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 30737

Title: Dimeric form of the trans-stabilized Hemolysin II C-terminal domain   PubMed: 33733504

Deposition date: 2020-03-24 Original release date: 2021-03-19

Authors: Kaplan, A.; Alexandrescu, A.

Citation: Kaplan, A.; Olson, R.; Alexandrescu, A.. "Protein Yoga: Conformational Versatility of the Hemolysin II C-terminal Domain Detailed by NMR Structures for Multiple States"  Protein Sci. ., .-. (2021).

Assembly members:
entity_1, polymer, 94 residues, 10461.706 Da.

Natural source:   Common Name: Bacillus cereus   Taxonomy ID: 226900   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus cereus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21   Vector: pET28b

Entity Sequences (FASTA):
entity_1: DNQKALEEQMNSINSVNDKL NKGKGKLSLSMNGNQLKATS SNAGYGISYEDKNWGIFVNG EKVYTFNEKSTVGNISNDIN KLNIKGMYIEIKQI

Data sets:
Data typeCount
13C chemical shifts241
15N chemical shifts91
1H chemical shifts92

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 94 residues - 10461.706 Da.

1   ASPASNGLNLYSALALEUGLUGLUGLNMET
2   ASNSERILEASNSERVALASNASPLYSLEU
3   ASNLYSGLYLYSGLYLYSLEUSERLEUSER
4   METASNGLYASNGLNLEULYSALATHRSER
5   SERASNALAGLYTYRGLYILESERTYRGLU
6   ASPLYSASNTRPGLYILEPHEVALASNGLY
7   GLULYSVALTYRTHRPHEASNGLULYSSER
8   THRVALGLYASNILESERASNASPILEASN
9   LYSLEUASNILELYSGLYMETTYRILEGLU
10   ILELYSGLNILE

Samples:

sample_1: HlyIIC, [U-99% 13C; U-99% 15N], 0.8 mM; sodium phosphate 20 mM; EDTA 1 mM; sodium azide 0.05 % w/v; AEBSF protease inhibitor 1 mM

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 303.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY (edited)sample_1isotropicsample_conditions_1
3D 1H-13C NOESY (filtered)sample_1isotropicsample_conditions_1

Software:

CcpNmr Analysis v2.4, CCPN - chemical shift assignment, data analysis, peak picking

TALOS vTALOS-N, Cornilescu, Delaglio and Bax - geometry optimization

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Varian INOVA 600 MHz

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