BMRB Entry 50405

Name: WT1(-KTS) backbone and side chain 13C, 15N and 1H assignments
Published: 2020-07-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50405

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:

WT1(-KTS) backbone and side chain 13C, 15N and 1H assignments

Deposition date:

2020-07-22

Original release date:

2020-07-27

Authors:

Nishikawa, Tadateru; Wojciak, Jonathan; Dyson, Helen Jane; Wright, Peter

Citation:

Citation: Laity, J.; Chung, J.; Dyson, H.; Wright, P.. "Alternative splicing of Wilms' tumor suppressor protein modulates DNA binding activity through isoform-specific DNA-induced conformational changes." Biochemistry 39, 5341-5348 (2000).
PubMed: 10820004

Assembly members:

Assembly members:
entity_1, polymer, 119 residues, 14450 Da.
entity_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: recombinant technology Host organism: Escherichia coli Vector: PET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ASEKRPFMCAYPGCNKRYFK LSHLQMHSRKHTGEKPYQCD FKDCERRFSRSDQLKRHQRR HTGVKPFQCKTCQRKFSRSD HLKTHTRTHTGEKPFSCRWP SCQKKFARSDELVRHHNMH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	395
15N chemical shifts	109
1H chemical shifts	724

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	WT1-KTS	1
2	Zn 1	2
3	Zn 2	2
4	Zn 3	2
5	Zn 4	2

Entities:

Entity 1, WT1-KTS 119 residues - 14450 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, Zn 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: WT1, [U-95% 13C; U-95% 15N], 0.55 mM; deuterated Tris 10 mM; KCl 20 mM; DTT 2 mM; NaN3 1 mM

sample_conditions_1: pH: 6.8; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N-HSQC	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH-	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_1	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

NMRView vNMRviewJ implemented in NMRBox - peak picking, analysis

NMR spectrometers:

Bruker AVANCE III 900 MHz
Bruker Avance 750 MHz
Bruker Avance 500 MHz
Bruker DRX 800 MHz
Bruker DRX 600 MHz

BMRB	15532 15533 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
AlphaFold	B5DE03 O62651 P79958 Q8IYZ5