BMRB Entry 19988

Name: Solution structure of the PR domain of FOG-1
Published: 2014-10-27

Click here to enlarge.

PDB ID: 2mpl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19988
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FOG-1_PR: PWSGPEELELALQDGQRCVR ARLSLTEGLSWGPFYGSIQT RALSPEREEPGPAVTLMVDE SCWLRMLPQVLTEEAANSEI YRKDDALWCRVTKVVPSGGL LYVRLVTEPHGAPRHPVQEP VEPGGLA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	474
15N chemical shifts	109
1H chemical shifts	740

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FOG-1_PR	1

Entities:

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

1

PRO

TRP

SER

GLY

PRO

GLU

LEU

GLU

LEU

2

ALA

LEU

GLN

ASP

GLY

GLN

ARG

CYS

VAL

ARG

3

ALA

ARG

LEU

SER

LEU

THR

GLU

GLY

LEU

SER

4

TRP

GLY

PRO

PHE

TYR

GLY

SER

ILE

GLN

THR

5

ARG

ALA

LEU

SER

PRO

GLU

ARG

GLU

PRO

6

GLY

PRO

ALA

VAL

THR

LEU

MET

VAL

ASP

GLU

7

SER

CYS

TRP

LEU

ARG

MET

LEU

PRO

GLN

VAL

8

LEU

THR

GLU

ALA

ASN

SER

GLU

ILE

9

TYR

ARG

LYS

ASP

ALA

LEU

TRP

CYS

ARG

10

VAL

THR

LYS

VAL

PRO

SER

GLY

LEU

11

LEU

TYR

VAL

ARG

LEU

VAL

THR

GLU

PRO

HIS

12

GLY

ALA

PRO

ARG

HIS

PRO

VAL

GLN

GLU

PRO

13

VAL

GLU

PRO

GLY

LEU

ALA

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N_labeled	isotropic	sample_conditions_1
2D 1H-1H NOESY	unlabelled	isotropic	sample_conditions_1
3D CBCA(CO)NH	15N-13C_labeled	isotropic	sample_conditions_1
3D HNCO	15N-13C_labeled	isotropic	sample_conditions_1
3D HNCACB	15N-13C_labeled	isotropic	sample_conditions_1
3D HBHA(CO)NH	15N-13C_labeled	isotropic	sample_conditions_1
3D HN(CO)CA	15N-13C_labeled	isotropic	sample_conditions_1
3D HNCA	15N-13C_labeled	isotropic	sample_conditions_1
3D HCCH-TOCSY	15N-13C_labeled	isotropic	sample_conditions_1
3D HNHA	15N-13C_labeled	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N-13C_labeled	isotropic	sample_conditions_1
3D 1H-15N TOCSY	15N-13C_labeled	isotropic	sample_conditions_1
3D HCCH-COSY	15N-13C_labeled	isotropic	sample_conditions_1
3D HNHB	15N-13C_labeled	isotropic	sample_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