BMRB Entry 7158

Name: Molecular characterization of the Ran binding zinc finger domain
Published: 2007-04-19

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PDB ID: 2gqe
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR7158
MolProbity Validation Chart

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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:

Molecular characterization of the Ran binding zinc finger domain

Deposition date:

2006-06-07

Original release date:

2007-04-19

Authors:

Alam, Steven; Higa, Meda; Ullman, Katharine; Sundquist, Wesley

Citation:

Citation: Higa, Meda; Alam, Steven; Sundquist, Wesley; Ullman, Katharine. "Molecular characterization of the ran-binding zinc finger domain of Nup153" J. Biol. Chem. 282, 17090-17100 (2007).
PubMed: 17426026

Assembly members:

Assembly members:
hNUP153, polymer, 32 residues, 3488 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hNUP153: GHMVIGTWDCDTCLVQNKPE AIKCVACETPKP

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
13C chemical shifts	136
15N chemical shifts	30
1H chemical shifts	218

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hNUP153 Zinc finger	1
2	ZINC (II) ION, 1	2

Entities:

Entity 1, hNUP153 Zinc finger 32 residues - 3488 Da.

Numbering starting at V3 represents V722 in the hNUP153 protein

1

GLY

HIS

MET

VAL

ILE

GLY

THR

TRP

ASP

CYS

2

ASP

THR

CYS

LEU

VAL

GLN

ASN

LYS

PRO

GLU

3

ALA

ILE

LYS

CYS

VAL

ALA

CYS

GLU

THR

PRO

4

LYS

PRO

Entity 2, ZINC (II) ION, 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: hNUP153, [U-95% 15N], 1.5 ± 0.1 mM; tris buffer 20 ± 0.01 mM; NaCl 50 ± 0.01 mM; BME 5 ± 0.01 mM; ZnCl2 10 ± 0.01 um

sample_2: hNUP153, [U-95% 13C; U-95% 15N], 1.0 ± 0.1 mM; tris buffer 20 ± 0.01 mM; NaCl 50 ± 0.01 mM; BME 5 ± 0.01 mM; ZnCl2 10 ± 0.01 micromolar

conditions_1: ionic strength: 70 mM; pH*: 7.0; pressure: 1.0 atm; temperature: 293 K

conditions_2: ionic strength: 70 mM; pH: 7.2; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H15N_HSQC	not available	not available	not available
1H13C HSQC	not available	not available	not available
HNCA	not available	not available	not available
HNCO	not available	not available	not available
HC(CO)CA	not available	not available	not available
HNCACB	not available	not available	not available
CBCAC(CO)NH	not available	not available	not available
H(CCO)NH-TOCSY	not available	not available	not available
HCCH-TOCSY	not available	not available	not available
(H)C(CO)NH-TOCSY	not available	not available	not available
HNHA	not available	not available	not available
HNHB	not available	not available	not available
HN(CO)HB	not available	not available	not available
LRCC	not available	not available	not available
1H13C 3D-NOESY	not available	not available	not available
1H15N 3D NOESY	not available	not available	not available
HCCH-COSY	not available	not available	not available

Software:

CYANA v2.1, CYANA - noe assignment, refinement

VNMR v3.1C, Varian - Aquisition of Data

SPARKY v3.110, Sparky - Assignments

FELIX v2004, Accelrys -

NMR spectrometers:

Varian INOVA 600 MHz

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