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 27859

Title: hCA II S50C C206S labelled with Lu-DOTA-M8   PubMed: 31183057

Deposition date: 2019-03-29 Original release date: 2019-04-03

Authors: Zimmermann, Kaspar; Joss, Daniel; Muentener, Thomas; Schaefer, Marc; Nogueira, Elisa; Knorr, Livia; Monnard, Fabien; Haeussinger, Daniel

Citation: Zimmermann, Kaspar; Joss, Daniel; Muentener, Thomas; Schaefer, Marc; Nogueira, Elisa; Knorr, Livia; Monnard, Fabien; Haeussinger, Daniel. "Localization of ligands within human carbonic anhydrase II using"  Chem. Sci. 10, 5064-5072 (2019).

Assembly members:
human_carbonic_anhydrase_II_S50C_C206S, polymer, 261 residues, 29372.2535 Da.

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):
human_carbonic_anhydrase_II_S50C_C206S: MAHHWGYGKHNGPEHWHKDF PIAKGERQSPVDIDTHTAKY DPSLKPLSVCYDQATSLRIL NNGHAFNVEFDDSQDKAVLK GGPLDGTYRLIQFHFHWGSL DGQGSEHTVDKKKYAAELHL VHWNTMKYGDFGKAVQQPDG LAVLGIFLKVGSAKPGLQKV VDVLDSIKTKGKSADFTNFD PRGLLPESLDYWTYPGSLTT PPLLESVTWIVLKEPISVSS EQVLKFRKLNFNGEGEPEEL MVDNWRPAQPLKNRQIKASF K

Data sets:
Data typeCount
13C chemical shifts682
15N chemical shifts220
1H chemical shifts220

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human carbonic anhydrase II S50C C206S1

Entities:

Entity 1, human carbonic anhydrase II S50C C206S 261 residues - 29372.2535 Da.

1   METALAHISHISTRPGLYTYRGLYLYSHIS
2   ASNGLYPROGLUHISTRPHISLYSASPPHE
3   PROILEALALYSGLYGLUARGGLNSERPRO
4   VALASPILEASPTHRHISTHRALALYSTYR
5   ASPPROSERLEULYSPROLEUSERVALCYS
6   TYRASPGLNALATHRSERLEUARGILELEU
7   ASNASNGLYHISALAPHEASNVALGLUPHE
8   ASPASPSERGLNASPLYSALAVALLEULYS
9   GLYGLYPROLEUASPGLYTHRTYRARGLEU
10   ILEGLNPHEHISPHEHISTRPGLYSERLEU
11   ASPGLYGLNGLYSERGLUHISTHRVALASP
12   LYSLYSLYSTYRALAALAGLULEUHISLEU
13   VALHISTRPASNTHRMETLYSTYRGLYASP
14   PHEGLYLYSALAVALGLNGLNPROASPGLY
15   LEUALAVALLEUGLYILEPHELEULYSVAL
16   GLYSERALALYSPROGLYLEUGLNLYSVAL
17   VALASPVALLEUASPSERILELYSTHRLYS
18   GLYLYSSERALAASPPHETHRASNPHEASP
19   PROARGGLYLEULEUPROGLUSERLEUASP
20   TYRTRPTHRTYRPROGLYSERLEUTHRTHR
21   PROPROLEULEUGLUSERVALTHRTRPILE
22   VALLEULYSGLUPROILESERVALSERSER
23   GLUGLNVALLEULYSPHEARGLYSLEUASN
24   PHEASNGLYGLUGLYGLUPROGLUGLULEU
25   METVALASPASNTRPARGPROALAGLNPRO
26   LEULYSASNARGGLNILELYSALASERPHE
27   LYS

Samples:

sample_1: human carbonic anhydrase II S50C C206S, [U-13C; U-15N; U-2H], 0.5 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker - collection

CCPNMR, CCPNMR - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance III HD 600.13 MHz

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