BMRB Entry 18714

Name: Solution NMR Structure of Homeobox 2 Domain from Human ZHX1 repressor, Northeast Structural Genomics Consortium (NESG) Target HR7907F
Published: 2012-11-12

Click here to enlarge.

PDB ID: 2ly9
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/BMR18714
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 NMR Structure of Homeobox 2 Domain from Human ZHX1 repressor, Northeast Structural Genomics Consortium (NESG) Target HR7907F

Deposition date:

2012-09-14

Original release date:

2012-11-12

Authors:

Xu, Xianzhong; Eletsky, Alexander; Mills, Jeffrey; Pulavarti, Surya; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Xu, Xianzhong; Eletsky, Alexander; Mills, Jeffrey; Pulavarti, Surya; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Homeobox 2 Domain from Human ZHX1 repressor, Northeast Structural Genomics Consortium (NESG) Target HR7907F" To be published ., .-..

Assembly members:

Assembly members:
HR7907F, polymer, 74 residues, 8710.092 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15Avi6HT_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR7907F: SHMPDSFGIRAKKTKEQLAE LKVSYLKNQFPHDSEIIRLM KITGLTKGEIKKWFSDTRYN QRNSKSNQCLHLNN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	332
15N chemical shifts	83
1H chemical shifts	537

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR7907F	1

Entities:

Entity 1, HR7907F 74 residues - 8710.092 Da.

Residues 4-74 correspond to residues 462-532 of the native protein. Residues 1-3 represent the remainder of the affinity tag.

1

SER

HIS

MET

PRO

ASP

SER

PHE

GLY

ILE

ARG

2

ALA

LYS

THR

LYS

GLU

GLN

LEU

ALA

GLU

3

LEU

LYS

VAL

SER

TYR

LEU

LYS

ASN

GLN

PHE

4

PRO

HIS

ASP

SER

GLU

ILE

ARG

LEU

MET

5

LYS

ILE

THR

GLY

LEU

THR

LYS

GLY

GLU

ILE

6

LYS

TRP

PHE

SER

ASP

THR

ARG

TYR

ASN

7

GLN

ARG

ASN

SER

LYS

SER

ASN

GLN

CYS

LEU

8

HIS

LEU

ASN

Samples:

NC: HR7907F, [U-100% 13C; U-100% 15N], 0.4 mM; sodium azide 0.02%; DTT 10 mM; calcium chloride 5 mM; sodium chloride 100 mM; Proteinase Inhibitors 1 x; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%

NC5: HR7907F, [5% 13C; U-100% 15N], 0.3 mM; sodium azide 0.02%; DTT 10 mM; calcium chloride 5 mM; sodium chloride 100 mM; Proteinase Inhibitors 1 x; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%

Conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	Conditions_1
2D 1H-13C HSQC	NC	isotropic	Conditions_1
3D HNCO	NC	isotropic	Conditions_1
(4,3)D GFT CABCA(CO)NHN	NC	isotropic	Conditions_1
(4,3)D GFT HNNCABCA	NC	isotropic	Conditions_1
2D 1H-13C HSQC	NC5	isotropic	Conditions_1
(4,3)D GFT HCCH-COSY alipahtic	NC	isotropic	Conditions_1
3D (H)CCH-TOCSY aliphatic	NC	isotropic	Conditions_1
3D 13C/15N-edited NOESY	NC	isotropic	Conditions_1
(4,3)D GFT HABCAB(CO)NH	NC	isotropic	Conditions_1
3D (H)CCH-COSY aromatic	NC	isotropic	Conditions_1

Software:

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AS-DP v1.0, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

XEASY, Bartels et al. - data analysis

VNMRJ, Varian - collection

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 750 MHz

UNP	Q9UKY1
PDB	2LY9
AlphaFold	Q8IWD8