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 34308

Title: Active-site conformational dynamics of carbonic anhydrase II under native conditions: An NMR perspective

Deposition date: 2018-08-17 Original release date: 2019-08-23

Authors: Singh, H.; Linser, R.

Citation: Singh, H.; Linser, R.. "Active-site conformational dynamics of carbonic anhydrase under native conditions: An NMR perspective"  . ., .-..

Assembly members:
entity_1, polymer, 260 residues, 29289.062 Da.
entity_ZN, non-polymer, 65.409 Da.
entity_HOH, water, 18.015 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity_1: MSHHWGYGKHNGPEHWHKDF PIAKGERQSPVDIDTHTAKY DPSLKPLSVSYDQATSLRIL NNGHAFNVEFDDSQDKAVLK GGPLDGTYRLIQFHFHWGSL DGQGSEHTVDKKKYAAELHL VHWNTKYGDFGKAVQQPDGL AVLGIFLKVGSAKPGLQKVV DVLDSIKTKGKSADFTNFDP RGLLPESLDYWTYPGSLTTP PLLECVTWIVLKEPISVSSE QVLKFRKLNFNGEGEPEELM VDNWRPAQPLKNRQIKASFK

Data sets:
Data typeCount
13C chemical shifts1006
15N chemical shifts263
1H chemical shifts1000

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_33

Entities:

Entity 1, entity_1 260 residues - 29289.062 Da.

1   METSERHISHISTRPGLYTYRGLYLYSHIS
2   ASNGLYPROGLUHISTRPHISLYSASPPHE
3   PROILEALALYSGLYGLUARGGLNSERPRO
4   VALASPILEASPTHRHISTHRALALYSTYR
5   ASPPROSERLEULYSPROLEUSERVALSER
6   TYRASPGLNALATHRSERLEUARGILELEU
7   ASNASNGLYHISALAPHEASNVALGLUPHE
8   ASPASPSERGLNASPLYSALAVALLEULYS
9   GLYGLYPROLEUASPGLYTHRTYRARGLEU
10   ILEGLNPHEHISPHEHISTRPGLYSERLEU
11   ASPGLYGLNGLYSERGLUHISTHRVALASP
12   LYSLYSLYSTYRALAALAGLULEUHISLEU
13   VALHISTRPASNTHRLYSTYRGLYASPPHE
14   GLYLYSALAVALGLNGLNPROASPGLYLEU
15   ALAVALLEUGLYILEPHELEULYSVALGLY
16   SERALALYSPROGLYLEUGLNLYSVALVAL
17   ASPVALLEUASPSERILELYSTHRLYSGLY
18   LYSSERALAASPPHETHRASNPHEASPPRO
19   ARGGLYLEULEUPROGLUSERLEUASPTYR
20   TRPTHRTYRPROGLYSERLEUTHRTHRPRO
21   PROLEULEUGLUCYSVALTHRTRPILEVAL
22   LEULYSGLUPROILESERVALSERSERGLU
23   GLNVALLEULYSPHEARGLYSLEUASNPHE
24   ASNGLYGLUGLYGLUPROGLUGLULEUMET
25   VALASPASNTRPARGPROALAGLNPROLEU
26   LYSASNARGGLNILELYSALASERPHELYS

Entity 2, entity_2 - Zn - 65.409 Da.

1   ZN

Entity 3, entity_3 - 18.015 Da.

1   HOH

Samples:

sample_1: hCAII 13C 15N, [U-13C; U-15N], 0.5 mM; hCAII 13C 15N 2H, [U-13C; U-15N]2H, 0.5 mM; hCAII 15N, [U-100% 15N], 0.6 mM; hCAII 13C, [U-100% 13C], 0.6 mM; hCAII 1 mM

sample_2: hCAII 13C 15N, [U-100% 13C; U-100% 15N], 0.5 mM; hCAII 13C 15N 2H, [U-13C; U-15N; U-2H], 0.6 mM; hCAII 15N, [U-99% 15N], 0.5 mM; hCAII 99% 13C 15N, [U-99% 13C; U-99% 15N], 0.5 mM; hCAII 10% 13C, [U-10% 13C], 0.6 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

ARIA v2.3, Linge, O'Donoghue and Nilges - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment

TopSpin, Bruker Biospin - processing

CcpNmr Analysis, CCPN - peak picking

NMR spectrometers:

  • Bruker AvanceIII 800 MHz
  • Bruker AvanceIII 800 MHz

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