BMRB Entry 19988

Title:
Solution structure of the PR domain of FOG-1
Deposition date:
2014-05-26
Original release date:
2014-10-27
Authors:
Mackay, Joel; Clifton, Molly; Westman, Belinda; Blobel, Gerd
Citation:

Citation: Clifton, Molly; Westman, Belinda; Thong, Sock Yue; O'Connell, Mitchell; Shepherd, Nicholas; Quinlan, Kate; Crossley, Merlin; Blobel, Gerd; Mackay, Joel. "The Identification and Structure of an N-Terminal PR Domain Show that FOG1 Is a Member of the PRDM Family of Proteins"  Plos One 9, e106011-e106011 (2014).
PubMed: 25162672

Assembly members:

Assembly members:
FOG-1_PR, polymer, 127 residues, 14061.062 Da.

Natural source:

Natural source:   Common Name: House 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: pGEX-2T

Data sets:
Data typeCount
13C chemical shifts474
15N chemical shifts109
1H chemical shifts740

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FOG-1_PR1

Entities:

Entity 1, FOG-1_PR 127 residues - 14061.062 Da.

1   PROTRPSERGLYPROGLUGLULEUGLULEU
2   ALALEUGLNASPGLYGLNARGCYSVALARG
3   ALAARGLEUSERLEUTHRGLUGLYLEUSER
4   TRPGLYPROPHETYRGLYSERILEGLNTHR
5   ARGALALEUSERPROGLUARGGLUGLUPRO
6   GLYPROALAVALTHRLEUMETVALASPGLU
7   SERCYSTRPLEUARGMETLEUPROGLNVAL
8   LEUTHRGLUGLUALAALAASNSERGLUILE
9   TYRARGLYSASPASPALALEUTRPCYSARG
10   VALTHRLYSVALVALPROSERGLYGLYLEU
11   LEUTYRVALARGLEUVALTHRGLUPROHIS
12   GLYALAPROARGHISPROVALGLNGLUPRO
13   VALGLUPROGLYGLYLEUALA

Samples:

unlabelled: FOG-1 PR 0.5-1 mM; sodium phosphate 20 mM; DSS 0.01 mM

15N_labeled: FOG-1 PR, [U-100% 15N], 0.5-1 mM; sodium phosphate 20 mM; DSS 0.01 mM

15N-13C_labeled: FOG-1 PR, [U-100% 13C; U-100% 15N], 0.5-1 mM; sodium phosphate 20 mM; DSS 0.01 mM

sample_conditions_1: ionic strength: 0.06 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_labeledisotropicsample_conditions_1
2D 1H-1H NOESYunlabelledisotropicsample_conditions_1
3D CBCA(CO)NH15N-13C_labeledisotropicsample_conditions_1
3D HNCO15N-13C_labeledisotropicsample_conditions_1
3D HNCACB15N-13C_labeledisotropicsample_conditions_1
3D HBHA(CO)NH15N-13C_labeledisotropicsample_conditions_1
3D HN(CO)CA15N-13C_labeledisotropicsample_conditions_1
3D HNCA15N-13C_labeledisotropicsample_conditions_1
3D HCCH-TOCSY15N-13C_labeledisotropicsample_conditions_1
3D HNHA15N-13C_labeledisotropicsample_conditions_1
3D 1H-15N NOESY15N-13C_labeledisotropicsample_conditions_1
3D 1H-15N TOCSY15N-13C_labeledisotropicsample_conditions_1
3D HCCH-COSY15N-13C_labeledisotropicsample_conditions_1
3D HNHB15N-13C_labeledisotropicsample_conditions_1

Software:

TOPSPIN v3, Bruker Biospin - processing

SPARKY v3, Goddard - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

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