BMRB Entry 10093

Name: Solution structure of the second CUT domain of human Homeobox protein Cux-2
Published: 2008-08-14

Click here to enlarge.

PDB ID: 1wh6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10093
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 second CUT domain of human Homeobox protein Cux-2

Deposition date:

2007-01-24

Original release date:

2008-08-14

Authors:

Nameki, N.; Tochio, N.; Koshiba, S.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Nameki, N.; Tochio, N.; Koshiba, S.; Kigawa, T.; Yokoyama, S.. "Solution structure of the second CUT domain of human Homeobox protein Cux-2" .

Assembly members:

Assembly members:
CUT domain, polymer, 101 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: cell free synthesis Vector: P040114-61

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CUT domain: GSSGSSGQYELYMYREVDTL ELTRQVKEKLAKNGICQRIF GEKVLGLSQGSVSDMLSRPK PWSKLTQKGREPFIRMQLWL SDQLGQAVGQQPGASSGPSS G

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	432
15N chemical shifts	108
1H chemical shifts	693

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Homeobox protein Cux-2	1

Entities:

Entity 1, Homeobox protein Cux-2 101 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

GLN

TYR

GLU

2

LEU

TYR

MET

TYR

ARG

GLU

VAL

ASP

THR

LEU

3

GLU

LEU

THR

ARG

GLN

VAL

LYS

GLU

LYS

LEU

4

ALA

LYS

ASN

GLY

ILE

CYS

GLN

ARG

ILE

PHE

5

GLY

GLU

LYS

VAL

LEU

GLY

LEU

SER

GLN

GLY

6

SER

VAL

SER

ASP

MET

LEU

SER

ARG

PRO

LYS

7

PRO

TRP

SER

LYS

LEU

THR

GLN

LYS

GLY

ARG

8

GLU

PRO

PHE

ILE

ARG

MET

GLN

LEU

TRP

LEU

9

SER

ASP

GLN

LEU

GLY

GLN

ALA

VAL

GLY

GLN

10

GLN

PRO

GLY

ALA

SER

GLY

PRO

SER

11

GLY

Samples:

sample_1: CUT domain, [U-13C; U-15N], 0.3 mM; phosphate 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated_NOESY	not available	not available	not available
3D 13C-separated_NOESY	not available	not available	not available

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.901, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - data analysis

OPALp, Billeter, M., Guntert, P., Koradi, R. - refinement

NMR spectrometers:

Bruker AVANCE 700 MHz