BMRB Entry 25684

Title:
SOLUTION STRUCTURE OF THE LIPID DROPLET ANCHORING PEPTIDE OF CGI-58 BOUND TO DPC MICELLES
Deposition date:
2015-07-01
Original release date:
2015-09-14
Authors:
Boeszoermenyi, Andras; Arthanari, Haribabu; Wagner, Gerhard; Nagy, Harald; Zangger, Klaus; Lindermuth, Hanna; Oberer, Monika
Citation:

Citation: Boeszoermenyi, Andras; Arthanari, Haribabu; Wagner, Gerhard; Nagy, Harald; Zangger, Klaus; Lindermuth, Hanna; Oberer, Monika. "Structure of a CGI-58 Motif Provides the Molecular Basis of Lipid Droplet Anchoring"  J. Biol. Chem. 290, 26361-26372 (2015).
PubMed: 26350461

Assembly members:

Assembly members:
wr10_43, polymer, 39 residues, 3976.3072 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: pSumo

Entity Sequences (FASTA):

Entity Sequences (FASTA):
wr10_43: GAMGSVDSADAGGGSGWLTG WLPTWCPTSTSHLKEAEEK

Data typeCount
13C chemical shifts216
15N chemical shifts71
1H chemical shifts662

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1wr10 431

Entities:

Entity 1, wr10 43 39 residues - 3976.3072 Da.

1   GLYALAMETGLYSERVALASPSERALAASP
2   ALAGLYGLYGLYSERGLYTRPLEUTHRGLY
3   TRPLEUPROTHRTRPCYSPROTHRSERTHR
4   SERHISLEULYSGLUALAGLUGLULYS

Samples:

sample_new_1: wr10_43, [U-13C; U-15N], 1 mM; NaPP 20 mM; NaCl 50 mM; EDTA 1 mM; DTT 5 mM

wr10_43_1: wr10_43, [U-13C; U-15N], 1 mM; NaPP 20 mM; NaCl 50 mM; EDTA 1 mM; DTT 5 mM

wr10_43_D2O: wr10_43, [U-13C; U-15N], 1 mM; NaPP 20 mM; NaCl 50 mM; EDTA 1 mM; DTT 5 mM

wr18_39: wr10_43, [U-13C; U-15N], 1 mM; NaPP 20 mM; NaCl 50 mM; EDTA 1 mM; DTT 5 mM

1: ionic strength: 70.000 mM; pH: 6.000; pressure: 1.000 atm; temperature: 310.000 K

2: ionic strength: 70.000 mM; pH: 6.000; pressure: 1.000 atm; temperature: 303.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQCwr10_43_1isotropic1
HNCACB (H[N[ca[CB]]])wr10_43_1isotropic1
3D HNCAwr10_43_1isotropic1
3D 1H-15N NOESYwr10_43_1isotropic1
HNCACO (H[N[ca[CO]]])wr10_43_1isotropic1
HCCONH (HccoNH)wr10_43_1isotropic1
CCONH (hC_cacoNH.relayed)wr10_43_1isotropic1
3D HCCH-TOCSYwr10_43_1isotropic1
2D 1H-13C HSQC/HMQCwr10_43_D2Oisotropic1
3D 1H-13C NOESYwr10_43_D2Oisotropic1
2D 1H-1H NOESYwr18_39isotropic2
2D 1H-15N HSQC/HMQCwr10_43_1isotropic1
2D 1H-1H TOCSYwr10_43_1isotropic2
HNCAsample_new_1solution1
HNCACBsample_new_1solution1
HNCACOsample_new_1solution1
HSQCsample_new_1solution1

Software:

CcpNmr_Analysis v2.4, CCPN - Spectrum analysis, peak integration, distance restraint calibration

Cyana v3.0, GUNTERT - Simulated annealing

TALOS+ v1, Shen, Cornilescu, Delaglio. and Bax - Prediction of dihedral angle restraints

nmrDraw vany, F. Delaglio - Spectrum display

nmrPipe vany, F. Delaglio - Spectrum processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Varian dd2 700 MHz
  • Bruker Avance 750 MHz
  • Varian UnityInova 500 MHz
  • Bruker Avance 900 MHz
  • Bruker DD2 600 MHz

Related Database Links:

PDB
UNP ABHD5_MOUSE
AlphaFold Q9CTY3