASPCYSPHEGLUTYRVAL
4   GLNLEUGLYARGPROPHEGLYARGASPTYR
5   GLUARGCYSGLNLEUARGLEUASPILEALA
6   LYSALAARGLEUSERARGTRPGLYGLUALA
7   VALLYSILEASNASPASPPROARGPHEHIS
8   SERSERALAPROTHRASPLYSSERVALGLN
9   LEUALALYSSERILEVALGLUGLUILELEU
10   LEULEUPHEGLUSERALAGLNLYSTHRSER
11   LYSARGTYRGLULEUVALALAASPGLNGLN
12   ASPLEUVALVALPHEGLUASPLYSASPMET
13   LYSPROILEGLYARGALALEUHISARGARG
14   LEUASNASPLEUVALSERARGARGGLNLYS
15   GLNTHRSERLEUALALYSLYSTHRALATRP
16   ALALEUTYRASPGLYLYSSERLEUGLULYS
17   ILEVALASPGLNVALALAARGPHEVALASP
18   GLULEUGLULYSALAPHEPROILEGLUALA
19   VALCYSHISLYSLEUALAGLUILEGLUILE
20   GLUGLUVALGLUASPGLUALASERLEUTHR
21   ILELEULYSASPALAALAGLYGLYILEASP
22   ALAALAMETSERASPALAALAALAGLNLYS
23   ILEASPALAILEVALGLYARGASNSER

Samples:

sample_1: HET-s, [U-100% 13C; U-100% 15N], 25 mg; DTT 0.5 mM; sodium azide 0.02%; DSS 1 mg; TRIS 20 mM; H2O 100%

sample_conditions_1: ionic strength: 20 mM; pH: 8.5; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
3D NCACOsample_1solidsample_conditions_1
3D NCOCAsample_1solidsample_conditions_1
3D CANCOsample_1solidsample_conditions_1
3D NCACB-DREAMsample_1solidsample_conditions_1
3D N(CO)CACBsample_1solidsample_conditions_1
3D CAN(CO)CAsample_1solidsample_conditions_1
3D CCCsample_1solidsample_conditions_1
3D NCACX-DARRsample_1solidsample_conditions_1
3D N(CA)CBCXsample_1solidsample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16965
PDB
GB AAB19707 AAB94631
PRF 1718317A
SP Q03689