BMRB Entry 17467

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17467

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Title:
NMR assignment of the second B3 domain of VERNALIZATION1 from Arabidopsis thaliana
Deposition date:
2011-02-13
Original release date:
2011-03-08
Authors:
Mylne, Joshua; Mas, Caroline; Hill, Justine
Citation:

Citation: Mylne, Joshua; Mas, Caroline; Hill, Justine. "NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1."  Biomol. NMR Assignments 6, 5-8 (2012).
PubMed: 21553305

Assembly members:

Assembly members:
VRN1_B3b, polymer, 134 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: pQE-30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VRN1_B3b: RSKFYESASARKRTVTAEER ERAINAAKTFEPTNPFFRVV LRPSYLYRGCIMYLPSGFAE KYLSGISGFIKVQLAEKQWP VRCLYKAGRAKFSQGWYEFT LENNLGEGDVCVFELLRTRD FVLKVTAFRVNEYV

Data sets:
Data typeCount
13C chemical shifts514
15N chemical shifts122
1H chemical shifts718

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VRN1_B3b1

Entities:

Entity 1, VRN1_B3b 134 residues - Formula weight is not available

fragment 208-341 include the C-terminal B3 domain and an upstream region that is highly conserved in VRN1 orthologs

1   ARGSERLYSPHETYRGLUSERALASERALA
2   ARGLYSARGTHRVALTHRALAGLUGLUARG
3   GLUARGALAILEASNALAALALYSTHRPHE
4   GLUPROTHRASNPROPHEPHEARGVALVAL
5   LEUARGPROSERTYRLEUTYRARGGLYCYS
6   ILEMETTYRLEUPROSERGLYPHEALAGLU
7   LYSTYRLEUSERGLYILESERGLYPHEILE
8   LYSVALGLNLEUALAGLULYSGLNTRPPRO
9   VALARGCYSLEUTYRLYSALAGLYARGALA
10   LYSPHESERGLNGLYTRPTYRGLUPHETHR
11   LEUGLUASNASNLEUGLYGLUGLYASPVAL
12   CYSVALPHEGLULEULEUARGTHRARGASP
13   PHEVALLEULYSVALTHRALAPHEARGVAL
14   ASNGLUTYRVAL

Samples:

1_15N_VRN1: VRN1_B3b, [U-100% 15N], 0.8 mM; sodium phosphate 50 mM; NaCl 50 mM; DTT 1 mM

2_15N_13C_VRN1: VRN1_B3b, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 50 mM; NaCl 50 mM; DTT 1 mM

3_15N_13C_VRN1: VRN1_B3b, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 50 mM; NaCl 50 mM; DTT 1 mM

1_conditions: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC1_15N_VRN1isotropic1_conditions
3D HNCO2_15N_13C_VRN1isotropic1_conditions
3D HN(CA)CO2_15N_13C_VRN1isotropic1_conditions
3D CBCA(CO)NH2_15N_13C_VRN1isotropic1_conditions
3D HNCACB2_15N_13C_VRN1isotropic1_conditions
3D HNHA2_15N_13C_VRN1isotropic1_conditions
3D HBHA(CO)NH2_15N_13C_VRN1isotropic1_conditions
3D HCCH-TOCSY3_15N_13C_VRN1isotropic1_conditions
2D (HB)CB(CGCD)HG3_15N_13C_VRN1isotropic1_conditions
2D (HB)CB(CGCDCE)HE3_15N_13C_VRN1isotropic1_conditions
3D 1H-13C HMQC-NOESY-HMQC3_15N_13C_VRN1isotropic1_conditions
3D C(CO)NH2_15N_13C_VRN1isotropic1_conditions
3D H(CC))NH2_15N_13C_VRN1isotropic1_conditions

Software:

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

PIPP, Garrett - chemical shift assignment

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAB01695 BAF02186 BAH30458 BAJ34355
EMBL CDX92293 CDX95476 CDX99291 CDY18562 CDY22996
GB AAM76972 AAM76973 ABD59069 AEE76178 AKX67933
REF NP_188529 XP_002885287 XP_006299472 XP_006406545 XP_009112206
SP Q8L3W1
AlphaFold Q8L3W1

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