BMRB Entry 16442

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16442
MolProbity Validation Chart

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Title:
Solution structure of At3g03773.1 protein from Arabidopsis thaliana
Deposition date:
2009-08-05
Original release date:
2010-09-03
Authors:
Sahu, Sarata; Singh, Shanteri; Tonelli, Marco; Markley, John
Citation:

Citation: Sahu, Sarata; Singh, Shanteri; Tonelli, Marco; Markley, John. "Solution structure of At3g03773.1 protein from Arabidopsis thaliana"  Structure ., .-..

Assembly members:

Assembly members:
At3g03773.1, polymer, 150 residues, 17342.326 Da.

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: pVP16

Entity Sequences (FASTA):

Entity Sequences (FASTA):
At3g03773.1: SSRNPEVLWAQRSDKVYLTV ALPDAKDISVKCEPQGLFSF SALGAQGERFEFSLELYGKI MTEYRKNVGLRNIIFSIQKE ERSWWTRLLKSEEKPAPYIK VDWNKWCDEDEEVNSETASD DESAFVNQDSESSDDDGLLY LPDLEKARNK

Data sets:
Data typeCount
13C chemical shifts536
15N chemical shifts140
1H chemical shifts1052

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1At3g03773.11

Entities:

Entity 1, At3g03773.1 150 residues - 17342.326 Da.

1   SERSERARGASNPROGLUVALLEUTRPALA
2   GLNARGSERASPLYSVALTYRLEUTHRVAL
3   ALALEUPROASPALALYSASPILESERVAL
4   LYSCYSGLUPROGLNGLYLEUPHESERPHE
5   SERALALEUGLYALAGLNGLYGLUARGPHE
6   GLUPHESERLEUGLULEUTYRGLYLYSILE
7   METTHRGLUTYRARGLYSASNVALGLYLEU
8   ARGASNILEILEPHESERILEGLNLYSGLU
9   GLUARGSERTRPTRPTHRARGLEULEULYS
10   SERGLUGLULYSPROALAPROTYRILELYS
11   VALASPTRPASNLYSTRPCYSASPGLUASP
12   GLUGLUVALASNSERGLUTHRALASERASP
13   ASPGLUSERALAPHEVALASNGLNASPSER
14   GLUSERSERASPASPASPGLYLEULEUTYR
15   LEUPROASPLEUGLULYSALAARGASNLYS

Samples:

sample_1: entity, [U-13C; U-15N], 1 ± 0.1 mM; H2O 93%; H2O 7%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

XEASY, Bartels et al. - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAT41786 AAT68743 AAT68744 AAT70471 AAX55169
REF NP_001154589 NP_683525
SP Q6ID70
AlphaFold Q6ID70

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