BMRB Entry 15533

Name: Structure of the Wilms' Tumor Suppressor Protein Zinc Finger Domain Bound to DNA
Published: 2008-02-14

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PDB ID: 2jpa
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15533
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Structure of the Wilms' Tumor Suppressor Protein Zinc Finger Domain Bound to DNA PubMed: 17716689

Deposition date: 2007-10-18 Original release date: 2008-02-14

Authors: Stoll, Raphael; Lee, Brian; Debler, Erik; Laity, John; Wilson, Ian; Dyson, Helen; Wright, Peter

Citation: Stoll, Raphael; Lee, Brian; Debler, Erik; Laity, John; Wilson, Ian; Dyson, Helen; Wright, Peter. "Structure of the Wilms Tumor Suppressor Protein Zinc Finger Domain Bound to DNA" J. Mol. Biol. 372, 1227-1245 (2007).

Assembly members:
wt1-zf14, polymer, 119 residues, 14494.849 Da.
ZN, non-polymer, 65.409 Da.
wt1-14mer_1, polymer, 14 residues, Formula weight is not available
wt1-14mer_2, polymer, 14 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
wt1-zf14: ASEKRPFMCAYPGCNKRYFK LSHLQMHSRKHTGEKPYQCD FKDCERRFSRSDQLKRHQRR HTGVKPFQCKTCQRKFSRSD HLKTHTRTHTGEKPFSCRWP SCQKKFARSDELVRHHNMH
wt1-14mer_1: CGCGGGGGCGTCTG
wt1-14mer_2: CAGACGCCCCCGCG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	115
1H chemical shifts	121

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	wt1-zf14	1
2	zinc1	2
3	zinc2	2
4	zinc3	2
5	zinc4	2
6	strand1	3
7	strand2	4

Entities:

Entity 1, wt1-zf14 119 residues - 14494.849 Da.

1

ALA

SER

GLU

LYS

ARG

PRO

PHE

MET

CYS

ALA

2

TYR

PRO

GLY

CYS

ASN

LYS

ARG

TYR

PHE

LYS

3

LEU

SER

HIS

LEU

GLN

MET

HIS

SER

ARG

LYS

4

HIS

THR

GLY

GLU

LYS

PRO

TYR

GLN

CYS

ASP

5

PHE

LYS

ASP

CYS

GLU

ARG

PHE

SER

ARG

6

SER

ASP

GLN

LEU

LYS

ARG

HIS

GLN

ARG

7

HIS

THR

GLY

VAL

LYS

PRO

PHE

GLN

CYS

LYS

8

THR

CYS

GLN

ARG

LYS

PHE

SER

ARG

SER

ASP

9

HIS

LEU

LYS

THR

HIS

THR

ARG

THR

HIS

THR

10

GLY

GLU

LYS

PRO

PHE

SER

CYS

ARG

TRP

PRO

11

SER

CYS

GLN

LYS

PHE

ALA

ARG

SER

ASP

12

GLU

LEU

VAL

ARG

HIS

ASN

MET

HIS

Entity 2, zinc1 - Zn - 65.409 Da.

1

ZN

Entity 3, strand1 14 residues - Formula weight is not available

1

DC

DG

DC

DG

DC

DG

2

DT

DC

DT

DG

Entity 4, strand2 14 residues - Formula weight is not available

1

DC

DA

DG

DA

DC

DG

DC

2

DC

DG

DC

DG

Samples:

sample_1: wt1-14mer, [U-100% 13C; U-100% 15N], 0.6 mM; Tris/HCl 10 mM; KCl 20 mM; ZnSO4 5 uM; NaN3 2 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.7; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
IPAP	sample_1	anisotropic	sample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - structure solution

NMR spectrometers:

Bruker DRX 600 MHz
Bruker DRX 800 MHz
Bruker Avance 900 MHz

BMRB	15532 4707 4708 4709 4710
PDB	2JP9 2JPA 2PRT
DBJ	BAA11522 BAA28147 BAA94793 BAF84425
EMBL	CAA35956 CAA43819 CDG23662
GB	AAA36810 AAA61299 AAB33443 AAB53152 AAH32861
PRF	1604420A
REF	NP_000369 NP_001001264 NP_001079057 NP_001079336 NP_001135625
SP	B5DE03 O62651 P19544 P79958
TPG	DAA21902

Biological Magnetic Resonance Data Bank