BMRB Entry 15547
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15547
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Title: Solution structure of ubiquitin domain N-terminal to S27a ribosome subunit from Giardia lamblia PubMed: 17599068
Deposition date: 2007-11-07 Original release date: 2008-11-03
Authors: Catic, Andre; Sun, Zhen-Yu; Ratner, Daniel; Misaghi, Shahram; Spooner, Eric; Samuelson, John; Wagner, Gerhard; Ploegh, Hidde
Citation: Catic, Andre; Sun, Zhen-Yu; Ratner, Daniel; Misaghi, Shahram; Spooner, Eric; Samuelson, John; Wagner, Gerhard; Ploegh, Hidde. "Sequence and structure evolved separately in a ribosomal ubiquitin variant" EMBO J. 26, 3474-3483 (2007).
Assembly members:
GlUb(S27a), polymer, 69 residues, 7307.402 Da.
Natural source: Common Name: Giardia intestinalis Taxonomy ID: 5741 Superkingdom: Eukaryota Kingdom: not available Genus/species: Giardia lamblia
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
GlUb(S27a): MLVIVRLQDQTLPFELPAGA
RASQLSNLLSSSGMAFSLHT
QGRVLSEAAELNDKMVIDAF
VPADGAGLE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 265 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 456 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GlUb(S27a) | 1 |
Entities:
Entity 1, GlUb(S27a) 69 residues - 7307.402 Da.
two C-terminal residues are from cloning artifact
| 1 | MET | LEU | VAL | ILE | VAL | ARG | LEU | GLN | ASP | GLN | ||||
| 2 | THR | LEU | PRO | PHE | GLU | LEU | PRO | ALA | GLY | ALA | ||||
| 3 | ARG | ALA | SER | GLN | LEU | SER | ASN | LEU | LEU | SER | ||||
| 4 | SER | SER | GLY | MET | ALA | PHE | SER | LEU | HIS | THR | ||||
| 5 | GLN | GLY | ARG | VAL | LEU | SER | GLU | ALA | ALA | GLU | ||||
| 6 | LEU | ASN | ASP | LYS | MET | VAL | ILE | ASP | ALA | PHE | ||||
| 7 | VAL | PRO | ALA | ASP | GLY | ALA | GLY | LEU | GLU |
Samples:
sample_1: GlUb(S27a), [U-99% 13C; U-99% 15N], 1 mM; potassium phosphate 10 mM; sodium chloride 100 mM; D2O 10%; H20 90%
sample_2: GlUb(S27a) 1 mM; potassium phosphate 10 mM; sodium chloride 100 mM; D2O 100%
sample_3: GlUb(S27a), [U-10% 13C], 1 mM; potassium phosphate 10 mM; sodium chloride 100 mM; D2O 100%
sample_conditions_1: ionic strength: 100 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
Software:
PROSA v3.7, Guntert - processing
CARA v1.8.2, Keller and Wuthrich - data analysis
RNMRTK v3, Stern and Hoch - processing
TALOS v2003.027.13.05, Cornilescu, Delaglio and Bax - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 750 MHz
- Varian INOVA 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts