BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 11264

Title: Solution Structure of Ras-binding Domain in Mouse AF-6 Protein

Deposition date: 2010-08-09 Original release date: 2011-08-18

Authors: Zhao, C.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Zhao, C.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of Ras-binding Domain in Mouse AF-6 Protein"  .

Assembly members:
Ras-binding domain, polymer, 116 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P040719-08

Entity Sequences (FASTA):
Ras-binding domain: GSSGSSGSGGTLRIYADSLK PNIPYKTILLSTTDTADFAV AESLEKYGLEKENPKDYCIA RVMLPPGAQHSDERGAKEII LDDDECPLQIFREWPSDKGI LVFQLKRRPPSGPSSG

Data sets:
Data typeCount
13C chemical shifts470
15N chemical shifts100
1H chemical shifts742

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ras-binding domain1

Entities:

Entity 1, Ras-binding domain 116 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYSERGLYGLY
2   THRLEUARGILETYRALAASPSERLEULYS
3   PROASNILEPROTYRLYSTHRILELEULEU
4   SERTHRTHRASPTHRALAASPPHEALAVAL
5   ALAGLUSERLEUGLULYSTYRGLYLEUGLU
6   LYSGLUASNPROLYSASPTYRCYSILEALA
7   ARGVALMETLEUPROPROGLYALAGLNHIS
8   SERASPGLUARGGLYALALYSGLUILEILE
9   LEUASPASPASPGLUCYSPROLEUGLNILE
10   PHEARGGLUTRPPROSERASPLYSGLYILE
11   LEUVALPHEGLNLEULYSARGARGPROPRO
12   SERGLYPROSERSERGLY

Samples:

sample_1: Ras-binding domain, [U-13C; U-15N], 1.28 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298.0 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.921, Kobayashi, N. - data analysis

CYANA v1.0.8, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
GB AAH14505

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