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 16710

Title: Backbone and C-beta chemical shifts of Spider Roll, NESG target OR24   PubMed: 20460129

Deposition date: 2010-02-05 Original release date: 2010-05-18

Authors: Wu, Yibing; Jha, Ramesh; Kuhlman, Brian; Szyperski, Thomas

Citation: Jha, Ramesh; Leaver-Fay, Andrew; Yin, Shuangye; Wu, Yibing; Butterfoss, Glenn; Szyperski, Thomas; Dokholyan, Nikolay; Kuhlman, Brian. "Computational design of a PAK1 binding protein."  J. Mol. Biol. 400, 257-270 (2010).

Assembly members:
Spider_Roll, polymer, 61 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
Spider_Roll: HRQALGERLYPRVQCMQPAF ASKITEMLLELSPAQLENLL ASEDSLRDQVRYAMAGIAFH G

Data sets:
Data typeCount
13C chemical shifts151
15N chemical shifts49
1H chemical shifts49

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1spider roll1

Entities:

Entity 1, spider roll 61 residues - Formula weight is not available

1   HISARGGLNALALEUGLYGLUARGLEUTYR
2   PROARGVALGLNCYSMETGLNPROALAPHE
3   ALASERLYSILETHRGLUMETLEULEUGLU
4   LEUSERPROALAGLNLEUGLUASNLEULEU
5   ALASERGLUASPSERLEUARGASPGLNVAL
6   ARGTYRALAMETALAGLYILEALAPHEHIS
7   GLY

Samples:

sample_1: Spider Roll 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.07 M; pH: 7; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data prcessing

XEASY, Bartels et al. - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

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