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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NMR-STAR v3 text file.
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Title: Solution structure of esf3 PubMed: 24723605
Deposition date: 2013-11-05 Original release date: 2014-04-22
Authors: Umetsu, Yoshitaka; Mori, Masashi; Ohki, Shinya
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).
Assembly members:
entity, polymer, 70 residues, 7976.471 Da.
Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: recombinant technology Host organism: TOMATO MOSAIC VIRUS Vector: PBICER8-C0.3-HUIFN-G-SRZ
Entity Sequences (FASTA):
entity: GPEKMEVKEIGRSSKIILPA
CMHETCSGGFSLKNDCWCCL
RLKTKQARCWKEKEFPNAKE
LCFANCPPLE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 177 |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 421 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 70 residues - 7976.471 Da.
| 1 | GLY | PRO | GLU | LYS | MET | GLU | VAL | LYS | GLU | ILE | |
| 2 | GLY | ARG | SER | SER | LYS | ILE | ILE | LEU | PRO | ALA | |
| 3 | CYS | MET | HIS | GLU | THR | CYS | SER | GLY | GLY | PHE | |
| 4 | SER | LEU | LYS | ASN | ASP | CYS | TRP | CYS | CYS | LEU | |
| 5 | ARG | LEU | LYS | THR | LYS | GLN | ALA | ARG | CYS | TRP | |
| 6 | LYS | GLU | LYS | GLU | PHE | PRO | ASN | ALA | LYS | GLU | |
| 7 | LEU | CYS | PHE | ALA | ASN | CYS | PRO | PRO | LEU | GLU |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_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
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts