BMRB Entry 15290
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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/BMR15290
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Title: Solution structure of Saccharomyces cerevisiae conserved oligomeric Golgi subunit 2 protein (Cog2p) PubMed: 17565980
Deposition date: 2007-06-06 Original release date: 2007-07-02
Authors: Cavanaugh, Lorraine; Chen, Xiaocheng; Pelczer, Istvan; Rizo, Josep; Hughson, Frederick
Citation: Cavanaugh, Lorraine; Chen, Xiaocheng; Richardson, Brian; Ungar, Daniel; Pelczer, Istvan; Rizo, Josep; Hughson, Frederick. "Structural analysis of Conserved Oligomeric Golgi complex subunit 2" J. Biol. Chem. 282, 23418-23426 (2007).
Assembly members:
Cog2p, polymer, 204 residues, 23454.13 Da.
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Cog2p: GSDSLIRDLSGLSQKMVQTL
LEQIRSNYDDYLTFSNTYTD
EENETLINLEKTQSDLQKFM
TQLDHLIKDDISNTQEIIKD
VLEYLKKLDEIYGSLRNHSQ
LTEALSLGKRLSKSLHEMCG
IEPLEEEICSGLIEQLYKLI
TASRRILESCADSNSPYIHH
LRNDYQDLLQEFQISLKILT
EKCLENPSSLQNLSLTLVSI
IKTA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 846 |
| 15N chemical shifts | 205 |
| 1H chemical shifts | 1395 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Cog2p monomer | 1 |
Entities:
Entity 1, Cog2p monomer 204 residues - 23454.13 Da.
Initial GS in sequence is remains of thrombin cleavage site. D3 is amino acid 61 in the native protein sequence.
| 1 | GLY | SER | ASP | SER | LEU | ILE | ARG | ASP | LEU | SER | ||||
| 2 | GLY | LEU | SER | GLN | LYS | MET | VAL | GLN | THR | LEU | ||||
| 3 | LEU | GLU | GLN | ILE | ARG | SER | ASN | TYR | ASP | ASP | ||||
| 4 | TYR | LEU | THR | PHE | SER | ASN | THR | TYR | THR | ASP | ||||
| 5 | GLU | GLU | ASN | GLU | THR | LEU | ILE | ASN | LEU | GLU | ||||
| 6 | LYS | THR | GLN | SER | ASP | LEU | GLN | LYS | PHE | MET | ||||
| 7 | THR | GLN | LEU | ASP | HIS | LEU | ILE | LYS | ASP | ASP | ||||
| 8 | ILE | SER | ASN | THR | GLN | GLU | ILE | ILE | LYS | ASP | ||||
| 9 | VAL | LEU | GLU | TYR | LEU | LYS | LYS | LEU | ASP | GLU | ||||
| 10 | ILE | TYR | GLY | SER | LEU | ARG | ASN | HIS | SER | GLN | ||||
| 11 | LEU | THR | GLU | ALA | LEU | SER | LEU | GLY | LYS | ARG | ||||
| 12 | LEU | SER | LYS | SER | LEU | HIS | GLU | MET | CYS | GLY | ||||
| 13 | ILE | GLU | PRO | LEU | GLU | GLU | GLU | ILE | CYS | SER | ||||
| 14 | GLY | LEU | ILE | GLU | GLN | LEU | TYR | LYS | LEU | ILE | ||||
| 15 | THR | ALA | SER | ARG | ARG | ILE | LEU | GLU | SER | CYS | ||||
| 16 | ALA | ASP | SER | ASN | SER | PRO | TYR | ILE | HIS | HIS | ||||
| 17 | LEU | ARG | ASN | ASP | TYR | GLN | ASP | LEU | LEU | GLN | ||||
| 18 | GLU | PHE | GLN | ILE | SER | LEU | LYS | ILE | LEU | THR | ||||
| 19 | GLU | LYS | CYS | LEU | GLU | ASN | PRO | SER | SER | LEU | ||||
| 20 | GLN | ASN | LEU | SER | LEU | THR | LEU | VAL | SER | ILE | ||||
| 21 | ILE | LYS | THR | ALA |
Samples:
H2O_Sample: Cog2p, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; TRIS 3 ± 0.05 mM; EDTA 50 ± 0.05 uM; sodium chloride 10 ± 0.05 mM; sodium azide 0.0025%
D2O_Sample: Cog2p, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; TRIS 3 ± 0.05 mM; EDTA 50 ± 0.05 uM; sodium chloride 10 ± 0.05 mM; sodium azide 0.0025%
10%_13C: Cog2p, [U-10% 13C; U-100% 15N], 1 ± 0.05 mM; TRIS 3 ± 0.05 mM; EDTA 50 ± 0.05 uM; sodium chloride 10 ± 0.05 mM; sodium azide 0.0025 ± 0.05 %
sample_conditions_1: ionic strength: 0.01 M; pH: 7; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | H2O_Sample | isotropic | sample_conditions_1 |
| 3D HNCACB | H2O_Sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | H2O_Sample | isotropic | sample_conditions_1 |
| 2D DQF-COSY | D2O_Sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | H2O_Sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | H2O_Sample | isotropic | sample_conditions_1 |
| 3D C(CO)NH | H2O_Sample | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | H2O_Sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | H2O_Sample | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC | 10%_13C | isotropic | sample_conditions_1 |
Software:
CNS v1.1, A Brunger, P Adams, M Clore, P Gros, M Nilges and R Read - refinement, structure solution
NMRPipe, F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax - processing
AQUA, T Rullmann, JF Doreleijers and R Kaptein - refinement
NMRView, B Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
TALOS, G Cornilescu, F Delaglio and A Bax - geometry optimization
xwinnmr, Bruker Biospin - collection
ProcheckNMR, RA Laskowski and M MacArthur - refinement
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | GAA23495 |
| EMBL | CAA58155 CAA97130 CAY79877 |
| GB | AJP38895 AJR76215 AJR76714 AJR77212 AJR77712 |
| REF | NP_011635 |
| SP | P53271 |
| TPG | DAA08212 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts