BMRB Entry 25849

Name: NMR Structure of the homeodomain transcription factor Gbx1[E17R,R52E} from Homo sapiens
Published: 2015-10-26

Click here to enlarge.

PDB ID: 2n8g
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25849
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:

NMR Structure of the homeodomain transcription factor Gbx1[E17R,R52E} from Homo sapiens

Deposition date:

2015-10-15

Original release date:

2015-10-26

Authors:

Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Proudfoot, Andrew; Geralt, Michael; Elsliger, Marc-Andre; Wilson, Ian; Wuthrich, Kurt; Serrano, Pedro. "Dynamic Local Polymorphisms in the Gbx1 Homeodomain Induced by DNA Binding" Structure 24, 1372-1379 (2016).
PubMed: 27396829

Assembly members:

Assembly members:
entity, polymer, 71 residues, 8316.757 Da.

Natural source:

Natural source: Common Name: humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GAPGGKSRRRRTAFTSEQLL ELRKEFHCKKYLSLTERSQI AHALKLSEVQVKIWFQNERA KWKRIKAGNVS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	298
15N chemical shifts	76
1H chemical shifts	462

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 71 residues - 8316.757 Da.

1

GLY

ALA

PRO

GLY

LYS

SER

ARG

2

ARG

THR

ALA

PHE

THR

SER

GLU

GLN

LEU

3

GLU

LEU

ARG

LYS

GLU

PHE

HIS

CYS

LYS

4

TYR

LEU

SER

LEU

THR

GLU

ARG

SER

GLN

ILE

5

ALA

HIS

ALA

LEU

LYS

LEU

SER

GLU

VAL

GLN

6

VAL

LYS

ILE

TRP

PHE

GLN

ASN

GLU

ARG

ALA

7

LYS

TRP

LYS

ARG

ILE

LYS

ALA

GLY

ASN

VAL

8

SER

Samples:

sample_1: entity, [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

DYANA, G??ntert P. - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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