BMRB Entry 10166

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PDB ID: 2em1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR10166
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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 structure of the C2H2 type zinc finger (region 637-667) of human Zinc finger protein 268

Deposition date:

2007-12-28

Original release date:

2009-02-23

Authors:

Tomizawa, T.; Tochio, N.; Abe, H.; Saito, K.; Li, H.; Sato, M.; Koshiba, S.; Kobayashi, N.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Tochio, N.; Tomizawa, T.; Abe, H.; Saito, K.; Li, H.; Sato, M.; Koshiba, S.; Kobayashi, N.; Kigawa, T.; Yokoyama, S.. "Solution structure of the C2H2 type zinc finger (region 637-667) of human Zinc finger protein 268" .

Assembly members:

Assembly members:
zf-C2H2 domain, polymer, 44 residues, Formula weight is not available
ZN, non-polymer, 65.409 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: cell free synthesis Vector: P061218-14

Entity Sequences (FASTA):

Entity Sequences (FASTA):
zf-C2H2 domain: GSSGSSGEKPYSCNECGKAF TFKSQLIVHKGVHTGVKPSG PSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	154
15N chemical shifts	32
1H chemical shifts	233

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Zinc finger protein 268	1
2	ZINC ION	2

Entities:

Entity 1, Zinc finger protein 268 44 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

GLU

LYS

PRO

2

TYR

SER

CYS

ASN

GLU

CYS

GLY

LYS

ALA

PHE

3

THR

PHE

LYS

SER

GLN

LEU

ILE

VAL

HIS

LYS

4

GLY

VAL

HIS

THR

GLY

VAL

LYS

PRO

SER

GLY

5

PRO

SER

GLY

Entity 2, ZINC ION - Zn - 65.409 Da.

Samples:

sample_1: Zinc finger protein 268, [U-13C; U-15N], 1.0 ± 0.1 mM; d-Tris-HCl 20 mM; NaCl 100 mM; ZnCl2 0.05 mM; IDA 1 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	not available	condition_1
3D 15N-separated NOESY	sample_1	not available	condition_1

Software:

TOPSPIN v1.3, Bruker - collection

NMRPipe v20030801, Delaglio, F - processing

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

Kujira v0.9820, Kobayashi, N. - data analysis

CYANA v2.0.17, Guentert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE II 900 MHz