BMRB Entry 34347

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34347
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Assessment of a large enzyme-drug complex by proton-detected solid-state NMR without deuteration
Deposition date:
2019-01-07
Original release date:
2019-12-06
Authors:
Vasa, S.
Citation:

Citation: Vasa, S.; Singh, H.; Grohe, K.; Linser, R.. "Assessment of a Large Enzyme-Drug Complex by Proton-Detected Solid-State NMR Spectroscopy without Deuteration."  Angew. Chem. Int. Ed. Engl. 58, 5758-5762 (2019).
PubMed: 30688395

Assembly members:

Assembly members:
entity_1, polymer, 260 residues, 29289.062 Da.
entity_ZN, non-polymer, 65.409 Da.
entity_AZM, non-polymer, 222.245 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli K-12

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts934
15N chemical shifts237
1H chemical shifts1280

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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 - C4 H6 N4 O3 S2 - 222.245 Da.

1   AZM

Samples:

sample_1: hCAII, [U-99% 13C; U-99% 15N], 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N RFDRsample_1isotropicsample_conditions_1
3D 1H-13C RFDRsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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