BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15290

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's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-4T1

Entity Sequences (FASTA):
Cog2p: GSDSLIRDLSGLSQKMVQTL LEQIRSNYDDYLTFSNTYTD EENETLINLEKTQSDLQKFM TQLDHLIKDDISNTQEIIKD VLEYLKKLDEIYGSLRNHSQ LTEALSLGKRLSKSLHEMCG IEPLEEEICSGLIEQLYKLI TASRRILESCADSNSPYIHH LRNDYQDLLQEFQISLKILT EKCLENPSSLQNLSLTLVSI IKTA

Data sets:
Data typeCount
13C chemical shifts846
15N chemical shifts205
1H chemical shifts1395

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Cog2p monomer1

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   GLYSERASPSERLEUILEARGASPLEUSER
2   GLYLEUSERGLNLYSMETVALGLNTHRLEU
3   LEUGLUGLNILEARGSERASNTYRASPASP
4   TYRLEUTHRPHESERASNTHRTYRTHRASP
5   GLUGLUASNGLUTHRLEUILEASNLEUGLU
6   LYSTHRGLNSERASPLEUGLNLYSPHEMET
7   THRGLNLEUASPHISLEUILELYSASPASP
8   ILESERASNTHRGLNGLUILEILELYSASP
9   VALLEUGLUTYRLEULYSLYSLEUASPGLU
10   ILETYRGLYSERLEUARGASNHISSERGLN
11   LEUTHRGLUALALEUSERLEUGLYLYSARG
12   LEUSERLYSSERLEUHISGLUMETCYSGLY
13   ILEGLUPROLEUGLUGLUGLUILECYSSER
14   GLYLEUILEGLUGLNLEUTYRLYSLEUILE
15   THRALASERARGARGILELEUGLUSERCYS
16   ALAASPSERASNSERPROTYRILEHISHIS
17   LEUARGASNASPTYRGLNASPLEULEUGLN
18   GLUPHEGLNILESERLEULYSILELEUTHR
19   GLULYSCYSLEUGLUASNPROSERSERLEU
20   GLNASNLEUSERLEUTHRLEUVALSERILE
21   ILELYSTHRALA

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:

NameSampleSample stateSample conditions
3D HNCOH2O_Sampleisotropicsample_conditions_1
3D HNCACBH2O_Sampleisotropicsample_conditions_1
3D CBCA(CO)NHH2O_Sampleisotropicsample_conditions_1
2D DQF-COSYD2O_Sampleisotropicsample_conditions_1
2D 1H-15N HSQCH2O_Sampleisotropicsample_conditions_1
3D HCCH-TOCSYH2O_Sampleisotropicsample_conditions_1
3D C(CO)NHH2O_Sampleisotropicsample_conditions_1
3D 1H-15N NOESYH2O_Sampleisotropicsample_conditions_1
3D 1H-13C NOESYH2O_Sampleisotropicsample_conditions_1
2D 1H-13C CT-HSQC10%_13Cisotropicsample_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
AlphaFold P53271

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