BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18265

Title: WIP C-terminal domain   PubMed: 23870269

Deposition date: 2012-02-15 Original release date: 2019-08-29

Authors: Novacek, Jiri; Haba, Noam; Shaked, Hadassa; Chill, Jordan; Zidek, Lukas; Sklenar, Vladimir

Citation: Haba, Noam; Gross, Renana; Novacek, Jiri; Shaked, Hadassa; Zidek, Lukas; Barda-Saad, Mira; Chill, Jordan. "NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein."  Biophys. J. 105, 481-493 (2013).

Assembly members:
WIPc, polymer, 114 residues, 12841.0 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):
WIPc: GSSHHHHHHVDSPRSGPRPP LPPDRPSAGAPPPPPPSTSI RNGFQDSPCEDEWESRFYFH PISDLPPPEPYVQTTKSYPS KLARNESRSSSNRRERGAPP LPPIPRLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts325
15N chemical shifts111
1H chemical shifts316

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WIPc1

Entities:

Entity 1, WIPc 114 residues - 12841.0 Da.

1   GLYSERSERHISHISHISHISHISHISVAL
2   ASPSERPROARGSERGLYPROARGPROPRO
3   LEUPROPROASPARGPROSERALAGLYALA
4   PROPROPROPROPROPROSERTHRSERILE
5   ARGASNGLYPHEGLNASPSERPROCYSGLU
6   ASPGLUTRPGLUSERARGPHETYRPHEHIS
7   PROILESERASPLEUPROPROPROGLUPRO
8   TYRVALGLNTHRTHRLYSSERTYRPROSER
9   LYSLEUALAARGASNGLUSERARGSERGLY
10   SERASNARGARGGLUARGGLYALAPROPRO
11   LEUPROPROILEPROARGLEUGLUHISHIS
12   HISHISHISHIS

Samples:

sample_1: WIPc, [U-98% 13C; U-98% 15N], 1.0 ± 0.03 mM; potassium phosphate 20 mM; sodium chloride 20 mM; beta-mercaptoethanol 10 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.06 M; pH: 5.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
CONsample_1isotropicsample_conditions_1
3D C_CANCOsample_1isotropicsample_conditions_1
3D C_CBCACONsample_1isotropicsample_conditions_1
3D C_CBCANCOsample_1isotropicsample_conditions_1
5D C_CACONCACOsample_1isotropicsample_conditions_1
5D C_NCOCANCOsample_1isotropicsample_conditions_1
4D C_HabCabCONsample_1isotropicsample_conditions_1
4D C_HabCabNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin, Goddard - collection, peak picking, processing

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 700 MHz