BMRB Entry 50205

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50205

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Title:
Solution NMR resonance assignments for segmentally labelled C-terminal fragment of plant villin-4 protein
Deposition date:
2020-02-25
Original release date:
2020-03-20
Authors:
Boyko, Kristina; Smirnov, Serge
Citation:

Citation: Boyko, Kristina; Rosenkranz, Erin; Smith, Derrick; Miears, Heather; Oueld es cheikh, Melissa; Lund, Micah; Young, Jeffery; Reardon, Patrick; Okon, Mark; Smirnov, Serge; Antos, John. "Sortase-mediated segmental labeling: A method for segmental assignment of intrinsically disordered regions in proteins"  PLOS One 16, e0258531-e0258531 (2021).
PubMed: 34710113

Assembly members:

Assembly members:
entity_1, polymer, 183 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-24a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PSVQEVEKLLHVLDRNGDGK VSAEELKAFADDSKCPLDSN KIKAFIKEHDKNKDGKLDLK ELVSILSSGTSENLYFQGEE KKENDKEEGSMSSRIESLTI QEDAKEGVEDEEDGLPETGG LPAHPYDRLKTTSTDPVSDI DVTRREAYLSSEEFKEKFGM TKEAFYKLPKWKQNKFKMAV QLF

Data sets:
Data typeCount
13C chemical shifts284
15N chemical shifts97
1H chemical shifts97

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FH8-IDR-HP631

Entities:

Entity 1, FH8-IDR-HP63 183 residues - Formula weight is not available

1   PROSERVALGLNGLUVALGLULYSLEULEU
2   HISVALLEUASPARGASNGLYASPGLYLYS
3   VALSERALAGLUGLULEULYSALAPHEALA
4   ASPASPSERLYSCYSPROLEUASPSERASN
5   LYSILELYSALAPHEILELYSGLUHISASP
6   LYSASNLYSASPGLYLYSLEUASPLEULYS
7   GLULEUVALSERILELEUSERSERGLYTHR
8   SERGLUASNLEUTYRPHEGLNGLYGLUGLU
9   LYSLYSGLUASNASPLYSGLUGLUGLYSER
10   METSERSERARGILEGLUSERLEUTHRILE
11   GLNGLUASPALALYSGLUGLYVALGLUASP
12   GLUGLUASPGLYLEUPROGLUTHRGLYGLY
13   LEUPROALAHISPROTYRASPARGLEULYS
14   THRTHRSERTHRASPPROVALSERASPILE
15   ASPVALTHRARGARGGLUALATYRLEUSER
16   SERGLUGLUPHELYSGLULYSPHEGLYMET
17   THRLYSGLUALAPHETYRLYSLEUPROLYS
18   TRPLYSGLNASNLYSPHELYSMETALAVAL
19   GLNLEUPHE

Samples:

sample_1: FH8-IDR-HP63, [U-99% 13C; U-99% 15N], 0.10 mM; NaCl 50 mM; NaN3 0.2 % w/v; EDTA 0.5 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 288 K

sample_conditions_2: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

I-PINE - Automated NMR resonance assignment

NMRViewJ v9.0.0-b77 - 2D/3D NMR spectra visualization and resonance analysis

NMRPipe v8.9 - NMR data processing and Bruker-to-NMRViewJ conversion

NMR spectrometers:

  • Bruker Avance III HD 11.7 Tesla, 500 MHz 1H frequency MHz
  • Bruker Avance III 14.1 Tesla, 600 MHz 1H frequency MHz

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