BMRB Entry 11540

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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/BMR11540
MolProbity Validation Chart

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Title:
Solution structure of esf3
Deposition date:
2013-11-05
Original release date:
2014-04-22
Authors:
Umetsu, Yoshitaka; Mori, Masashi; Ohki, Shinya
Citation:

Citation: Costa, Liliana; Marshall, Eleanor; Tesfaye, Mesfin; Silverstein, Kevin; Mori, Masashi; Umetsu, Yoshitaka; Otterbach, Sophie; Papareddy, Ranjith; Dickinson, Hugh; Boutiller, Kim; VandenBosch, Kathryn; Ohki, Shinya; Gutierrez-Marcos, Jose. "Central cell-derived peptides regulate early embryo patterning in flowering plants"  Science 344, 168-172 (2014).
PubMed: 24723605

Assembly members:

Assembly members:
entity, polymer, 70 residues, 7976.471 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: TOMATO MOSAIC VIRUS   Vector: PBICER8-C0.3-HUIFN-G-SRZ

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GPEKMEVKEIGRSSKIILPA CMHETCSGGFSLKNDCWCCL RLKTKQARCWKEKEFPNAKE LCFANCPPLE

Data sets:
Data typeCount
13C chemical shifts177
15N chemical shifts68
1H chemical shifts421

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 70 residues - 7976.471 Da.

1   GLYPROGLULYSMETGLUVALLYSGLUILE
2   GLYARGSERSERLYSILEILELEUPROALA
3   CYSMETHISGLUTHRCYSSERGLYGLYPHE
4   SERLEULYSASNASPCYSTRPCYSCYSLEU
5   ARGLEULYSTHRLYSGLNALAARGCYSTRP
6   LYSGLULYSGLUPHEPROASNALALYSGLU
7   LEUCYSPHEALAASNCYSPROPROLEUGLU

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 50 mM; potassium chloride 50 mM; H2O 90%; D2O 10%

sample_2: entity, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 50 mM; potassium chloride 50 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 5.8; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AEE28633
REF NP_001077509
SP A8MQA5
AlphaFold A8MQA5

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