BMRB Entry 16558

Title:
MAGI-1 PDZ1
Deposition date:
2009-10-16
Original release date:
2012-05-09
Authors:
Charbonier, Sebastian; Nomine, Yves; Ramirez, Juan; Luck, Katja; Stote, Roland; Trave, Gilles; Kieffer, Bruno; Atkinson, Robert
Citation:

Citation: Charbonier, Sebastian; Nomine, Yves; Ramirez, Juan; Luck, Katja; Chapelle, Anne; Stote, Roland; Trave, Gilles; Kieffer, Bruno; Atkinson, Robert. "The Structural and Dynamic Response of MAGI-1 PDZ1 with Noncanonical Domain Boundaries to the Binding of Human Papillomavirus E6"  J. Mol. Biol. 406, 745-763 (2011).
PubMed: 21238461

Assembly members:

Assembly members:
MAGI-1_PDZ1, polymer, 129 residues, 13871.942 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-41

Data sets:
Data typeCount
13C chemical shifts555
15N chemical shifts125
1H chemical shifts889

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MAGI-1 PDZ11

Entities:

Entity 1, MAGI-1 PDZ1 129 residues - 13871.942 Da.

1   GLYALAMETGLYLYSPROPHEPHETHRARG
2   ASNPROSERGLULEULYSGLYLYSPHEILE
3   HISTHRLYSLEUARGLYSSERSERARGGLY
4   PHEGLYPHETHRVALVALGLYGLYASPGLU
5   PROASPGLUPHELEUGLNILELYSSERLEU
6   VALLEUASPGLYPROALAALALEUASPGLY
7   LYSMETGLUTHRGLYASPVALILEVALSER
8   VALASNASPTHRCYSVALLEUGLYHISTHR
9   HISALAGLNVALVALLYSILEPHEGLNSER
10   ILEPROILEGLYALASERVALASPLEUGLU
11   LEUCYSARGGLYTYRPROLEUPROPHEASP
12   PROASPASPPROASNTHRSERLEUVALTHR
13   SERVALALAILELEUASPLYSGLUPRO

Samples:

Unlabelled: MAGI-1 PDZ10.2 – 0.6 mM; sodium phosphate0.02 – 0.10 mM; sodium chloride 50 mM; DTT 2 mM; H2O 90%; D2O 10%

15N: MAGI-1 PDZ1, [U-15N], 0.2 – 0.6 mM; sodium phosphate0.02 – 0.10 mM; sodium chloride 50 mM; DTT 2 mM; H2O 90%; D2O 10%

13C-15N: MAGI-1 PDZ1, [U-100% 13C; U-100% 15N], 0.2 – 0.6 mM; sodium phosphate0.02 – 0.10 mM; sodium chloride 50 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
3D HN(CO)CA13C-15Nisotropicsample_conditions_1
3D HNCA13C-15Nisotropicsample_conditions_1
3D HN(CO)CACB13C-15Nisotropicsample_conditions_1
3D HNCACB13C-15Nisotropicsample_conditions_1
3D HNCO13C-15Nisotropicsample_conditions_1
3D HCCH-TOCSY13C-15Nisotropicsample_conditions_1
3D HCCH-COSY13C-15Nisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
3D 1H-15N TOCSY15Nisotropicsample_conditions_1
3D 1H-13C NOESY15Nisotropicsample_conditions_1
2D 1H-1H TOCSYUnlabelledisotropicsample_conditions_1
2D 1H-1H NOESYUnlabelledisotropicsample_conditions_1
2D 15N T115Nisotropicsample_conditions_1
2D 15N T215Nisotropicsample_conditions_1
2D 1H-15N NOE15Nisotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

XEASY vCARA, Bartels et al. - chemical shift assignment

ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 16559
PDB
REF XP_006108887

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