BMRB Entry 16293

Title:
Solution structure of CA150 FF1 domain and FF1-FF2 interdomain linker
Deposition date:
2009-05-08
Original release date:
2009-09-04
Authors:
Murphy, James; Hansen, D. Flemming; Wiesner, Silke; Muhandiram, D. Ranjith; Borg, Mikael; Smith, Matthew; Sicheri, Frank; Kay, Lewis; Forman-Kay, Julie; Pawson, Tony
Citation:

Citation: Murphy, James; Hansen, D. Flemming; Wiesner, Silke; Muhandiram, D. Ranjith; Borg, Mikael; Smith, Matthew; Sicheri, Frank; Kay, Lewis; Forman-Kay, Julie; Pawson, Tony. "Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays."  J. Mol. Biol. 393, 409-424 (2009).
PubMed: 19715701

Assembly members:

Assembly members:
CA150_FF1+linker, polymer, 71 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts251
15N chemical shifts78
1H chemical shifts941

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CA150 FF1+linker1

Entities:

Entity 1, CA150 FF1+linker 71 residues - Formula weight is not available

First 5 residues, GAMGS, arise from a cloning artifact. Remainder corresponds to residues 618-683 of murine CA150

1   GLYALAMETGLYSERLEUGLUALAARGMET
2   LYSGLNPHELYSASPMETLEULEUGLUARG
3   GLYVALSERALAPHESERTHRTRPGLULYS
4   GLULEUHISLYSILEVALPHEASPPROARG
5   TYRLEULEULEUASNPROLYSGLUARGLYS
6   GLNVALPHEASPGLNTYRVALLYSTHRARG
7   ALAGLUGLUGLUARGARGGLULYSLYSASN
8   LYS

Samples:

sample_1: CA150_FF1+linker, [U-99% 13C; U-99% 15N], 1.0 – 1.7 mM; H20 95%; D20 5%

sample_conditions_1: ionic strength: 0.137 M; pH: 6.5; pressure: 1.0 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

ARIA v1.1, Dr. Michael Nilges, Institut Pasteur - Automated NOE assignment, NMR structure calculation

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
GB EDL10032