BMRB Entry 18522

Title:
Chemical Shift Assignments for the PICK1 PDZ domain fused to the C10 DAT ligand
Deposition date:
2012-06-14
Original release date:
2013-06-17
Authors:
Erlendsson, Simon; Teilum, Kaare
Citation:

Citation: Erlendsson, Simon; Rathje, Mette; Heidarsson, Petur; Poulsen, Flemming; Madsen, Kenneth; Teilum, Kaare; Gether, Ulrik. "Protein interacting with C-kinase 1 (PICK1) binding promiscuity relies on unconventional PSD-95/discs-large/ZO-1 homology (PDZ) binding modes for nonclass II PDZ ligand"  J. Biol. Chem. 289, 25327-25340 (2014).
PubMed: 25023278

Assembly members:

Assembly members:
entity, polymer, 232 residues, 24838.865 Da.

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX4t2

Data sets:
Data typeCount
13C chemical shifts382
15N chemical shifts106
1H chemical shifts638

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PICK1 PDZ domain fused to the C10 DAT ligand1

Entities:

Entity 1, PICK1 PDZ domain fused to the C10 DAT ligand 232 residues - 24838.865 Da.

1   GLYSERPROGLYILEPROVALPROGLYLYS
2   VALTHRLEUGLNLYSASPALAGLNASNLEU
3   ILEGLYILESERILEGLYGLYGLYALAGLN
4   TYRCYSPROCYSLEUTYRILEVALGLNVAL
5   PHEASPASNTHRPROALAALALEUASPGLY
6   THRVALALAALAGLYASPGLUILETHRGLY
7   VALASNGLYARGSERILELYSGLYLYSTHR
8   LYSVALGLUVALALALYSMETILEGLNGLU
9   VALLYSGLYGLUVALTHRILEHISTYRASN
10   LYSLEUGLNALAASPPROLYSGLNLEUGLU
11   VALLEUPHEGLNGLYPROGLNPHETHRLEU
12   ARGHISTRPLEULYSVALGLYSERPROGLY
13   ILEPROVALPROGLYLYSVALTHRLEUGLN
14   LYSASPALAGLNASNLEUILEGLYILESER
15   ILEGLYGLYGLYALAGLNTYRCYSPROCYS
16   LEUTYRILEVALGLNVALPHEASPASNTHR
17   PROALAALALEUASPGLYTHRVALALAALA
18   GLYASPGLUILETHRGLYVALASNGLYARG
19   SERILELYSGLYLYSTHRLYSVALGLUVAL
20   ALALYSMETILEGLNGLUVALLYSGLYGLU
21   VALTHRILEHISTYRASNLYSLEUGLNALA
22   ASPPROLYSGLNLEUGLUVALLEUPHEGLN
23   GLYPROGLNPHETHRLEUARGHISTRPLEU
24   LYSVAL

Samples:

backbone: TRIS 50 mM; sodium chloride 125 mM; DTT 2 mM; protein, [U-100% 13C; U-100% 15N], 600 uM; DSS 0.25 mM; sodium azide 0.01%; H2O 90%; D2O 10%

13C-HSQC-NOESY: TRIS, [U-99% 2H], 50 mM; sodium chloride 125 mM; DTT 2 mM; protein, [U-100% 13C; U-100% 15N], 600 uM; DSS 0.25 mM; sodium azide 0.01%; D2O 100%

sample_conditions_1: ionic strength: 0.175 M; pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCbackboneisotropicsample_conditions_1
2D 1H-13C HSQC13C-HSQC-NOESYisotropicsample_conditions_1
3D CBCA(CO)NHbackboneisotropicsample_conditions_1
3D HNCObackboneisotropicsample_conditions_1
3D HNCAbackboneisotropicsample_conditions_1
3D HNCACBbackboneisotropicsample_conditions_1
3D HN(CO)CAbackboneisotropicsample_conditions_1
3D HCCH-TOCSYbackboneisotropicsample_conditions_1
3D 1H-15N NOESYbackboneisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic13C-HSQC-NOESYisotropicsample_conditions_1

Software:

VNMRJ v2.2D, Varian - collection

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

ARIA, Linge, O'Donoghue and Nilges - refinement, structure solution

CING, Geerten W. Vuister , Alan Wilter Sousa da Silva , and Jurgen F. Doreleijers - validation

Molmol, Koradi, Billeter and Wuthrich - representation

Analysis, CCPN - chemical shift assignment, data analysis, peak picking, refinement

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

X-PLOR, Brunger - restraint deposition

NMR spectrometers:

  • Varian INOVA 800 MHz

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