BMRB Entry 11012

Name: 1H, 13C and 15N resonance assignments for the 25.8 kDa DNA binding domain of the human p63 protein
Published: 2015-06-16

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PDB ID: 2rmn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11012
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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:

1H, 13C and 15N resonance assignments for the 25.8 kDa DNA binding domain of the human p63 protein

Deposition date:

2007-11-01

Original release date:

2015-06-16

Authors:

Enthart, Andreas; Kessler, Horst

Citation:

Citation: Enthart, Andreas; Furrer, Julien; Dehner, Alexander; Kessler, Horst. "Solution structure and binding studies of the p63 DNA binding domain" .

Assembly members:

Assembly members:
p63BDB, polymer, 233 residues, 25883.586 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: p20020

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p63BDB: GSSTFDALSPSPAIPSNTDY PGPHSFDVSFQQSSTAKSAT WTYSTELKKLYCQIAKTCPI QIKVMTPPPQGAVIRAMPVY KKAEHVTEVVKRCPNHELSR EFNEGQIAPPSHLIRVEGNS HAQYVEDPITGRQSVLVPYE PPQVGTEFTTVLYNFMCNSS CVGGMNRRPILIIVTLETRD GQVLGRRCFEARICACPGRD RKADEDSIRKQQVSDSTKNG DAFRQNTHGIQMT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	877
15N chemical shifts	215
1H chemical shifts	1418

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p63BDB	1
2	ZINC ION	2

Entities:

Entity 1, p63BDB 233 residues - 25883.586 Da.

1

GLY

SER

THR

PHE

ASP

ALA

LEU

SER

PRO

2

SER

PRO

ALA

ILE

PRO

SER

ASN

THR

ASP

TYR

3

PRO

GLY

PRO

HIS

SER

PHE

ASP

VAL

SER

PHE

4

GLN

SER

THR

ALA

LYS

SER

ALA

THR

5

TRP

THR

TYR

SER

THR

GLU

LEU

LYS

LEU

6

TYR

CYS

GLN

ILE

ALA

LYS

THR

CYS

PRO

ILE

7

GLN

ILE

LYS

VAL

MET

THR

PRO

GLN

8

GLY

ALA

VAL

ILE

ARG

ALA

MET

PRO

VAL

TYR

9

LYS

ALA

GLU

HIS

VAL

THR

GLU

VAL

10

LYS

ARG

CYS

PRO

ASN

HIS

GLU

LEU

SER

ARG

11

GLU

PHE

ASN

GLU

GLY

GLN

ILE

ALA

PRO

12

SER

HIS

LEU

ILE

ARG

VAL

GLU

GLY

ASN

SER

13

HIS

ALA

GLN

TYR

VAL

GLU

ASP

PRO

ILE

THR

14

GLY

ARG

GLN

SER

VAL

LEU

VAL

PRO

TYR

GLU

15

PRO

GLN

VAL

GLY

THR

GLU

PHE

THR

16

VAL

LEU

TYR

ASN

PHE

MET

CYS

ASN

SER

17

CYS

VAL

GLY

MET

ASN

ARG

PRO

ILE

18

LEU

ILE

VAL

THR

LEU

GLU

THR

ARG

ASP

19

GLY

GLN

VAL

LEU

GLY

ARG

CYS

PHE

GLU

20

ALA

ARG

ILE

CYS

ALA

CYS

PRO

GLY

ARG

ASP

21

ARG

LYS

ALA

ASP

GLU

ASP

SER

ILE

ARG

LYS

22

GLN

VAL

SER

ASP

SER

THR

LYS

ASN

GLY

23

ASP

ALA

PHE

ARG

GLN

ASN

THR

HIS

GLY

ILE

24

GLN

MET

THR

Entity 2, ZINC ION - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: p63BDB, [U-15N], 0.7 ± 0.1 mM; potassium chloride 50 mM; potassium phosphate 50 mM; DTT 5 mM

sample_2: p63BDB, [U-13C; U-15N], 0.7 ± 0.1 mM; potassium chloride 50 mM; potassium phosphate 50 mM; DTT 5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D CNH NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1

Software:

SPARKY v3.110, Goddard - chemical shift assignment, data analysis, peak picking

X-PLOR NIH v2.16.0, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

xwinnmr, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 900 MHz
Bruker DMX 600 MHz

PDB	2RMN 3QYM 3QYN 3US0 3US1 3US2
DBJ	BAA32432 BAA32433 BAA32592 BAA32593 BAB20631
EMBL	CAA76562 CAB88216 CAC37098 CAC37099 CAC37100
GB	AAC24830 AAC43038 AAC62633 AAC62634 AAC62635
REF	NP_001079107 NP_001108450 NP_001108451 NP_001108452 NP_001108453
SP	O88898 Q9H3D4 Q9JJP6
TPG	DAA33389
AlphaFold	O88898 Q9H3D4 Q9JJP6