BMRB Entry 5180

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PDB ID: 1hbw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5180
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution nmr structure of the dimerization domain of the yeast transcriptional activator Gal4 (residues 50-106)

Deposition date:

2001-10-16

Original release date:

2001-11-12

Authors:

Hidalgo, P.; Ansari, A.; Schmidt, P.; Hare, B.; Simkovic, N.; Farrell, S.; Shin, E.; Ptashne, M.; Wagner, G.

Citation:

Citation: Hidalgo, Patricia; Ansari, A.; Schmidt, P.; Hare, B.; Simkovic, N.; Farrell, S.; Shin, E.; Ptashne, M.; Wagner, G.. "Recruitment of the transcriptional machinery through GAL11P:structure and interactions of the GAL4 dimerization domain" Genes Dev. 15, 1007-1020 (2001).
PubMed: 11316794

Assembly members:

Assembly members:
GAL4 dimerization domain, polymer, 57 residues, 6812 Da.

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GAL4 dimerization domain: TRAHLTEVESRLERLEQLFL LIFPREDLDMILKMDSLRDI EALLTGLFVQDNVNKDA

Data sets:

assigned_chemical_shifts
- chem_shift_set_1

Data type	Count
13C chemical shifts	34
15N chemical shifts	39
1H chemical shifts	150

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Gal4 subunit A, monomer	1
2	Gal4 subunit B, monomer	1

Entities:

Entity 1, Gal4 subunit A, monomer 57 residues - 6812 Da.

1

THR

ARG

ALA

HIS

LEU

THR

GLU

VAL

GLU

SER

2

ARG

LEU

GLU

ARG

LEU

GLU

GLN

LEU

PHE

LEU

3

LEU

ILE

PHE

PRO

ARG

GLU

ASP

LEU

ASP

MET

4

ILE

LEU

LYS

MET

ASP

SER

LEU

ARG

ASP

ILE

5

GLU

ALA

LEU

THR

GLY

LEU

PHE

VAL

GLN

6

ASP

ASN

VAL

ASN

LYS

ASP

ALA

Samples:

gal4_sample1: GAL4 dimerization domain1 – 2.0 mM

gal4_sample2: GAL4 dimerization domain, [U-15N; U-2H], 1.0 – 2.0 mM

gal4_sample3: GAL4 dimerization domain, [U-15N], 1.0 – 2.0 mM

gal4_sample4: GAL4 dimerization domain, [U-15N; U-13C], 1.0 – 2.0 mM

sample_cond_1: ionic strength: 0.1 M; pH: 7.4; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	not available	not available	not available
2D 1H-13C HSQC	not available	not available	not available
2D 1H-15N HSQC	not available	not available	not available
3D 1H-1H-15N NOESY	not available	not available	not available
3D 13C-1H-1H NOESY	not available	not available	not available
3D HNCA	not available	not available	not available
3D HN(CO)CA	not available	not available	not available
3D HNHA	not available	not available	not available
3D HNHB	not available	not available	not available

Software:

FELIX - Data processing

XEASY - Assignments

Molmol - Visual inspection of structures

InsightII - Visual inspection of structures

Procheck - Assesment quality of structures

NMR spectrometers:

Varian UnityPlus 400 MHz
Varian Unity 500 MHz
Varian INOVA 500 MHz
Varian UnityPlus 750 MHz
Bruker AMX 500 MHz